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Database: PDB
Entry: 2G76
LinkDB: 2G76
Original site: 2G76 
HEADER    OXIDOREDUCTASE                          27-FEB-06   2G76              
TITLE     CRYSTAL STRUCTURE OF HUMAN 3-PHOSPHOGLYCERATE DEHYDROGENASE           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-3-PHOSPHOGLYCERATE DEHYDROGENASE;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 3-314;                                            
COMPND   5 SYNONYM: 3-PGDH;                                                     
COMPND   6 EC: 1.1.1.95;                                                        
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: PHGDH, PGDH3;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL-21(DE3)R3;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    OXIDOREDUCTASE, PHOSPHOGLYCERATE DEHYDROGENASE DEFICIENCY, SERINE     
KEYWDS   2 METABOLISM, 2-HYDROXYACID DEHYDROGENASES, STRUCTURAL GENOMICS,       
KEYWDS   3 STRUCTURAL GENOMICS CONSORTIUM, SGC                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.P.TURNBULL,E.SALAH,P.SAVITSKY,O.GILEADI,F.VON DELFT,A.EDWARDS,      
AUTHOR   2 C.ARROWSMITH,J.WEIGELT,M.SUNDSTROM,U.OPPERMANN,STRUCTURAL GENOMICS   
AUTHOR   3 CONSORTIUM (SGC)                                                     
REVDAT   3   13-JUL-11 2G76    1       VERSN                                    
REVDAT   2   24-FEB-09 2G76    1       VERSN                                    
REVDAT   1   21-MAR-06 2G76    0                                                
JRNL        AUTH   A.P.TURNBULL,E.SALAH,P.SAVITSKY,O.GILEADI,F.VON DELFT,       
JRNL        AUTH 2 A.EDWARDS,C.ARROWSMITH,J.WEIGELT,M.SUNDSTROM,U.OPPERMANN     
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN 3-PHOSPHOGLYCERATE DEHYDROGENASE  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 63219                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3371                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4353                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.84                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 203                          
REMARK   3   BIN FREE R VALUE                    : 0.2540                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4413                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 106                                     
REMARK   3   SOLVENT ATOMS            : 278                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.46                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.12000                                              
REMARK   3    B22 (A**2) : 2.00000                                              
REMARK   3    B33 (A**2) : -2.15000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.08000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.104         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.104         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.082         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.638         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4638 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3057 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6314 ; 1.453 ; 2.009       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7550 ; 0.932 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   623 ; 5.893 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   171 ;39.940 ;25.205       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   794 ;12.983 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;12.396 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   758 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5168 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   810 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   912 ; 0.221 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3269 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2271 ; 0.169 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2433 ; 0.085 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   240 ; 0.139 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     4 ; 0.046 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    23 ; 0.194 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.129 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3140 ; 0.709 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1247 ; 0.186 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4843 ; 1.014 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1712 ; 1.759 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1460 ; 2.637 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      6       A     100      5                      
