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Database: PDB
Entry: 4L04
LinkDB: 4L04
Original site: 4L04 
HEADER    OXIDOREDUCTASE                          30-MAY-13   4L04              
TITLE     CRYSTAL STRUCTURE ANALYSIS OF HUMAN IDH1 MUTANTS IN COMPLEX WITH NADP+
TITLE    2 AND CA2+/ALPHA-KETOGLUTARATE                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ISOCITRATE DEHYDROGENASE [NADP] CYTOPLASMIC;               
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: IDH, CYTOSOLIC NADP-ISOCITRATE DEHYDROGENASE, IDP, NADP(+)- 
COMPND   5 SPECIFIC ICDH, OXALOSUCCINATE DECARBOXYLASE;                         
COMPND   6 EC: 1.1.1.42;                                                        
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: IDH1, PICD;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2(DE3);                            
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET41A                                    
KEYWDS    CYTOSOLIC, OXIDOREDUCTASE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.O.CONCHA,A.M.SMALLWOOD                                              
REVDAT   2   15-NOV-17 4L04    1       REMARK                                   
REVDAT   1   31-JUL-13 4L04    0                                                
JRNL        AUTH   A.R.RENDINA,B.PIETRAK,A.SMALLWOOD,H.ZHAO,H.QI,C.QUINN,       
JRNL        AUTH 2 N.D.ADAMS,N.CONCHA,C.DURAISWAMI,S.H.THRALL,S.SWEITZER,       
JRNL        AUTH 3 B.SCHWARTZ                                                   
JRNL        TITL   MUTANT IDH1 ENHANCES THE PRODUCTION OF 2-HYDROXYGLUTARATE    
JRNL        TITL 2 DUE TO ITS KINETIC MECHANISM.                                
JRNL        REF    BIOCHEMISTRY                  V.  52  4563 2013              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   23731180                                                     
JRNL        DOI    10.1021/BI400514K                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.87 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.87                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.24                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 70733                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3578                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1  2.9400 -  2.8700    0.98     4313   226  0.2381 0.3043        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.170           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 71.28                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 72.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.81080                                             
REMARK   3    B22 (A**2) : -1.96740                                             
REMARK   3    B33 (A**2) : 7.77820                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009          19997                                  
REMARK   3   ANGLE     :  1.140          27106                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           2895                                  
REMARK   3   DIHEDRAL  :   NULL           7002                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|504 - A|504 C|503 - C|503 B|502 - B|502 E|503 -    
REMARK   3               E|503 D|503 - D|503 F|503 - F|503 }                    
REMARK   3    ORIGIN FOR THE GROUP (A):   8.8620 -48.6530 -98.2878              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3197 T22:   0.0300                                     
REMARK   3      T33:  -0.1267 T12:   0.0215                                     
REMARK   3      T13:  -0.0674 T23:  -0.0547                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.4249 L12:  -0.1238                                     
REMARK   3      L13:  -0.2623 L23:   0.2618                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0401 S12:  -0.0224 S13:   0.0474                       
REMARK   3      S21:  -0.0125 S22:   0.1856 S23:  -0.1064                       
REMARK   3      S31:   0.1438 S32:   0.1608 S33:  -0.2257                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|5 - A|415 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):  20.6685 -44.7945 -69.4636              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2312 T22:  -0.1447                                     
REMARK   3      T33:   0.0503 T12:   0.1233                                     
REMARK   3      T13:  -0.2071 T23:  -0.1839                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6178 L22:   2.2334                                     
REMARK   3      L33:   1.0923 L12:  -1.4635                                     
REMARK   3      L13:  -0.0517 L23:   0.0731                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2630 S12:  -0.0025 S13:  -0.7908                       
REMARK   3      S21:  -0.1612 S22:   0.0018 S23:   0.6622                       
REMARK   3      S31:   0.3891 S32:   0.3684 S33:  -0.2648                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { B|3 - B|414 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):  21.0931 -13.9543 -67.0476              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2057 T22:  -0.0025                                     
REMARK   3      T33:  -0.1098 T12:  -0.0266                                     
REMARK   3      T13:   0.0855 T23:  -0.1630                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0575 L22:   1.6737                                     
REMARK   3      L33:   1.0806 L12:   0.0956                                     
REMARK   3      L13:   0.3828 L23:   0.0919                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1028 S12:   0.0455 S13:   0.1301                       
REMARK   3      S21:  -0.0325 S22:   0.0702 S23:   0.1756                       
REMARK   3      S31:  -0.1780 S32:   0.4242 S33:  -0.1730                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { C|4 - C|415 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A): -23.7184 -47.6629-110.6550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2190 T22:  -0.1621                                     
REMARK   3      T33:  -0.1218 T12:  -0.0633                                     
REMARK   3      T13:   0.2626 T23:  -0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6056 L22:   1.9150                                     
REMARK   3      L33:   2.0270 L12:   0.2413                                     
REMARK   3      L13:   0.0393 L23:   0.0543                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1004 S12:   0.1072 S13:  -0.0232                       
REMARK   3      S21:  -0.8484 S22:   0.2071 S23:  -0.5040                       
REMARK   3      S31:   0.2059 S32:  -0.0007 S33:  -0.1068                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { D|3 - D|414 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A): -27.1869 -17.2212-106.6400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3317 T22:  -0.1526                                     
REMARK   3      T33:  -0.1581 T12:   0.1496                                     
REMARK   3      T13:   0.2148 T23:   0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2082 L22:   2.7028                                     
REMARK   3      L33:   2.2614 L12:   0.2333                                     
REMARK   3      L13:   0.0982 L23:  -0.8349                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0227 S12:   0.0538 S13:   0.1395                       
REMARK   3      S21:  -0.5808 S22:   0.0683 S23:  -0.2888                       
REMARK   3      S31:  -0.5930 S32:  -0.3157 S33:  -0.0455                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { E|4 - E|415 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):  25.9117 -68.9448-112.2680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2690 T22:  -0.2098                                     
REMARK   3      T33:  -0.0909 T12:  -0.0086                                     
REMARK   3      T13:  -0.2962 T23:  -0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7152 L22:   1.9826                                     
REMARK   3      L33:   1.8283 L12:   0.3435                                     
REMARK   3      L13:   0.0498 L23:  -0.2489                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0926 S12:   0.1071 S13:   0.1632                       
REMARK   3      S21:  -0.7874 S22:   0.2370 S23:   0.5412                       
REMARK   3      S31:  -0.2266 S32:   0.0006 S33:  -0.1444                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { F|3 - F|414 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):  28.3992 -99.4718-107.9520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3781 T22:  -0.1521                                     
REMARK   3      T33:  -0.2035 T12:   0.2198                                     
REMARK   3      T13:  -0.2487 T23:  -0.0577                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3536 L22:   2.0585                                     
REMARK   3      L33:   2.4294 L12:   0.4850                                     
REMARK   3      L13:  -0.4919 L23:   0.4007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0254 S12:   0.0358 S13:  -0.1044                       
REMARK   3      S21:  -0.6470 S22:   0.0342 S23:   0.1916                       
REMARK   3      S31:   0.6184 S32:   0.2384 S33:  -0.0089                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4L04 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000080012.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9786                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70831                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.866                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.87                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63100                            
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16-20% PEG MME 2000, 100MM MES, PH       
