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Database: PDB
Entry: 4YBQ
LinkDB: 4YBQ
Original site: 4YBQ 
HEADER    TRANSPORT PROTEIN/IMMUNE SYSTEM         19-FEB-15   4YBQ              
TITLE     RAT GLUT5 WITH FV IN THE OUTWARD-OPEN FORM                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SOLUTE CARRIER FAMILY 2, FACILITATED GLUCOSE TRANSPORTER   
COMPND   3 MEMBER 5;                                                            
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: FRUCTOSE TRANSPORTER,GLUCOSE TRANSPORTER TYPE 5,SMALL       
COMPND   6 INTESTINE,GLUT-5;                                                    
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: ANTIBODY FV FRAGMENT LIGHT CHAIN;                          
COMPND  11 CHAIN: C, E;                                                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: ANTIBODY FV FRAGMENT HEAVY CHAIN;                          
COMPND  15 CHAIN: D, F;                                                         
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: SLC2A5, GLUT5;                                                 
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_TAXID: 10090;                                               
SOURCE  12 EXPRESSION_SYSTEM: BREVIBACILLUS CHOSHINENSIS;                       
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 54911;                                      
SOURCE  14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  17 ORGANISM_TAXID: 10090;                                               
SOURCE  18 EXPRESSION_SYSTEM: BREVIBACILLUS CHOSHINENSIS;                       
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 54911;                                      
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    SUGAR TRANSPORTER, MAJOR FACILITATOR SUPERFAMILY, TRANSPORT PROTEIN-  
KEYWDS   2 IMMUNE SYSTEM COMPLEX                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.NOMURA,T.SHIMAMURA,S.IWATA                                          
REVDAT   2   28-OCT-15 4YBQ    1       JRNL                                     
REVDAT   1   07-OCT-15 4YBQ    0                                                
JRNL        AUTH   N.NOMURA,G.VERDON,H.J.KANG,T.SHIMAMURA,Y.NOMURA,Y.SONODA,    
JRNL        AUTH 2 S.A.HUSSIEN,A.A.QURESHI,M.COINCON,Y.SATO,H.ABE,              
JRNL        AUTH 3 Y.NAKADA-NAKURA,T.HINO,T.ARAKAWA,O.KUSANO-ARAI,H.IWANARI,    
JRNL        AUTH 4 T.MURATA,T.KOBAYASHI,T.HAMAKUBO,M.KASAHARA,S.IWATA,D.DREW    
JRNL        TITL   STRUCTURE AND MECHANISM OF THE MAMMALIAN FRUCTOSE            
JRNL        TITL 2 TRANSPORTER GLUT5                                            
JRNL        REF    NATURE                        V. 526   397 2015              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   26416735                                                     
JRNL        DOI    10.1038/NATURE14909                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.27 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) : 3.27                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.49                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 37289                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.244                           
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.940                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1842                            
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 36.4933 -  7.6669    0.99     2748   137  0.2355 0.2744        
REMARK   3     2  7.6669 -  6.0947    1.00     2781   132  0.2759 0.3267        
REMARK   3     3  6.0947 -  5.3270    1.00     2741   132  0.2673 0.3234        
REMARK   3     4  5.3270 -  4.8411    1.00     2723   142  0.2273 0.2793        
REMARK   3     5  4.8411 -  4.4948    1.00     2725   140  0.1955 0.2323        
REMARK   3     6  4.4948 -  4.2302    1.00     2719   147  0.1902 0.2440        
REMARK   3     7  4.2302 -  4.0186    1.00     2734   131  0.2147 0.2494        
REMARK   3     8  4.0186 -  3.8439    1.00     2709   148  0.2282 0.2810        
REMARK   3     9  3.8439 -  3.6961    1.00     2721   157  0.2496 0.3070        
REMARK   3    10  3.6961 -  3.5686    1.00     2720   149  0.2758 0.3267        
REMARK   3    11  3.5686 -  3.4571    1.00     2711   138  0.2983 0.3439        
REMARK   3    12  3.4571 -  3.3584    1.00     2692   145  0.3147 0.3826        
REMARK   3    13  3.3584 -  3.2700    1.00     2723   144  0.3441 0.3888        
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)     : 0.460            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.440           
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      :  0.004          10901                                  
REMARK   3   ANGLE     :  0.972          14793                                  
REMARK   3   CHIRALITY :  0.036           1716                                  
REMARK   3   PLANARITY :  0.005           1840                                  
REMARK   3   DIHEDRAL  : 11.899           3862                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN 'A' AND RESID 7 THROUGH 480)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  28.0605 -19.9080 126.3221              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4314 T22:   0.8537                                     
REMARK   3      T33:   0.7050 T12:  -0.1071                                     
REMARK   3      T13:  -0.0255 T23:  -0.0295                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9343 L22:   2.0846                                     
