GenomeNet

Database: PDB
Entry: 4ZWC
LinkDB: 4ZWC
Original site: 4ZWC 
HEADER    TRANSPORT PROTEIN                       19-MAY-15   4ZWC              
TITLE     CRYSTAL STRUCTURE OF MALTOSE-BOUND HUMAN GLUT3 IN THE OUTWARD-OPEN    
TITLE    2 CONFORMATION AT 2.6 ANGSTROM                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SOLUTE CARRIER FAMILY 2, FACILITATED GLUCOSE TRANSPORTER   
COMPND   3 MEMBER 3;                                                            
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: GLUCOSE TRANSPORTER TYPE 3,BRAIN,GLUT-3;                    
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SLC2A3, GLUT3;                                                 
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    TRANSPORTER, TRANSPORT PROTEIN                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.DENG,P.C.SUN,C.Y.YAN,N.YAN                                          
REVDAT   3   21-OCT-15 4ZWC    1       JRNL                                     
REVDAT   2   29-JUL-15 4ZWC    1       JRNL                                     
REVDAT   1   22-JUL-15 4ZWC    0                                                
JRNL        AUTH   D.DENG,P.C.SUN,C.Y.YAN,M.KE,X.JIANG,L.XIONG,W.REN,K.HIRATA,  
JRNL        AUTH 2 M.YAMAMOTO,S.FAN,N.YAN                                       
JRNL        TITL   MOLECULAR BASIS OF LIGAND RECOGNITION AND TRANSPORT BY       
JRNL        TITL 2 GLUCOSE TRANSPORTERS                                         
JRNL        REF    NATURE                        V. 526   391 2015              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   26176916                                                     
JRNL        DOI    10.1038/NATURE14655                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 49536                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2477                            
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 31.6998 -  6.8006    0.95     2686   137  0.1523 0.1804        
REMARK   3     2  6.8006 -  5.4065    0.97     2723   139  0.2123 0.2426        
REMARK   3     3  5.4065 -  4.7257    0.96     2681   129  0.2133 0.2310        
REMARK   3     4  4.7257 -  4.2947    0.57     1598    76  0.2424 0.3106        
REMARK   3     5  4.2947 -  3.9875    0.97     2671   147  0.2158 0.2544        
REMARK   3     6  3.9875 -  3.7528    0.97     2671   164  0.2148 0.2472        
REMARK   3     7  3.7528 -  3.5651    0.97     2665   137  0.2229 0.2475        
REMARK   3     8  3.5651 -  3.4101    0.97     2686   149  0.2157 0.2571        
REMARK   3     9  3.4101 -  3.2790    0.97     2660   154  0.2222 0.2746        
REMARK   3    10  3.2790 -  3.1660    0.98     2727   130  0.2296 0.2616        
REMARK   3    11  3.1660 -  3.0671    0.97     2660   152  0.2370 0.2906        
REMARK   3    12  3.0671 -  2.9794    0.97     2678   149  0.2327 0.3062        
REMARK   3    13  2.9794 -  2.9011    0.97     2665   144  0.2256 0.2481        
REMARK   3    14  2.9011 -  2.8303    0.98     2681   155  0.2317 0.2480        
REMARK   3    15  2.8303 -  2.7660    0.98     2737   112  0.2301 0.2630        
REMARK   3    16  2.7660 -  2.7072    0.98     2686   142  0.2368 0.2498        
REMARK   3    17  2.7072 -  2.6531    0.97     2696   141  0.2440 0.2904        
REMARK   3    18  2.6531 -  2.6030    0.90     2488   120  0.2490 0.2852        
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)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.980           
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      :  0.010           7516                                  
REMARK   3   ANGLE     :  1.260          10167                                  
REMARK   3   CHIRALITY :  0.052           1197                                  
REMARK   3   PLANARITY :  0.007           1262                                  
REMARK   3   DIHEDRAL  : 16.336           2727                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -60.0423  35.6376  -9.4388              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3760 T22:   0.3757                                     
REMARK   3      T33:   0.3728 T12:  -0.0113                                     
REMARK   3      T13:   0.0127 T23:  -0.0153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1845 L22:   0.3947                                     
REMARK   3      L33:   0.3374 L12:  -0.2030                                     
REMARK   3      L13:   0.1715 L23:  -0.3296                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0108 S12:   0.0266 S13:  -0.0055                       
REMARK   3      S21:  -0.0311 S22:  -0.0000 S23:   0.0398                       