REMARK   3           1     B      6       B     100      5                      
REMARK   3           2     A    290       A     306      5                      
REMARK   3           2     B    290       B     306      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    658 ;  0.23 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    574 ;  0.37 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    658 ;  0.62 ;  2.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):    574 ;  0.87 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    101       A     289      5                      
REMARK   3           1     B    101       B     289      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):   1103 ;  0.12 ;  0.50           
REMARK   3   LOOSE POSITIONAL   2    A    (A):   1275 ;  0.54 ;  5.00           
REMARK   3   MEDIUM THERMAL     2    A (A**2):   1103 ;  0.63 ;  2.00           
REMARK   3   LOOSE THERMAL      2    A (A**2):   1275 ;  1.10 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     6        A   100                          
REMARK   3    RESIDUE RANGE :   A   290        A   306                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.3680  45.2781   1.6769              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2102 T22:   0.0006                                     
REMARK   3      T33:   0.0796 T12:   0.1543                                     
REMARK   3      T13:   0.0645 T23:   0.0649                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6041 L22:   3.3899                                     
REMARK   3      L33:   7.6322 L12:  -1.3483                                     
REMARK   3      L13:   2.4223 L23:  -2.0423                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2391 S12:  -0.2632 S13:   0.2981                       
REMARK   3      S21:   0.3354 S22:   0.3545 S23:   0.2230                       
REMARK   3      S31:  -1.2142 S32:  -0.8573 S33:  -0.1153                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   101        A   289                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.9754  17.1719   3.8216              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1425 T22:  -0.0922                                     
REMARK   3      T33:  -0.1141 T12:   0.0445                                     
REMARK   3      T13:   0.0072 T23:  -0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4582 L22:   0.7801                                     
REMARK   3      L33:   1.9589 L12:  -0.0965                                     
REMARK   3      L13:   0.1938 L23:  -0.2699                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0551 S12:   0.1753 S13:  -0.0487                       
REMARK   3      S21:  -0.1090 S22:  -0.0591 S23:   0.0181                       
REMARK   3      S31:   0.1489 S32:   0.0688 S33:   0.0040                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     6        B   100                          
REMARK   3    RESIDUE RANGE :   B   290        B   306                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.0254 -12.6290  28.1536              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3423 T22:  -0.0958                                     
REMARK   3      T33:   0.0728 T12:   0.0951                                     
REMARK   3      T13:  -0.0113 T23:   0.0203                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8336 L22:   4.7920                                     
REMARK   3      L33:   2.7131 L12:   0.6273                                     
REMARK   3      L13:  -0.8816 L23:   0.1096                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0732 S12:  -0.1354 S13:  -0.4697                       
REMARK   3      S21:   0.2717 S22:  -0.0440 S23:  -0.1305                       
REMARK   3      S31:   0.9208 S32:   0.0542 S33:   0.1172                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   101        B   289                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.9803  17.2672  27.6450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1502 T22:  -0.1064                                     
REMARK   3      T33:  -0.1062 T12:   0.0416                                     
REMARK   3      T13:   0.0038 T23:   0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2883 L22:   0.5560                                     
REMARK   3      L33:   2.3539 L12:  -0.0293                                     