REMARK   3      L33:   3.2444 L12:  -0.3183                                     
REMARK   3      L13:  -0.2816 L23:   0.8445                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1161 S12:   0.2265 S13:  -0.4945                       
REMARK   3      S21:   0.1976 S22:  -0.1662 S23:   0.2305                       
REMARK   3      S31:   0.5457 S32:  -0.6965 S33:  -0.0252                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN 'B' AND RESID 7 THROUGH 480)                    
REMARK   3    ORIGIN FOR THE GROUP (A): 117.7244  -2.7865 167.1603              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3735 T22:   0.7396                                     
REMARK   3      T33:   0.7415 T12:  -0.0587                                     
REMARK   3      T13:   0.0181 T23:  -0.0248                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2263 L22:   2.1193                                     
REMARK   3      L33:   5.3260 L12:  -0.2260                                     
REMARK   3      L13:   1.3721 L23:  -0.4720                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3277 S12:  -0.4261 S13:  -0.0451                       
REMARK   3      S21:   0.1361 S22:  -0.0349 S23:  -0.3905                       
REMARK   3      S31:   0.4573 S32:   0.1225 S33:  -0.1308                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN 'C' AND RESID 1 THROUGH 115)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  76.2839  17.6763 148.7588              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5592 T22:   0.9948                                     
REMARK   3      T33:   1.3935 T12:   0.0098                                     
REMARK   3      T13:  -0.0542 T23:  -0.2512                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6862 L22:   4.6813                                     
REMARK   3      L33:   4.8220 L12:  -0.1299                                     
REMARK   3      L13:  -0.1126 L23:  -1.7034                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2405 S12:   0.3435 S13:   0.2002                       
REMARK   3      S21:  -0.2103 S22:  -0.2139 S23:   1.7358                       
REMARK   3      S31:  -0.1903 S32:   0.1273 S33:  -0.0646                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN 'D' AND RESID 1 THROUGH 120)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  90.0112  31.6695 141.2780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7237 T22:   0.9174                                     
REMARK   3      T33:   1.0529 T12:  -0.0986                                     
REMARK   3      T13:  -0.0492 T23:   0.1060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3167 L22:   7.5089                                     
REMARK   3      L33:   4.2423 L12:  -0.8313                                     
REMARK   3      L13:   4.0922 L23:  -1.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9287 S12:   0.1119 S13:   1.4743                       
REMARK   3      S21:  -0.7676 S22:   0.0762 S23:   0.2480                       
REMARK   3      S31:  -0.4639 S32:  -1.1122 S33:   0.7393                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN 'E' AND RESID 1 THROUGH 115)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  69.2573   7.0419 124.0377              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6896 T22:   2.0286                                     
REMARK   3      T33:   1.1606 T12:  -0.2224                                     
REMARK   3      T13:  -0.0082 T23:   0.2989                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2751 L22:   5.7712                                     
REMARK   3      L33:   0.1639 L12:   0.7922                                     
REMARK   3      L13:   0.5895 L23:   0.0061                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2454 S12:  -1.2734 S13:  -0.4212                       
REMARK   3      S21:   0.2449 S22:  -0.6911 S23:  -0.1944                       
REMARK   3      S31:  -0.0598 S32:   1.7689 S33:   0.1702                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN 'F' AND RESID 2 THROUGH 120)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  55.4399  22.0430 119.1056              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8294 T22:   0.8803                                     
REMARK   3      T33:   1.8789 T12:   0.0766                                     
REMARK   3      T13:   0.3905 T23:   0.1677                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1754 L22:   7.3396                                     
REMARK   3      L33:   4.3858 L12:   4.0131                                     
REMARK   3      L13:  -1.6194 L23:   0.0531                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.0633 S12:   1.3860 S13:   3.7984                       
REMARK   3      S21:  -0.7356 S22:   0.3837 S23:   1.5656                       
REMARK   3      S31:  -1.2390 S32:  -0.8932 S33:  -0.5661                       
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 4YBQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000207146.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-NOV-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38017                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.270                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 13.00                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 1.2200                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 3O7Q                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 33-35% PEG400, 0.12 M CACL2, 0.1 M       
