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Database: PDB
Entry: 5WI0
LinkDB: 5WI0
Original site: 5WI0 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       18-JUL-17   5WI0              
TITLE     CRYSTAL STRUCTURE OF HUMAN NAMPT WITH FRAGMENT 2: 2-[(2-FLUOROPHENYL) 
TITLE    2 AMINO]-6-PROPYLPYRIMIDIN-4(3H)-ONE                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE;                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: NAMPT,PRE-B-CELL COLONY-ENHANCING FACTOR 1,PRE-B CELL-      
COMPND   5 ENHANCING FACTOR,VISFATIN;                                           
COMPND   6 EC: 2.4.2.12;                                                        
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: NAMPT, PBEF, PBEF1;                                            
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK 293-6E                              
KEYWDS    NAMPT, INHIBITOR, TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR      
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.L.LONGENECKER,D.RAICH,A.V.KOREPANOVA                                
REVDAT   4   04-OCT-23 5WI0    1       REMARK                                   
REVDAT   3   01-MAY-19 5WI0    1       JRNL                                     
REVDAT   2   21-MAR-18 5WI0    1       REMARK                                   
REVDAT   1   10-JAN-18 5WI0    0                                                
JRNL        AUTH   A.KOREPANOVA,K.L.LONGENECKER,S.D.PRATT,S.C.PANCHAL,          
JRNL        AUTH 2 R.F.CLARK,M.LAKE,S.M.GOPALAKRISHNAN,D.RAICH,C.SUN,A.M.PETROS 
JRNL        TITL   FRAGMENT-BASED DISCOVERY OF A POTENT NAMPT INHIBITOR.        
JRNL        REF    BIOORG. MED. CHEM. LETT.      V.  28   437 2018              
JRNL        REFN                   ESSN 1464-3405                               
JRNL        PMID   29287958                                                     
JRNL        DOI    10.1016/J.BMCL.2017.12.023                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.7                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.66                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 65452                          
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)  : 0.221                          
REMARK   3   R VALUE            (WORKING SET)  : 0.219                          
REMARK   3   FREE R VALUE                      : 0.247                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.110                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3347                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.05                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.10                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 89.73                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4378                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2561                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 4161                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2541                   
REMARK   3   BIN FREE R VALUE                        : 0.2956                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.96                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 217                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7422                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 629                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.93                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.90000                                             
REMARK   3    B22 (A**2) : 1.55740                                              