REMARK   3      S31:   0.0147 S32:   0.0143 S33:  -0.0223                       
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 4ZWC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000210002.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL32XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49602                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.14300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
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: 4ZW9                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 34% PEG 400, 400 MM (NH4)2HPO4, 50 MM    
REMARK 280  MALTOSE, 100 MM ADA, PH 6.9, LIPIDIC CUBIC PHASE, TEMPERATURE       
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       60.94000            
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                                                    
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 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   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     ASP A    -8                                                      
REMARK 465     GLU A    -7                                                      
REMARK 465     VAL A    -6                                                      
REMARK 465     ASP A    -5                                                      
REMARK 465     ALA A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     GLY A   471                                                      
REMARK 465     ALA A   472                                                      
REMARK 465     ASP A   473                                                      
REMARK 465     ARG A   474                                                      
REMARK 465     SER A   475                                                      
REMARK 465     GLY A   476                                                      
REMARK 465     LYS A   477                                                      
REMARK 465     ASP A   478                                                      
REMARK 465     GLY A   479                                                      
REMARK 465     VAL A   480                                                      
REMARK 465     MET A   481                                                      
REMARK 465     GLU A   482                                                      
REMARK 465     MET A   483                                                      
REMARK 465     ASN A   484                                                      
REMARK 465     SER A   485                                                      
REMARK 465     ILE A   486                                                      
REMARK 465     GLU A   487                                                      
REMARK 465     PRO A   488                                                      
REMARK 465     ALA A   489                                                      
REMARK 465     LYS A   490                                                      
REMARK 465     GLU A   491                                                      
REMARK 465     THR A   492                                                      
REMARK 465     THR A   493                                                      
REMARK 465     THR A   494                                                      
REMARK 465     ASN A   495                                                      
REMARK 465     VAL A   496                                                      
REMARK 465     MET B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     ASP B    -8                                                      
REMARK 465     GLU B    -7                                                      
REMARK 465     VAL B    -6                                                      
REMARK 465     ASP B    -5                                                      
REMARK 465     ALA B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     GLY B   471                                                      
REMARK 465     ALA B   472                                                      
REMARK 465     ASP B   473                                                      
REMARK 465     ARG B   474                                                      
REMARK 465     SER B   475                                                      
REMARK 465     GLY B   476                                                      
REMARK 465     LYS B   477                                                      
REMARK 465     ASP B   478                                                      
REMARK 465     GLY B   479                                                      