REMARK 280  TRIS-HCL PH8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       75.77050            
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, F                               
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D                               
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     GLU A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     ASN A    39                                                      
REMARK 465     SER A    40                                                      
REMARK 465     PRO A    41                                                      
REMARK 465     SER A    42                                                      
REMARK 465     GLU A    43                                                      
REMARK 465     PHE A    44                                                      
REMARK 465     MET A    45                                                      
REMARK 465     GLN A    46                                                      
REMARK 465     GLN A    47                                                      
REMARK 465     PHE A    48                                                      
REMARK 465     TYR A    49                                                      
REMARK 465     TYR A    50                                                      
REMARK 465     ASP A    51                                                      
REMARK 465     THR A    52                                                      
REMARK 465     TYR A    53                                                      
REMARK 465     TYR A    54                                                      
REMARK 465     ASP A    55                                                      
REMARK 465     ARG A    56                                                      
REMARK 465     ASN A    57                                                      
REMARK 465     LYS A    58                                                      
REMARK 465     GLU A    59                                                      
REMARK 465     ASN A    60                                                      
REMARK 465     SER A   481                                                      
REMARK 465     ASP A   482                                                      
REMARK 465     VAL A   483                                                      
REMARK 465     TYR A   484                                                      
REMARK 465     PRO A   485                                                      
REMARK 465     GLU A   486                                                      
REMARK 465     LYS A   487                                                      
REMARK 465     GLU A   488                                                      
REMARK 465     GLU A   489                                                      
REMARK 465     LYS A   490                                                      
REMARK 465     GLU A   491                                                      
REMARK 465     LEU A   492                                                      
REMARK 465     ASN A   493                                                      
REMARK 465     ASP A   494                                                      
REMARK 465     LEU A   495                                                      
REMARK 465     PRO A   496                                                      
REMARK 465     PRO A   497                                                      
REMARK 465     ALA A   498                                                      
REMARK 465     THR A   499                                                      
REMARK 465     ARG A   500                                                      
REMARK 465     GLU A   501                                                      
REMARK 465     GLN A   502                                                      
REMARK 465     GLU A   503                                                      
REMARK 465     ASN A   504                                                      
REMARK 465     LEU A   505                                                      
REMARK 465     TYR A   506                                                      
REMARK 465     PHE A   507                                                      
REMARK 465     GLN A   508                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     GLN B     6                                                      
REMARK 465     MET B    45                                                      
REMARK 465     GLN B    46                                                      
REMARK 465     GLN B    47                                                      
REMARK 465     PHE B    48                                                      
REMARK 465     TYR B    49                                                      
REMARK 465     TYR B    50                                                      
REMARK 465     ASP B    51                                                      
REMARK 465     THR B    52                                                      
REMARK 465     TYR B    53                                                      
REMARK 465     TYR B    54                                                      
REMARK 465     ASP B    55                                                      
REMARK 465     ARG B    56                                                      
