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Database: PDB
Entry: 3OTK
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Original site: 3OTK 
HEADER    TRANSFERASE                             13-SEP-10   3OTK              
TITLE     STRUCTURE AND MECHANISIM OF CORE 2 BETA1,6-N-                         
TITLE    2 ACETYLGLUCOSAMINYLTRANSFERASE: A METAL-ION INDEPENDENT GT-A          
TITLE    3 GLYCOSYLTRANSFERASE                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-1,3-GALACTOSYL-O-GLYCOSYL-GLYCOPROTEIN BETA-1,6-N-    
COMPND   3 ACETYLGLUCOSAMINYLTRANSFERASE;                                       
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 FRAGMENT: SOLUBLE CATALYTIC DOMAIN (UNP RESIDUES 38-428);            
COMPND   6 SYNONYM: CORE 2-BRANCHING ENZYME, CORE2-GLCNAC-TRANSFERASE, C2GNT;   
COMPND   7 EC: 2.4.1.102;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: GCNT1;                                                         
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL: HUMAN EMBRYONIC KIDNEY (HEK) 293 CELLS       
KEYWDS    GLYCOSYLTRANSFERASE, GOLGI, TRANSFERASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.PAK,J.M.RINI                                                      
REVDAT   3   29-JUL-20 3OTK    1       COMPND REMARK SEQADV HETNAM              
REVDAT   3 2                   1       LINK   SITE   ATOM                       
REVDAT   2   02-OCT-13 3OTK    1       JRNL                                     
REVDAT   1   14-SEP-11 3OTK    0                                                
JRNL        AUTH   J.E.PAK,M.SATKUNARAJAH,J.SEETHARAMAN,J.M.RINI                
JRNL        TITL   STRUCTURAL AND MECHANISTIC CHARACTERIZATION OF               
JRNL        TITL 2 LEUKOCYTE-TYPE CORE 2 BETA                                   
JRNL        TITL 3 1,6-N-ACETYLGLUCOSAMINYLTRANSFERASE: A METAL-ION-INDEPENDENT 
JRNL        TITL 4 GT-A GLYCOSYLTRANSFERASE.                                    
JRNL        REF    J.MOL.BIOL.                   V. 414   798 2011              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   22056345                                                     
JRNL        DOI    10.1016/J.JMB.2011.10.039                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 80656                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4289                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5713                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.34                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2010                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 291                          
REMARK   3   BIN FREE R VALUE                    : 0.2670                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11832                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 254                                     
REMARK   3   SOLVENT ATOMS            : 533                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.54000                                             
REMARK   3    B22 (A**2) : -1.80000                                             
REMARK   3    B33 (A**2) : 3.46000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.05000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.206         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.140         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.961        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12463 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 16941 ; 1.172 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1461 ; 5.258 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   581 ;33.334 ;23.959       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2125 ;14.852 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    77 ;17.594 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1845 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9348 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  5627 ; 0.220 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  8653 ; 0.323 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1115 ; 0.175 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     4 ; 0.112 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    62 ; 0.181 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    25 ; 0.188 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  7324 ; 1.020 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11920 ; 2.599 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5361 ;14.092 ;30.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5018 ;19.005 ;50.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    86        A   424                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.2000 -34.2710 -70.6630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0366 T22:  -0.0192                                     
REMARK   3      T33:  -0.0664 T12:  -0.0051                                     
REMARK   3      T13:   0.0063 T23:   0.0115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4387 L22:   0.9496                                     
REMARK   3      L33:   0.2505 L12:   0.2176                                     
REMARK   3      L13:   0.0516 L23:   0.2148                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0388 S12:   0.0063 S13:  -0.0420                       