REMARK   3      L13:   0.0511 L23:  -0.2771                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0447 S12:  -0.1771 S13:  -0.0112                       
REMARK   3      S21:   0.0687 S22:   0.0706 S23:   0.0411                       
REMARK   3      S31:   0.0231 S32:  -0.1127 S33:  -0.0259                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2G76 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB036773.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-FEB-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99806                            
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66626                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1YGY, 1PSD                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MMT, 30 % PEG1K, 5MM NAD+, PH      
REMARK 280  7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       62.05650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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 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   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     SER A   -13                                                      
REMARK 465     SER A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     VAL A   -10                                                      
REMARK 465     ASP A    -9                                                      
REMARK 465     LEU A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     THR A    -6                                                      
REMARK 465     GLU A    -5                                                      
REMARK 465     ASN A    -4                                                      
REMARK 465     LEU A    -3                                                      
REMARK 465     TYR A    -2                                                      
REMARK 465     PHE A    -1                                                      
REMARK 465     GLN A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     MET A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     LYS A   307                                                      
REMARK 465     GLY A   308                                                      
REMARK 465     LYS A   309                                                      
REMARK 465     SER A   310                                                      
REMARK 465     LEU A   311                                                      
REMARK 465     THR A   312                                                      
REMARK 465     GLY A   313                                                      
REMARK 465     VAL A   314                                                      
REMARK 465     MET B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     SER B   -13                                                      
REMARK 465     SER B   -12                                                      
REMARK 465     GLY B   -11                                                      
REMARK 465     VAL B   -10                                                      
REMARK 465     ASP B    -9                                                      
REMARK 465     LEU B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     THR B    -6                                                      
REMARK 465     GLU B    -5                                                      
REMARK 465     ASN B    -4                                                      
REMARK 465     LEU B    -3                                                      
REMARK 465     TYR B    -2                                                      
REMARK 465     PHE B    -1                                                      
REMARK 465     GLN B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     MET B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ASN B     4                                                      
REMARK 465     LEU B     5                                                      
REMARK 465     LYS B   307                                                      
REMARK 465     GLY B   308                                                      
REMARK 465     LYS B   309                                                      
REMARK 465     SER B   310                                                      
REMARK 465     LEU B   311                                                      
REMARK 465     THR B   312                                                      
REMARK 465     GLY B   313                                                      