REMARK 280  6.9, VAPOR DIFFUSION, TEMPERATURE 298K                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       48.20500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      137.86450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.31100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      137.86450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       48.20500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.31100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10870 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 30560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10940 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 30530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10960 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 29910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     LEU A   416                                                      
REMARK 465     GLU A   417                                                      
REMARK 465     HIS A   418                                                      
REMARK 465     HIS A   419                                                      
REMARK 465     HIS A   420                                                      
REMARK 465     HIS A   421                                                      
REMARK 465     HIS A   422                                                      
REMARK 465     HIS A   423                                                      
REMARK 465     HIS A   424                                                      
REMARK 465     HIS A   425                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     SER B   415                                                      
REMARK 465     LEU B   416                                                      
REMARK 465     GLU B   417                                                      
REMARK 465     HIS B   418                                                      
REMARK 465     HIS B   419                                                      
REMARK 465     HIS B   420                                                      
REMARK 465     HIS B   421                                                      
REMARK 465     HIS B   422                                                      
REMARK 465     HIS B   423                                                      
REMARK 465     HIS B   424                                                      
REMARK 465     HIS B   425                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     LEU C   416                                                      
REMARK 465     GLU C   417                                                      
REMARK 465     HIS C   418                                                      
REMARK 465     HIS C   419                                                      
REMARK 465     HIS C   420                                                      
REMARK 465     HIS C   421                                                      
REMARK 465     HIS C   422                                                      
REMARK 465     HIS C   423                                                      
REMARK 465     HIS C   424                                                      
REMARK 465     HIS C   425                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     SER D   415                                                      
REMARK 465     LEU D   416                                                      
REMARK 465     GLU D   417                                                      
REMARK 465     HIS D   418                                                      
REMARK 465     HIS D   419                                                      
REMARK 465     HIS D   420                                                      
REMARK 465     HIS D   421                                                      
REMARK 465     HIS D   422                                                      
REMARK 465     HIS D   423                                                      
REMARK 465     HIS D   424                                                      
REMARK 465     HIS D   425                                                      
REMARK 465     MET E     1                                                      
REMARK 465     SER E     2                                                      
REMARK 465     LYS E     3                                                      
REMARK 465     LEU E   416                                                      
REMARK 465     GLU E   417                                                      
REMARK 465     HIS E   418                                                      
REMARK 465     HIS E   419                                                      
REMARK 465     HIS E   420                                                      
REMARK 465     HIS E   421                                                      
REMARK 465     HIS E   422                                                      
REMARK 465     HIS E   423                                                      
REMARK 465     HIS E   424                                                      
REMARK 465     HIS E   425                                                      
REMARK 465     MET F     1                                                      
REMARK 465     SER F     2                                                      
REMARK 465     SER F   415                                                      
REMARK 465     LEU F   416                                                      
REMARK 465     GLU F   417                                                      
REMARK 465     HIS F   418                                                      
REMARK 465     HIS F   419                                                      
REMARK 465     HIS F   420                                                      
REMARK 465     HIS F   421                                                      
REMARK 465     HIS F   422                                                      
REMARK 465     HIS F   423                                                      
REMARK 465     HIS F   424                                                      
REMARK 465     HIS F   425                                                      
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 A  36    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  80    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  81    CE   NZ                                             
REMARK 470     GLU A 174    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 187    CG   CD   CE   NZ                                   
REMARK 470     LYS A 233    CG   CD   CE   NZ                                   
REMARK 470     GLU A 262    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 350    CG   CD   CE   NZ                                   
REMARK 470     LYS A 406    CE   NZ                                             
REMARK 470     LYS A 413    CG   CD   CE   NZ                                   
REMARK 470     SER A 415    OG                                                  
REMARK 470     LYS B   3    CG   CD   CE   NZ                                   
REMARK 470     GLN B  90    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 233    CG   CD   CE   NZ                                   
REMARK 470     LYS B 301    CG   CD   CE   NZ                                   
REMARK 470     GLU B 324    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 350    CG   CD   CE   NZ                                   
REMARK 470     LYS C 115    CG   CD   CE   NZ                                   
REMARK 470     GLU C 174    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 233    CG   CD   CE   NZ                                   
REMARK 470     GLU C 240    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 346    CG   CD1  CD2                                       
REMARK 470     ASN C 348    CG   OD1  ND2                                       
REMARK 470     LYS C 350    CG   CD   CE   NZ                                   
REMARK 470     PHE C 354    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS C 381    CD   CE   NZ                                        
REMARK 470     LEU C 383    CG   CD1  CD2                                       
REMARK 470     GLN C 387    CG   CD   OE1  NE2                                  
REMARK 470     ASP C 390    CG   OD1  OD2                                       
REMARK 470     PHE C 395    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU C 401    CG   CD1  CD2                                       
REMARK 470     LEU C 409    CG   CD1  CD2                                       
REMARK 470     LYS C 413    CG   CD   CE   NZ                                   
REMARK 470     LYS D   3    CG   CD   CE   NZ                                   
REMARK 470     GLU D  24    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  27    CG   CD   CE   NZ                                   
REMARK 470     GLU D  28    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  29    CG   CD   CE   NZ                                   
REMARK 470     GLU D  36    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  47    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  58    CG   CD   CE   NZ                                   
REMARK 470     GLU D  80    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  81    CG   CD   CE   NZ                                   
REMARK 470     VAL D  83    CG1  CG2                                            
REMARK 470     GLU D  84    CG   CD   OE1  OE2                                  
REMARK 470     PHE D  86    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS D  87    CG   CD   CE   NZ                                   
REMARK 470     MET D  91    CG   SD   CE                                        
REMARK 470     LYS D 236    CE   NZ                                             
