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Database: PDB
Entry: 5K10
LinkDB: 5K10
Original site: 5K10 
HEADER    OXIDOREDUCTASE                          17-MAY-16   5K10              
TITLE     CRYO-EM STRUCTURE OF ISOCITRATE DEHYDROGENASE (IDH1)                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ISOCITRATE DEHYDROGENASE [NADP] CYTOPLASMIC;               
COMPND   3 CHAIN: A, B;                                                         
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: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    ISOCITRATE DEHYDROGENASE, SMALL METABOLIC COMPLEX, OXIDOREDUCTASE     
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    A.MERK,A.BARTESAGHI,S.BANERJEE,V.FALCONIERI,P.RAO,L.EARL,J.MILNE,     
AUTHOR   2 S.SUBRAMANIAM                                                        
REVDAT   4   18-JUL-18 5K10    1       REMARK                                   
REVDAT   3   23-NOV-16 5K10    1                                                
REVDAT   2   29-JUN-16 5K10    1       JRNL                                     
REVDAT   1   08-JUN-16 5K10    0                                                
JRNL        AUTH   A.MERK,A.BARTESAGHI,S.BANERJEE,V.FALCONIERI,P.RAO,M.I.DAVIS, 
JRNL        AUTH 2 R.PRAGANI,M.B.BOXER,L.A.EARL,J.L.MILNE,S.SUBRAMANIAM         
JRNL        TITL   BREAKING CRYO-EM RESOLUTION BARRIERS TO FACILITATE DRUG      
JRNL        TITL 2 DISCOVERY.                                                   
JRNL        REF    CELL                          V. 165  1698 2016              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   27238019                                                     
JRNL        DOI    10.1016/J.CELL.2016.05.040                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : FREALIGN, UCSF CHIMERA, PHENIX, COOT,     
REMARK   3                            FREALIGN, FREALIGN, FREALIGN              
REMARK   3   RECONSTRUCTION SCHEMA  : FOURIER SPACE                             
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 3MAP                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : FLEXIBLE FIT                        
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.800                          
REMARK   3   NUMBER OF PARTICLES               : 49936                          
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: THE PRIMARY MAP FOR THIS ENTRY CORRESPONDS TO THE     
REMARK   3  UNCORRECTED RECONSTRUCTION. A VERSION SHARPENED USING A B-FACTOR    
REMARK   3  OF -180 IS PROVIDED AS ADDITIONAL VOLUME DATA. THE                  
REMARK   3  RECONSTRUCTION, OBTAINED WITHOUT IMPOSING SYMMETRY, IS ALSO         
REMARK   3  PROVIDED WITH THIS ENTRY AS ADDITIONAL VOLUME DATA.                 
REMARK   4                                                                      
REMARK   4 5K10 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000221269.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : ISOCITRATE DEHYDROGENASE R132C    
REMARK 245                                    MUTANT                            
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 1.50                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : PLUNGED INTO LIQUID ETHANE        
REMARK 245                                    (LEICA EM GP)                     
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : 1506                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 QUANTUM (4K X 4K)     
REMARK 245   MINIMUM DEFOCUS (NM)              : 700.00                         
REMARK 245   MAXIMUM DEFOCUS (NM)              : 3000.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 60.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 270000                         
REMARK 245   CALIBRATED MAGNIFICATION          : 101000                         
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     TYR A   135                                                      
REMARK 465     GLY A   136                                                      
REMARK 465     ASP A   137                                                      
REMARK 465     GLN A   138                                                      
REMARK 465     TYR A   139                                                      
REMARK 465     TYR A   272                                                      
REMARK 465     ASP A   273                                                      
REMARK 465     GLY A   274                                                      
REMARK 465     ASP A   275                                                      
REMARK 465     VAL A   276                                                      