REMARK 465     VAL B   314                                                      
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   6    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  19    CZ   NH1  NH2                                       
REMARK 470     LYS A  20    CG   CD   CE   NZ                                   
REMARK 470     GLN A  28    CD   OE1  NE2                                       
REMARK 470     LYS A  32    CD   CE   NZ                                        
REMARK 470     LYS A  37    CD   CE   NZ                                        
REMARK 470     GLU A  38    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  45    CG   CD   OE1  NE2                                  
REMARK 470     ASP A  46    CG   OD1  OD2                                       
REMARK 470     ASP A  61    OD1  OD2                                            
REMARK 470     LYS A  68    CE   NZ                                             
REMARK 470     GLN A  70    CG   CD   OE1  NE2                                  
REMARK 470     LEU A  93    CD1  CD2                                            
REMARK 470     LYS A 135    CD   CE   NZ                                        
REMARK 470     LYS A 226    CD   CE   NZ                                        
REMARK 470     MET A 305    CB   CG   SD   CE                                   
REMARK 470     VAL A 306    CG1  CG2                                            
REMARK 470     ARG B   6    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  20    CD   CE   NZ                                        
REMARK 470     LYS B  32    CD   CE   NZ                                        
REMARK 470     GLN B  33    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  37    CD   CE   NZ                                        
REMARK 470     GLN B  45    CD   OE1  NE2                                       
REMARK 470     GLU B  48    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  68    CD   CE   NZ                                        
REMARK 470     GLN B  70    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  85    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  89    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B  90    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP A   259     SG   CYS A   280              2.06            
REMARK 500   O    ASP A   174     O    HOH A   537              2.10            
REMARK 500   OD1  ASP B   259     SG   CYS B   280              2.16            
REMARK 500   O    ASP B   174     O    HOH B   535              2.18            
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    ARG A   6      -52.10   -144.92                                   
REMARK 500    ARG A  53     -102.09   -106.18                                   
REMARK 500    GLU A 133       74.67   -117.07                                   
REMARK 500    HIS A 205       50.91   -141.73                                   
REMARK 500    ALA A 234      -86.73   -109.28                                   
REMARK 500    ARG B  53     -103.79   -109.98                                   
REMARK 500    GLU B 133       76.80   -106.95                                   
REMARK 500    ALA B 234      -87.77   -103.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 594        DISTANCE =  5.69 ANGSTROMS                       
REMARK 525    HOH B 645        DISTANCE =  5.27 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLT A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLT B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 502                 
DBREF  2G76 A    3   314  UNP    O43175   SERA_HUMAN       3    314             
DBREF  2G76 B    3   314  UNP    O43175   SERA_HUMAN       3    314             
SEQADV 2G76 MET A  -20  UNP  O43175              INITIATING METHIONINE          
SEQADV 2G76 HIS A  -19  UNP  O43175              EXPRESSION TAG                 
SEQADV 2G76 HIS A  -18  UNP  O43175              EXPRESSION TAG                 
SEQADV 2G76 HIS A  -17  UNP  O43175              EXPRESSION TAG                 
SEQADV 2G76 HIS A  -16  UNP  O43175              EXPRESSION TAG                 
SEQADV 2G76 HIS A  -15  UNP  O43175              EXPRESSION TAG                 
SEQADV 2G76 HIS A  -14  UNP  O43175              EXPRESSION TAG                 
