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Database: PDB
Entry: 4QUV
LinkDB: 4QUV
Original site: 4QUV 
HEADER    OXIDOREDUCTASE, MEMBRANE PROTEIN        12-JUL-14   4QUV              
TITLE     STRUCTURE OF AN INTEGRAL MEMBRANE DELTA(14)-STEROL REDUCTASE          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DELTA(14)-STEROL REDUCTASE;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.3.1.70;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: METHYLOMICROBIUM ALCALIPHILUM;                  
SOURCE   3 ORGANISM_TAXID: 1091494;                                             
SOURCE   4 STRAIN: DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z;                  
SOURCE   5 GENE: ERG, MEALZ_1312;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    MEMBRANE PROTEIN, CHOLESTEROL BIOSYNTHESIS, OXIDOREDUCTASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.LI,G.BLOBEL                                                         
REVDAT   3   28-JAN-15 4QUV    1       JRNL                                     
REVDAT   2   29-OCT-14 4QUV    1       JRNL                                     
REVDAT   1   08-OCT-14 4QUV    0                                                
JRNL        AUTH   X.LI,R.ROBERTI,G.BLOBEL                                      
JRNL        TITL   STRUCTURE OF AN INTEGRAL MEMBRANE STEROL REDUCTASE FROM      
JRNL        TITL 2 METHYLOMICROBIUM ALCALIPHILUM.                               
JRNL        REF    NATURE                        V. 517   104 2015              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   25307054                                                     
JRNL        DOI    10.1038/NATURE13797                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.74 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.4_1496)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.74                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.26                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 74.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 30541                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.235                           
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1526                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 37.2588 -  6.0931    0.95     3340   182  0.2322 0.2751        
REMARK   3     2  6.0931 -  4.8397    0.98     3485   210  0.2235 0.2580        
REMARK   3     3  4.8397 -  4.2289    0.97     3429   184  0.1889 0.2538        
REMARK   3     4  4.2289 -  3.8426    0.98     3474   165  0.2114 0.2877        
REMARK   3     5  3.8426 -  3.5675    0.97     3429   176  0.2397 0.3010        
REMARK   3     6  3.5675 -  3.3573    0.89     3145   154  0.2634 0.3098        
REMARK   3     7  3.3573 -  3.1892    0.73     2568   125  0.2945 0.3276        
REMARK   3     8  3.1892 -  3.0505    0.60     2132   107  0.3149 0.3474        
REMARK   3     9  3.0505 -  2.9331    0.49     1710   102  0.2988 0.3629        
REMARK   3    10  2.9331 -  2.8319    0.37     1327    68  0.2990 0.3213        
REMARK   3    11  2.8319 -  2.7434    0.28      976    53  0.2509 0.3653        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.430            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.460           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.013           6736                                  
REMARK   3   ANGLE     :  1.646           9216                                  
REMARK   3   CHIRALITY :  0.084            975                                  
REMARK   3   PLANARITY :  0.009           1104                                  
REMARK   3   DIHEDRAL  : 16.652           2297                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -34.9950  -6.2620  13.7212              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4399 T22:   0.7669                                     
REMARK   3      T33:   0.8130 T12:   0.0621                                     
REMARK   3      T13:  -0.1006 T23:   0.4188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0578 L22:   1.1621                                     