REMARK   3      S21:  -0.0322 S22:   0.0172 S23:   0.0261                       
REMARK   3      S31:   0.0011 S32:  -0.0043 S33:   0.0216                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    86        B   424                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.2670 -14.2920 -56.6470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0485 T22:  -0.0257                                     
REMARK   3      T33:  -0.0654 T12:   0.0151                                     
REMARK   3      T13:  -0.0172 T23:  -0.0377                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1643 L22:   0.7441                                     
REMARK   3      L33:   0.4267 L12:  -0.0433                                     
REMARK   3      L13:  -0.2176 L23:  -0.0753                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0720 S12:  -0.1442 S13:   0.0565                       
REMARK   3      S21:   0.0655 S22:   0.0554 S23:  -0.1288                       
REMARK   3      S31:   0.0039 S32:   0.0243 S33:   0.0166                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    86        C   424                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.6890  -0.0130  -2.5630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0368 T22:  -0.0384                                     
REMARK   3      T33:  -0.0544 T12:  -0.0084                                     
REMARK   3      T13:  -0.0048 T23:  -0.0034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4101 L22:   1.2733                                     
REMARK   3      L33:   0.2020 L12:   0.3354                                     
REMARK   3      L13:  -0.1609 L23:  -0.2876                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0641 S12:   0.0092 S13:   0.0556                       
REMARK   3      S21:  -0.0762 S22:   0.0557 S23:  -0.0137                       
REMARK   3      S31:   0.0077 S32:   0.0106 S33:   0.0085                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    86        D   424                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.1230 -19.7810  11.6130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0415 T22:  -0.0436                                     
REMARK   3      T33:  -0.0527 T12:   0.0127                                     
REMARK   3      T13:   0.0159 T23:   0.0213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8491 L22:   0.7464                                     
REMARK   3      L33:   0.4406 L12:  -0.0174                                     
REMARK   3      L13:   0.0495 L23:   0.0343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0631 S12:  -0.0587 S13:  -0.0267                       
REMARK   3      S21:   0.0630 S22:   0.0392 S23:   0.1326                       
REMARK   3      S31:   0.0119 S32:  -0.0081 S33:   0.0239                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3OTK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000061555.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9771                             
REMARK 200  MONOCHROMATOR                  : HORIZONTAL FOCUSING 5.05           
REMARK 200                                   ASYMMETRIC CUT SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 93761                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.13400                            
REMARK 200  R SYM                      (I) : 0.11600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.67600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% POLYETHYLENE GLYCOL 4000, 0.15 M     
REMARK 280  GLYCINE PH 9.0, 0.6 M LICL, 1.5% 1,2,3 HEPTANETRIOL, 25 MM UDP-     
REMARK 280  GLCNAC, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 296K             
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       50.51000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E                               
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: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 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     PRO A    38                                                      
REMARK 465     GLU A    39                                                      
REMARK 465     PHE A    40                                                      
REMARK 465     PHE A    41                                                      
REMARK 465     SER A    42                                                      
REMARK 465     VAL A    43                                                      
REMARK 465     ARG A    44                                                      
REMARK 465     HIS A    45                                                      
REMARK 465     LEU A    46                                                      
REMARK 465     GLU A    47                                                      
REMARK 465     LEU A    48                                                      
REMARK 465     ALA A    49                                                      
REMARK 465     GLY A    50                                                      
REMARK 465     ASP A    51                                                      
REMARK 465     ASP A    52                                                      
REMARK 465     PRO A    53                                                      
REMARK 465     TYR A    54                                                      