REMARK   3    B33 (A**2) : 4.34250                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.86000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.290               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.226               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.178               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.223               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.179               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.911                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.884                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 7636   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 10348  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2632   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 194    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1114   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 7636   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 972    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 9504   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.06                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.40                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.58                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5WI0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229060.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000000                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 65534                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 82.290                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.16200                            
REMARK 200  R SYM                      (I) : 0.16200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.69700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 2GVJ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 10K, SODIUM CHLORIDE, GLYCEROL,      
REMARK 280  TRIS, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K       
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       53.42800            
REMARK 290   SMTRY3   2  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: 8380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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     ASN A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     LYS A    42                                                      
REMARK 465     LYS A    43                                                      
REMARK 465     THR A    44                                                      
REMARK 465     GLU A    45                                                      
REMARK 465     ASN A    46                                                      
REMARK 465     SER A    47                                                      
REMARK 465     LYS A    48                                                      
REMARK 465     LEU A    49                                                      
REMARK 465     ARG A    50                                                      
REMARK 465     LYS A    51                                                      
REMARK 465     VAL A    52                                                      
REMARK 465     LYS A    53                                                      
REMARK 465     GLU A   485                                                      
REMARK 465     LEU A   486                                                      
REMARK 465     GLU A   487                                                      
REMARK 465     ALA A   488                                                      
REMARK 465     ALA A   489                                                      
REMARK 465     HIS A   490                                                      
REMARK 465     HIS A   491                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     GLU B     8                                                      
REMARK 465     LYS B    42                                                      
REMARK 465     LYS B    43                                                      
REMARK 465     THR B    44                                                      
REMARK 465     GLU B    45                                                      
REMARK 465     ASN B    46                                                      
REMARK 465     SER B    47                                                      
REMARK 465     LYS B    48                                                      
REMARK 465     LEU B    49                                                      
REMARK 465     ARG B    50                                                      
REMARK 465     LYS B    51                                                      
REMARK 465     VAL B    52                                                      