REMARK 465     SER B   481                                                      
REMARK 465     ASP B   482                                                      
REMARK 465     VAL B   483                                                      
REMARK 465     TYR B   484                                                      
REMARK 465     PRO B   485                                                      
REMARK 465     GLU B   486                                                      
REMARK 465     LYS B   487                                                      
REMARK 465     GLU B   488                                                      
REMARK 465     GLU B   489                                                      
REMARK 465     LYS B   490                                                      
REMARK 465     GLU B   491                                                      
REMARK 465     LEU B   492                                                      
REMARK 465     ASN B   493                                                      
REMARK 465     ASP B   494                                                      
REMARK 465     LEU B   495                                                      
REMARK 465     PRO B   496                                                      
REMARK 465     PRO B   497                                                      
REMARK 465     ALA B   498                                                      
REMARK 465     THR B   499                                                      
REMARK 465     ARG B   500                                                      
REMARK 465     GLU B   501                                                      
REMARK 465     GLN B   502                                                      
REMARK 465     GLU B   503                                                      
REMARK 465     ASN B   504                                                      
REMARK 465     LEU B   505                                                      
REMARK 465     TYR B   506                                                      
REMARK 465     PHE B   507                                                      
REMARK 465     GLN B   508                                                      
REMARK 465     SER C   116                                                      
REMARK 465     GLU C   117                                                      
REMARK 465     ASN C   118                                                      
REMARK 465     LEU C   119                                                      
REMARK 465     TYR C   120                                                      
REMARK 465     PHE C   121                                                      
REMARK 465     GLN C   122                                                      
REMARK 465     ALA D   121                                                      
REMARK 465     LYS D   122                                                      
REMARK 465     THR D   123                                                      
REMARK 465     THR D   124                                                      
REMARK 465     PRO D   125                                                      
REMARK 465     PRO D   126                                                      
REMARK 465     SER D   127                                                      
REMARK 465     VAL D   128                                                      
REMARK 465     THR D   129                                                      
REMARK 465     SER D   130                                                      
REMARK 465     GLU D   131                                                      
REMARK 465     ASN D   132                                                      
REMARK 465     LEU D   133                                                      
REMARK 465     TYR D   134                                                      
REMARK 465     PHE D   135                                                      
REMARK 465     GLN D   136                                                      
REMARK 465     SER E   116                                                      
REMARK 465     GLU E   117                                                      
REMARK 465     ASN E   118                                                      
REMARK 465     LEU E   119                                                      
REMARK 465     TYR E   120                                                      
REMARK 465     PHE E   121                                                      
REMARK 465     GLN E   122                                                      
REMARK 465     LEU F     1                                                      
REMARK 465     ALA F   121                                                      
REMARK 465     LYS F   122                                                      
REMARK 465     THR F   123                                                      
REMARK 465     THR F   124                                                      
REMARK 465     PRO F   125                                                      
REMARK 465     PRO F   126                                                      
REMARK 465     SER F   127                                                      
REMARK 465     VAL F   128                                                      
REMARK 465     THR F   129                                                      
REMARK 465     SER F   130                                                      
REMARK 465     GLU F   131                                                      