REMARK 470     LYS D 243    CG   CD   CE   NZ                                   
REMARK 470     LYS D 301    CG   CD   CE   NZ                                   
REMARK 470     TYR D 319    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN D 320    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 321    CG   CD   CE   NZ                                   
REMARK 470     GLN D 323    CG   CD   OE1  NE2                                  
REMARK 470     GLU D 324    CG   CD   OE1  OE2                                  
REMARK 470     THR D 325    OG1  CG2                                            
REMARK 470     LYS D 350    CG   CD   CE   NZ                                   
REMARK 470     ILE D 380    CG1  CG2  CD1                                       
REMARK 470     LYS D 381    CG   CD   CE   NZ                                   
REMARK 470     LEU D 383    CG   CD1  CD2                                       
REMARK 470     VAL D 386    CG1  CG2                                            
REMARK 470     GLN D 387    CG   CD   OE1  NE2                                  
REMARK 470     ARG D 388    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN D 393    CG   OD1  ND2                                       
REMARK 470     THR D 394    OG1  CG2                                            
REMARK 470     PHE D 395    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU D 396    CG   CD   OE1  OE2                                  
REMARK 470     MET D 398    CG   SD   CE                                        
REMARK 470     LYS D 413    CG   CD   CE   NZ                                   
REMARK 470     LEU D 414    CG   CD1  CD2                                       
REMARK 470     LYS E   4    CG   CD   CE   NZ                                   
REMARK 470     GLU E 174    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 233    CG   CD   CE   NZ                                   
REMARK 470     LYS E 243    CG   CD   CE   NZ                                   
REMARK 470     LYS E 301    CG   CD   CE   NZ                                   
REMARK 470     LYS E 350    CG   CD   CE   NZ                                   
REMARK 470     GLU E 351    CG   CD   OE1  OE2                                  
REMARK 470     GLN E 387    CG   CD   OE1  NE2                                  
REMARK 470     PHE E 395    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU E 403    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 413    CG   CD   CE   NZ                                   
REMARK 470     LYS F   3    CG   CD   CE   NZ                                   
REMARK 470     SER F   6    OG                                                  
REMARK 470     ILE F  31    CG1  CG2  CD1                                       
REMARK 470     GLU F  36    CG   CD   OE1  OE2                                  
REMARK 470     GLU F  47    CG   CD   OE1  OE2                                  
REMARK 470     GLU F  80    CG   CD   OE1  OE2                                  
REMARK 470     LYS F  81    CG   CD   CE   NZ                                   
REMARK 470     GLU F  84    CG   CD   OE1  OE2                                  
REMARK 470     LYS F  87    CG   CD   CE   NZ                                   
REMARK 470     GLN F 163    CG   CD   OE1  NE2                                  
REMARK 470     LYS F 243    CG   CD   CE   NZ                                   
REMARK 470     GLU F 262    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 301    CG   CD   CE   NZ                                   
REMARK 470     LYS F 321    CG   CD   CE   NZ                                   
REMARK 470     GLN F 323    CG   CD   OE1  NE2                                  
REMARK 470     GLU F 324    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 350    CG   CD   CE   NZ                                   
REMARK 470     GLU F 351    CG   CD   OE1  OE2                                  
REMARK 470     ILE F 380    CG1  CG2  CD1                                       
REMARK 470     GLN F 387    CG   CD   OE1  NE2                                  
REMARK 470     GLU F 396    CG   CD   OE1  OE2                                  
REMARK 470     GLN F 411    CG   CD   OE1  NE2                                  
REMARK 470     LYS F 413    CG   CD   CE   NZ                                   
REMARK 470     LEU F 414    CG   CD1  CD2                                       
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  17     -132.49     49.23                                   
REMARK 500    ILE A  31      -60.89   -103.35                                   
REMARK 500    ASN A  68      -12.73     64.20                                   
REMARK 500    ASP A  79     -161.17   -115.21                                   
REMARK 500    TRP A 124       82.88    -61.07                                   
REMARK 500    ASP A 137     -137.22     54.10                                   
REMARK 500    ARG A 140       61.47   -154.29                                   
REMARK 500    TYR A 167      115.71   -168.43                                   
REMARK 500    HIS A 170      139.56   -173.57                                   
REMARK 500    LEU A 216       68.73   -102.36                                   
REMARK 500    GLN A 234      -41.49   -138.66                                   
REMARK 500    ASN A 271      -64.62    -28.43                                   
REMARK 500    MET A 290       58.86   -116.38                                   
REMARK 500    THR A 325      171.55     62.53                                   
REMARK 500    SER A 326       88.53   -168.10                                   
REMARK 500    GLU B  17     -131.20     36.67                                   
REMARK 500    ILE B  31      -66.90    -96.72                                   
REMARK 500    LEU B  44       31.76    -95.23                                   
REMARK 500    ASN B  68       -7.07     67.59                                   
REMARK 500    TRP B 124       72.30    -56.00                                   
REMARK 500    ASP B 137     -134.55     50.87                                   
REMARK 500    ARG B 140       32.69   -160.00                                   
REMARK 500    PHE B 172       98.58    -69.91                                   
REMARK 500    LEU B 216       65.41   -104.17                                   
REMARK 500    GLN B 234      -14.43   -140.63                                   
REMARK 500    ASN B 271      -72.19    -17.71                                   
REMARK 500    GLU C  17     -135.29     48.30                                   
REMARK 500    ASN C  68      -26.40     68.58                                   
REMARK 500    ASP C  79     -161.39   -105.82                                   
REMARK 500    ASP C 137     -133.64     61.28                                   
REMARK 500    ARG C 140       43.75   -160.44                                   
REMARK 500    HIS C 170      142.18    179.43                                   
REMARK 500    LEU C 216       66.98   -106.37                                   
REMARK 500    ASN C 271      -56.10    -26.98                                   
REMARK 500    MET C 290       58.40   -113.02                                   
REMARK 500    ASN C 348       41.69     71.63                                   
REMARK 500    LYS C 413       10.40    -66.81                                   
REMARK 500    GLU D  17     -139.40     49.39                                   
REMARK 500    ILE D  31      -67.03    -93.96                                   
REMARK 500    LEU D  44       32.98    -86.10                                   
REMARK 500    ASP D  54       -3.44     79.10                                   
REMARK 500    ASN D  68      -25.36     74.67                                   
REMARK 500    ASP D  79     -165.02   -119.76                                   
REMARK 500    TRP D  92      153.36    -48.23                                   
REMARK 500    TRP D 124       69.00    -64.51                                   
REMARK 500    ASP D 137     -134.11     56.90                                   
REMARK 500    ARG D 140       57.72   -147.25                                   
REMARK 500    GLN D 163      133.81    157.51                                   
REMARK 500    HIS D 170      144.18   -178.67                                   
REMARK 500    LYS D 243       19.05     59.44                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      74 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 252   OD2                                                    
REMARK 620 2 AKG C 501   O2  122.9                                              
REMARK 620 3 ASP C 275   OD1  78.8  86.7                                        
REMARK 620 4 ASP C 279   OD2  71.6 165.5  96.8                                  
REMARK 620 5 AKG C 501   O5   64.4  60.9  90.6 132.9                            
REMARK 620 6 HOH C 601   O    76.5 106.2 155.2  76.1  78.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 252   OD2                                                    
REMARK 620 2 AKG B 501   O2  138.5                                              
REMARK 620 3 ASP B 275   OD1  71.3  81.7                                        
REMARK 620 4 AKG B 501   O5   73.4  69.0  73.2                                  
REMARK 620 5 ASP B 279   OD2  70.5 144.4  94.7 143.9                            
REMARK 620 6 HOH B 611   O   125.6  79.9  83.5 143.2  64.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 252   OD2                                                    
REMARK 620 2 AKG A 501   O2  142.2                                              
REMARK 620 3 AKG A 501   O5   72.4  74.0                                        
REMARK 620 4 ASP A 275   OD1  76.3  85.0  87.0                                  
REMARK 620 5 ASP A 279   OD2  71.9 143.9 142.0  96.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 252   OD2                                                    