REMARK 465     LYS B    53                                                      
REMARK 465     GLU B   485                                                      
REMARK 465     LEU B   486                                                      
REMARK 465     GLU B   487                                                      
REMARK 465     ALA B   488                                                      
REMARK 465     ALA B   489                                                      
REMARK 465     HIS B   490                                                      
REMARK 465     HIS B   491                                                      
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    TYR A 231      -55.84   -127.72                                   
REMARK 500    PHE A 269       54.70   -119.74                                   
REMARK 500    TYR A 281      -52.84   -127.31                                   
REMARK 500    GLU A 293      -75.64   -128.46                                   
REMARK 500    ASP A 313       21.73   -142.38                                   
REMARK 500    ASP A 416       70.80   -152.47                                   
REMARK 500    TYR A 453     -165.27   -109.99                                   
REMARK 500    CYS B 141       32.04    -99.92                                   
REMARK 500    TYR B 231      -56.40   -128.07                                   
REMARK 500    PHE B 269       54.70   -118.97                                   
REMARK 500    TYR B 281      -51.75   -129.34                                   
REMARK 500    GLU B 293      -75.67   -128.07                                   
REMARK 500    ASP B 313       21.79   -141.21                                   
REMARK 500    ASP B 416       71.51   -152.91                                   
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 A1310        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH A1311        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH A1312        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH A1313        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH A1314        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH A1315        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH A1316        DISTANCE =  6.90 ANGSTROMS                       
REMARK 525    HOH A1317        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH A1318        DISTANCE =  7.13 ANGSTROMS                       
REMARK 525    HOH A1319        DISTANCE =  7.15 ANGSTROMS                       
REMARK 525    HOH A1320        DISTANCE =  7.37 ANGSTROMS                       
REMARK 525    HOH B 908        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH B 909        DISTANCE =  6.95 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AQ1 A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AQ1 B 501                 
DBREF  5WI0 A    1   491  UNP    P43490   NAMPT_HUMAN      1    491             
DBREF  5WI0 B    1   491  UNP    P43490   NAMPT_HUMAN      1    491             
SEQRES   1 A  491  MET ASN PRO ALA ALA GLU ALA GLU PHE ASN ILE LEU LEU          
SEQRES   2 A  491  ALA THR ASP SER TYR LYS VAL THR HIS TYR LYS GLN TYR          
SEQRES   3 A  491  PRO PRO ASN THR SER LYS VAL TYR SER TYR PHE GLU CYS          
SEQRES   4 A  491  ARG GLU LYS LYS THR GLU ASN SER LYS LEU ARG LYS VAL          
SEQRES   5 A  491  LYS TYR GLU GLU THR VAL PHE TYR GLY LEU GLN TYR ILE          
SEQRES   6 A  491  LEU ASN LYS TYR LEU LYS GLY LYS VAL VAL THR LYS GLU          
SEQRES   7 A  491  LYS ILE GLN GLU ALA LYS ASP VAL TYR LYS GLU HIS PHE          
SEQRES   8 A  491  GLN ASP ASP VAL PHE ASN GLU LYS GLY TRP ASN TYR ILE          
SEQRES   9 A  491  LEU GLU LYS TYR ASP GLY HIS LEU PRO ILE GLU ILE LYS          
SEQRES  10 A  491  ALA VAL PRO GLU GLY PHE VAL ILE PRO ARG GLY ASN VAL          
SEQRES  11 A  491  LEU PHE THR VAL GLU ASN THR ASP PRO GLU CYS TYR TRP          
SEQRES  12 A  491  LEU THR ASN TRP ILE GLU THR ILE LEU VAL GLN SER TRP          
SEQRES  13 A  491  TYR PRO ILE THR VAL ALA THR ASN SER ARG GLU GLN LYS          
SEQRES  14 A  491  LYS ILE LEU ALA LYS TYR LEU LEU GLU THR SER GLY ASN          
SEQRES  15 A  491  LEU ASP GLY LEU GLU TYR LYS LEU HIS ASP PHE GLY TYR          