REMARK 465     ASN F   132                                                      
REMARK 465     LEU F   133                                                      
REMARK 465     TYR F   134                                                      
REMARK 465     PHE F   135                                                      
REMARK 465     GLN F   136                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ALA B    37     OG   SER B    40              2.10            
REMARK 500   O    MET A   327     OG1  THR A   331              2.11            
REMARK 500   O    MET B   327     OG1  THR B   331              2.15            
REMARK 500   O    ASN A   324     OG1  THR A   328              2.16            
REMARK 500   O    ALA A    24     OG   SER A    28              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A 221      -68.44    -90.70                                   
REMARK 500    VAL A 388      -74.60    -89.84                                   
REMARK 500    VAL A 458      -64.17   -127.78                                   
REMARK 500    ASN B  94      -63.51   -109.72                                   
REMARK 500    ILE B 221      -68.88    -90.26                                   
REMARK 500    VAL B 388      -74.64    -89.47                                   
REMARK 500    VAL B 458      -64.10   -128.76                                   
REMARK 500    VAL C  58      -49.33     71.52                                   
REMARK 500    VAL E  58      -49.82     71.02                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4YBQ A    1   502  UNP    P43427   GTR5_RAT         1    502             
DBREF  4YBQ B    1   502  UNP    P43427   GTR5_RAT         1    502             
DBREF  4YBQ C    1   122  PDB    4YBQ     4YBQ             1    122             
DBREF  4YBQ D    1   136  PDB    4YBQ     4YBQ             1    136             
DBREF  4YBQ E    1   122  PDB    4YBQ     4YBQ             1    122             
DBREF  4YBQ F    1   136  PDB    4YBQ     4YBQ             1    136             
SEQADV 4YBQ TYR A   50  UNP  P43427    ASN    50 ENGINEERED MUTATION            
SEQADV 4YBQ GLU A  503  UNP  P43427              EXPRESSION TAG                 
SEQADV 4YBQ ASN A  504  UNP  P43427              EXPRESSION TAG                 
SEQADV 4YBQ LEU A  505  UNP  P43427              EXPRESSION TAG                 
SEQADV 4YBQ TYR A  506  UNP  P43427              EXPRESSION TAG                 
SEQADV 4YBQ PHE A  507  UNP  P43427              EXPRESSION TAG                 
SEQADV 4YBQ GLN A  508  UNP  P43427              EXPRESSION TAG                 
SEQADV 4YBQ TYR B   50  UNP  P43427    ASN    50 ENGINEERED MUTATION            
SEQADV 4YBQ GLU B  503  UNP  P43427              EXPRESSION TAG                 
SEQADV 4YBQ ASN B  504  UNP  P43427              EXPRESSION TAG                 
SEQADV 4YBQ LEU B  505  UNP  P43427              EXPRESSION TAG                 
SEQADV 4YBQ TYR B  506  UNP  P43427              EXPRESSION TAG                 
SEQADV 4YBQ PHE B  507  UNP  P43427              EXPRESSION TAG                 
SEQADV 4YBQ GLN B  508  UNP  P43427              EXPRESSION TAG                 
SEQRES   1 A  508  MET GLU LYS GLU ASP GLN GLU LYS THR GLY LYS LEU THR          
SEQRES   2 A  508  LEU VAL LEU ALA LEU ALA THR PHE LEU ALA ALA PHE GLY          
SEQRES   3 A  508  SER SER PHE GLN TYR GLY TYR ASN VAL ALA ALA VAL ASN          
SEQRES   4 A  508  SER PRO SER GLU PHE MET GLN GLN PHE TYR TYR ASP THR          
SEQRES   5 A  508  TYR TYR ASP ARG ASN LYS GLU ASN ILE GLU SER PHE THR          
SEQRES   6 A  508  LEU THR LEU LEU TRP SER LEU THR VAL SER MET PHE PRO          
SEQRES   7 A  508  PHE GLY GLY PHE ILE GLY SER LEU MET VAL GLY PHE LEU          
SEQRES   8 A  508  VAL ASN ASN LEU GLY ARG LYS GLY ALA LEU LEU PHE ASN          
SEQRES   9 A  508  ASN ILE PHE SER ILE LEU PRO ALA ILE LEU MET GLY CYS          
SEQRES  10 A  508  SER LYS ILE ALA LYS SER PHE GLU ILE ILE ILE ALA SER          
SEQRES  11 A  508  ARG LEU LEU VAL GLY ILE CYS ALA GLY ILE SER SER ASN          
SEQRES  12 A  508  VAL VAL PRO MET TYR LEU GLY GLU LEU ALA PRO LYS ASN          
SEQRES  13 A  508  LEU ARG GLY ALA LEU GLY VAL VAL PRO GLN LEU PHE ILE          
SEQRES  14 A  508  THR VAL GLY ILE LEU VAL ALA GLN LEU PHE GLY LEU ARG          
SEQRES  15 A  508  SER VAL LEU ALA SER GLU GLU GLY TRP PRO ILE LEU LEU          
SEQRES  16 A  508  GLY LEU THR GLY VAL PRO ALA GLY LEU GLN LEU LEU LEU          
SEQRES  17 A  508  LEU PRO PHE PHE PRO GLU SER PRO ARG TYR LEU LEU ILE          
SEQRES  18 A  508  GLN LYS LYS ASN GLU SER ALA ALA GLU LYS ALA LEU GLN          
SEQRES  19 A  508  THR LEU ARG GLY TRP LYS ASP VAL ASP MET GLU MET GLU          
SEQRES  20 A  508  GLU ILE ARG LYS GLU ASP GLU ALA GLU LYS ALA ALA GLY          
SEQRES  21 A  508  PHE ILE SER VAL TRP LYS LEU PHE ARG MET GLN SER LEU          
SEQRES  22 A  508  ARG TRP GLN LEU ILE SER THR ILE VAL LEU MET ALA GLY          
SEQRES  23 A  508  GLN GLN LEU SER GLY VAL ASN ALA ILE TYR TYR TYR ALA          
SEQRES  24 A  508  ASP GLN ILE TYR LEU SER ALA GLY VAL LYS SER ASN ASP          
SEQRES  25 A  508  VAL GLN TYR VAL THR ALA GLY THR GLY ALA VAL ASN VAL          
SEQRES  26 A  508  PHE MET THR MET VAL THR VAL PHE VAL VAL GLU LEU TRP          
SEQRES  27 A  508  GLY ARG ARG ASN LEU LEU LEU ILE GLY PHE SER THR CYS          
SEQRES  28 A  508  LEU THR ALA CYS ILE VAL LEU THR VAL ALA LEU ALA LEU          
SEQRES  29 A  508  GLN ASN THR ILE SER TRP MET PRO TYR VAL SER ILE VAL          
SEQRES  30 A  508  CYS VAL ILE VAL TYR VAL ILE GLY HIS ALA VAL GLY PRO          