REMARK 620 2 ASP E 275   OD1  86.3                                              
REMARK 620 3 AKG E 501   O5   67.8  82.5                                        
REMARK 620 4 AKG E 501   O2  127.1  94.0  59.9                                  
REMARK 620 5 ASP E 279   OD2  68.5 102.4 135.6 158.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 275   OD1                                                    
REMARK 620 2 AKG D 501   O2   90.5                                              
REMARK 620 3 AKG D 501   O5   74.6  62.6                                        
REMARK 620 4 ASP D 279   OD1 127.2 132.4 145.7                                  
REMARK 620 5 ASP D 275   O    66.9 125.8 140.2  63.0                            
REMARK 620 6 ASP C 252   OD2  73.1 115.7  53.1 103.7 104.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 AKG F 501   O2                                                     
REMARK 620 2 ASP E 252   OD2 123.3                                              
REMARK 620 3 AKG F 501   O5   66.8  57.3                                        
REMARK 620 4 ASP F 279   OD1 134.4  94.4 147.6                                  
REMARK 620 5 ASP F 275   OD1 101.0  70.3  71.5 116.5                            
REMARK 620 6 ASP F 275   O   117.8 110.3 139.4  60.6  68.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG E 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP E 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG F 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP F 503                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4KZO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4L03   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4L06   RELATED DB: PDB                                   
DBREF  4L04 A    1   414  UNP    O75874   IDHC_HUMAN       1    414             
DBREF  4L04 B    1   414  UNP    O75874   IDHC_HUMAN       1    414             
DBREF  4L04 C    1   414  UNP    O75874   IDHC_HUMAN       1    414             
DBREF  4L04 D    1   414  UNP    O75874   IDHC_HUMAN       1    414             
DBREF  4L04 E    1   414  UNP    O75874   IDHC_HUMAN       1    414             
DBREF  4L04 F    1   414  UNP    O75874   IDHC_HUMAN       1    414             
SEQADV 4L04 ASN A   97  UNP  O75874    GLY    97 CONFLICT                       
SEQADV 4L04 SER A  415  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 LEU A  416  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 GLU A  417  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS A  418  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS A  419  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS A  420  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS A  421  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS A  422  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS A  423  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS A  424  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS A  425  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 ASN B   97  UNP  O75874    GLY    97 CONFLICT                       
SEQADV 4L04 SER B  415  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 LEU B  416  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 GLU B  417  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS B  418  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS B  419  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS B  420  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS B  421  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS B  422  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS B  423  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS B  424  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS B  425  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 ASN C   97  UNP  O75874    GLY    97 CONFLICT                       
SEQADV 4L04 SER C  415  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 LEU C  416  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 GLU C  417  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS C  418  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS C  419  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS C  420  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS C  421  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS C  422  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS C  423  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS C  424  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS C  425  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 ASN D   97  UNP  O75874    GLY    97 CONFLICT                       
SEQADV 4L04 SER D  415  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 LEU D  416  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 GLU D  417  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS D  418  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS D  419  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS D  420  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS D  421  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS D  422  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS D  423  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS D  424  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS D  425  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 ASN E   97  UNP  O75874    GLY    97 CONFLICT                       
SEQADV 4L04 SER E  415  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 LEU E  416  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 GLU E  417  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS E  418  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS E  419  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS E  420  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS E  421  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS E  422  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS E  423  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS E  424  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS E  425  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 ASN F   97  UNP  O75874    GLY    97 CONFLICT                       
SEQADV 4L04 SER F  415  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 LEU F  416  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 GLU F  417  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS F  418  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS F  419  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS F  420  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS F  421  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS F  422  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS F  423  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS F  424  UNP  O75874              EXPRESSION TAG                 
SEQADV 4L04 HIS F  425  UNP  O75874              EXPRESSION TAG                 
SEQRES   1 A  425  MET SER LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET          
SEQRES   2 A  425  GLN GLY ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE          
SEQRES   3 A  425  LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU          
SEQRES   4 A  425  HIS SER TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR          
SEQRES   5 A  425  ASN ASP GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS          
SEQRES   6 A  425  LYS HIS ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO          
SEQRES   7 A  425  ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET          
SEQRES   8 A  425  TRP LYS SER PRO ASN ASN THR ILE ARG ASN ILE LEU GLY          
SEQRES   9 A  425  GLY THR VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE          
SEQRES  10 A  425  PRO ARG LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE          
SEQRES  11 A  425  GLY ARG HIS ALA TYR GLY ASP GLN TYR ARG ALA THR ASP          
SEQRES  12 A  425  PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR          
SEQRES  13 A  425  THR PRO SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL          
SEQRES  14 A  425  HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET          
SEQRES  15 A  425  TYR ASN GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER          
SEQRES  16 A  425  SER PHE GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR          
SEQRES  17 A  425  LEU SER THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY          
SEQRES  18 A  425  ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN          
SEQRES  19 A  425  TYR LYS SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU          
SEQRES  20 A  425  HIS ARG LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS          
SEQRES  21 A  425  SER GLU GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP          
SEQRES  22 A  425  GLY ASP VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY          
SEQRES  23 A  425  SER LEU GLY MET MET THR SER VAL LEU VAL CYS PRO ASP          
SEQRES  24 A  425  GLY LYS THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL          
SEQRES  25 A  425  THR ARG HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR          
SEQRES  26 A  425  SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG          
SEQRES  27 A  425  GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU          
SEQRES  28 A  425  LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE          
SEQRES  29 A  425  GLU THR ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA          
SEQRES  30 A  425  ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP          
SEQRES  31 A  425  TYR LEU ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU          
SEQRES  32 A  425  ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS LEU SER LEU          
SEQRES  33 A  425  GLU HIS HIS HIS HIS HIS HIS HIS HIS                          
SEQRES   1 B  425  MET SER LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET          
SEQRES   2 B  425  GLN GLY ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE          