REMARK 465     VAL B   480                                                      
REMARK 465     MET B   481                                                      
REMARK 465     GLU B   482                                                      
REMARK 465     MET B   483                                                      
REMARK 465     ASN B   484                                                      
REMARK 465     SER B   485                                                      
REMARK 465     ILE B   486                                                      
REMARK 465     GLU B   487                                                      
REMARK 465     PRO B   488                                                      
REMARK 465     ALA B   489                                                      
REMARK 465     LYS B   490                                                      
REMARK 465     GLU B   491                                                      
REMARK 465     THR B   492                                                      
REMARK 465     THR B   493                                                      
REMARK 465     THR B   494                                                      
REMARK 465     ASN B   495                                                      
REMARK 465     VAL B   496                                                      
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     THR A   3    OG1  CG2                                            
REMARK 470     THR B   3    OG1  CG2                                            
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    LYS A 115       53.90     39.36                                   
REMARK 500    ILE A 177      -91.44   -102.12                                   
REMARK 500    PRO B  34       31.97    -85.79                                   
REMARK 500    LYS B  49      -96.76    -92.53                                   
REMARK 500    ASN B  51     -162.30   -121.01                                   
REMARK 500    ILE B 177      -73.27   -124.63                                   
REMARK 500    GLU B 218       78.30   -108.63                                   
REMARK 500    LYS B 356      -60.20    -28.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLN A  254     VAL A  255                 -146.70                    
REMARK 500 ASP B  357     ASN B  358                  148.64                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MAL A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MAL B 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ZW9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZWB   RELATED DB: PDB                                   
DBREF  4ZWC A    1   496  UNP    P11169   GTR3_HUMAN       1    496             
DBREF  4ZWC B    1   496  UNP    P11169   GTR3_HUMAN       1    496             
SEQADV 4ZWC MET A  -21  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS A  -20  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS A  -19  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS A  -18  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS A  -17  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS A  -16  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS A  -15  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS A  -14  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS A  -13  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS A  -12  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS A  -11  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC SER A  -10  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC GLY A   -9  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC ASP A   -8  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC GLU A   -7  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC VAL A   -6  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC ASP A   -5  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC ALA A   -4  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC GLY A   -3  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC SER A   -2  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC GLY A   -1  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS A    0  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC THR A   43  UNP  P11169    ASN    43 ENGINEERED MUTATION            