SEQRES  31 A  508  SER PRO ILE PRO ALA LEU PHE ILE THR GLU ILE PHE LEU          
SEQRES  32 A  508  GLN SER SER ARG PRO SER ALA TYR MET ILE GLY GLY SER          
SEQRES  33 A  508  VAL HIS TRP LEU SER ASN PHE ILE VAL GLY LEU ILE PHE          
SEQRES  34 A  508  PRO PHE ILE GLN VAL GLY LEU GLY PRO TYR SER PHE ILE          
SEQRES  35 A  508  ILE PHE ALA ILE ILE CYS LEU LEU THR THR ILE TYR ILE          
SEQRES  36 A  508  PHE MET VAL VAL PRO GLU THR LYS GLY ARG THR PHE VAL          
SEQRES  37 A  508  GLU ILE ASN GLN ILE PHE ALA LYS LYS ASN LYS VAL SER          
SEQRES  38 A  508  ASP VAL TYR PRO GLU LYS GLU GLU LYS GLU LEU ASN ASP          
SEQRES  39 A  508  LEU PRO PRO ALA THR ARG GLU GLN GLU ASN LEU TYR PHE          
SEQRES  40 A  508  GLN                                                          
SEQRES   1 B  508  MET GLU LYS GLU ASP GLN GLU LYS THR GLY LYS LEU THR          
SEQRES   2 B  508  LEU VAL LEU ALA LEU ALA THR PHE LEU ALA ALA PHE GLY          
SEQRES   3 B  508  SER SER PHE GLN TYR GLY TYR ASN VAL ALA ALA VAL ASN          
SEQRES   4 B  508  SER PRO SER GLU PHE MET GLN GLN PHE TYR TYR ASP THR          
SEQRES   5 B  508  TYR TYR ASP ARG ASN LYS GLU ASN ILE GLU SER PHE THR          
SEQRES   6 B  508  LEU THR LEU LEU TRP SER LEU THR VAL SER MET PHE PRO          
SEQRES   7 B  508  PHE GLY GLY PHE ILE GLY SER LEU MET VAL GLY PHE LEU          
SEQRES   8 B  508  VAL ASN ASN LEU GLY ARG LYS GLY ALA LEU LEU PHE ASN          
SEQRES   9 B  508  ASN ILE PHE SER ILE LEU PRO ALA ILE LEU MET GLY CYS          
SEQRES  10 B  508  SER LYS ILE ALA LYS SER PHE GLU ILE ILE ILE ALA SER          
SEQRES  11 B  508  ARG LEU LEU VAL GLY ILE CYS ALA GLY ILE SER SER ASN          
SEQRES  12 B  508  VAL VAL PRO MET TYR LEU GLY GLU LEU ALA PRO LYS ASN          
SEQRES  13 B  508  LEU ARG GLY ALA LEU GLY VAL VAL PRO GLN LEU PHE ILE          
SEQRES  14 B  508  THR VAL GLY ILE LEU VAL ALA GLN LEU PHE GLY LEU ARG          
SEQRES  15 B  508  SER VAL LEU ALA SER GLU GLU GLY TRP PRO ILE LEU LEU          
SEQRES  16 B  508  GLY LEU THR GLY VAL PRO ALA GLY LEU GLN LEU LEU LEU          
SEQRES  17 B  508  LEU PRO PHE PHE PRO GLU SER PRO ARG TYR LEU LEU ILE          
SEQRES  18 B  508  GLN LYS LYS ASN GLU SER ALA ALA GLU LYS ALA LEU GLN          
SEQRES  19 B  508  THR LEU ARG GLY TRP LYS ASP VAL ASP MET GLU MET GLU          
SEQRES  20 B  508  GLU ILE ARG LYS GLU ASP GLU ALA GLU LYS ALA ALA GLY          
SEQRES  21 B  508  PHE ILE SER VAL TRP LYS LEU PHE ARG MET GLN SER LEU          
SEQRES  22 B  508  ARG TRP GLN LEU ILE SER THR ILE VAL LEU MET ALA GLY          
SEQRES  23 B  508  GLN GLN LEU SER GLY VAL ASN ALA ILE TYR TYR TYR ALA          
SEQRES  24 B  508  ASP GLN ILE TYR LEU SER ALA GLY VAL LYS SER ASN ASP          
SEQRES  25 B  508  VAL GLN TYR VAL THR ALA GLY THR GLY ALA VAL ASN VAL          
SEQRES  26 B  508  PHE MET THR MET VAL THR VAL PHE VAL VAL GLU LEU TRP          
SEQRES  27 B  508  GLY ARG ARG ASN LEU LEU LEU ILE GLY PHE SER THR CYS          
SEQRES  28 B  508  LEU THR ALA CYS ILE VAL LEU THR VAL ALA LEU ALA LEU          
SEQRES  29 B  508  GLN ASN THR ILE SER TRP MET PRO TYR VAL SER ILE VAL          
SEQRES  30 B  508  CYS VAL ILE VAL TYR VAL ILE GLY HIS ALA VAL GLY PRO          
SEQRES  31 B  508  SER PRO ILE PRO ALA LEU PHE ILE THR GLU ILE PHE LEU          
SEQRES  32 B  508  GLN SER SER ARG PRO SER ALA TYR MET ILE GLY GLY SER          
SEQRES  33 B  508  VAL HIS TRP LEU SER ASN PHE ILE VAL GLY LEU ILE PHE          
SEQRES  34 B  508  PRO PHE ILE GLN VAL GLY LEU GLY PRO TYR SER PHE ILE          
SEQRES  35 B  508  ILE PHE ALA ILE ILE CYS LEU LEU THR THR ILE TYR ILE          
SEQRES  36 B  508  PHE MET VAL VAL PRO GLU THR LYS GLY ARG THR PHE VAL          
SEQRES  37 B  508  GLU ILE ASN GLN ILE PHE ALA LYS LYS ASN LYS VAL SER          
SEQRES  38 B  508  ASP VAL TYR PRO GLU LYS GLU GLU LYS GLU LEU ASN ASP          
SEQRES  39 B  508  LEU PRO PRO ALA THR ARG GLU GLN GLU ASN LEU TYR PHE          
SEQRES  40 B  508  GLN                                                          
SEQRES   1 C  122  GLU LEU ASP ILE VAL LEU THR GLN SER PRO LEU SER LEU          
SEQRES   2 C  122  PRO VAL SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG          
SEQRES   3 C  122  SER SER GLN SER ILE VAL HIS SER ASN GLY ASN THR TYR          
SEQRES   4 C  122  LEU GLU TRP TYR LEU GLN LYS PRO GLY GLN SER PRO LYS          
SEQRES   5 C  122  LEU LEU ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL          
SEQRES   6 C  122  PRO ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE          
SEQRES   7 C  122  THR LEU LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY          
SEQRES   8 C  122  VAL TYR TYR CYS PHE GLN GLY SER HIS VAL PRO TYR THR          
SEQRES   9 C  122  PHE GLY GLY GLY THR LYS LEU GLU ILE LYS THR SER GLU          
SEQRES  10 C  122  ASN LEU TYR PHE GLN                                          
SEQRES   1 D  136  LEU GLU VAL ASN LEU VAL GLU SER GLY GLY GLY LEU VAL          
SEQRES   2 D  136  GLN PRO GLY GLY SER ARG LYS LEU SER CYS ALA ALA SER          
SEQRES   3 D  136  GLY PHE THR PHE SER SER PHE GLY MET HIS TRP VAL ARG          
SEQRES   4 D  136  GLN ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA HIS ILE          
SEQRES   5 D  136  SER SER GLY SER ARG THR ILE ASP TYR ALA ASP THR VAL          
SEQRES   6 D  136  LYS GLY ARG PHE THR ILE SER ARG ASP ASN PRO LYS ASN          
SEQRES   7 D  136  THR LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP          
SEQRES   8 D  136  THR ALA ILE TYR TYR CYS ALA ARG GLY ASN GLY TYR TYR          