REMARK   3      L33:   3.0582 L12:   0.2142                                     
REMARK   3      L13:   0.1193 L23:   0.2509                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1819 S12:  -0.7167 S13:  -1.3086                       
REMARK   3      S21:   0.3181 S22:   0.1559 S23:   0.1382                       
REMARK   3      S31:   0.2445 S32:  -0.4679 S33:  -0.3491                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain B                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -13.3106   6.4695 -13.6064              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3488 T22:   0.7887                                     
REMARK   3      T33:   0.3986 T12:   0.1652                                     
REMARK   3      T13:  -0.1149 T23:   0.0477                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9161 L22:   2.6286                                     
REMARK   3      L33:   2.5769 L12:  -0.0574                                     
REMARK   3      L13:   0.1889 L23:  -0.2693                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3091 S12:   1.4954 S13:  -0.3261                       
REMARK   3      S21:  -0.1914 S22:  -0.1818 S23:   0.2339                       
REMARK   3      S31:  -0.0846 S32:   0.1055 S33:  -0.0522                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4QUV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB086542.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-OCT-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30541                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.740                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.250                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 74.8                               
REMARK 200  DATA REDUNDANCY                : 2.100                              
REMARK 200  R MERGE                    (I) : 0.04100                            
REMARK 200  R SYM                      (I) : 0.05800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 28.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.51400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, 0.2 M NH4AC, 30% (V/V)       
REMARK 280  PENTAERYTHRITOL ETHOXYLATE (15/4 EO/OH), PH 7, VAPOR DIFFUSION,     
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 36960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     ASN A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     VAL A    12                                                      
REMARK 465     ASP A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     ARG A    16                                                      
REMARK 465     GLN A    17                                                      
REMARK 465     LYS A    18                                                      
REMARK 465     TYR A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     PHE A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     LEU A   165                                                      
REMARK 465     ASN A   166                                                      
REMARK 465     GLY A   167                                                      
REMARK 465     LYS A   168                                                      
REMARK 465     GLN A   169                                                      
REMARK 465     TRP A   170                                                      
REMARK 465     GLU A   171                                                      
REMARK 465     ARG A   172                                                      
REMARK 465     PRO A   173                                                      
REMARK 465     THR A   174                                                      
REMARK 465     GLY A   175                                                      
REMARK 465     ARG A   176                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     ARG B     7                                                      
REMARK 465     ASP B     8                                                      