REMARK 465     SER A    55                                                      
REMARK 465     ASN A   425                                                      
REMARK 465     LEU A   426                                                      
REMARK 465     GLU A   427                                                      
REMARK 465     HIS A   428                                                      
REMARK 465     PRO B    38                                                      
REMARK 465     GLU B    39                                                      
REMARK 465     PHE B    40                                                      
REMARK 465     PHE B    41                                                      
REMARK 465     SER B    42                                                      
REMARK 465     VAL B    43                                                      
REMARK 465     ARG B    44                                                      
REMARK 465     HIS B    45                                                      
REMARK 465     LEU B    46                                                      
REMARK 465     GLU B    47                                                      
REMARK 465     LEU B    48                                                      
REMARK 465     ALA B    49                                                      
REMARK 465     GLY B    50                                                      
REMARK 465     ASP B    51                                                      
REMARK 465     ASP B    52                                                      
REMARK 465     PRO B    53                                                      
REMARK 465     TYR B    54                                                      
REMARK 465     SER B    55                                                      
REMARK 465     VAL B    80                                                      
REMARK 465     GLN B    81                                                      
REMARK 465     PHE B    82                                                      
REMARK 465     LYS B    83                                                      
REMARK 465     LYS B    84                                                      
REMARK 465     ARG B    85                                                      
REMARK 465     ASN B   425                                                      
REMARK 465     LEU B   426                                                      
REMARK 465     GLU B   427                                                      
REMARK 465     HIS B   428                                                      
REMARK 465     PRO C    38                                                      
REMARK 465     GLU C    39                                                      
REMARK 465     PHE C    40                                                      
REMARK 465     PHE C    41                                                      
REMARK 465     SER C    42                                                      
REMARK 465     VAL C    43                                                      
REMARK 465     ARG C    44                                                      
REMARK 465     HIS C    45                                                      
REMARK 465     LEU C    46                                                      
REMARK 465     GLU C    47                                                      
REMARK 465     LEU C    48                                                      
REMARK 465     ALA C    49                                                      
REMARK 465     GLY C    50                                                      
REMARK 465     ASP C    51                                                      
REMARK 465     ASP C    52                                                      
REMARK 465     PRO C    53                                                      
REMARK 465     TYR C    54                                                      
REMARK 465     SER C    55                                                      
REMARK 465     ILE C    77                                                      
REMARK 465     LEU C    78                                                      
REMARK 465     THR C    79                                                      
REMARK 465     VAL C    80                                                      
REMARK 465     GLN C    81                                                      
REMARK 465     PHE C    82                                                      
REMARK 465     LYS C    83                                                      
REMARK 465     LYS C    84                                                      
REMARK 465     ARG C    85                                                      
REMARK 465     ASN C   425                                                      
REMARK 465     LEU C   426                                                      
REMARK 465     GLU C   427                                                      
REMARK 465     HIS C   428                                                      
REMARK 465     PRO D    38                                                      
REMARK 465     GLU D    39                                                      
REMARK 465     PHE D    40                                                      