SEQRES   9 D  136  ASP ALA LEU ASP TYR TRP GLY GLN GLY THR SER VAL THR          
SEQRES  10 D  136  VAL SER SER ALA LYS THR THR PRO PRO SER VAL THR SER          
SEQRES  11 D  136  GLU ASN LEU TYR PHE GLN                                      
SEQRES   1 E  122  GLU LEU ASP ILE VAL LEU THR GLN SER PRO LEU SER LEU          
SEQRES   2 E  122  PRO VAL SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG          
SEQRES   3 E  122  SER SER GLN SER ILE VAL HIS SER ASN GLY ASN THR TYR          
SEQRES   4 E  122  LEU GLU TRP TYR LEU GLN LYS PRO GLY GLN SER PRO LYS          
SEQRES   5 E  122  LEU LEU ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL          
SEQRES   6 E  122  PRO ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE          
SEQRES   7 E  122  THR LEU LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY          
SEQRES   8 E  122  VAL TYR TYR CYS PHE GLN GLY SER HIS VAL PRO TYR THR          
SEQRES   9 E  122  PHE GLY GLY GLY THR LYS LEU GLU ILE LYS THR SER GLU          
SEQRES  10 E  122  ASN LEU TYR PHE GLN                                          
SEQRES   1 F  136  LEU GLU VAL ASN LEU VAL GLU SER GLY GLY GLY LEU VAL          
SEQRES   2 F  136  GLN PRO GLY GLY SER ARG LYS LEU SER CYS ALA ALA SER          
SEQRES   3 F  136  GLY PHE THR PHE SER SER PHE GLY MET HIS TRP VAL ARG          
SEQRES   4 F  136  GLN ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA HIS ILE          
SEQRES   5 F  136  SER SER GLY SER ARG THR ILE ASP TYR ALA ASP THR VAL          
SEQRES   6 F  136  LYS GLY ARG PHE THR ILE SER ARG ASP ASN PRO LYS ASN          
SEQRES   7 F  136  THR LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP          
SEQRES   8 F  136  THR ALA ILE TYR TYR CYS ALA ARG GLY ASN GLY TYR TYR          
SEQRES   9 F  136  ASP ALA LEU ASP TYR TRP GLY GLN GLY THR SER VAL THR          
SEQRES  10 F  136  VAL SER SER ALA LYS THR THR PRO PRO SER VAL THR SER          
SEQRES  11 F  136  GLU ASN LEU TYR PHE GLN                                      
HELIX    1 AA1 THR A   13  VAL A   38  1                                  26    
HELIX    2 AA2 GLU A   62  MET A   87  1                                  26    
HELIX    3 AA3 MET A   87  ALA A  121  1                                  35    
HELIX    4 AA4 SER A  123  ALA A  153  1                                  31    
HELIX    5 AA5 PRO A  154  SER A  187  1                                  34    
HELIX    6 AA6 GLY A  190  LEU A  209  1                                  20    
HELIX    7 AA7 PRO A  210  PHE A  212  5                                   3    
HELIX    8 AA8 SER A  215  ILE A  221  1                                   7    
HELIX    9 AA9 ASN A  225  GLY A  238  1                                  14    
HELIX   10 AB1 VAL A  242  ALA A  258  1                                  17    
HELIX   11 AB2 SER A  263  MET A  270  1                                   8    
HELIX   12 AB3 LEU A  273  LEU A  289  1                                  17    
HELIX   13 AB4 GLY A  291  GLY A  307  1                                  17    
HELIX   14 AB5 LYS A  309  GLY A  339  1                                  31    
HELIX   15 AB6 GLY A  339  ILE A  368  1                                  30    
HELIX   16 AB7 TRP A  370  GLY A  389  1                                  20    
HELIX   17 AB8 PRO A  392  PHE A  402  1                                  11    
HELIX   18 AB9 SER A  406  GLY A  437  1                                  32    
HELIX   19 AC1 TYR A  439  VAL A  458  1                                  20    
HELIX   20 AC2 THR A  466  VAL A  480  1                                  15    
HELIX   21 AC3 THR B   13  VAL B   38  1                                  26    
HELIX   22 AC4 LYS B   58  MET B   87  1                                  30    
HELIX   23 AC5 MET B   87  ALA B  121  1                                  35    
HELIX   24 AC6 SER B  123  ALA B  153  1                                  31    
HELIX   25 AC7 PRO B  154  SER B  187  1                                  34    
HELIX   26 AC8 GLY B  190  LEU B  209  1                                  20    
HELIX   27 AC9 PRO B  210  PHE B  212  5                                   3    
HELIX   28 AD1 SER B  215  ILE B  221  1                                   7    
HELIX   29 AD2 ASN B  225  GLY B  238  1                                  14    
HELIX   30 AD3 VAL B  242  LYS B  257  1                                  16    
HELIX   31 AD4 SER B  263  ARG B  269  1                                   7    
HELIX   32 AD5 LEU B  273  LEU B  289  1                                  17    
HELIX   33 AD6 GLY B  291  GLY B  307  1                                  17    
HELIX   34 AD7 LYS B  309  GLY B  339  1                                  31    
HELIX   35 AD8 GLY B  339  ASN B  366  1                                  28    
HELIX   36 AD9 TRP B  370  GLY B  389  1                                  20    
HELIX   37 AE1 PRO B  392  PHE B  402  1                                  11    
HELIX   38 AE2 SER B  405  GLY B  437  1                                  33    
HELIX   39 AE3 SER B  440  VAL B  458  1                                  19    
HELIX   40 AE4 THR B  466  VAL B  480  1                                  15    
HELIX   41 AE5 GLU C   86  LEU C   90  5                                   5    
HELIX   42 AE6 THR D   29  PHE D   33  5                                   5    
HELIX   43 AE7 ARG D   88  THR D   92  5                                   5    
HELIX   44 AE8 GLU E   86  LEU E   90  5                                   5    
HELIX   45 AE9 THR F   29  PHE F   33  5                                   5    