SEQADV 2G76 SER A  -13  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 SER A  -12  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 GLY A  -11  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 VAL A  -10  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 ASP A   -9  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 LEU A   -8  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 GLY A   -7  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 THR A   -6  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 GLU A   -5  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 ASN A   -4  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 LEU A   -3  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 TYR A   -2  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 PHE A   -1  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 GLN A    0  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 SER A    1  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 MET A    2  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 MET B  -20  UNP  O43175              INITIATING METHIONINE          
SEQADV 2G76 HIS B  -19  UNP  O43175              EXPRESSION TAG                 
SEQADV 2G76 HIS B  -18  UNP  O43175              EXPRESSION TAG                 
SEQADV 2G76 HIS B  -17  UNP  O43175              EXPRESSION TAG                 
SEQADV 2G76 HIS B  -16  UNP  O43175              EXPRESSION TAG                 
SEQADV 2G76 HIS B  -15  UNP  O43175              EXPRESSION TAG                 
SEQADV 2G76 HIS B  -14  UNP  O43175              EXPRESSION TAG                 
SEQADV 2G76 SER B  -13  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 SER B  -12  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 GLY B  -11  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 VAL B  -10  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 ASP B   -9  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 LEU B   -8  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 GLY B   -7  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 THR B   -6  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 GLU B   -5  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 ASN B   -4  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 LEU B   -3  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 TYR B   -2  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 PHE B   -1  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 GLN B    0  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 SER B    1  UNP  O43175              CLONING ARTIFACT               
SEQADV 2G76 MET B    2  UNP  O43175              CLONING ARTIFACT               
SEQRES   1 A  335  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  335  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA ASN LEU          
SEQRES   3 A  335  ARG LYS VAL LEU ILE SER ASP SER LEU ASP PRO CYS CYS          
SEQRES   4 A  335  ARG LYS ILE LEU GLN ASP GLY GLY LEU GLN VAL VAL GLU          
SEQRES   5 A  335  LYS GLN ASN LEU SER LYS GLU GLU LEU ILE ALA GLU LEU          
SEQRES   6 A  335  GLN ASP CYS GLU GLY LEU ILE VAL ARG SER ALA THR LYS          
SEQRES   7 A  335  VAL THR ALA ASP VAL ILE ASN ALA ALA GLU LYS LEU GLN          
SEQRES   8 A  335  VAL VAL GLY ARG ALA GLY THR GLY VAL ASP ASN VAL ASP          
SEQRES   9 A  335  LEU GLU ALA ALA THR ARG LYS GLY ILE LEU VAL MET ASN          
SEQRES  10 A  335  THR PRO ASN GLY ASN SER LEU SER ALA ALA GLU LEU THR          
SEQRES  11 A  335  CYS GLY MET ILE MET CYS LEU ALA ARG GLN ILE PRO GLN          
SEQRES  12 A  335  ALA THR ALA SER MET LYS ASP GLY LYS TRP GLU ARG LYS          
SEQRES  13 A  335  LYS PHE MET GLY THR GLU LEU ASN GLY LYS THR LEU GLY          
SEQRES  14 A  335  ILE LEU GLY LEU GLY ARG ILE GLY ARG GLU VAL ALA THR          
SEQRES  15 A  335  ARG MET GLN SER PHE GLY MET LYS THR ILE GLY TYR ASP          
SEQRES  16 A  335  PRO ILE ILE SER PRO GLU VAL SER ALA SER PHE GLY VAL          
SEQRES  17 A  335  GLN GLN LEU PRO LEU GLU GLU ILE TRP PRO LEU CYS ASP          
SEQRES  18 A  335  PHE ILE THR VAL HIS THR PRO LEU LEU PRO SER THR THR          
SEQRES  19 A  335  GLY LEU LEU ASN ASP ASN THR PHE ALA GLN CYS LYS LYS          
SEQRES  20 A  335  GLY VAL ARG VAL VAL ASN CYS ALA ARG GLY GLY ILE VAL          
SEQRES  21 A  335  ASP GLU GLY ALA LEU LEU ARG ALA LEU GLN SER GLY GLN          
SEQRES  22 A  335  CYS ALA GLY ALA ALA LEU ASP VAL PHE THR GLU GLU PRO          
SEQRES  23 A  335  PRO ARG ASP ARG ALA LEU VAL ASP HIS GLU ASN VAL ILE          
SEQRES  24 A  335  SER CYS PRO HIS LEU GLY ALA SER THR LYS GLU ALA GLN          
SEQRES  25 A  335  SER ARG CYS GLY GLU GLU ILE ALA VAL GLN PHE VAL ASP          
SEQRES  26 A  335  MET VAL LYS GLY LYS SER LEU THR GLY VAL                      
SEQRES   1 B  335  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  335  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA ASN LEU          