REMARK 465     GLN A   277                                                      
REMARK 465     SER A   278                                                      
REMARK 465     ASP A   279                                                      
REMARK 465     SER A   280                                                      
REMARK 465     TYR B   135                                                      
REMARK 465     GLY B   136                                                      
REMARK 465     ASP B   137                                                      
REMARK 465     GLN B   138                                                      
REMARK 465     TYR B   139                                                      
REMARK 465     TYR B   272                                                      
REMARK 465     ASP B   273                                                      
REMARK 465     GLY B   274                                                      
REMARK 465     ASP B   275                                                      
REMARK 465     VAL B   276                                                      
REMARK 465     GLN B   277                                                      
REMARK 465     SER B   278                                                      
REMARK 465     ASP B   279                                                      
REMARK 465     SER B   280                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 140    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 281    CG1  CG2                                            
REMARK 470     GLN A 283    CG   CD   OE1  NE2                                  
REMARK 470     TYR A 285    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG B 140    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 281    CG1  CG2                                            
REMARK 470     GLN B 283    CG   CD   OE1  NE2                                  
REMARK 470     TYR B 285    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG A   314     O3X  NDP A   501              2.01            
REMARK 500   NH1  ARG B   314     O3X  NDP B   501              2.01            
REMARK 500   O    GLY A   148     OH   TYR B   156              2.14            
REMARK 500   OH   TYR A   156     O    GLY B   148              2.17            
REMARK 500   OD2  ASP B   347     ND2  ASN B   349              2.17            
REMARK 500   OD2  ASP A   347     ND2  ASN A   349              2.18            
REMARK 500   OE2  GLU B    12     NE1  TRP B    23              2.19            
REMARK 500   OE2  GLU A    12     NE1  TRP A    23              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  17     -136.14     52.14                                   
REMARK 500    LYS A  29      -64.35    -99.07                                   
REMARK 500    ALA A  51      -70.51   -101.99                                   
REMARK 500    ASP A  54      -12.68     78.93                                   
REMARK 500    ASN A  68       -9.57     71.99                                   
REMARK 500    VAL A 146       67.33     33.66                                   
REMARK 500    VAL A 169      -71.33    -73.78                                   
REMARK 500    GLU A 173      -76.98   -117.31                                   
REMARK 500    ASP A 232      -72.02    -94.49                                   
REMARK 500    GLN A 234      -65.50   -128.27                                   
REMARK 500    LYS A 243       -9.71     63.81                                   
REMARK 500    MET A 254      -65.58    -93.06                                   
REMARK 500    ALA A 282      -77.83   -104.99                                   
REMARK 500    GLN A 283     -141.48     51.43                                   
REMARK 500    PRO A 298      -22.70    -33.09                                   
REMARK 500    LYS A 301      -71.51   -104.72                                   
REMARK 500    VAL A 312       73.27     67.75                                   
REMARK 500    HIS A 315      -30.50     73.78                                   
REMARK 500    PRO A 329       42.23    -91.94                                   
REMARK 500    GLU A 403      -70.02    -55.76                                   
REMARK 500    GLU B  17     -136.13     52.10                                   
REMARK 500    LYS B  29      -64.29    -99.11                                   
REMARK 500    ALA B  51      -70.55   -101.98                                   
REMARK 500    ASP B  54      -12.68     78.94                                   
REMARK 500    ASN B  68       -9.54     72.01                                   