REMARK 465     ASN B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     VAL B    12                                                      
REMARK 465     ASP B    13                                                      
REMARK 465     ALA B    14                                                      
REMARK 465     VAL B    15                                                      
REMARK 465     ARG B    16                                                      
REMARK 465     GLN B    17                                                      
REMARK 465     LYS B    18                                                      
REMARK 465     TYR B    19                                                      
REMARK 465     GLY B    20                                                      
REMARK 465     PHE B    21                                                      
REMARK 465     GLY B    22                                                      
REMARK 465     PHE B    23                                                      
REMARK 465     PHE B   162                                                      
REMARK 465     TRP B   163                                                      
REMARK 465     GLY B   164                                                      
REMARK 465     LEU B   165                                                      
REMARK 465     ASN B   166                                                      
REMARK 465     GLY B   167                                                      
REMARK 465     LYS B   168                                                      
REMARK 465     GLN B   169                                                      
REMARK 465     TRP B   170                                                      
REMARK 465     GLU B   171                                                      
REMARK 465     ARG B   172                                                      
REMARK 465     PRO B   173                                                      
REMARK 465     THR B   174                                                      
REMARK 465     GLY B   175                                                      
REMARK 465     ARG B   176                                                      
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     SER B 193    CB   OG                                             
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   O    GLY A   158     CD2  PHE A   162              1.93            
REMARK 500   O    ARG B   328     N    ALA B   335              2.14            
REMARK 500   O    PRO B    92     ND2  ASN B   112              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 293   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
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    MET A  99     -158.00     62.79                                   
REMARK 500    ASP A 103      -50.94     75.01                                   
REMARK 500    MET A 130        1.12    -69.78                                   
REMARK 500    ALA A 186       11.40     84.59                                   
REMARK 500    LEU A 187     -125.77     59.55                                   
REMARK 500    ALA A 202      -71.03   -112.40                                   
REMARK 500    ARG A 203      -70.84    -66.52                                   
REMARK 500    HIS A 224       -3.68   -142.38                                   
REMARK 500    VAL A 252        3.48    -69.21                                   
REMARK 500    PHE A 263     -130.08     56.28                                   
REMARK 500    THR A 290       52.54   -101.37                                   
REMARK 500    ASP A 325       78.97   -165.39                                   
REMARK 500    ALA A 375     -146.68     62.95                                   
REMARK 500    ILE A 422      -54.11   -129.68                                   
REMARK 500    TYR B  46       30.18    -90.63                                   
REMARK 500    ALA B  56      -60.26     66.77                                   
REMARK 500    MET B  99     -146.39     59.05                                   