SEQADV 4ZWC MET B  -21  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS B  -20  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS B  -19  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS B  -18  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS B  -17  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS B  -16  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS B  -15  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS B  -14  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS B  -13  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS B  -12  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS B  -11  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC SER B  -10  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC GLY B   -9  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC ASP B   -8  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC GLU B   -7  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC VAL B   -6  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC ASP B   -5  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC ALA B   -4  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC GLY B   -3  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC SER B   -2  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC GLY B   -1  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC HIS B    0  UNP  P11169              EXPRESSION TAG                 
SEQADV 4ZWC THR B   43  UNP  P11169    ASN    43 ENGINEERED MUTATION            
SEQRES   1 A  518  MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER GLY          
SEQRES   2 A  518  ASP GLU VAL ASP ALA GLY SER GLY HIS MET GLY THR GLN          
SEQRES   3 A  518  LYS VAL THR PRO ALA LEU ILE PHE ALA ILE THR VAL ALA          
SEQRES   4 A  518  THR ILE GLY SER PHE GLN PHE GLY TYR ASN THR GLY VAL          
SEQRES   5 A  518  ILE ASN ALA PRO GLU LYS ILE ILE LYS GLU PHE ILE THR          
SEQRES   6 A  518  LYS THR LEU THR ASP LYS GLY ASN ALA PRO PRO SER GLU          
SEQRES   7 A  518  VAL LEU LEU THR SER LEU TRP SER LEU SER VAL ALA ILE          
SEQRES   8 A  518  PHE SER VAL GLY GLY MET ILE GLY SER PHE SER VAL GLY          
SEQRES   9 A  518  LEU PHE VAL ASN ARG PHE GLY ARG ARG ASN SER MET LEU          
SEQRES  10 A  518  ILE VAL ASN LEU LEU ALA VAL THR GLY GLY CYS PHE MET          
SEQRES  11 A  518  GLY LEU CYS LYS VAL ALA LYS SER VAL GLU MET LEU ILE          
SEQRES  12 A  518  LEU GLY ARG LEU VAL ILE GLY LEU PHE CYS GLY LEU CYS          
SEQRES  13 A  518  THR GLY PHE VAL PRO MET TYR ILE GLY GLU ILE SER PRO          
SEQRES  14 A  518  THR ALA LEU ARG GLY ALA PHE GLY THR LEU ASN GLN LEU          
SEQRES  15 A  518  GLY ILE VAL VAL GLY ILE LEU VAL ALA GLN ILE PHE GLY          
SEQRES  16 A  518  LEU GLU PHE ILE LEU GLY SER GLU GLU LEU TRP PRO LEU          
SEQRES  17 A  518  LEU LEU GLY PHE THR ILE LEU PRO ALA ILE LEU GLN SER          
SEQRES  18 A  518  ALA ALA LEU PRO PHE CYS PRO GLU SER PRO ARG PHE LEU          
SEQRES  19 A  518  LEU ILE ASN ARG LYS GLU GLU GLU ASN ALA LYS GLN ILE          
SEQRES  20 A  518  LEU GLN ARG LEU TRP GLY THR GLN ASP VAL SER GLN ASP          
SEQRES  21 A  518  ILE GLN GLU MET LYS ASP GLU SER ALA ARG MET SER GLN          
SEQRES  22 A  518  GLU LYS GLN VAL THR VAL LEU GLU LEU PHE ARG VAL SER          
SEQRES  23 A  518  SER TYR ARG GLN PRO ILE ILE ILE SER ILE VAL LEU GLN          
SEQRES  24 A  518  LEU SER GLN GLN LEU SER GLY ILE ASN ALA VAL PHE TYR          
SEQRES  25 A  518  TYR SER THR GLY ILE PHE LYS ASP ALA GLY VAL GLN GLU          
SEQRES  26 A  518  PRO ILE TYR ALA THR ILE GLY ALA GLY VAL VAL ASN THR          
SEQRES  27 A  518  ILE PHE THR VAL VAL SER LEU PHE LEU VAL GLU ARG ALA          
SEQRES  28 A  518  GLY ARG ARG THR LEU HIS MET ILE GLY LEU GLY GLY MET          
SEQRES  29 A  518  ALA PHE CYS SER THR LEU MET THR VAL SER LEU LEU LEU          
SEQRES  30 A  518  LYS ASP ASN TYR ASN GLY MET SER PHE VAL CYS ILE GLY          
SEQRES  31 A  518  ALA ILE LEU VAL PHE VAL ALA PHE PHE GLU ILE GLY PRO          
SEQRES  32 A  518  GLY PRO ILE PRO TRP PHE ILE VAL ALA GLU LEU PHE SER          
SEQRES  33 A  518  GLN GLY PRO ARG PRO ALA ALA MET ALA VAL ALA GLY CYS          
SEQRES  34 A  518  SER ASN TRP THR SER ASN PHE LEU VAL GLY LEU LEU PHE          
SEQRES  35 A  518  PRO SER ALA ALA HIS TYR LEU GLY ALA TYR VAL PHE ILE          
SEQRES  36 A  518  ILE PHE THR GLY PHE LEU ILE THR PHE LEU ALA PHE THR          
SEQRES  37 A  518  PHE PHE LYS VAL PRO GLU THR ARG GLY ARG THR PHE GLU          
SEQRES  38 A  518  ASP ILE THR ARG ALA PHE GLU GLY GLN ALA HIS GLY ALA          
SEQRES  39 A  518  ASP ARG SER GLY LYS ASP GLY VAL MET GLU MET ASN SER          
SEQRES  40 A  518  ILE GLU PRO ALA LYS GLU THR THR THR ASN VAL                  
SEQRES   1 B  518  MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER GLY          
SEQRES   2 B  518  ASP GLU VAL ASP ALA GLY SER GLY HIS MET GLY THR GLN          