SEQRES   3 B  425  LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU          
SEQRES   4 B  425  HIS SER TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR          
SEQRES   5 B  425  ASN ASP GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS          
SEQRES   6 B  425  LYS HIS ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO          
SEQRES   7 B  425  ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET          
SEQRES   8 B  425  TRP LYS SER PRO ASN ASN THR ILE ARG ASN ILE LEU GLY          
SEQRES   9 B  425  GLY THR VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE          
SEQRES  10 B  425  PRO ARG LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE          
SEQRES  11 B  425  GLY ARG HIS ALA TYR GLY ASP GLN TYR ARG ALA THR ASP          
SEQRES  12 B  425  PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR          
SEQRES  13 B  425  THR PRO SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL          
SEQRES  14 B  425  HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET          
SEQRES  15 B  425  TYR ASN GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER          
SEQRES  16 B  425  SER PHE GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR          
SEQRES  17 B  425  LEU SER THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY          
SEQRES  18 B  425  ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN          
SEQRES  19 B  425  TYR LYS SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU          
SEQRES  20 B  425  HIS ARG LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS          
SEQRES  21 B  425  SER GLU GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP          
SEQRES  22 B  425  GLY ASP VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY          
SEQRES  23 B  425  SER LEU GLY MET MET THR SER VAL LEU VAL CYS PRO ASP          
SEQRES  24 B  425  GLY LYS THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL          
SEQRES  25 B  425  THR ARG HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR          
SEQRES  26 B  425  SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG          
SEQRES  27 B  425  GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU          
SEQRES  28 B  425  LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE          
SEQRES  29 B  425  GLU THR ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA          
SEQRES  30 B  425  ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP          
SEQRES  31 B  425  TYR LEU ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU          
SEQRES  32 B  425  ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS LEU SER LEU          
SEQRES  33 B  425  GLU HIS HIS HIS HIS HIS HIS HIS HIS                          
SEQRES   1 C  425  MET SER LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET          
SEQRES   2 C  425  GLN GLY ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE          
SEQRES   3 C  425  LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU          
SEQRES   4 C  425  HIS SER TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR          
SEQRES   5 C  425  ASN ASP GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS          
SEQRES   6 C  425  LYS HIS ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO          
SEQRES   7 C  425  ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET          
SEQRES   8 C  425  TRP LYS SER PRO ASN ASN THR ILE ARG ASN ILE LEU GLY          
SEQRES   9 C  425  GLY THR VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE          
SEQRES  10 C  425  PRO ARG LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE          
SEQRES  11 C  425  GLY ARG HIS ALA TYR GLY ASP GLN TYR ARG ALA THR ASP          
SEQRES  12 C  425  PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR          
SEQRES  13 C  425  THR PRO SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL          
SEQRES  14 C  425  HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET          
SEQRES  15 C  425  TYR ASN GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER          
SEQRES  16 C  425  SER PHE GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR          
SEQRES  17 C  425  LEU SER THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY          
SEQRES  18 C  425  ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN          
SEQRES  19 C  425  TYR LYS SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU          
SEQRES  20 C  425  HIS ARG LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS          
SEQRES  21 C  425  SER GLU GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP          
SEQRES  22 C  425  GLY ASP VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY          
SEQRES  23 C  425  SER LEU GLY MET MET THR SER VAL LEU VAL CYS PRO ASP          
SEQRES  24 C  425  GLY LYS THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL          
SEQRES  25 C  425  THR ARG HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR          
SEQRES  26 C  425  SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG          
SEQRES  27 C  425  GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU          
SEQRES  28 C  425  LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE          
SEQRES  29 C  425  GLU THR ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA          
SEQRES  30 C  425  ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP          
SEQRES  31 C  425  TYR LEU ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU          
SEQRES  32 C  425  ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS LEU SER LEU          
SEQRES  33 C  425  GLU HIS HIS HIS HIS HIS HIS HIS HIS                          
SEQRES   1 D  425  MET SER LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET          
SEQRES   2 D  425  GLN GLY ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE          
SEQRES   3 D  425  LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU          
SEQRES   4 D  425  HIS SER TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR          
SEQRES   5 D  425  ASN ASP GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS          
SEQRES   6 D  425  LYS HIS ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO          
SEQRES   7 D  425  ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET          
SEQRES   8 D  425  TRP LYS SER PRO ASN ASN THR ILE ARG ASN ILE LEU GLY          
SEQRES   9 D  425  GLY THR VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE          
SEQRES  10 D  425  PRO ARG LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE          
SEQRES  11 D  425  GLY ARG HIS ALA TYR GLY ASP GLN TYR ARG ALA THR ASP          
SEQRES  12 D  425  PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR          
SEQRES  13 D  425  THR PRO SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL          
SEQRES  14 D  425  HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET          
SEQRES  15 D  425  TYR ASN GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER          
SEQRES  16 D  425  SER PHE GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR          
SEQRES  17 D  425  LEU SER THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY          
SEQRES  18 D  425  ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN          
SEQRES  19 D  425  TYR LYS SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU          
SEQRES  20 D  425  HIS ARG LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS          
SEQRES  21 D  425  SER GLU GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP          
SEQRES  22 D  425  GLY ASP VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY          
SEQRES  23 D  425  SER LEU GLY MET MET THR SER VAL LEU VAL CYS PRO ASP          
SEQRES  24 D  425  GLY LYS THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL          
SEQRES  25 D  425  THR ARG HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR          
SEQRES  26 D  425  SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG          
SEQRES  27 D  425  GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU          
SEQRES  28 D  425  LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE          
SEQRES  29 D  425  GLU THR ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA          
SEQRES  30 D  425  ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP          
SEQRES  31 D  425  TYR LEU ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU          
SEQRES  32 D  425  ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS LEU SER LEU          
SEQRES  33 D  425  GLU HIS HIS HIS HIS HIS HIS HIS HIS                          
SEQRES   1 E  425  MET SER LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET          
SEQRES   2 E  425  GLN GLY ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE          
SEQRES   3 E  425  LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU          
SEQRES   4 E  425  HIS SER TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR          
SEQRES   5 E  425  ASN ASP GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS          
SEQRES   6 E  425  LYS HIS ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO          
SEQRES   7 E  425  ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET          
SEQRES   8 E  425  TRP LYS SER PRO ASN ASN THR ILE ARG ASN ILE LEU GLY          
SEQRES   9 E  425  GLY THR VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE          
SEQRES  10 E  425  PRO ARG LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE          
SEQRES  11 E  425  GLY ARG HIS ALA TYR GLY ASP GLN TYR ARG ALA THR ASP          
SEQRES  12 E  425  PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR          
SEQRES  13 E  425  THR PRO SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL          
SEQRES  14 E  425  HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET          
SEQRES  15 E  425  TYR ASN GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER          
SEQRES  16 E  425  SER PHE GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR          