SEQRES  16 A  491  ARG GLY VAL SER SER GLN GLU THR ALA GLY ILE GLY ALA          
SEQRES  17 A  491  SER ALA HIS LEU VAL ASN PHE LYS GLY THR ASP THR VAL          
SEQRES  18 A  491  ALA GLY LEU ALA LEU ILE LYS LYS TYR TYR GLY THR LYS          
SEQRES  19 A  491  ASP PRO VAL PRO GLY TYR SER VAL PRO ALA ALA GLU HIS          
SEQRES  20 A  491  SER THR ILE THR ALA TRP GLY LYS ASP HIS GLU LYS ASP          
SEQRES  21 A  491  ALA PHE GLU HIS ILE VAL THR GLN PHE SER SER VAL PRO          
SEQRES  22 A  491  VAL SER VAL VAL SER ASP SER TYR ASP ILE TYR ASN ALA          
SEQRES  23 A  491  CYS GLU LYS ILE TRP GLY GLU ASP LEU ARG HIS LEU ILE          
SEQRES  24 A  491  VAL SER ARG SER THR GLN ALA PRO LEU ILE ILE ARG PRO          
SEQRES  25 A  491  ASP SER GLY ASN PRO LEU ASP THR VAL LEU LYS VAL LEU          
SEQRES  26 A  491  GLU ILE LEU GLY LYS LYS PHE PRO VAL THR GLU ASN SER          
SEQRES  27 A  491  LYS GLY TYR LYS LEU LEU PRO PRO TYR LEU ARG VAL ILE          
SEQRES  28 A  491  GLN GLY ASP GLY VAL ASP ILE ASN THR LEU GLN GLU ILE          
SEQRES  29 A  491  VAL GLU GLY MET LYS GLN LYS MET TRP SER ILE GLU ASN          
SEQRES  30 A  491  ILE ALA PHE GLY SER GLY GLY GLY LEU LEU GLN LYS LEU          
SEQRES  31 A  491  THR ARG ASP LEU LEU ASN CYS SER PHE LYS CYS SER TYR          
SEQRES  32 A  491  VAL VAL THR ASN GLY LEU GLY ILE ASN VAL PHE LYS ASP          
SEQRES  33 A  491  PRO VAL ALA ASP PRO ASN LYS ARG SER LYS LYS GLY ARG          
SEQRES  34 A  491  LEU SER LEU HIS ARG THR PRO ALA GLY ASN PHE VAL THR          
SEQRES  35 A  491  LEU GLU GLU GLY LYS GLY ASP LEU GLU GLU TYR GLY GLN          
SEQRES  36 A  491  ASP LEU LEU HIS THR VAL PHE LYS ASN GLY LYS VAL THR          
SEQRES  37 A  491  LYS SER TYR SER PHE ASP GLU ILE ARG LYS ASN ALA GLN          
SEQRES  38 A  491  LEU ASN ILE GLU LEU GLU ALA ALA HIS HIS                      
SEQRES   1 B  491  MET ASN PRO ALA ALA GLU ALA GLU PHE ASN ILE LEU LEU          
SEQRES   2 B  491  ALA THR ASP SER TYR LYS VAL THR HIS TYR LYS GLN TYR          
SEQRES   3 B  491  PRO PRO ASN THR SER LYS VAL TYR SER TYR PHE GLU CYS          
SEQRES   4 B  491  ARG GLU LYS LYS THR GLU ASN SER LYS LEU ARG LYS VAL          
SEQRES   5 B  491  LYS TYR GLU GLU THR VAL PHE TYR GLY LEU GLN TYR ILE          
SEQRES   6 B  491  LEU ASN LYS TYR LEU LYS GLY LYS VAL VAL THR LYS GLU          
SEQRES   7 B  491  LYS ILE GLN GLU ALA LYS ASP VAL TYR LYS GLU HIS PHE          
SEQRES   8 B  491  GLN ASP ASP VAL PHE ASN GLU LYS GLY TRP ASN TYR ILE          
SEQRES   9 B  491  LEU GLU LYS TYR ASP GLY HIS LEU PRO ILE GLU ILE LYS          
SEQRES  10 B  491  ALA VAL PRO GLU GLY PHE VAL ILE PRO ARG GLY ASN VAL          
SEQRES  11 B  491  LEU PHE THR VAL GLU ASN THR ASP PRO GLU CYS TYR TRP          
SEQRES  12 B  491  LEU THR ASN TRP ILE GLU THR ILE LEU VAL GLN SER TRP          
SEQRES  13 B  491  TYR PRO ILE THR VAL ALA THR ASN SER ARG GLU GLN LYS          
SEQRES  14 B  491  LYS ILE LEU ALA LYS TYR LEU LEU GLU THR SER GLY ASN          
SEQRES  15 B  491  LEU ASP GLY LEU GLU TYR LYS LEU HIS ASP PHE GLY TYR          
SEQRES  16 B  491  ARG GLY VAL SER SER GLN GLU THR ALA GLY ILE GLY ALA          
SEQRES  17 B  491  SER ALA HIS LEU VAL ASN PHE LYS GLY THR ASP THR VAL          
SEQRES  18 B  491  ALA GLY LEU ALA LEU ILE LYS LYS TYR TYR GLY THR LYS          
SEQRES  19 B  491  ASP PRO VAL PRO GLY TYR SER VAL PRO ALA ALA GLU HIS          
SEQRES  20 B  491  SER THR ILE THR ALA TRP GLY LYS ASP HIS GLU LYS ASP          
SEQRES  21 B  491  ALA PHE GLU HIS ILE VAL THR GLN PHE SER SER VAL PRO          
SEQRES  22 B  491  VAL SER VAL VAL SER ASP SER TYR ASP ILE TYR ASN ALA          
SEQRES  23 B  491  CYS GLU LYS ILE TRP GLY GLU ASP LEU ARG HIS LEU ILE          
SEQRES  24 B  491  VAL SER ARG SER THR GLN ALA PRO LEU ILE ILE ARG PRO          
SEQRES  25 B  491  ASP SER GLY ASN PRO LEU ASP THR VAL LEU LYS VAL LEU          
SEQRES  26 B  491  GLU ILE LEU GLY LYS LYS PHE PRO VAL THR GLU ASN SER          
SEQRES  27 B  491  LYS GLY TYR LYS LEU LEU PRO PRO TYR LEU ARG VAL ILE          
SEQRES  28 B  491  GLN GLY ASP GLY VAL ASP ILE ASN THR LEU GLN GLU ILE          
SEQRES  29 B  491  VAL GLU GLY MET LYS GLN LYS MET TRP SER ILE GLU ASN          
SEQRES  30 B  491  ILE ALA PHE GLY SER GLY GLY GLY LEU LEU GLN LYS LEU          
SEQRES  31 B  491  THR ARG ASP LEU LEU ASN CYS SER PHE LYS CYS SER TYR          