REMARK 500    ASP B 103      -55.42     75.22                                   
REMARK 500    ASP B 140      -74.74    -59.76                                   
REMARK 500    LEU B 187     -119.86     63.79                                   
REMARK 500    SER B 193       -6.06     97.19                                   
REMARK 500    ARG B 203      -72.37    -64.82                                   
REMARK 500    HIS B 224       -2.94   -145.71                                   
REMARK 500    THR B 290       54.67    -97.49                                   
REMARK 500    TRP B 331     -151.05     58.63                                   
REMARK 500    ALA B 375     -145.34     64.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NDP A  501                                                       
REMARK 610     NDP B  501                                                       
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                 
DBREF  4QUV A    1   427  UNP    G4SW86   G4SW86_META2     1    427             
DBREF  4QUV B    1   427  UNP    G4SW86   G4SW86_META2     1    427             
SEQRES   1 A  427  MET SER GLU GLN GLU SER ARG ASP ASN ALA ALA VAL ASP          
SEQRES   2 A  427  ALA VAL ARG GLN LYS TYR GLY PHE GLY PHE SER TRP LEU          
SEQRES   3 A  427  VAL LEU MET ILE ALA LEU PRO PRO LEU VAL TYR TYR LEU          
SEQRES   4 A  427  TRP ILE CYS VAL THR TYR TYR GLN GLY GLU LEU VAL PHE          
SEQRES   5 A  427  THR SER ASP ALA ALA ALA TRP ARG ARG PHE TRP SER HIS          
SEQRES   6 A  427  VAL ALA PRO PRO THR TRP HIS ALA ALA GLY LEU TYR ALA          
SEQRES   7 A  427  ALA TRP PHE LEU GLY GLN ALA ALA LEU GLN VAL TRP ALA          
SEQRES   8 A  427  PRO GLY PRO THR VAL GLN GLY MET LYS LEU PRO ASP GLY          
SEQRES   9 A  427  SER ARG LEU ASP TYR ARG MET ASN GLY ILE PHE SER PHE          
SEQRES  10 A  427  LEU PHE THR LEU ALA VAL VAL PHE GLY LEU VAL THR MET          
SEQRES  11 A  427  GLY TRP LEU ASP ALA THR VAL LEU TYR ASP GLN LEU GLY          
SEQRES  12 A  427  PRO LEU LEU THR VAL VAL ASN ILE PHE THR PHE VAL PHE          
SEQRES  13 A  427  ALA GLY PHE LEU TYR PHE TRP GLY LEU ASN GLY LYS GLN          
SEQRES  14 A  427  TRP GLU ARG PRO THR GLY ARG PRO PHE TYR ASP TYR PHE          
SEQRES  15 A  427  MET GLY THR ALA LEU ASN PRO ARG ILE GLY SER LEU ASP          
SEQRES  16 A  427  LEU LYS LEU PHE CYS GLU ALA ARG PRO GLY MET ILE PHE          
SEQRES  17 A  427  TRP LEU LEU MET ASN LEU SER MET ALA ALA LYS GLN TYR          
SEQRES  18 A  427  GLU LEU HIS GLY THR VAL THR VAL PRO MET LEU LEU VAL          
SEQRES  19 A  427  VAL GLY PHE GLN SER PHE TYR LEU ILE ASP TYR PHE ILE          
SEQRES  20 A  427  HIS GLU GLU ALA VAL LEU THR THR TRP ASP ILE LYS HIS          
SEQRES  21 A  427  GLU LYS PHE GLY TRP MET LEU CYS TRP GLY ASP LEU VAL          
SEQRES  22 A  427  TRP LEU PRO PHE THR TYR THR LEU GLN ALA GLN TYR LEU          
SEQRES  23 A  427  VAL HIS HIS THR HIS ASP LEU PRO VAL TRP GLY ILE ILE          
SEQRES  24 A  427  ALA ILE VAL ALA LEU ASN LEU ALA GLY TYR ALA ILE PHE          
SEQRES  25 A  427  ARG GLY ALA ASN ILE GLN LYS HIS HIS PHE ARG ARG ASP          
SEQRES  26 A  427  PRO ASN ARG ILE VAL TRP GLY LYS PRO ALA LYS TYR ILE          
SEQRES  27 A  427  LYS THR LYS GLN GLY SER LEU LEU LEU THR SER GLY TRP          
SEQRES  28 A  427  TRP GLY ILE ALA ARG HIS MET ASN TYR PHE GLY ASP LEU          
SEQRES  29 A  427  MET ILE ALA LEU SER TRP CYS LEU PRO ALA ALA PHE GLY          
SEQRES  30 A  427  SER PRO ILE PRO TYR PHE HIS ILE VAL TYR PHE THR ILE          
SEQRES  31 A  427  LEU LEU LEU HIS ARG GLU LYS ARG ASP ASP ALA MET CYS          
SEQRES  32 A  427  LEU ALA LYS TYR GLY GLU ASP TRP LEU GLN TYR ARG LYS          
SEQRES  33 A  427  LYS VAL PRO TRP ARG ILE VAL PRO LYS ILE TYR                  
SEQRES   1 B  427  MET SER GLU GLN GLU SER ARG ASP ASN ALA ALA VAL ASP          
SEQRES   2 B  427  ALA VAL ARG GLN LYS TYR GLY PHE GLY PHE SER TRP LEU          
SEQRES   3 B  427  VAL LEU MET ILE ALA LEU PRO PRO LEU VAL TYR TYR LEU          
SEQRES   4 B  427  TRP ILE CYS VAL THR TYR TYR GLN GLY GLU LEU VAL PHE          
SEQRES   5 B  427  THR SER ASP ALA ALA ALA TRP ARG ARG PHE TRP SER HIS          