REMARK 465     PHE D    41                                                      
REMARK 465     SER D    42                                                      
REMARK 465     VAL D    43                                                      
REMARK 465     ARG D    44                                                      
REMARK 465     HIS D    45                                                      
REMARK 465     LEU D    46                                                      
REMARK 465     GLU D    47                                                      
REMARK 465     LEU D    48                                                      
REMARK 465     ALA D    49                                                      
REMARK 465     GLY D    50                                                      
REMARK 465     ASP D    51                                                      
REMARK 465     ASP D    52                                                      
REMARK 465     PRO D    53                                                      
REMARK 465     TYR D    54                                                      
REMARK 465     SER D    55                                                      
REMARK 465     GLN D    81                                                      
REMARK 465     PHE D    82                                                      
REMARK 465     LYS D    83                                                      
REMARK 465     LYS D    84                                                      
REMARK 465     ARG D    85                                                      
REMARK 465     ASN D   425                                                      
REMARK 465     LEU D   426                                                      
REMARK 465     GLU D   427                                                      
REMARK 465     HIS D   428                                                      
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    HIS A 130      -16.08   -149.99                                   
REMARK 500    LYS A 132       73.30     56.90                                   
REMARK 500    THR A 244      102.36   -162.00                                   
REMARK 500    ASP A 263       62.55     63.60                                   
REMARK 500    SER A 317       60.89     39.48                                   
REMARK 500    GLU A 331      -22.70     88.19                                   
REMARK 500    SER A 379       -5.44     76.83                                   
REMARK 500    ASP A 403      113.06   -162.31                                   
REMARK 500    LEU A 423       19.82    -69.54                                   
REMARK 500    LYS B 108       41.32     70.17                                   
REMARK 500    HIS B 130      -16.37   -150.93                                   
REMARK 500    LYS B 132       74.57     55.00                                   
REMARK 500    GLU B 331      -16.95     86.98                                   
REMARK 500    SER B 379       -4.62     75.24                                   
REMARK 500    LEU C  75      -88.32    -89.01                                   
REMARK 500    HIS C 130      -12.05   -150.14                                   
REMARK 500    LYS C 132       72.76     58.50                                   
REMARK 500    THR C 244      100.87   -160.13                                   
REMARK 500    GLU C 331      -12.82     85.92                                   
REMARK 500    SER C 379       -3.92     74.04                                   
REMARK 500    VAL C 406      -62.01    -94.16                                   
REMARK 500    LYS D 108       40.29     72.98                                   
REMARK 500    HIS D 130      -13.86   -152.62                                   
REMARK 500    LYS D 132       68.45     60.85                                   
REMARK 500    GLU D 331       -9.54     82.79                                   
REMARK 500    SER D 379       -1.84     73.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 586  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 170   O                                                      
REMARK 620 2 PHE A 173   O    73.2                                              
REMARK 620 3 VAL A 176   O    86.1  80.6                                        
REMARK 620 4 HOH A 438   O    96.4 169.0 102.6                                  
REMARK 620 5 HOH A 484   O   170.3  97.5  89.8  93.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 587  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C  29   O                                                      
REMARK 620 2 ALA C 170   O   171.1                                              
REMARK 620 3 PHE C 173   O   109.4  79.6                                        
REMARK 620 4 VAL C 176   O    95.9  84.9  87.0                                  
REMARK 620 N                    1     2     3                                   
DBREF  3OTK A   38   428  UNP    Q09324   GCNT1_MOUSE     38    428             
DBREF  3OTK B   38   428  UNP    Q09324   GCNT1_MOUSE     38    428             
DBREF  3OTK C   38   428  UNP    Q09324   GCNT1_MOUSE     38    428             
DBREF  3OTK D   38   428  UNP    Q09324   GCNT1_MOUSE     38    428             
SEQADV 3OTK SER A  217  UNP  Q09324    CYS   217 ENGINEERED MUTATION            