SEQRES  32 B  491  VAL VAL THR ASN GLY LEU GLY ILE ASN VAL PHE LYS ASP          
SEQRES  33 B  491  PRO VAL ALA ASP PRO ASN LYS ARG SER LYS LYS GLY ARG          
SEQRES  34 B  491  LEU SER LEU HIS ARG THR PRO ALA GLY ASN PHE VAL THR          
SEQRES  35 B  491  LEU GLU GLU GLY LYS GLY ASP LEU GLU GLU TYR GLY GLN          
SEQRES  36 B  491  ASP LEU LEU HIS THR VAL PHE LYS ASN GLY LYS VAL THR          
SEQRES  37 B  491  LYS SER TYR SER PHE ASP GLU ILE ARG LYS ASN ALA GLN          
SEQRES  38 B  491  LEU ASN ILE GLU LEU GLU ALA ALA HIS HIS                      
HET    AQ1  A 901      18                                                       
HET    AQ1  B 501      18                                                       
HETNAM     AQ1 2-[(2-FLUOROPHENYL)AMINO]-6-PROPYLPYRIMIDIN-4(3H)-ONE            
FORMUL   3  AQ1    2(C13 H14 F N3 O)                                            
FORMUL   5  HOH   *629(H2 O)                                                    
HELIX    1 AA1 ASN A   10  ALA A   14  5                                   5    
HELIX    2 AA2 ASP A   16  GLN A   25  5                                  10    
HELIX    3 AA3 GLY A   61  LEU A   70  1                                  10    
HELIX    4 AA4 THR A   76  GLN A   92  1                                  17    
HELIX    5 AA5 ASN A   97  ASP A  109  1                                  13    
HELIX    6 AA6 ASP A  138  TYR A  142  5                                   5    
HELIX    7 AA7 TRP A  143  ILE A  148  1                                   6    
HELIX    8 AA8 ILE A  148  GLN A  154  1                                   7    
HELIX    9 AA9 SER A  155  GLY A  181  1                                  27    
HELIX   10 AB1 GLY A  185  TYR A  188  5                                   4    
HELIX   11 AB2 SER A  200  VAL A  213  1                                  14    
HELIX   12 AB3 VAL A  221  TYR A  231  1                                  11    
HELIX   13 AB4 GLU A  246  ALA A  252  1                                   7    
HELIX   14 AB5 TRP A  253  ASP A  256  5                                   4    
HELIX   15 AB6 HIS A  257  PHE A  269  1                                  13    
HELIX   16 AB7 ASP A  282  LYS A  289  1                                   8    
HELIX   17 AB8 LEU A  295  ILE A  299  5                                   5    
HELIX   18 AB9 ASN A  316  PHE A  332  1                                  17    
HELIX   19 AC1 ASP A  357  LYS A  371  1                                  15    
HELIX   20 AC2 SER A  374  GLU A  376  5                                   3    
HELIX   21 AC3 GLY A  383  GLN A  388  1                                   6    
HELIX   22 AC4 ASP A  420  ARG A  424  5                                   5    
HELIX   23 AC5 GLY A  446  LEU A  450  5                                   5    
HELIX   24 AC6 SER A  472  ALA A  480  1                                   9    
HELIX   25 AC7 ASN B   10  ALA B   14  5                                   5    
HELIX   26 AC8 ASP B   16  GLN B   25  5                                  10    
HELIX   27 AC9 GLY B   61  LEU B   70  1                                  10    
HELIX   28 AD1 THR B   76  GLN B   92  1                                  17    
HELIX   29 AD2 ASN B   97  ASP B  109  1                                  13    
HELIX   30 AD3 ASP B  138  TYR B  142  5                                   5    
HELIX   31 AD4 TRP B  143  ILE B  148  1                                   6    
HELIX   32 AD5 ILE B  148  GLN B  154  1                                   7    
HELIX   33 AD6 SER B  155  GLY B  181  1                                  27    
HELIX   34 AD7 GLY B  185  TYR B  188  5                                   4    
HELIX   35 AD8 SER B  200  VAL B  213  1                                  14    
HELIX   36 AD9 VAL B  221  TYR B  231  1                                  11    
HELIX   37 AE1 GLU B  246  ALA B  252  1                                   7    
HELIX   38 AE2 TRP B  253  ASP B  256  5                                   4    
HELIX   39 AE3 HIS B  257  PHE B  269  1                                  13    
HELIX   40 AE4 ASP B  282  LYS B  289  1                                   8    
HELIX   41 AE5 LEU B  295  ILE B  299  5                                   5    