HELIX   46 AF1 ARG F   88  THR F   92  5                                   5    
SHEET    1 AA1 4 LEU C   6  SER C   9  0                                        
SHEET    2 AA1 4 ALA C  21  SER C  27 -1  O  SER C  24   N  SER C   9           
SHEET    3 AA1 4 ASP C  77  ILE C  82 -1  O  ILE C  82   N  ALA C  21           
SHEET    4 AA1 4 PHE C  69  SER C  74 -1  N  SER C  70   O  LYS C  81           
SHEET    1 AA2 6 SER C  12  VAL C  15  0                                        
SHEET    2 AA2 6 THR C 109  ILE C 113  1  O  LYS C 110   N  LEU C  13           
SHEET    3 AA2 6 GLY C  91  GLN C  97 -1  N  GLY C  91   O  LEU C 111           
SHEET    4 AA2 6 LEU C  40  GLN C  45 -1  N  GLN C  45   O  VAL C  92           
SHEET    5 AA2 6 LYS C  52  TYR C  56 -1  O  LEU C  54   N  TRP C  42           
SHEET    6 AA2 6 ASN C  60  ARG C  61 -1  O  ASN C  60   N  TYR C  56           
SHEET    1 AA3 4 SER C  12  VAL C  15  0                                        
SHEET    2 AA3 4 THR C 109  ILE C 113  1  O  LYS C 110   N  LEU C  13           
SHEET    3 AA3 4 GLY C  91  GLN C  97 -1  N  GLY C  91   O  LEU C 111           
SHEET    4 AA3 4 THR C 104  PHE C 105 -1  O  THR C 104   N  GLN C  97           
SHEET    1 AA4 4 ASN D   4  SER D   8  0                                        
SHEET    2 AA4 4 ARG D  19  SER D  26 -1  O  ALA D  24   N  VAL D   6           
SHEET    3 AA4 4 THR D  79  MET D  84 -1  O  MET D  84   N  ARG D  19           
SHEET    4 AA4 4 PHE D  69  ASP D  74 -1  N  SER D  72   O  PHE D  81           
SHEET    1 AA5 6 GLY D  11  VAL D  13  0                                        
SHEET    2 AA5 6 THR D 114  VAL D 118  1  O  THR D 117   N  VAL D  13           
SHEET    3 AA5 6 ALA D  93  ASN D 101 -1  N  TYR D  95   O  THR D 114           
SHEET    4 AA5 6 GLY D  34  GLN D  40 -1  N  VAL D  38   O  TYR D  96           
SHEET    5 AA5 6 LEU D  46  ILE D  52 -1  O  GLU D  47   N  ARG D  39           
SHEET    6 AA5 6 ILE D  59  TYR D  61 -1  O  ASP D  60   N  HIS D  51           
SHEET    1 AA6 4 GLY D  11  VAL D  13  0                                        
SHEET    2 AA6 4 THR D 114  VAL D 118  1  O  THR D 117   N  VAL D  13           
SHEET    3 AA6 4 ALA D  93  ASN D 101 -1  N  TYR D  95   O  THR D 114           
SHEET    4 AA6 4 ALA D 106  TRP D 110 -1  O  TYR D 109   N  ARG D  99           
SHEET    1 AA7 4 LEU E   6  SER E   9  0                                        
SHEET    2 AA7 4 ALA E  21  SER E  27 -1  O  SER E  24   N  SER E   9           
SHEET    3 AA7 4 ASP E  77  ILE E  82 -1  O  ILE E  82   N  ALA E  21           
SHEET    4 AA7 4 PHE E  69  SER E  74 -1  N  SER E  70   O  LYS E  81           
SHEET    1 AA8 6 SER E  12  VAL E  15  0                                        
SHEET    2 AA8 6 THR E 109  ILE E 113  1  O  LYS E 110   N  LEU E  13           
SHEET    3 AA8 6 GLY E  91  GLN E  97 -1  N  GLY E  91   O  LEU E 111           
SHEET    4 AA8 6 LEU E  40  GLN E  45 -1  N  GLN E  45   O  VAL E  92           
SHEET    5 AA8 6 LYS E  52  TYR E  56 -1  O  LEU E  54   N  TRP E  42           
SHEET    6 AA8 6 ASN E  60  ARG E  61 -1  O  ASN E  60   N  TYR E  56           
SHEET    1 AA9 4 SER E  12  VAL E  15  0                                        
SHEET    2 AA9 4 THR E 109  ILE E 113  1  O  LYS E 110   N  LEU E  13           
SHEET    3 AA9 4 GLY E  91  GLN E  97 -1  N  GLY E  91   O  LEU E 111           
SHEET    4 AA9 4 THR E 104  PHE E 105 -1  O  THR E 104   N  GLN E  97           
SHEET    1 AB1 4 ASN F   4  SER F   8  0                                        
SHEET    2 AB1 4 ARG F  19  SER F  26 -1  O  SER F  22   N  SER F   8           
SHEET    3 AB1 4 THR F  79  MET F  84 -1  O  LEU F  82   N  LEU F  21           
SHEET    4 AB1 4 PHE F  69  ASP F  74 -1  N  ASP F  74   O  THR F  79           
SHEET    1 AB2 6 GLY F  11  VAL F  13  0                                        
SHEET    2 AB2 6 THR F 114  VAL F 118  1  O  THR F 117   N  VAL F  13           
SHEET    3 AB2 6 ALA F  93  ASN F 101 -1  N  ALA F  93   O  VAL F 116           
SHEET    4 AB2 6 GLY F  34  GLN F  40 -1  N  GLY F  34   O  GLY F 100           
SHEET    5 AB2 6 LEU F  46  ILE F  52 -1  O  GLU F  47   N  ARG F  39           
SHEET    6 AB2 6 ILE F  59  TYR F  61 -1  O  ASP F  60   N  HIS F  51           
SHEET    1 AB3 4 GLY F  11  VAL F  13  0                                        
SHEET    2 AB3 4 THR F 114  VAL F 118  1  O  THR F 117   N  VAL F  13           
SHEET    3 AB3 4 ALA F  93  ASN F 101 -1  N  ALA F  93   O  VAL F 116           
SHEET    4 AB3 4 ALA F 106  TRP F 110 -1  O  TYR F 109   N  ARG F  99           
SSBOND   1 CYS C   25    CYS C   95                          1555   1555  2.04  
SSBOND   2 CYS D   23    CYS D   97                          1555   1555  2.03  
SSBOND   3 CYS E   25    CYS E   95                          1555   1555  2.04  
SSBOND   4 CYS F   23    CYS F   97                          1555   1555  2.03  
CISPEP   1 SER C    9    PRO C   10          0        -5.69                     
CISPEP   2 VAL C  101    PRO C  102          0        -1.86                     
CISPEP   3 SER E    9    PRO E   10          0        -5.75                     
CISPEP   4 VAL E  101    PRO E  102          0        -3.58                     
CRYST1   76.773  151.541  106.396  90.00  97.25  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      0.013025  0.000000  0.001657        0.00000                         
SCALE2      0.000000  0.006599  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009475        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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