SEQRES   6 B  427  VAL ALA PRO PRO THR TRP HIS ALA ALA GLY LEU TYR ALA          
SEQRES   7 B  427  ALA TRP PHE LEU GLY GLN ALA ALA LEU GLN VAL TRP ALA          
SEQRES   8 B  427  PRO GLY PRO THR VAL GLN GLY MET LYS LEU PRO ASP GLY          
SEQRES   9 B  427  SER ARG LEU ASP TYR ARG MET ASN GLY ILE PHE SER PHE          
SEQRES  10 B  427  LEU PHE THR LEU ALA VAL VAL PHE GLY LEU VAL THR MET          
SEQRES  11 B  427  GLY TRP LEU ASP ALA THR VAL LEU TYR ASP GLN LEU GLY          
SEQRES  12 B  427  PRO LEU LEU THR VAL VAL ASN ILE PHE THR PHE VAL PHE          
SEQRES  13 B  427  ALA GLY PHE LEU TYR PHE TRP GLY LEU ASN GLY LYS GLN          
SEQRES  14 B  427  TRP GLU ARG PRO THR GLY ARG PRO PHE TYR ASP TYR PHE          
SEQRES  15 B  427  MET GLY THR ALA LEU ASN PRO ARG ILE GLY SER LEU ASP          
SEQRES  16 B  427  LEU LYS LEU PHE CYS GLU ALA ARG PRO GLY MET ILE PHE          
SEQRES  17 B  427  TRP LEU LEU MET ASN LEU SER MET ALA ALA LYS GLN TYR          
SEQRES  18 B  427  GLU LEU HIS GLY THR VAL THR VAL PRO MET LEU LEU VAL          
SEQRES  19 B  427  VAL GLY PHE GLN SER PHE TYR LEU ILE ASP TYR PHE ILE          
SEQRES  20 B  427  HIS GLU GLU ALA VAL LEU THR THR TRP ASP ILE LYS HIS          
SEQRES  21 B  427  GLU LYS PHE GLY TRP MET LEU CYS TRP GLY ASP LEU VAL          
SEQRES  22 B  427  TRP LEU PRO PHE THR TYR THR LEU GLN ALA GLN TYR LEU          
SEQRES  23 B  427  VAL HIS HIS THR HIS ASP LEU PRO VAL TRP GLY ILE ILE          
SEQRES  24 B  427  ALA ILE VAL ALA LEU ASN LEU ALA GLY TYR ALA ILE PHE          
SEQRES  25 B  427  ARG GLY ALA ASN ILE GLN LYS HIS HIS PHE ARG ARG ASP          
SEQRES  26 B  427  PRO ASN ARG ILE VAL TRP GLY LYS PRO ALA LYS TYR ILE          
SEQRES  27 B  427  LYS THR LYS GLN GLY SER LEU LEU LEU THR SER GLY TRP          
SEQRES  28 B  427  TRP GLY ILE ALA ARG HIS MET ASN TYR PHE GLY ASP LEU          
SEQRES  29 B  427  MET ILE ALA LEU SER TRP CYS LEU PRO ALA ALA PHE GLY          
SEQRES  30 B  427  SER PRO ILE PRO TYR PHE HIS ILE VAL TYR PHE THR ILE          
SEQRES  31 B  427  LEU LEU LEU HIS ARG GLU LYS ARG ASP ASP ALA MET CYS          
SEQRES  32 B  427  LEU ALA LYS TYR GLY GLU ASP TRP LEU GLN TYR ARG LYS          
SEQRES  33 B  427  LYS VAL PRO TRP ARG ILE VAL PRO LYS ILE TYR                  
HET    NDP  A 501      31                                                       
HET    NDP  B 501      31                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
FORMUL   3  NDP    2(C21 H30 N7 O17 P3)                                         
HELIX    1   1 PHE A   23  TYR A   46  1                                  24    
HELIX    2   2 ASP A   55  SER A   64  1                                  10    
HELIX    3   3 THR A   70  ALA A   91  1                                  22    
HELIX    4   4 ASN A  112  MET A  130  1                                  19    
HELIX    5   5 THR A  136  GLN A  141  1                                   6    
HELIX    6   6 GLN A  141  GLY A  164  1                                  24    
HELIX    7   7 TYR A  179  GLY A  184  1                                   6    
HELIX    8   8 LEU A  196  GLY A  225  1                                  30    
HELIX    9   9 THR A  228  HIS A  248  1                                  21    
HELIX   10  10 GLU A  249  THR A  254  5                                   6    
HELIX   11  11 THR A  255  HIS A  260  1                                   6    
HELIX   12  12 GLY A  264  VAL A  273  1                                  10    
HELIX   13  13 VAL A  273  THR A  280  1                                   8    
HELIX   14  14 THR A  280  HIS A  288  1                                   9    
HELIX   15  15 PRO A  294  ARG A  324  1                                  31    
HELIX   16  16 GLY A  350  ALA A  355  1                                   6    
HELIX   17  17 HIS A  357  LEU A  372  1                                  16    
HELIX   18  18 PRO A  373  ALA A  375  5                                   3    
HELIX   19  19 PRO A  379  PRO A  381  5                                   3    
HELIX   20  20 TYR A  382  VAL A  418  1                                  37    