SEQADV 3OTK SER B  217  UNP  Q09324    CYS   217 ENGINEERED MUTATION            
SEQADV 3OTK SER C  217  UNP  Q09324    CYS   217 ENGINEERED MUTATION            
SEQADV 3OTK SER D  217  UNP  Q09324    CYS   217 ENGINEERED MUTATION            
SEQRES   1 A  391  PRO GLU PHE PHE SER VAL ARG HIS LEU GLU LEU ALA GLY          
SEQRES   2 A  391  ASP ASP PRO TYR SER ASN VAL ASN CYS THR LYS ILE LEU          
SEQRES   3 A  391  GLN GLY ASP PRO GLU GLU ILE GLN LYS VAL LYS LEU GLU          
SEQRES   4 A  391  ILE LEU THR VAL GLN PHE LYS LYS ARG PRO ARG TRP THR          
SEQRES   5 A  391  PRO HIS ASP TYR ILE ASN MET THR ARG ASP CYS ALA SER          
SEQRES   6 A  391  PHE ILE ARG THR ARG LYS TYR ILE VAL GLU PRO LEU THR          
SEQRES   7 A  391  LYS GLU GLU VAL GLY PHE PRO ILE ALA TYR SER ILE VAL          
SEQRES   8 A  391  VAL HIS HIS LYS ILE GLU MET LEU ASP ARG LEU LEU ARG          
SEQRES   9 A  391  ALA ILE TYR MET PRO GLN ASN PHE TYR CYS ILE HIS VAL          
SEQRES  10 A  391  ASP ARG LYS ALA GLU GLU SER PHE LEU ALA ALA VAL GLN          
SEQRES  11 A  391  GLY ILE ALA SER CYS PHE ASP ASN VAL PHE VAL ALA SER          
SEQRES  12 A  391  GLN LEU GLU SER VAL VAL TYR ALA SER TRP THR ARG VAL          
SEQRES  13 A  391  LYS ALA ASP LEU ASN CYS MET LYS ASP LEU TYR ARG MET          
SEQRES  14 A  391  ASN ALA ASN TRP LYS TYR LEU ILE ASN LEU SER GLY MET          
SEQRES  15 A  391  ASP PHE PRO ILE LYS THR ASN LEU GLU ILE VAL ARG LYS          
SEQRES  16 A  391  LEU LYS CYS SER THR GLY GLU ASN ASN LEU GLU THR GLU          
SEQRES  17 A  391  LYS MET PRO PRO ASN LYS GLU GLU ARG TRP LYS LYS ARG          
SEQRES  18 A  391  TYR ALA VAL VAL ASP GLY LYS LEU THR ASN THR GLY ILE          
SEQRES  19 A  391  VAL LYS ALA PRO PRO PRO LEU LYS THR PRO LEU PHE SER          
SEQRES  20 A  391  GLY SER ALA TYR PHE VAL VAL THR ARG GLU TYR VAL GLY          
SEQRES  21 A  391  TYR VAL LEU GLU ASN GLU ASN ILE GLN LYS LEU MET GLU          
SEQRES  22 A  391  TRP ALA GLN ASP THR TYR SER PRO ASP GLU PHE LEU TRP          
SEQRES  23 A  391  ALA THR ILE GLN ARG ILE PRO GLU VAL PRO GLY SER PHE          
SEQRES  24 A  391  PRO SER SER ASN LYS TYR ASP LEU SER ASP MET ASN ALA          
SEQRES  25 A  391  ILE ALA ARG PHE VAL LYS TRP GLN TYR PHE GLU GLY ASP          
SEQRES  26 A  391  VAL SER ASN GLY ALA PRO TYR PRO PRO CYS SER GLY VAL          
SEQRES  27 A  391  HIS VAL ARG SER VAL CYS VAL PHE GLY ALA GLY ASP LEU          
SEQRES  28 A  391  SER TRP MET LEU ARG GLN HIS HIS LEU PHE ALA ASN LYS          
SEQRES  29 A  391  PHE ASP MET ASP VAL ASP PRO PHE ALA ILE GLN CYS LEU          
SEQRES  30 A  391  ASP GLU HIS LEU ARG ARG LYS ALA LEU GLU ASN LEU GLU          
SEQRES  31 A  391  HIS                                                          
SEQRES   1 B  391  PRO GLU PHE PHE SER VAL ARG HIS LEU GLU LEU ALA GLY          
SEQRES   2 B  391  ASP ASP PRO TYR SER ASN VAL ASN CYS THR LYS ILE LEU          
SEQRES   3 B  391  GLN GLY ASP PRO GLU GLU ILE GLN LYS VAL LYS LEU GLU          
SEQRES   4 B  391  ILE LEU THR VAL GLN PHE LYS LYS ARG PRO ARG TRP THR          
SEQRES   5 B  391  PRO HIS ASP TYR ILE ASN MET THR ARG ASP CYS ALA SER          
SEQRES   6 B  391  PHE ILE ARG THR ARG LYS TYR ILE VAL GLU PRO LEU THR          
SEQRES   7 B  391  LYS GLU GLU VAL GLY PHE PRO ILE ALA TYR SER ILE VAL          
SEQRES   8 B  391  VAL HIS HIS LYS ILE GLU MET LEU ASP ARG LEU LEU ARG          
SEQRES   9 B  391  ALA ILE TYR MET PRO GLN ASN PHE TYR CYS ILE HIS VAL          
SEQRES  10 B  391  ASP ARG LYS ALA GLU GLU SER PHE LEU ALA ALA VAL GLN          
SEQRES  11 B  391  GLY ILE ALA SER CYS PHE ASP ASN VAL PHE VAL ALA SER          
SEQRES  12 B  391  GLN LEU GLU SER VAL VAL TYR ALA SER TRP THR ARG VAL          
SEQRES  13 B  391  LYS ALA ASP LEU ASN CYS MET LYS ASP LEU TYR ARG MET          
SEQRES  14 B  391  ASN ALA ASN TRP LYS TYR LEU ILE ASN LEU SER GLY MET          
SEQRES  15 B  391  ASP PHE PRO ILE LYS THR ASN LEU GLU ILE VAL ARG LYS          
SEQRES  16 B  391  LEU LYS CYS SER THR GLY GLU ASN ASN LEU GLU THR GLU          
SEQRES  17 B  391  LYS MET PRO PRO ASN LYS GLU GLU ARG TRP LYS LYS ARG          
SEQRES  18 B  391  TYR ALA VAL VAL ASP GLY LYS LEU THR ASN THR GLY ILE          
SEQRES  19 B  391  VAL LYS ALA PRO PRO PRO LEU LYS THR PRO LEU PHE SER          
SEQRES  20 B  391  GLY SER ALA TYR PHE VAL VAL THR ARG GLU TYR VAL GLY          
SEQRES  21 B  391  TYR VAL LEU GLU ASN GLU ASN ILE GLN LYS LEU MET GLU          
SEQRES  22 B  391  TRP ALA GLN ASP THR TYR SER PRO ASP GLU PHE LEU TRP          
SEQRES  23 B  391  ALA THR ILE GLN ARG ILE PRO GLU VAL PRO GLY SER PHE          
SEQRES  24 B  391  PRO SER SER ASN LYS TYR ASP LEU SER ASP MET ASN ALA          
SEQRES  25 B  391  ILE ALA ARG PHE VAL LYS TRP GLN TYR PHE GLU GLY ASP          
SEQRES  26 B  391  VAL SER ASN GLY ALA PRO TYR PRO PRO CYS SER GLY VAL          
SEQRES  27 B  391  HIS VAL ARG SER VAL CYS VAL PHE GLY ALA GLY ASP LEU          
SEQRES  28 B  391  SER TRP MET LEU ARG GLN HIS HIS LEU PHE ALA ASN LYS          
SEQRES  29 B  391  PHE ASP MET ASP VAL ASP PRO PHE ALA ILE GLN CYS LEU          
SEQRES  30 B  391  ASP GLU HIS LEU ARG ARG LYS ALA LEU GLU ASN LEU GLU          
SEQRES  31 B  391  HIS                                                          
SEQRES   1 C  391  PRO GLU PHE PHE SER VAL ARG HIS LEU GLU LEU ALA GLY          
SEQRES   2 C  391  ASP ASP PRO TYR SER ASN VAL ASN CYS THR LYS ILE LEU          