SEQRES   3 B  518  LYS VAL THR PRO ALA LEU ILE PHE ALA ILE THR VAL ALA          
SEQRES   4 B  518  THR ILE GLY SER PHE GLN PHE GLY TYR ASN THR GLY VAL          
SEQRES   5 B  518  ILE ASN ALA PRO GLU LYS ILE ILE LYS GLU PHE ILE THR          
SEQRES   6 B  518  LYS THR LEU THR ASP LYS GLY ASN ALA PRO PRO SER GLU          
SEQRES   7 B  518  VAL LEU LEU THR SER LEU TRP SER LEU SER VAL ALA ILE          
SEQRES   8 B  518  PHE SER VAL GLY GLY MET ILE GLY SER PHE SER VAL GLY          
SEQRES   9 B  518  LEU PHE VAL ASN ARG PHE GLY ARG ARG ASN SER MET LEU          
SEQRES  10 B  518  ILE VAL ASN LEU LEU ALA VAL THR GLY GLY CYS PHE MET          
SEQRES  11 B  518  GLY LEU CYS LYS VAL ALA LYS SER VAL GLU MET LEU ILE          
SEQRES  12 B  518  LEU GLY ARG LEU VAL ILE GLY LEU PHE CYS GLY LEU CYS          
SEQRES  13 B  518  THR GLY PHE VAL PRO MET TYR ILE GLY GLU ILE SER PRO          
SEQRES  14 B  518  THR ALA LEU ARG GLY ALA PHE GLY THR LEU ASN GLN LEU          
SEQRES  15 B  518  GLY ILE VAL VAL GLY ILE LEU VAL ALA GLN ILE PHE GLY          
SEQRES  16 B  518  LEU GLU PHE ILE LEU GLY SER GLU GLU LEU TRP PRO LEU          
SEQRES  17 B  518  LEU LEU GLY PHE THR ILE LEU PRO ALA ILE LEU GLN SER          
SEQRES  18 B  518  ALA ALA LEU PRO PHE CYS PRO GLU SER PRO ARG PHE LEU          
SEQRES  19 B  518  LEU ILE ASN ARG LYS GLU GLU GLU ASN ALA LYS GLN ILE          
SEQRES  20 B  518  LEU GLN ARG LEU TRP GLY THR GLN ASP VAL SER GLN ASP          
SEQRES  21 B  518  ILE GLN GLU MET LYS ASP GLU SER ALA ARG MET SER GLN          
SEQRES  22 B  518  GLU LYS GLN VAL THR VAL LEU GLU LEU PHE ARG VAL SER          
SEQRES  23 B  518  SER TYR ARG GLN PRO ILE ILE ILE SER ILE VAL LEU GLN          
SEQRES  24 B  518  LEU SER GLN GLN LEU SER GLY ILE ASN ALA VAL PHE TYR          
SEQRES  25 B  518  TYR SER THR GLY ILE PHE LYS ASP ALA GLY VAL GLN GLU          
SEQRES  26 B  518  PRO ILE TYR ALA THR ILE GLY ALA GLY VAL VAL ASN THR          
SEQRES  27 B  518  ILE PHE THR VAL VAL SER LEU PHE LEU VAL GLU ARG ALA          
SEQRES  28 B  518  GLY ARG ARG THR LEU HIS MET ILE GLY LEU GLY GLY MET          
SEQRES  29 B  518  ALA PHE CYS SER THR LEU MET THR VAL SER LEU LEU LEU          
SEQRES  30 B  518  LYS ASP ASN TYR ASN GLY MET SER PHE VAL CYS ILE GLY          
SEQRES  31 B  518  ALA ILE LEU VAL PHE VAL ALA PHE PHE GLU ILE GLY PRO          
SEQRES  32 B  518  GLY PRO ILE PRO TRP PHE ILE VAL ALA GLU LEU PHE SER          
SEQRES  33 B  518  GLN GLY PRO ARG PRO ALA ALA MET ALA VAL ALA GLY CYS          
SEQRES  34 B  518  SER ASN TRP THR SER ASN PHE LEU VAL GLY LEU LEU PHE          
SEQRES  35 B  518  PRO SER ALA ALA HIS TYR LEU GLY ALA TYR VAL PHE ILE          
SEQRES  36 B  518  ILE PHE THR GLY PHE LEU ILE THR PHE LEU ALA PHE THR          
SEQRES  37 B  518  PHE PHE LYS VAL PRO GLU THR ARG GLY ARG THR PHE GLU          
SEQRES  38 B  518  ASP ILE THR ARG ALA PHE GLU GLY GLN ALA HIS GLY ALA          
SEQRES  39 B  518  ASP ARG SER GLY LYS ASP GLY VAL MET GLU MET ASN SER          
SEQRES  40 B  518  ILE GLU PRO ALA LYS GLU THR THR THR ASN VAL                  
HET    OLC  A 501      25                                                       
HET    OLC  A 502      25                                                       
HET    MAL  A 503      23                                                       
HET    OLC  B 501      25                                                       
HET    MAL  B 502      23                                                       
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     MAL MALTOSE                                                          
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   3  OLC    3(C21 H40 O4)                                                
FORMUL   5  MAL    2(C12 H22 O11)                                               
FORMUL   8  HOH   *52(H2 O)                                                     
HELIX    1 AA1 THR A    7  THR A   18  1                                  12    
HELIX    2 AA2 THR A   18  VAL A   30  1                                  13    
HELIX    3 AA3 PRO A   34  LYS A   49  1                                  16    
HELIX    4 AA4 SER A   55  SER A   80  1                                  26    
HELIX    5 AA5 VAL A   81  LEU A   83  5                                   3    
HELIX    6 AA6 PHE A   84  GLY A   89  1                                   6    
HELIX    7 AA7 GLY A   89  CYS A  111  1                                  23    
HELIX    8 AA8 SER A  116  SER A  146  1                                  31    
HELIX    9 AA9 PRO A  147  ALA A  149  5                                   3    
HELIX   10 AB1 LEU A  150  GLY A  173  1                                  24    