HELIX   21  21 TRP B   25  TYR B   45  1                                  21    
HELIX   22  22 ALA B   56  SER B   64  1                                   9    
HELIX   23  23 THR B   70  ALA B   91  1                                  22    
HELIX   24  24 ASN B  112  MET B  130  1                                  19    
HELIX   25  25 THR B  136  GLN B  141  1                                   6    
HELIX   26  26 GLN B  141  TYR B  161  1                                  21    
HELIX   27  27 LEU B  196  GLY B  225  1                                  30    
HELIX   28  28 THR B  228  HIS B  248  1                                  21    
HELIX   29  29 GLU B  249  THR B  254  5                                   6    
HELIX   30  30 THR B  255  HIS B  260  1                                   6    
HELIX   31  31 GLY B  264  VAL B  273  1                                  10    
HELIX   32  32 VAL B  273  THR B  280  1                                   8    
HELIX   33  33 THR B  280  HIS B  288  1                                   9    
HELIX   34  34 PRO B  294  ARG B  324  1                                  31    
HELIX   35  35 GLY B  350  ALA B  355  1                                   6    
HELIX   36  36 HIS B  357  LEU B  372  1                                  16    
HELIX   37  37 PRO B  373  ALA B  375  5                                   3    
HELIX   38  38 PRO B  379  PRO B  381  5                                   3    
HELIX   39  39 TYR B  382  GLY B  408  1                                  27    
HELIX   40  40 GLY B  408  VAL B  418  1                                  11    
SHEET    1   A 2 THR A  95  GLY A  98  0                                        
SHEET    2   A 2 LEU A 107  ARG A 110 -1  O  TYR A 109   N  VAL A  96           
SHEET    1   B 2 ARG A 190  ILE A 191  0                                        
SHEET    2   B 2 LEU A 194  ASP A 195 -1  O  LEU A 194   N  ILE A 191           
SHEET    1   C 2 TYR A 337  THR A 340  0                                        
SHEET    2   C 2 SER A 344  LEU A 347 -1  O  LEU A 346   N  ILE A 338           
SHEET    1   D 2 THR B  95  GLY B  98  0                                        
SHEET    2   D 2 LEU B 107  ARG B 110 -1  O  TYR B 109   N  VAL B  96           
SHEET    1   E 2 ARG B 190  ILE B 191  0                                        
SHEET    2   E 2 LEU B 194  ASP B 195 -1  O  LEU B 194   N  ILE B 191           
SHEET    1   F 2 ILE B 329  VAL B 330  0                                        
SHEET    2   F 2 LYS B 333  PRO B 334 -1  O  LYS B 333   N  VAL B 330           
SHEET    1   G 2 TYR B 337  THR B 340  0                                        
SHEET    2   G 2 SER B 344  LEU B 347 -1  O  SER B 344   N  THR B 340           
CISPEP   1 GLY A   93    PRO A   94          0         1.28                     
CISPEP   2 GLY A  104    SER A  105          0        18.92                     
CISPEP   3 VAL A  423    PRO A  424          0        -8.42                     
CISPEP   4 GLY B  104    SER B  105          0         2.71                     
SITE     1 AC1 16 THR A 254  ASN A 316  LYS A 319  ARG A 323                    
SITE     2 AC1 16 LEU A 345  LEU A 346  LEU A 347  TRP A 352                    
SITE     3 AC1 16 HIS A 357  ASN A 359  TYR A 360  ASP A 399                    
SITE     4 AC1 16 CYS A 403  LYS A 406  TYR A 407  TYR A 414                    
SITE     1 AC2 14 LYS B 319  ARG B 323  LEU B 345  LEU B 346                    
SITE     2 AC2 14 LEU B 347  TRP B 352  HIS B 357  ASN B 359                    
SITE     3 AC2 14 TYR B 360  ASP B 399  CYS B 403  LYS B 406                    
SITE     4 AC2 14 TYR B 407  TYR B 414                                          
CRYST1   74.660   74.615   79.549  66.00  90.37  86.86 P 1           2          
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      0.013394 -0.000736  0.000423        0.00000                         
SCALE2      0.000000  0.013422 -0.005995        0.00000                         
SCALE3      0.000000  0.000000  0.013768        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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