HELIX   42 AE6 ASN B  316  PHE B  332  1                                  17    
HELIX   43 AE7 ASP B  357  LYS B  371  1                                  15    
HELIX   44 AE8 SER B  374  GLU B  376  5                                   3    
HELIX   45 AE9 GLY B  383  GLN B  388  1                                   6    
HELIX   46 AF1 ASP B  420  ARG B  424  5                                   5    
HELIX   47 AF2 GLY B  446  GLU B  451  5                                   6    
HELIX   48 AF3 SER B  472  ALA B  480  1                                   9    
SHEET    1 AA1 7 LEU A 409  ASN A 412  0                                        
SHEET    2 AA1 7 CYS A 397  THR A 406 -1  N  VAL A 404   O  ILE A 411           
SHEET    3 AA1 7 THR A  30  CYS A  39 -1  N  TYR A  34   O  TYR A 403           
SHEET    4 AA1 7 PHE A 132  ASN A 136 -1  O  VAL A 134   N  SER A  35           
SHEET    5 AA1 7 ILE A 114  ALA A 118 -1  N  GLU A 115   O  GLU A 135           
SHEET    6 AA1 7 HIS A 459  LYS A 463 -1  O  HIS A 459   N  ALA A 118           
SHEET    7 AA1 7 LYS A 466  VAL A 467 -1  O  LYS A 466   N  LYS A 463           
SHEET    1 AA2 2 GLU A  56  VAL A  58  0                                        
SHEET    2 AA2 2 VAL A 124  PRO A 126 -1  O  ILE A 125   N  THR A  57           
SHEET    1 AA3 5 LEU A 190  ASP A 192  0                                        
SHEET    2 AA3 5 ILE A 378  SER A 382  1  O  PHE A 380   N  HIS A 191           
SHEET    3 AA3 5 LEU A 348  GLN A 352  1  N  GLN A 352   O  ALA A 379           
SHEET    4 AA3 5 LEU A 308  ARG A 311  1  N  ILE A 310   O  ARG A 349           
SHEET    5 AA3 5 VAL A 274  VAL A 277  1  N  VAL A 274   O  ILE A 309           
SHEET    1 AA4 2 THR A 335  GLU A 336  0                                        
SHEET    2 AA4 2 LYS A 342  LEU A 343 -1  O  LEU A 343   N  THR A 335           
SHEET    1 AA5 2 SER A 431  ARG A 434  0                                        
SHEET    2 AA5 2 PHE A 440  LEU A 443 -1  O  VAL A 441   N  HIS A 433           
SHEET    1 AA6 7 LEU B 409  ASN B 412  0                                        
SHEET    2 AA6 7 CYS B 397  THR B 406 -1  N  VAL B 404   O  ILE B 411           
SHEET    3 AA6 7 THR B  30  CYS B  39 -1  N  TYR B  34   O  TYR B 403           
SHEET    4 AA6 7 PHE B 132  ASN B 136 -1  O  VAL B 134   N  SER B  35           
SHEET    5 AA6 7 ILE B 114  ALA B 118 -1  N  GLU B 115   O  GLU B 135           
SHEET    6 AA6 7 HIS B 459  LYS B 463 -1  O  HIS B 459   N  ALA B 118           
SHEET    7 AA6 7 LYS B 466  VAL B 467 -1  O  LYS B 466   N  LYS B 463           
SHEET    1 AA7 2 GLU B  56  VAL B  58  0                                        
SHEET    2 AA7 2 VAL B 124  PRO B 126 -1  O  ILE B 125   N  THR B  57           
SHEET    1 AA8 5 LEU B 190  ASP B 192  0                                        
SHEET    2 AA8 5 ILE B 378  SER B 382  1  O  PHE B 380   N  HIS B 191           
SHEET    3 AA8 5 LEU B 348  GLN B 352  1  N  GLN B 352   O  ALA B 379           
SHEET    4 AA8 5 LEU B 308  ARG B 311  1  N  ILE B 310   O  ARG B 349           
SHEET    5 AA8 5 VAL B 274  VAL B 277  1  N  VAL B 274   O  ILE B 309           
SHEET    1 AA9 2 THR B 335  GLU B 336  0                                        
SHEET    2 AA9 2 LYS B 342  LEU B 343 -1  O  LEU B 343   N  THR B 335           
SHEET    1 AB1 2 SER B 431  ARG B 434  0                                        
SHEET    2 AB1 2 PHE B 440  LEU B 443 -1  O  VAL B 441   N  HIS B 433           
SITE     1 AC1 11 HIS A 191  PHE A 193  ARG A 196  ASP A 219                    
SITE     2 AC1 11 SER A 241  VAL A 242  ALA A 244  SER A 275                    
SITE     3 AC1 11 ARG A 311  ASP B  16  TYR B  18                               
SITE     1 AC2 12 ASP A  16  TYR A  18  HIS B 191  PHE B 193                    
SITE     2 AC2 12 ARG B 196  ASP B 219  SER B 241  VAL B 242                    
SITE     3 AC2 12 ALA B 244  SER B 275  ARG B 311  HOH B 612                    
CRYST1   61.226  106.856   82.881  90.00  96.83  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      0.016333  0.000000  0.001956        0.00000                         
SCALE2      0.000000  0.009358  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012152        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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