REMARK 500    VAL B 146       67.34     33.59                                   
REMARK 500    VAL B 169      -71.34    -73.80                                   
REMARK 500    GLU B 173      -76.96   -117.31                                   
REMARK 500    ASP B 232      -72.02    -94.53                                   
REMARK 500    GLN B 234      -65.48   -128.30                                   
REMARK 500    LYS B 243       -9.63     63.78                                   
REMARK 500    MET B 254      -65.57    -93.03                                   
REMARK 500    ALA B 282      -77.88   -105.00                                   
REMARK 500    GLN B 283     -141.47     51.44                                   
REMARK 500    PRO B 298      -22.71    -33.07                                   
REMARK 500    LYS B 301      -71.44   -104.78                                   
REMARK 500    VAL B 312       73.29     67.77                                   
REMARK 500    HIS B 315      -30.54     73.80                                   
REMARK 500    PRO B 329       42.23    -91.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 314         0.26    SIDE CHAIN                              
REMARK 500    ARG B 314         0.26    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP B 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-8192   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8191   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8193   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8194   RELATED DB: EMDB                              
REMARK 900 RELATED ID: 5K0Z   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5K11   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5K12   RELATED DB: PDB                                   
DBREF  5K10 A    3   413  UNP    O75874   IDHC_HUMAN       3    413             
DBREF  5K10 B    3   413  UNP    O75874   IDHC_HUMAN       3    413             
SEQADV 5K10 CYS A  132  UNP  O75874    ARG   132 CONFLICT                       
SEQADV 5K10 CYS B  132  UNP  O75874    ARG   132 CONFLICT                       
SEQRES   1 A  411  LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET GLN GLY          
SEQRES   2 A  411  ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE LYS GLU          
SEQRES   3 A  411  LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU HIS SER          
SEQRES   4 A  411  TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR ASN ASP          
SEQRES   5 A  411  GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS LYS HIS          
SEQRES   6 A  411  ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO ASP GLU          
SEQRES   7 A  411  LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET TRP LYS          
SEQRES   8 A  411  SER PRO ASN GLY THR ILE ARG ASN ILE LEU GLY GLY THR          
SEQRES   9 A  411  VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE PRO ARG          
SEQRES  10 A  411  LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE GLY CYS          
SEQRES  11 A  411  HIS ALA TYR GLY ASP GLN TYR ARG ALA THR ASP PHE VAL          
SEQRES  12 A  411  VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR THR PRO          
SEQRES  13 A  411  SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL HIS ASN          
SEQRES  14 A  411  PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET TYR ASN          
SEQRES  15 A  411  GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER SER PHE          
SEQRES  16 A  411  GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR LEU SER          
SEQRES  17 A  411  THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY ARG PHE          
SEQRES  18 A  411  LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN TYR LYS          
SEQRES  19 A  411  SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU HIS ARG          
SEQRES  20 A  411  LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS SER GLU          
SEQRES  21 A  411  GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP GLY ASP          
SEQRES  22 A  411  VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY SER LEU          
SEQRES  23 A  411  GLY MET MET THR SER VAL LEU VAL CYS PRO ASP GLY LYS          
SEQRES  24 A  411  THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL THR ARG          
SEQRES  25 A  411  HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR SER THR          
SEQRES  26 A  411  ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG GLY LEU          
SEQRES  27 A  411  ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU LEU ALA          
SEQRES  28 A  411  PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE GLU THR          