SEQRES   3 C  391  GLN GLY ASP PRO GLU GLU ILE GLN LYS VAL LYS LEU GLU          
SEQRES   4 C  391  ILE LEU THR VAL GLN PHE LYS LYS ARG PRO ARG TRP THR          
SEQRES   5 C  391  PRO HIS ASP TYR ILE ASN MET THR ARG ASP CYS ALA SER          
SEQRES   6 C  391  PHE ILE ARG THR ARG LYS TYR ILE VAL GLU PRO LEU THR          
SEQRES   7 C  391  LYS GLU GLU VAL GLY PHE PRO ILE ALA TYR SER ILE VAL          
SEQRES   8 C  391  VAL HIS HIS LYS ILE GLU MET LEU ASP ARG LEU LEU ARG          
SEQRES   9 C  391  ALA ILE TYR MET PRO GLN ASN PHE TYR CYS ILE HIS VAL          
SEQRES  10 C  391  ASP ARG LYS ALA GLU GLU SER PHE LEU ALA ALA VAL GLN          
SEQRES  11 C  391  GLY ILE ALA SER CYS PHE ASP ASN VAL PHE VAL ALA SER          
SEQRES  12 C  391  GLN LEU GLU SER VAL VAL TYR ALA SER TRP THR ARG VAL          
SEQRES  13 C  391  LYS ALA ASP LEU ASN CYS MET LYS ASP LEU TYR ARG MET          
SEQRES  14 C  391  ASN ALA ASN TRP LYS TYR LEU ILE ASN LEU SER GLY MET          
SEQRES  15 C  391  ASP PHE PRO ILE LYS THR ASN LEU GLU ILE VAL ARG LYS          
SEQRES  16 C  391  LEU LYS CYS SER THR GLY GLU ASN ASN LEU GLU THR GLU          
SEQRES  17 C  391  LYS MET PRO PRO ASN LYS GLU GLU ARG TRP LYS LYS ARG          
SEQRES  18 C  391  TYR ALA VAL VAL ASP GLY LYS LEU THR ASN THR GLY ILE          
SEQRES  19 C  391  VAL LYS ALA PRO PRO PRO LEU LYS THR PRO LEU PHE SER          
SEQRES  20 C  391  GLY SER ALA TYR PHE VAL VAL THR ARG GLU TYR VAL GLY          
SEQRES  21 C  391  TYR VAL LEU GLU ASN GLU ASN ILE GLN LYS LEU MET GLU          
SEQRES  22 C  391  TRP ALA GLN ASP THR TYR SER PRO ASP GLU PHE LEU TRP          
SEQRES  23 C  391  ALA THR ILE GLN ARG ILE PRO GLU VAL PRO GLY SER PHE          
SEQRES  24 C  391  PRO SER SER ASN LYS TYR ASP LEU SER ASP MET ASN ALA          
SEQRES  25 C  391  ILE ALA ARG PHE VAL LYS TRP GLN TYR PHE GLU GLY ASP          
SEQRES  26 C  391  VAL SER ASN GLY ALA PRO TYR PRO PRO CYS SER GLY VAL          
SEQRES  27 C  391  HIS VAL ARG SER VAL CYS VAL PHE GLY ALA GLY ASP LEU          
SEQRES  28 C  391  SER TRP MET LEU ARG GLN HIS HIS LEU PHE ALA ASN LYS          
SEQRES  29 C  391  PHE ASP MET ASP VAL ASP PRO PHE ALA ILE GLN CYS LEU          
SEQRES  30 C  391  ASP GLU HIS LEU ARG ARG LYS ALA LEU GLU ASN LEU GLU          
SEQRES  31 C  391  HIS                                                          
SEQRES   1 D  391  PRO GLU PHE PHE SER VAL ARG HIS LEU GLU LEU ALA GLY          
SEQRES   2 D  391  ASP ASP PRO TYR SER ASN VAL ASN CYS THR LYS ILE LEU          
SEQRES   3 D  391  GLN GLY ASP PRO GLU GLU ILE GLN LYS VAL LYS LEU GLU          
SEQRES   4 D  391  ILE LEU THR VAL GLN PHE LYS LYS ARG PRO ARG TRP THR          
SEQRES   5 D  391  PRO HIS ASP TYR ILE ASN MET THR ARG ASP CYS ALA SER          
SEQRES   6 D  391  PHE ILE ARG THR ARG LYS TYR ILE VAL GLU PRO LEU THR          
SEQRES   7 D  391  LYS GLU GLU VAL GLY PHE PRO ILE ALA TYR SER ILE VAL          
SEQRES   8 D  391  VAL HIS HIS LYS ILE GLU MET LEU ASP ARG LEU LEU ARG          
SEQRES   9 D  391  ALA ILE TYR MET PRO GLN ASN PHE TYR CYS ILE HIS VAL          
SEQRES  10 D  391  ASP ARG LYS ALA GLU GLU SER PHE LEU ALA ALA VAL GLN          
SEQRES  11 D  391  GLY ILE ALA SER CYS PHE ASP ASN VAL PHE VAL ALA SER          
SEQRES  12 D  391  GLN LEU GLU SER VAL VAL TYR ALA SER TRP THR ARG VAL          
SEQRES  13 D  391  LYS ALA ASP LEU ASN CYS MET LYS ASP LEU TYR ARG MET          
SEQRES  14 D  391  ASN ALA ASN TRP LYS TYR LEU ILE ASN LEU SER GLY MET          
SEQRES  15 D  391  ASP PHE PRO ILE LYS THR ASN LEU GLU ILE VAL ARG LYS          
SEQRES  16 D  391  LEU LYS CYS SER THR GLY GLU ASN ASN LEU GLU THR GLU          
SEQRES  17 D  391  LYS MET PRO PRO ASN LYS GLU GLU ARG TRP LYS LYS ARG          
SEQRES  18 D  391  TYR ALA VAL VAL ASP GLY LYS LEU THR ASN THR GLY ILE          
SEQRES  19 D  391  VAL LYS ALA PRO PRO PRO LEU LYS THR PRO LEU PHE SER          
SEQRES  20 D  391  GLY SER ALA TYR PHE VAL VAL THR ARG GLU TYR VAL GLY          
SEQRES  21 D  391  TYR VAL LEU GLU ASN GLU ASN ILE GLN LYS LEU MET GLU          
SEQRES  22 D  391  TRP ALA GLN ASP THR TYR SER PRO ASP GLU PHE LEU TRP          
SEQRES  23 D  391  ALA THR ILE GLN ARG ILE PRO GLU VAL PRO GLY SER PHE          
SEQRES  24 D  391  PRO SER SER ASN LYS TYR ASP LEU SER ASP MET ASN ALA          
SEQRES  25 D  391  ILE ALA ARG PHE VAL LYS TRP GLN TYR PHE GLU GLY ASP          
SEQRES  26 D  391  VAL SER ASN GLY ALA PRO TYR PRO PRO CYS SER GLY VAL          
SEQRES  27 D  391  HIS VAL ARG SER VAL CYS VAL PHE GLY ALA GLY ASP LEU          
SEQRES  28 D  391  SER TRP MET LEU ARG GLN HIS HIS LEU PHE ALA ASN LYS          
SEQRES  29 D  391  PHE ASP MET ASP VAL ASP PRO PHE ALA ILE GLN CYS LEU          
SEQRES  30 D  391  ASP GLU HIS LEU ARG ARG LYS ALA LEU GLU ASN LEU GLU          
SEQRES  31 D  391  HIS                                                          
MODRES 3OTK ASN C   95  ASN  GLYCOSYLATION SITE                                 
MODRES 3OTK ASN A   95  ASN  GLYCOSYLATION SITE                                 
MODRES 3OTK ASN D   58  ASN  GLYCOSYLATION SITE                                 
MODRES 3OTK ASN A   58  ASN  GLYCOSYLATION SITE                                 
MODRES 3OTK ASN B   58  ASN  GLYCOSYLATION SITE                                 
MODRES 3OTK ASN C   58  ASN  GLYCOSYLATION SITE                                 
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    FUC  E   3      10                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    FUC  F   3      10                                                       