SEQRES   3 B  335  ARG LYS VAL LEU ILE SER ASP SER LEU ASP PRO CYS CYS          
SEQRES   4 B  335  ARG LYS ILE LEU GLN ASP GLY GLY LEU GLN VAL VAL GLU          
SEQRES   5 B  335  LYS GLN ASN LEU SER LYS GLU GLU LEU ILE ALA GLU LEU          
SEQRES   6 B  335  GLN ASP CYS GLU GLY LEU ILE VAL ARG SER ALA THR LYS          
SEQRES   7 B  335  VAL THR ALA ASP VAL ILE ASN ALA ALA GLU LYS LEU GLN          
SEQRES   8 B  335  VAL VAL GLY ARG ALA GLY THR GLY VAL ASP ASN VAL ASP          
SEQRES   9 B  335  LEU GLU ALA ALA THR ARG LYS GLY ILE LEU VAL MET ASN          
SEQRES  10 B  335  THR PRO ASN GLY ASN SER LEU SER ALA ALA GLU LEU THR          
SEQRES  11 B  335  CYS GLY MET ILE MET CYS LEU ALA ARG GLN ILE PRO GLN          
SEQRES  12 B  335  ALA THR ALA SER MET LYS ASP GLY LYS TRP GLU ARG LYS          
SEQRES  13 B  335  LYS PHE MET GLY THR GLU LEU ASN GLY LYS THR LEU GLY          
SEQRES  14 B  335  ILE LEU GLY LEU GLY ARG ILE GLY ARG GLU VAL ALA THR          
SEQRES  15 B  335  ARG MET GLN SER PHE GLY MET LYS THR ILE GLY TYR ASP          
SEQRES  16 B  335  PRO ILE ILE SER PRO GLU VAL SER ALA SER PHE GLY VAL          
SEQRES  17 B  335  GLN GLN LEU PRO LEU GLU GLU ILE TRP PRO LEU CYS ASP          
SEQRES  18 B  335  PHE ILE THR VAL HIS THR PRO LEU LEU PRO SER THR THR          
SEQRES  19 B  335  GLY LEU LEU ASN ASP ASN THR PHE ALA GLN CYS LYS LYS          
SEQRES  20 B  335  GLY VAL ARG VAL VAL ASN CYS ALA ARG GLY GLY ILE VAL          
SEQRES  21 B  335  ASP GLU GLY ALA LEU LEU ARG ALA LEU GLN SER GLY GLN          
SEQRES  22 B  335  CYS ALA GLY ALA ALA LEU ASP VAL PHE THR GLU GLU PRO          
SEQRES  23 B  335  PRO ARG ASP ARG ALA LEU VAL ASP HIS GLU ASN VAL ILE          
SEQRES  24 B  335  SER CYS PRO HIS LEU GLY ALA SER THR LYS GLU ALA GLN          
SEQRES  25 B  335  SER ARG CYS GLY GLU GLU ILE ALA VAL GLN PHE VAL ASP          
SEQRES  26 B  335  MET VAL LYS GLY LYS SER LEU THR GLY VAL                      
HET    MLT  A 503       9                                                       
HET    MLT  B 504       9                                                       
HET    NAD  A 501      44                                                       
HET    NAD  B 502      44                                                       
HETNAM     MLT MALATE ION                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
FORMUL   3  MLT    2(C4 H5 O5 1-)                                               
FORMUL   5  NAD    2(C21 H27 N7 O14 P2)                                         
FORMUL   7  HOH   *278(H2 O)                                                    
HELIX    1   1 PRO A   16  GLY A   26  1                                  11    
HELIX    2   2 SER A   36  LEU A   44  1                                   9    
HELIX    3   3 GLN A   45  CYS A   47  5                                   3    
HELIX    4   4 THR A   59  ALA A   66  1                                   8    
HELIX    5   5 ASP A   83  GLY A   91  1                                   9    
HELIX    6   6 ASN A  101  GLN A  119  1                                  19    
HELIX    7   7 GLN A  119  ASP A  129  1                                  11    
HELIX    8   8 ARG A  134  MET A  138  5                                   5    
HELIX    9   9 GLY A  153  SER A  165  1                                  13    
HELIX   10  10 SER A  178  PHE A  185  1                                   8    
HELIX   11  11 PRO A  191  TRP A  196  1                                   6    
HELIX   12  12 PRO A  197  CYS A  199  5                                   3    
HELIX   13  13 ASN A  217  ALA A  222  1                                   6    
HELIX   14  14 ASP A  240  GLY A  251  1                                  12    
HELIX   15  15 ARG A  269  HIS A  274  1                                   6    
HELIX   16  16 THR A  287  VAL A  306  1                                  20    
HELIX   17  17 ASP B   15  GLY B   25  1                                  11    
HELIX   18  18 SER B   36  GLN B   45  1                                  10    
HELIX   19  19 THR B   59  ALA B   66  1                                   8    
HELIX   20  20 ASP B   83  LYS B   90  1                                   8    
HELIX   21  21 ASN B  101  GLN B  119  1                                  19    
HELIX   22  22 GLN B  119  ASP B  129  1                                  11    
HELIX   23  23 GLY B  153  SER B  165  1                                  13    
HELIX   24  24 SER B  178  SER B  184  1                                   7    
HELIX   25  25 PRO B  191  TRP B  196  1                                   6    