SEQRES  17 E  425  LEU SER THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY          
SEQRES  18 E  425  ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN          
SEQRES  19 E  425  TYR LYS SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU          
SEQRES  20 E  425  HIS ARG LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS          
SEQRES  21 E  425  SER GLU GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP          
SEQRES  22 E  425  GLY ASP VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY          
SEQRES  23 E  425  SER LEU GLY MET MET THR SER VAL LEU VAL CYS PRO ASP          
SEQRES  24 E  425  GLY LYS THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL          
SEQRES  25 E  425  THR ARG HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR          
SEQRES  26 E  425  SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG          
SEQRES  27 E  425  GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU          
SEQRES  28 E  425  LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE          
SEQRES  29 E  425  GLU THR ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA          
SEQRES  30 E  425  ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP          
SEQRES  31 E  425  TYR LEU ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU          
SEQRES  32 E  425  ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS LEU SER LEU          
SEQRES  33 E  425  GLU HIS HIS HIS HIS HIS HIS HIS HIS                          
SEQRES   1 F  425  MET SER LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET          
SEQRES   2 F  425  GLN GLY ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE          
SEQRES   3 F  425  LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU          
SEQRES   4 F  425  HIS SER TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR          
SEQRES   5 F  425  ASN ASP GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS          
SEQRES   6 F  425  LYS HIS ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO          
SEQRES   7 F  425  ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET          
SEQRES   8 F  425  TRP LYS SER PRO ASN ASN THR ILE ARG ASN ILE LEU GLY          
SEQRES   9 F  425  GLY THR VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE          
SEQRES  10 F  425  PRO ARG LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE          
SEQRES  11 F  425  GLY ARG HIS ALA TYR GLY ASP GLN TYR ARG ALA THR ASP          
SEQRES  12 F  425  PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR          
SEQRES  13 F  425  THR PRO SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL          
SEQRES  14 F  425  HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET          
SEQRES  15 F  425  TYR ASN GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER          
SEQRES  16 F  425  SER PHE GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR          
SEQRES  17 F  425  LEU SER THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY          
SEQRES  18 F  425  ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN          
SEQRES  19 F  425  TYR LYS SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU          
SEQRES  20 F  425  HIS ARG LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS          
SEQRES  21 F  425  SER GLU GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP          
SEQRES  22 F  425  GLY ASP VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY          
SEQRES  23 F  425  SER LEU GLY MET MET THR SER VAL LEU VAL CYS PRO ASP          
SEQRES  24 F  425  GLY LYS THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL          
SEQRES  25 F  425  THR ARG HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR          
SEQRES  26 F  425  SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG          
SEQRES  27 F  425  GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU          
SEQRES  28 F  425  LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE          
SEQRES  29 F  425  GLU THR ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA          
SEQRES  30 F  425  ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP          
SEQRES  31 F  425  TYR LEU ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU          
SEQRES  32 F  425  ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS LEU SER LEU          
SEQRES  33 F  425  GLU HIS HIS HIS HIS HIS HIS HIS HIS                          
HET    AKG  A 501      10                                                       
HET     CA  A 502       1                                                       
HET     CA  A 503       1                                                       
HET    NAP  A 504      48                                                       
HET    AKG  B 501      10                                                       
HET    NAP  B 502      48                                                       
HET    AKG  C 501      10                                                       
HET     CA  C 502       1                                                       
HET    NAP  C 503      48                                                       
HET    AKG  D 501      10                                                       
HET     CA  D 502       1                                                       
HET    NAP  D 503      48                                                       
HET    AKG  E 501      10                                                       
HET     CA  E 502       1                                                       
HET    NAP  E 503      48                                                       
HET    AKG  F 501      10                                                       
HET     CA  F 502       1                                                       
HET    NAP  F 503      48                                                       
HETNAM     AKG 2-OXOGLUTARIC ACID                                               
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
FORMUL   7  AKG    6(C5 H6 O5)                                                  
FORMUL   8   CA    6(CA 2+)                                                     
FORMUL  10  NAP    6(C21 H28 N7 O17 P3)                                         
FORMUL  25  HOH   *69(H2 O)                                                     
HELIX    1   1 ASP A   16  LEU A   30  1                                  15    
HELIX    2   2 GLY A   45  THR A   52  1                                   8    
HELIX    3   3 ASP A   54  ASN A   68  1                                  15    
HELIX    4   4 ASP A   79  LYS A   87  1                                   9    
HELIX    5   5 SER A   94  GLY A  104  1                                  11    
HELIX    6   6 GLY A  136  ARG A  140  5                                   5    
HELIX    7   7 ASP A  186  GLY A  204  1                                  19    
HELIX    8   8 LEU A  216  TYR A  235  1                                  20    
HELIX    9   9 TYR A  235  GLN A  242  1                                   8    
HELIX   10  10 ILE A  251  SER A  261  1                                  11    
HELIX   11  11 LYS A  270  GLY A  286  1                                  17    
HELIX   12  12 VAL A  312  LYS A  321  1                                  10    
HELIX   13  13 PRO A  329  ASN A  348  1                                  20    
HELIX   14  14 ASN A  349  ALA A  369  1                                  21    
HELIX   15  15 THR A  373  GLY A  382  1                                  10    
HELIX   16  16 LEU A  383  VAL A  386  5                                   4    
HELIX   17  17 GLN A  387  TYR A  391  5                                   5    
HELIX   18  18 ASN A  393  LYS A  413  1                                  21    
HELIX   19  19 ASP B   16  LEU B   30  1                                  15    
HELIX   20  20 GLY B   45  THR B   52  1                                   8    
HELIX   21  21 ASP B   54  ASN B   68  1                                  15    
HELIX   22  22 ASP B   79  LYS B   87  1                                   9    
HELIX   23  23 SER B   94  GLY B  104  1                                  11    
HELIX   24  24 GLY B  136  ALA B  141  5                                   6    
HELIX   25  25 ASP B  186  GLY B  204  1                                  19    
HELIX   26  26 LYS B  218  TYR B  235  1                                  18    
HELIX   27  27 TYR B  235  GLN B  242  1                                   8    
HELIX   28  28 ILE B  251  LYS B  260  1                                  10    
HELIX   29  29 LYS B  270  GLY B  286  1                                  17    
HELIX   30  30 VAL B  312  LYS B  321  1                                  10    
HELIX   31  31 PRO B  329  ASN B  348  1                                  20    
HELIX   32  32 ASN B  349  GLU B  368  1                                  20    
HELIX   33  33 THR B  373  GLY B  382  1                                  10    
HELIX   34  34 LEU B  383  VAL B  386  5                                   4    
HELIX   35  35 GLN B  387  TYR B  391  5                                   5    
HELIX   36  36 ASN B  393  LYS B  413  1                                  21    
HELIX   37  37 ASP C   16  ILE C   31  1                                  16    
HELIX   38  38 GLY C   45  THR C   52  1                                   8    
HELIX   39  39 ASP C   54  ASN C   68  1                                  15    
HELIX   40  40 ASP C   79  LYS C   87  1                                   9    
HELIX   41  41 SER C   94  GLY C  104  1                                  11    
HELIX   42  42 GLY C  136  ALA C  141  5                                   6    
HELIX   43  43 ASP C  186  SER C  202  1                                  17    
HELIX   44  44 ASP C  220  TYR C  235  1                                  16    
HELIX   45  45 TYR C  235  GLN C  242  1                                   8    
HELIX   46  46 ILE C  251  SER C  261  1                                  11    