HET    HTO  A 584      10                                                       
HET    HTO  A 585      10                                                       
HET     NA  A 586       1                                                       
HET    NAG  A 588      14                                                       
HET    UDP  A 598      25                                                       
HET    NAG  B 592      14                                                       
HET    UDP  B 599      25                                                       
HET     NA  C 587       1                                                       
HET    NAG  C 593      14                                                       
HET    UDP  C 600      25                                                       
HET    NAG  D 597      14                                                       
HET    UDP  D 601      25                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     HTO HEPTANE-1,2,3-TRIOL                                              
HETNAM      NA SODIUM ION                                                       
HETNAM     UDP URIDINE-5'-DIPHOSPHATE                                           
FORMUL   5  NAG    8(C8 H15 N O6)                                               
FORMUL   5  FUC    2(C6 H12 O5)                                                 
FORMUL   7  HTO    2(C7 H16 O3)                                                 
FORMUL   9   NA    2(NA 1+)                                                     
FORMUL  11  UDP    4(C9 H14 N2 O12 P2)                                          
FORMUL  19  HOH   *533(H2 O)                                                    
HELIX    1   1 ASN A   58  GLY A   65  1                                   8    
HELIX    2   2 ASP A   66  THR A   79  1                                  14    
HELIX    3   3 THR A   79  LYS A   84  1                                   6    
HELIX    4   4 THR A   89  THR A   97  1                                   9    
HELIX    5   5 ASP A   99  LYS A  108  1                                  10    
HELIX    6   6 THR A  115  GLY A  120  1                                   6    
HELIX    7   7 LYS A  132  TYR A  144  1                                  13    
HELIX    8   8 GLU A  159  CYS A  172  1                                  14    
HELIX    9   9 SER A  189  ASN A  207  1                                  19    
HELIX   10  10 THR A  225  THR A  237  1                                  13    
HELIX   11  11 PRO A  248  LYS A  251  5                                   4    
HELIX   12  12 GLU A  252  LYS A  256  1                                   5    
HELIX   13  13 ARG A  293  ASN A  302  1                                  10    
HELIX   14  14 ASN A  302  GLN A  313  1                                  12    
HELIX   15  15 SER A  317  GLU A  320  5                                   4    
HELIX   16  16 PHE A  321  GLN A  327  1                                   7    
HELIX   17  17 SER A  339  ASP A  343  5                                   5    
HELIX   18  18 TRP A  356  GLU A  360  5                                   5    
HELIX   19  19 ASP A  362  GLY A  366  5                                   5    
HELIX   20  20 GLY A  384  GLY A  386  5                                   3    
HELIX   21  21 ASP A  387  LEU A  392  1                                   6    
HELIX   22  22 ASP A  407  LEU A  423  1                                  17    
HELIX   23  23 ASN B   58  GLY B   65  1                                   8    
HELIX   24  24 ASP B   66  THR B   79  1                                  14    
HELIX   25  25 THR B   89  THR B   97  1                                   9    
HELIX   26  26 ASP B   99  LYS B  108  1                                  10    
HELIX   27  27 THR B  115  GLY B  120  1                                   6    
HELIX   28  28 LYS B  132  TYR B  144  1                                  13    
HELIX   29  29 GLU B  159  SER B  171  1                                  13    
HELIX   30  30 SER B  189  ASN B  207  1                                  19    
HELIX   31  31 THR B  225  SER B  236  1                                  12    
HELIX   32  32 GLU B  252  LYS B  256  1                                   5    
HELIX   33  33 ARG B  293  ASN B  302  1                                  10    
HELIX   34  34 ASN B  302  GLN B  313  1                                  12    
HELIX   35  35 SER B  317  GLU B  320  5                                   4    
HELIX   36  36 PHE B  321  GLN B  327  1                                   7    
HELIX   37  37 SER B  339  ASP B  343  5                                   5    
HELIX   38  38 ASP B  362  GLY B  366  5                                   5    
HELIX   39  39 GLY B  384  GLY B  386  5                                   3    
HELIX   40  40 ASP B  387  LEU B  392  1                                   6    
HELIX   41  41 ASP B  407  LEU B  423  1                                  17    
HELIX   42  42 ASN C   58  GLY C   65  1                                   8    
HELIX   43  43 ASP C   66  GLU C   76  1                                  11    
HELIX   44  44 THR C   89  THR C   97  1                                   9    
HELIX   45  45 ASP C   99  LYS C  108  1                                  10    