HELIX   11 AB2 LEU A  183  PHE A  190  1                                   8    
HELIX   12 AB3 THR A  191  LEU A  202  1                                  12    
HELIX   13 AB4 PRO A  203  CYS A  205  5                                   3    
HELIX   14 AB5 SER A  208  ASN A  215  1                                   8    
HELIX   15 AB6 GLU A  218  GLY A  231  1                                  14    
HELIX   16 AB7 VAL A  235  GLN A  251  1                                  17    
HELIX   17 AB8 THR A  256  VAL A  263  1                                   8    
HELIX   18 AB9 VAL A  263  LEU A  282  1                                  20    
HELIX   19 AC1 GLY A  284  ALA A  299  1                                  16    
HELIX   20 AC2 PRO A  304  GLY A  330  1                                  27    
HELIX   21 AC3 GLY A  330  LEU A  355  1                                  26    
HELIX   22 AC4 GLY A  361  GLY A  380  1                                  20    
HELIX   23 AC5 PRO A  383  PHE A  393  1                                  11    
HELIX   24 AC6 PRO A  397  GLY A  428  1                                  32    
HELIX   25 AC7 TYR A  430  VAL A  450  1                                  21    
HELIX   26 AC8 THR A  457  HIS A  470  1                                  14    
HELIX   27 AC9 THR B    7  THR B   18  1                                  12    
HELIX   28 AD1 THR B   18  VAL B   30  1                                  13    
HELIX   29 AD2 PRO B   34  ASP B   48  1                                  15    
HELIX   30 AD3 SER B   55  SER B   80  1                                  26    
HELIX   31 AD4 VAL B   81  LEU B   83  5                                   3    
HELIX   32 AD5 PHE B   84  GLY B   89  1                                   6    
HELIX   33 AD6 GLY B   89  VAL B   97  1                                   9    
HELIX   34 AD7 VAL B   97  LEU B  110  1                                  14    
HELIX   35 AD8 SER B  116  SER B  146  1                                  31    
HELIX   36 AD9 PRO B  147  ALA B  149  5                                   3    
HELIX   37 AE1 LEU B  150  GLY B  173  1                                  24    
HELIX   38 AE2 LEU B  183  PHE B  190  1                                   8    
HELIX   39 AE3 THR B  191  LEU B  202  1                                  12    
HELIX   40 AE4 PRO B  203  CYS B  205  5                                   3    
HELIX   41 AE5 SER B  208  LYS B  217  1                                  10    
HELIX   42 AE6 GLU B  218  TRP B  230  1                                  13    
HELIX   43 AE7 VAL B  235  GLU B  252  1                                  18    
HELIX   44 AE8 THR B  256  PHE B  261  1                                   6    
HELIX   45 AE9 VAL B  263  LEU B  282  1                                  20    
HELIX   46 AF1 GLY B  284  GLY B  300  1                                  17    
HELIX   47 AF2 PRO B  304  PHE B  324  1                                  21    
HELIX   48 AF3 GLY B  330  LEU B  355  1                                  26    
HELIX   49 AF4 GLY B  361  GLY B  380  1                                  20    
HELIX   50 AF5 GLY B  382  PHE B  393  1                                  12    
HELIX   51 AF6 PRO B  397  GLY B  428  1                                  32    
HELIX   52 AF7 TYR B  430  VAL B  450  1                                  21    
HELIX   53 AF8 THR B  457  ALA B  469  1                                  13    
SITE     1 AC1  2 VAL A 320  ARG A 328                                          
SITE     1 AC2 11 ARG A 332  PHE A 447  PHE A 448  PRO A 451                    
SITE     2 AC2 11 GLU A 452  ARG A 456  ASP A 460  ILE A 461                    
SITE     3 AC2 11 ALA A 464  PHE A 465  GLN A 468                               
SITE     1 AC3 10 THR A  28  GLN A 159  ILE A 162  GLN A 280                    
SITE     2 AC3 10 GLN A 281  PHE A 289  ASN A 315  GLU A 378                    
SITE     3 AC3 10 TRP A 386  ASN A 413                                          
SITE     1 AC4  3 ILE B 317  PHE B 324  ARG B 328                               
SITE     1 AC5  9 THR B  28  GLN B 159  GLN B 280  GLN B 281                    
SITE     2 AC5  9 PHE B 289  PHE B 377  GLU B 378  TRP B 386                    
SITE     3 AC5  9 ASN B 413                                                     
CRYST1   78.109  121.880   96.078  90.00 108.14  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      0.012803  0.000000  0.004195        0.00000                         
SCALE2      0.000000  0.008205  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010953        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system