HELIX   47  47 LYS C  270  GLY C  286  1                                  17    
HELIX   48  48 VAL C  312  LYS C  321  1                                  10    
HELIX   49  49 PRO C  329  ASN C  348  1                                  20    
HELIX   50  50 ASN C  349  ALA C  369  1                                  21    
HELIX   51  51 THR C  373  LYS C  381  1                                   9    
HELIX   52  52 GLY C  382  VAL C  386  5                                   5    
HELIX   53  53 GLN C  387  TYR C  391  5                                   5    
HELIX   54  54 ASN C  393  LYS C  413  1                                  21    
HELIX   55  55 ASP D   16  ILE D   31  1                                  16    
HELIX   56  56 GLY D   45  THR D   52  1                                   8    
HELIX   57  57 ASP D   54  ASN D   68  1                                  15    
HELIX   58  58 ASP D   79  PHE D   86  1                                   8    
HELIX   59  59 SER D   94  GLY D  104  1                                  11    
HELIX   60  60 GLY D  136  ALA D  141  5                                   6    
HELIX   61  61 ASP D  186  GLY D  204  1                                  19    
HELIX   62  62 LYS D  218  TYR D  235  1                                  18    
HELIX   63  63 TYR D  235  ALA D  241  1                                   7    
HELIX   64  64 ILE D  251  LYS D  260  1                                  10    
HELIX   65  65 LYS D  270  TYR D  285  1                                  16    
HELIX   66  66 VAL D  312  LYS D  321  1                                  10    
HELIX   67  67 PRO D  329  ASN D  348  1                                  20    
HELIX   68  68 ASN D  349  ALA D  369  1                                  21    
HELIX   69  69 THR D  373  GLY D  382  1                                  10    
HELIX   70  70 LEU D  383  VAL D  386  5                                   4    
HELIX   71  71 GLN D  387  TYR D  391  5                                   5    
HELIX   72  72 ASN D  393  LYS D  413  1                                  21    
HELIX   73  73 ASP E   16  LEU E   30  1                                  15    
HELIX   74  74 GLY E   45  THR E   52  1                                   8    
HELIX   75  75 ASP E   54  ASN E   68  1                                  15    
HELIX   76  76 ASP E   79  LYS E   87  1                                   9    
HELIX   77  77 SER E   94  GLY E  104  1                                  11    
HELIX   78  78 GLY E  136  ALA E  141  5                                   6    
HELIX   79  79 ASP E  186  GLY E  204  1                                  19    
HELIX   80  80 LYS E  218  TYR E  235  1                                  18    
HELIX   81  81 TYR E  235  ALA E  241  1                                   7    
HELIX   82  82 ILE E  251  SER E  261  1                                  11    
HELIX   83  83 LYS E  270  GLY E  286  1                                  17    
HELIX   84  84 VAL E  312  LYS E  321  1                                  10    
HELIX   85  85 PRO E  329  ASN E  348  1                                  20    
HELIX   86  86 ASN E  349  ALA E  369  1                                  21    
HELIX   87  87 THR E  373  GLY E  382  1                                  10    
HELIX   88  88 GLN E  387  TYR E  391  5                                   5    
HELIX   89  89 ASN E  393  LYS E  413  1                                  21    
HELIX   90  90 GLU F   17  LEU F   30  1                                  14    
HELIX   91  91 GLY F   45  THR F   52  1                                   8    
HELIX   92  92 ASP F   54  ASN F   68  1                                  15    
HELIX   93  93 ASP F   79  LYS F   87  1                                   9    
HELIX   94  94 SER F   94  GLY F  104  1                                  11    
HELIX   95  95 GLY F  136  ALA F  141  5                                   6    
HELIX   96  96 ASP F  186  GLY F  204  1                                  19    
HELIX   97  97 LYS F  218  TYR F  235  1                                  18    
HELIX   98  98 TYR F  235  GLN F  242  1                                   8    
HELIX   99  99 ILE F  251  SER F  261  1                                  11    
HELIX  100 100 LYS F  270  GLY F  286  1                                  17    
HELIX  101 101 VAL F  312  GLY F  322  1                                  11    
HELIX  102 102 PRO F  329  ASN F  348  1                                  20    
HELIX  103 103 ASN F  349  ALA F  369  1                                  21    
HELIX  104 104 THR F  373  GLY F  382  1                                  10    
HELIX  105 105 LEU F  383  VAL F  386  5                                   4    
HELIX  106 106 GLN F  387  TYR F  391  5                                   5    
HELIX  107 107 ASN F  393  LEU F  414  1                                  22    
SHEET    1   A10 GLU A  36  ASP A  43  0                                        
SHEET    2   A10 SER A   6  GLN A  14  1  N  GLU A  12   O  HIS A  40           
SHEET    3   A10 VAL A  69  LYS A  72  1  O  VAL A  71   N  VAL A  11           
SHEET    4   A10 VAL A 303  ALA A 307  1  O  ALA A 305   N  LYS A  72           
SHEET    5   A10 MET A 291  VAL A 296 -1  N  LEU A 295   O  GLU A 304           
SHEET    6   A10 THR A 106  ALA A 111 -1  N  THR A 106   O  VAL A 296           
SHEET    7   A10 ILE A 128  HIS A 133 -1  O  ARG A 132   N  VAL A 107           
SHEET    8   A10 PHE A 265  CYS A 269  1  O  CYS A 269   N  GLY A 131           
SHEET    9   A10 LEU A 207  THR A 211  1  N  TYR A 208   O  ALA A 268           
SHEET   10   A10 TYR A 246  LEU A 250  1  O  ARG A 249   N  LEU A 209           
SHEET    1   B 4 THR A 142  VAL A 146  0                                        
SHEET    2   B 4 GLY A 177  GLN A 185 -1  O  GLY A 181   N  THR A 142           
SHEET    3   B 4 GLY B 177  GLN B 185 -1  O  VAL B 178   N  ASN A 184           
SHEET    4   B 4 THR B 142  VAL B 146 -1  N  PHE B 144   O  ALA B 179           
SHEET    1   C 8 LEU A 168  PHE A 172  0                                        
SHEET    2   C 8 GLY A 150  PRO A 158 -1  N  GLY A 150   O  PHE A 172           
SHEET    3   C 8 GLY B 150  PRO B 158 -1  O  THR B 155   N  GLU A 153           
SHEET    4   C 8 GLN B 163  PHE B 172 -1  O  TYR B 167   N  ILE B 154           
SHEET    5   C 8 GLN C 163  PHE C 172 -1  O  THR C 166   N  LYS B 164           
SHEET    6   C 8 GLY C 150  PRO C 158 -1  N  TYR C 156   O  VAL C 165           
SHEET    7   C 8 GLY D 150  PRO D 158 -1  O  THR D 155   N  GLU C 153           
SHEET    8   C 8 VAL D 165  PHE D 172 -1  O  TYR D 167   N  ILE D 154           
SHEET    1   D10 VAL B  35  ASP B  43  0                                        
SHEET    2   D10 ILE B   5  GLN B  14  1  N  GLY B   8   O  ASP B  38           
SHEET    3   D10 VAL B  69  LYS B  72  1  O  VAL B  71   N  MET B  13           
SHEET    4   D10 VAL B 303  ALA B 307  1  O  ALA B 305   N  GLY B  70           
SHEET    5   D10 MET B 291  VAL B 296 -1  N  LEU B 295   O  GLU B 304           
SHEET    6   D10 THR B 106  ALA B 111 -1  N  PHE B 108   O  VAL B 294           
SHEET    7   D10 ILE B 128  HIS B 133 -1  O  ARG B 132   N  VAL B 107           
SHEET    8   D10 PHE B 265  CYS B 269  1  O  TRP B 267   N  ILE B 129           
SHEET    9   D10 LEU B 207  THR B 211  1  N  TYR B 208   O  ALA B 268           
SHEET   10   D10 TYR B 246  LEU B 250  1  O  ARG B 249   N  LEU B 209           
SHEET    1   E10 VAL C  35  ASP C  43  0                                        
SHEET    2   E10 ILE C   5  GLN C  14  1  N  ILE C   5   O  GLU C  36           
SHEET    3   E10 VAL C  69  LYS C  72  1  O  VAL C  71   N  VAL C  11           
SHEET    4   E10 VAL C 303  ALA C 307  1  O  ALA C 305   N  GLY C  70           
SHEET    5   E10 MET C 291  VAL C 296 -1  N  LEU C 295   O  GLU C 304           
SHEET    6   E10 THR C 106  ALA C 111 -1  N  THR C 106   O  VAL C 296           
SHEET    7   E10 ILE C 128  HIS C 133 -1  O  ILE C 130   N  ARG C 109           
SHEET    8   E10 PHE C 265  CYS C 269  1  O  TRP C 267   N  ILE C 129           
SHEET    9   E10 LEU C 207  THR C 211  1  N  TYR C 208   O  ALA C 268           
SHEET   10   E10 TYR C 246  LEU C 250  1  O  ARG C 249   N  LEU C 209           
SHEET    1   F 4 THR C 142  VAL C 146  0                                        
SHEET    2   F 4 GLY C 177  GLN C 185 -1  O  GLY C 181   N  THR C 142           
SHEET    3   F 4 GLY D 177  GLN D 185 -1  O  MET D 182   N  MET C 180           
SHEET    4   F 4 THR D 142  VAL D 146 -1  N  PHE D 144   O  ALA D 179           
SHEET    1   G10 VAL D  35  ASP D  43  0                                        
SHEET    2   G10 ILE D   5  GLN D  14  1  N  ILE D   5   O  GLU D  36           
SHEET    3   G10 VAL D  69  LYS D  72  1  O  VAL D  71   N  VAL D  11           
SHEET    4   G10 VAL D 303  ALA D 307  1  O  ALA D 305   N  LYS D  72           
SHEET    5   G10 MET D 291  VAL D 296 -1  N  LEU D 295   O  GLU D 304           
SHEET    6   G10 THR D 106  ALA D 111 -1  N  GLU D 110   O  THR D 292           
SHEET    7   G10 ILE D 128  HIS D 133 -1  O  ARG D 132   N  VAL D 107           
SHEET    8   G10 PHE D 265  CYS D 269  1  O  TRP D 267   N  ILE D 129           
SHEET    9   G10 LEU D 207  THR D 211  1  N  TYR D 208   O  ALA D 268           
SHEET   10   G10 TYR D 246  LEU D 250  1  O  GLU D 247   N  LEU D 207           
SHEET    1   H10 VAL E  35  ASP E  43  0                                        
SHEET    2   H10 ILE E   5  GLN E  14  1  N  ILE E   5   O  GLU E  36           
SHEET    3   H10 VAL E  69  LYS E  72  1  O  VAL E  69   N  VAL E  11           
SHEET    4   H10 VAL E 303  GLU E 306  1  O  ALA E 305   N  GLY E  70           
SHEET    5   H10 MET E 291  VAL E 296 -1  N  LEU E 295   O  GLU E 304           
SHEET    6   H10 THR E 106  ALA E 111 -1  N  GLU E 110   O  THR E 292           
SHEET    7   H10 ILE E 128  HIS E 133 -1  O  ARG E 132   N  VAL E 107           
SHEET    8   H10 PHE E 265  CYS E 269  1  O  TRP E 267   N  ILE E 129           