SEQRES  29 A  411  ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA ALA CYS          
SEQRES  30 A  411  ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP TYR LEU          
SEQRES  31 A  411  ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU ASN LEU          
SEQRES  32 A  411  LYS ILE LYS LEU ALA GLN ALA LYS                              
SEQRES   1 B  411  LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET GLN GLY          
SEQRES   2 B  411  ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE LYS GLU          
SEQRES   3 B  411  LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU HIS SER          
SEQRES   4 B  411  TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR ASN ASP          
SEQRES   5 B  411  GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS LYS HIS          
SEQRES   6 B  411  ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO ASP GLU          
SEQRES   7 B  411  LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET TRP LYS          
SEQRES   8 B  411  SER PRO ASN GLY THR ILE ARG ASN ILE LEU GLY GLY THR          
SEQRES   9 B  411  VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE PRO ARG          
SEQRES  10 B  411  LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE GLY CYS          
SEQRES  11 B  411  HIS ALA TYR GLY ASP GLN TYR ARG ALA THR ASP PHE VAL          
SEQRES  12 B  411  VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR THR PRO          
SEQRES  13 B  411  SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL HIS ASN          
SEQRES  14 B  411  PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET TYR ASN          
SEQRES  15 B  411  GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER SER PHE          
SEQRES  16 B  411  GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR LEU SER          
SEQRES  17 B  411  THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY ARG PHE          
SEQRES  18 B  411  LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN TYR LYS          
SEQRES  19 B  411  SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU HIS ARG          
SEQRES  20 B  411  LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS SER GLU          
SEQRES  21 B  411  GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP GLY ASP          
SEQRES  22 B  411  VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY SER LEU          
SEQRES  23 B  411  GLY MET MET THR SER VAL LEU VAL CYS PRO ASP GLY LYS          
SEQRES  24 B  411  THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL THR ARG          
SEQRES  25 B  411  HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR SER THR          
SEQRES  26 B  411  ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG GLY LEU          
SEQRES  27 B  411  ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU LEU ALA          
SEQRES  28 B  411  PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE GLU THR          
SEQRES  29 B  411  ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA ALA CYS          
SEQRES  30 B  411  ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP TYR LEU          
SEQRES  31 B  411  ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU ASN LEU          
SEQRES  32 B  411  LYS ILE LYS LEU ALA GLN ALA LYS                              
HET    NDP  A 501      48                                                       
HET    NDP  B 501      48                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
FORMUL   3  NDP    2(C21 H30 N7 O17 P3)                                         
HELIX    1 AA1 ASP A   16  ILE A   31  1                                  16    
HELIX    2 AA2 GLY A   45  ARG A   49  5                                   5    
HELIX    3 AA3 ASP A   54  ASN A   68  1                                  15    
HELIX    4 AA4 ASP A   79  PHE A   86  1                                   8    
HELIX    5 AA5 SER A   94  GLY A  104  1                                  11    
HELIX    6 AA6 GLN A  185  GLY A  204  1                                  20    
HELIX    7 AA7 LEU A  216  GLN A  234  1                                  19    
HELIX    8 AA8 TYR A  235  ALA A  241  1                                   7    
HELIX    9 AA9 GLN A  242  ILE A  244  5                                   3    
HELIX   10 AB1 ILE A  251  LYS A  260  1                                  10    
HELIX   11 AB2 PRO A  329  ASN A  348  1                                  20    
HELIX   12 AB3 ASN A  349  ALA A  369  1                                  21    
HELIX   13 AB4 THR A  373  LYS A  381  1                                   9    
HELIX   14 AB5 GLN A  387  TYR A  391  5                                   5    
HELIX   15 AB6 GLU A  396  GLN A  411  1                                  16    