HELIX   26  26 PRO B  197  CYS B  199  5                                   3    
HELIX   27  27 LEU B  209  THR B  213  5                                   5    
HELIX   28  28 ASN B  217  ALA B  222  1                                   6    
HELIX   29  29 ASP B  240  GLY B  251  1                                  12    
HELIX   30  30 THR B  287  MET B  305  1                                  19    
SHEET    1   A 5 GLN A  28  GLU A  31  0                                        
SHEET    2   A 5 LYS A   7  ILE A  10  1  N  ILE A  10   O  VAL A  30           
SHEET    3   A 5 GLY A  49  VAL A  52  1  O  GLY A  49   N  LEU A   9           
SHEET    4   A 5 VAL A  71  ARG A  74  1  O  GLY A  73   N  LEU A  50           
SHEET    5   A 5 LEU A  93  MET A  95  1  O  LEU A  93   N  VAL A  72           
SHEET    1   B 7 GLN A 188  GLN A 189  0                                        
SHEET    2   B 7 LYS A 169  TYR A 173  1  N  GLY A 172   O  GLN A 188           
SHEET    3   B 7 THR A 146  LEU A 150  1  N  LEU A 147   O  LYS A 169           
SHEET    4   B 7 PHE A 201  VAL A 204  1  O  PHE A 201   N  GLY A 148           
SHEET    5   B 7 ARG A 229  ASN A 232  1  O  VAL A 231   N  ILE A 202           
SHEET    6   B 7 GLY A 255  LEU A 258  1  O  ALA A 257   N  ASN A 232           
SHEET    7   B 7 VAL A 277  SER A 279  1  O  ILE A 278   N  ALA A 256           
SHEET    1   C 5 GLN B  28  GLU B  31  0                                        
SHEET    2   C 5 LYS B   7  ILE B  10  1  N  ILE B  10   O  VAL B  30           
SHEET    3   C 5 GLY B  49  VAL B  52  1  O  ILE B  51   N  LEU B   9           
SHEET    4   C 5 VAL B  71  ARG B  74  1  O  GLY B  73   N  VAL B  52           
SHEET    5   C 5 LEU B  93  MET B  95  1  O  LEU B  93   N  VAL B  72           
SHEET    1   D 7 GLN B 188  GLN B 189  0                                        
SHEET    2   D 7 LYS B 169  TYR B 173  1  N  GLY B 172   O  GLN B 188           
SHEET    3   D 7 THR B 146  LEU B 150  1  N  LEU B 147   O  LYS B 169           
SHEET    4   D 7 PHE B 201  VAL B 204  1  O  PHE B 201   N  GLY B 148           
SHEET    5   D 7 ARG B 229  ASN B 232  1  O  VAL B 231   N  ILE B 202           
SHEET    6   D 7 GLY B 255  LEU B 258  1  O  ALA B 257   N  ASN B 232           
SHEET    7   D 7 VAL B 277  SER B 279  1  O  ILE B 278   N  ALA B 256           
CISPEP   1 GLU A  264    PRO A  265          0        -4.45                     
CISPEP   2 GLU B  264    PRO B  265          0         0.97                     
SITE     1 AC1 12 ARG A  53  SER A  54  ARG A  74  THR A  77                    
SITE     2 AC1 12 ASN A 101  ARG A 235  HIS A 282  ALA A 285                    
SITE     3 AC1 12 NAD A 501  HOH A 511  HOH A 534  ARG B 134                    
SITE     1 AC2 12 ARG A 134  ARG B  53  SER B  54  ARG B  74                    
SITE     2 AC2 12 THR B  77  ASN B 101  ARG B 235  HIS B 282                    
SITE     3 AC2 12 ALA B 285  NAD B 502  HOH B 519  HOH B 576                    
SITE     1 AC3 28 THR A  77  GLY A 151  GLY A 153  ARG A 154                    
SITE     2 AC3 28 ILE A 155  TYR A 173  ASP A 174  PRO A 175                    
SITE     3 AC3 28 HIS A 205  THR A 206  PRO A 207  SER A 211                    
SITE     4 AC3 28 THR A 212  CYS A 233  ALA A 234  ARG A 235                    
SITE     5 AC3 28 ASP A 259  HIS A 282  GLY A 284  ALA A 285                    
SITE     6 AC3 28 MLT A 503  HOH A 516  HOH A 535  HOH A 550                    
SITE     7 AC3 28 HOH A 554  HOH A 555  HOH A 576  HOH A 590                    
SITE     1 AC4 33 GLU A 193  THR B  77  ASN B 101  ALA B 105                    
SITE     2 AC4 33 GLY B 151  GLY B 153  ARG B 154  ILE B 155                    
SITE     3 AC4 33 TYR B 173  ASP B 174  PRO B 175  ILE B 176                    
SITE     4 AC4 33 HIS B 205  THR B 206  PRO B 207  THR B 212                    
SITE     5 AC4 33 CYS B 233  ALA B 234  ARG B 235  ASP B 259                    
SITE     6 AC4 33 HIS B 282  GLY B 284  ALA B 285  MLT B 504                    
SITE     7 AC4 33 HOH B 526  HOH B 557  HOH B 561  HOH B 570                    
SITE     8 AC4 33 HOH B 580  HOH B 582  HOH B 592  HOH B 602                    
SITE     9 AC4 33 HOH B 618                                                     
CRYST1   43.084  124.113   59.502  90.00 100.99  90.00 P 1 21 1      4          
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      0.023210  0.000000  0.004507        0.00000                         
SCALE2      0.000000  0.008057  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017120        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system