SHEET    9   H10 LEU E 207  THR E 211  1  N  TYR E 208   O  ILE E 266           
SHEET   10   H10 TYR E 246  LEU E 250  1  O  ARG E 249   N  LEU E 209           
SHEET    1   I 4 THR E 142  VAL E 146  0                                        
SHEET    2   I 4 GLY E 177  GLN E 185 -1  O  GLY E 181   N  THR E 142           
SHEET    3   I 4 GLY F 177  GLN F 185 -1  O  MET F 182   N  MET E 180           
SHEET    4   I 4 THR F 142  VAL F 146 -1  N  VAL F 146   O  GLY F 177           
SHEET    1   J 4 VAL E 165  PHE E 172  0                                        
SHEET    2   J 4 GLY E 150  PRO E 158 -1  N  TYR E 156   O  VAL E 165           
SHEET    3   J 4 GLY F 150  PRO F 158 -1  O  THR F 155   N  GLU E 153           
SHEET    4   J 4 VAL F 165  PHE F 172 -1  O  TYR F 167   N  ILE F 154           
SHEET    1   K10 VAL F  35  ASP F  43  0                                        
SHEET    2   K10 ILE F   5  GLN F  14  1  N  GLY F   7   O  GLU F  36           
SHEET    3   K10 VAL F  69  LYS F  72  1  O  VAL F  71   N  VAL F  11           
SHEET    4   K10 VAL F 303  ALA F 307  1  O  ALA F 305   N  LYS F  72           
SHEET    5   K10 MET F 291  VAL F 296 -1  N  SER F 293   O  GLU F 306           
SHEET    6   K10 THR F 106  ALA F 111 -1  N  PHE F 108   O  VAL F 294           
SHEET    7   K10 ILE F 129  HIS F 133 -1  O  ILE F 130   N  ARG F 109           
SHEET    8   K10 ILE F 266  CYS F 269  1  O  CYS F 269   N  GLY F 131           
SHEET    9   K10 LEU F 207  THR F 211  1  N  TYR F 208   O  ALA F 268           
SHEET   10   K10 TYR F 246  LEU F 250  1  O  ARG F 249   N  LEU F 209           
LINK         OD2 ASP D 252                CA    CA C 502     1555   1555  2.12  
LINK         OD2 ASP A 252                CA    CA A 503     1555   1555  2.12  
LINK         OD2 ASP B 252                CA    CA A 502     1555   1555  2.13  
LINK         O2  AKG C 501                CA    CA C 502     1555   1555  2.14  
LINK         OD2 ASP F 252                CA    CA E 502     1555   1555  2.16  
LINK         OD1 ASP E 275                CA    CA E 502     1555   1555  2.17  
LINK        CA    CA A 503                 O2  AKG B 501     1555   1555  2.19  
LINK         O2  AKG A 501                CA    CA A 502     1555   1555  2.26  
LINK         O5  AKG A 501                CA    CA A 502     1555   1555  2.30  
LINK         OD1 ASP D 275                CA    CA D 502     1555   1555  2.33  
LINK         O2  AKG F 501                CA    CA F 502     1555   1555  2.34  
LINK         OD2 ASP E 252                CA    CA F 502     1555   1555  2.35  
LINK         OD1 ASP C 275                CA    CA C 502     1555   1555  2.36  
LINK         OD1 ASP B 275                CA    CA A 503     1555   1555  2.40  
LINK         O5  AKG F 501                CA    CA F 502     1555   1555  2.54  
LINK        CA    CA A 503                 O5  AKG B 501     1555   1555  2.60  
LINK         O2  AKG D 501                CA    CA D 502     1555   1555  2.60  
LINK         OD1 ASP A 275                CA    CA A 502     1555   1555  2.60  
LINK         O5  AKG D 501                CA    CA D 502     1555   1555  2.65  
LINK         OD1 ASP D 279                CA    CA D 502     1555   1555  2.72  
LINK         OD2 ASP A 279                CA    CA A 502     1555   1555  2.75  
LINK         OD1 ASP F 279                CA    CA F 502     1555   1555  2.76  
LINK         O5  AKG E 501                CA    CA E 502     1555   1555  2.78  
LINK         OD2 ASP C 279                CA    CA C 502     1555   1555  2.83  
LINK         OD1 ASP F 275                CA    CA F 502     1555   1555  2.83  
LINK         O2  AKG E 501                CA    CA E 502     1555   1555  2.85  
LINK         OD2 ASP B 279                CA    CA A 503     1555   1555  2.87  
LINK         OD2 ASP E 279                CA    CA E 502     1555   1555  2.91  
LINK         O5  AKG C 501                CA    CA C 502     1555   1555  2.98  
LINK         O   ASP F 275                CA    CA F 502     1555   1555  3.01  
LINK         O   ASP D 275                CA    CA D 502     1555   1555  3.04  
LINK         OD2 ASP C 252                CA    CA D 502     1555   1555  3.19  
LINK        CA    CA A 503                 O   HOH B 611     1555   1555  2.18  
LINK        CA    CA C 502                 O   HOH C 601     1555   1555  2.90  
SITE     1 AC1 11 THR A  77  SER A  94  ASN A  96  ARG A 100                    
SITE     2 AC1 11 ARG A 109  ARG A 132  ASP A 275   CA A 502                    
SITE     3 AC1 11 NAP A 504  LYS B 212  ASP B 252                               
SITE     1 AC2  5 ARG A 109  ASP A 275  ASP A 279  AKG A 501                    
SITE     2 AC2  5 ASP B 252                                                     
SITE     1 AC3  5 ASP A 252  ASP B 275  ASP B 279  AKG B 501                    
SITE     2 AC3  5 HOH B 611                                                     
SITE     1 AC4 22 LYS A  72  ALA A  74  THR A  75  THR A  77                    
SITE     2 AC4 22 ARG A  82  ASN A  96  LEU A 288  GLY A 289                    
SITE     3 AC4 22 HIS A 309  GLY A 310  THR A 311  VAL A 312                    
SITE     4 AC4 22 THR A 313  ARG A 314  HIS A 315  THR A 327                    
SITE     5 AC4 22 ASN A 328  ASP A 375  AKG A 501  HOH A 601                    
SITE     6 AC4 22 ASP B 253  LYS B 260                                          
SITE     1 AC5 13 ILE A 215  ASP A 252   CA A 503  THR B  77                    
SITE     2 AC5 13 SER B  94  ASN B  96  ARG B 100  ARG B 109                    
SITE     3 AC5 13 ARG B 132  ASP B 275  ALA B 308  NAP B 502                    
SITE     4 AC5 13 HOH B 611                                                     
SITE     1 AC6 23 LEU A 250  ASP A 253  GLN A 257  LYS A 260                    
SITE     2 AC6 23 LYS B  72  ALA B  74  THR B  75  ILE B  76                    
SITE     3 AC6 23 THR B  77  ARG B  82  ASN B  96  LEU B 288                    
SITE     4 AC6 23 GLY B 289  ALA B 307  HIS B 309  GLY B 310                    
SITE     5 AC6 23 THR B 311  VAL B 312  THR B 313  ARG B 314                    
SITE     6 AC6 23 HIS B 315  ASN B 328  AKG B 501                               
SITE     1 AC7 10 THR C  77  SER C  94  ASN C  96  ARG C 100                    
SITE     2 AC7 10 ARG C 109  ARG C 132  ASP C 275   CA C 502                    
SITE     3 AC7 10 NAP C 503  ASP D 252                                          
SITE     1 AC8  5 ASP C 275  ASP C 279  AKG C 501  HOH C 601                    
SITE     2 AC8  5 ASP D 252                                                     
SITE     1 AC9 21 LYS C  72  ALA C  74  THR C  75  ILE C  76                    
SITE     2 AC9 21 THR C  77  ARG C  82  ASN C  96  LEU C 288                    
SITE     3 AC9 21 HIS C 309  GLY C 310  THR C 311  VAL C 312                    
SITE     4 AC9 21 THR C 313  ARG C 314  HIS C 315  THR C 327                    
SITE     5 AC9 21 ASN C 328  AKG C 501  HOH C 602  ASP D 253                    
SITE     6 AC9 21 LYS D 260                                                     
SITE     1 BC1 11 ILE C 215  ASP C 252  THR D  77  SER D  94                    
SITE     2 BC1 11 ASN D  96  ARG D 100  ARG D 109  ARG D 132                    
SITE     3 BC1 11 ASP D 275   CA D 502  NAP D 503                               
SITE     1 BC2  5 ASP C 252  ARG D 109  ASP D 275  ASP D 279                    
SITE     2 BC2  5 AKG D 501                                                     
SITE     1 BC3 20 LEU C 250  ASP C 253  LYS C 260  LYS D  72                    
SITE     2 BC3 20 ALA D  74  THR D  75  THR D  77  ARG D  82                    
SITE     3 BC3 20 ASN D  96  LEU D 288  HIS D 309  GLY D 310                    
SITE     4 BC3 20 THR D 311  VAL D 312  THR D 313  ARG D 314                    
SITE     5 BC3 20 HIS D 315  THR D 327  ASN D 328  AKG D 501                    
SITE     1 BC4 11 THR E  77  SER E  94  ASN E  96  ARG E 100                    
SITE     2 BC4 11 ARG E 109  ARG E 132  ASP E 275  ALA E 308                    
SITE     3 BC4 11  CA E 502  NAP E 503  ASP F 252                               
SITE     1 BC5  5 ARG E 109  ASP E 275  ASP E 279  AKG E 501                    
SITE     2 BC5  5 ASP F 252                                                     
SITE     1 BC6 23 LYS E  72  ALA E  74  THR E  75  ILE E  76                    
SITE     2 BC6 23 THR E  77  ARG E  82  ASN E  96  LEU E 288                    
SITE     3 BC6 23 HIS E 309  GLY E 310  THR E 311  VAL E 312                    
SITE     4 BC6 23 THR E 313  ARG E 314  HIS E 315  THR E 327                    
SITE     5 BC6 23 ASN E 328  AKG E 501  HOH E 601  HOH E 602                    
SITE     6 BC6 23 LEU F 250  ASP F 253  LYS F 260                               
SITE     1 BC7 13 LYS E 212  ILE E 215  ASP E 252  THR F  77                    
SITE     2 BC7 13 SER F  94  ASN F  96  ARG F 100  ARG F 109                    
SITE     3 BC7 13 ARG F 132  ASP F 275  ALA F 308   CA F 502                    
SITE     4 BC7 13 NAP F 503                                                     
SITE     1 BC8  5 ASP E 252  ARG F 109  ASP F 275  ASP F 279                    
SITE     2 BC8  5 AKG F 501                                                     
SITE     1 BC9 21 LEU E 250  ASP E 253  LYS E 260  LYS F  72                    
SITE     2 BC9 21 ALA F  74  THR F  75  THR F  77  ARG F  82                    
SITE     3 BC9 21 ASN F  96  LEU F 288  GLY F 289  ALA F 307                    
SITE     4 BC9 21 HIS F 309  GLY F 310  THR F 311  VAL F 312                    
SITE     5 BC9 21 THR F 313  ARG F 314  HIS F 315  ASN F 328                    
SITE     6 BC9 21 AKG F 501                                                     
CRYST1   96.410  116.622  275.729  90.00  90.00  90.00 P 21 21 21   24          
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      0.010372  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008575  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003627        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system