HELIX   16 AB7 ASP B   16  ILE B   31  1                                  16    
HELIX   17 AB8 GLY B   45  ARG B   49  5                                   5    
HELIX   18 AB9 ASP B   54  ASN B   68  1                                  15    
HELIX   19 AC1 ASP B   79  PHE B   86  1                                   8    
HELIX   20 AC2 SER B   94  GLY B  104  1                                  11    
HELIX   21 AC3 GLN B  185  GLY B  204  1                                  20    
HELIX   22 AC4 LEU B  216  GLN B  234  1                                  19    
HELIX   23 AC5 TYR B  235  ALA B  241  1                                   7    
HELIX   24 AC6 GLN B  242  ILE B  244  5                                   3    
HELIX   25 AC7 ILE B  251  LYS B  260  1                                  10    
HELIX   26 AC8 PRO B  329  ASN B  348  1                                  20    
HELIX   27 AC9 ASN B  349  ALA B  369  1                                  21    
HELIX   28 AD1 THR B  373  LYS B  381  1                                   9    
HELIX   29 AD2 GLN B  387  TYR B  391  5                                   5    
HELIX   30 AD3 GLU B  396  GLN B  411  1                                  16    
SHEET    1 AA1 2 ILE A   5  SER A   9  0                                        
SHEET    2 AA1 2 VAL A  35  ASP A  38  1  O  ASP A  38   N  GLY A   8           
SHEET    1 AA2 2 GLU A  12  GLN A  14  0                                        
SHEET    2 AA2 2 SER A  41  ASP A  43  1  O  TYR A  42   N  GLN A  14           
SHEET    1 AA3 8 VAL A  69  LYS A  72  0                                        
SHEET    2 AA3 8 VAL A 303  ALA A 307  1  O  ALA A 305   N  LYS A  72           
SHEET    3 AA3 8 THR A 292  VAL A 296 -1  N  LEU A 295   O  GLU A 304           
SHEET    4 AA3 8 THR A 106  ARG A 109 -1  N  PHE A 108   O  VAL A 294           
SHEET    5 AA3 8 ILE A 129  CYS A 132 -1  O  ILE A 130   N  ARG A 109           
SHEET    6 AA3 8 ILE A 266  CYS A 269  1  O  TRP A 267   N  ILE A 129           
SHEET    7 AA3 8 LEU A 207  THR A 211  1  N  TYR A 208   O  ILE A 266           
SHEET    8 AA3 8 ARG A 249  LEU A 250  1  O  ARG A 249   N  LEU A 209           
SHEET    1 AA4 4 ALA A 141  PHE A 144  0                                        
SHEET    2 AA4 4 VAL A 178  ASN A 184 -1  O  GLY A 181   N  THR A 142           
SHEET    3 AA4 4 VAL B 178  ASN B 184 -1  O  VAL B 178   N  ASN A 184           
SHEET    4 AA4 4 ALA B 141  PHE B 144 -1  N  THR B 142   O  GLY B 181           
SHEET    1 AA5 4 ASN A 171  PHE A 172  0                                        
SHEET    2 AA5 4 GLY A 150  PRO A 158 -1  N  GLY A 150   O  PHE A 172           
SHEET    3 AA5 4 GLY B 150  PRO B 158 -1  O  THR B 155   N  GLU A 153           
SHEET    4 AA5 4 ASN B 171  PHE B 172 -1  O  PHE B 172   N  GLY B 150           
SHEET    1 AA6 2 ILE B   5  SER B   9  0                                        
SHEET    2 AA6 2 VAL B  35  ASP B  38  1  O  ASP B  38   N  GLY B   8           
SHEET    1 AA7 2 GLU B  12  GLN B  14  0                                        
SHEET    2 AA7 2 SER B  41  ASP B  43  1  O  TYR B  42   N  GLN B  14           
SHEET    1 AA8 8 VAL B  69  LYS B  72  0                                        
SHEET    2 AA8 8 VAL B 303  ALA B 307  1  O  ALA B 305   N  LYS B  72           
SHEET    3 AA8 8 THR B 292  VAL B 296 -1  N  LEU B 295   O  GLU B 304           
SHEET    4 AA8 8 THR B 106  ARG B 109 -1  N  PHE B 108   O  VAL B 294           
SHEET    5 AA8 8 ILE B 129  CYS B 132 -1  O  ILE B 130   N  ARG B 109           
SHEET    6 AA8 8 ILE B 266  CYS B 269  1  O  TRP B 267   N  ILE B 129           
SHEET    7 AA8 8 LEU B 207  THR B 211  1  N  TYR B 208   O  ILE B 266           
SHEET    8 AA8 8 ARG B 249  LEU B 250  1  O  ARG B 249   N  LEU B 209           
SITE     1 AC1 17 LYS A  72  THR A  75  ILE A  76  THR A  77                    
SITE     2 AC1 17 ARG A  82  ASN A  96  LEU A 288  HIS A 309                    
SITE     3 AC1 17 GLY A 310  THR A 311  VAL A 312  THR A 313                    
SITE     4 AC1 17 ARG A 314  HIS A 315  THR A 327  ASN A 328                    
SITE     5 AC1 17 ASP A 375                                                     
SITE     1 AC2 17 LYS B  72  THR B  75  ILE B  76  THR B  77                    
SITE     2 AC2 17 ARG B  82  ASN B  96  LEU B 288  HIS B 309                    
SITE     3 AC2 17 GLY B 310  THR B 311  VAL B 312  THR B 313                    
SITE     4 AC2 17 ARG B 314  HIS B 315  THR B 327  ASN B 328                    
SITE     5 AC2 17 ASP B 375                                                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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