HELIX   46  46 THR C  115  GLY C  120  1                                   6    
HELIX   47  47 LYS C  132  TYR C  144  1                                  13    
HELIX   48  48 GLU C  159  SER C  171  1                                  13    
HELIX   49  49 SER C  189  ASN C  207  1                                  19    
HELIX   50  50 THR C  225  THR C  237  1                                  13    
HELIX   51  51 PRO C  248  LYS C  251  5                                   4    
HELIX   52  52 GLU C  252  LYS C  256  1                                   5    
HELIX   53  53 ARG C  293  ASN C  302  1                                  10    
HELIX   54  54 ASN C  302  GLN C  313  1                                  12    
HELIX   55  55 SER C  317  GLU C  320  5                                   4    
HELIX   56  56 PHE C  321  GLN C  327  1                                   7    
HELIX   57  57 SER C  339  ASP C  343  5                                   5    
HELIX   58  58 TRP C  356  GLU C  360  5                                   5    
HELIX   59  59 ASP C  362  GLY C  366  5                                   5    
HELIX   60  60 GLY C  384  GLY C  386  5                                   3    
HELIX   61  61 ASP C  387  LEU C  392  1                                   6    
HELIX   62  62 ASP C  407  GLU C  424  1                                  18    
HELIX   63  63 ASN D   58  GLY D   65  1                                   8    
HELIX   64  64 ASP D   66  ILE D   77  1                                  12    
HELIX   65  65 THR D   89  THR D   97  1                                   9    
HELIX   66  66 ASP D   99  LYS D  108  1                                  10    
HELIX   67  67 THR D  115  GLY D  120  1                                   6    
HELIX   68  68 LYS D  132  TYR D  144  1                                  13    
HELIX   69  69 GLU D  159  CYS D  172  1                                  14    
HELIX   70  70 SER D  189  ASN D  207  1                                  19    
HELIX   71  71 THR D  225  SER D  236  1                                  12    
HELIX   72  72 GLU D  252  LYS D  256  1                                   5    
HELIX   73  73 ARG D  293  ASN D  302  1                                  10    
HELIX   74  74 ASN D  302  GLN D  313  1                                  12    
HELIX   75  75 SER D  317  GLU D  320  5                                   4    
HELIX   76  76 PHE D  321  GLN D  327  1                                   7    
HELIX   77  77 SER D  339  ASP D  343  5                                   5    
HELIX   78  78 ASP D  362  GLY D  366  5                                   5    
HELIX   79  79 GLY D  384  GLY D  386  5                                   3    
HELIX   80  80 ASP D  387  ARG D  393  1                                   7    
HELIX   81  81 ASP D  407  GLU D  424  1                                  18    
SHEET    1   A 5 VAL A 176  VAL A 178  0                                        
SHEET    2   A 5 PHE A 149  VAL A 154  1  N  ILE A 152   O  PHE A 177           
SHEET    3   A 5 ILE A 123  VAL A 129  1  N  ILE A 127   O  HIS A 153           
SHEET    4   A 5 TYR A 212  SER A 217  1  O  LEU A 216   N  SER A 126           
SHEET    5   A 5 VAL A 290  THR A 292 -1  O  VAL A 291   N  LEU A 213           
SHEET    1   B 3 ASP A 220  PRO A 222  0                                        
SHEET    2   B 3 PHE A 398  ASN A 400 -1  O  ALA A 399   N  PHE A 221           
SHEET    3   B 3 ARG A 352  PHE A 353  1  N  PHE A 353   O  PHE A 398           
SHEET    1   C 2 GLU A 245  LYS A 246  0                                        
SHEET    2   C 2 PHE A 283  SER A 284 -1  O  SER A 284   N  GLU A 245           
SHEET    1   D 2 LYS A 257  VAL A 261  0                                        
SHEET    2   D 2 LEU A 266  VAL A 272 -1  O  THR A 267   N  ALA A 260           
SHEET    1   E 2 VAL A 375  VAL A 377  0                                        
SHEET    2   E 2 VAL A 380  VAL A 382 -1  O  VAL A 382   N  VAL A 375           
SHEET    1   F 5 VAL B 176  VAL B 178  0                                        
SHEET    2   F 5 PHE B 149  VAL B 154  1  N  ILE B 152   O  PHE B 177           
SHEET    3   F 5 ILE B 123  VAL B 129  1  N  TYR B 125   O  PHE B 149           
SHEET    4   F 5 TYR B 212  SER B 217  1  O  LEU B 216   N  SER B 126           
SHEET    5   F 5 VAL B 290  THR B 292 -1  O  VAL B 291   N  LEU B 213           
SHEET    1   G 3 ASP B 220  PRO B 222  0                                        
SHEET    2   G 3 PHE B 398  ASN B 400 -1  O  ALA B 399   N  PHE B 221           
SHEET    3   G 3 ARG B 352  PHE B 353  1  N  PHE B 353   O  PHE B 398           
SHEET    1   H 2 GLU B 245  LYS B 246  0                                        
SHEET    2   H 2 PHE B 283  SER B 284 -1  O  SER B 284   N  GLU B 245           
SHEET    1   I 2 LYS B 257  VAL B 262  0                                        
SHEET    2   I 2 LYS B 265  VAL B 272 -1  O  LYS B 265   N  VAL B 262           
SHEET    1   J 2 VAL B 375  VAL B 377  0                                        
SHEET    2   J 2 VAL B 380  VAL B 382 -1  O  VAL B 382   N  VAL B 375           
SHEET    1   K 5 VAL C 176  VAL C 178  0                                        
SHEET    2   K 5 PHE C 149  VAL C 154  1  N  ILE C 152   O  PHE C 177           
SHEET    3   K 5 ILE C 123  VAL C 129  1  N  ILE C 127   O  HIS C 153           
SHEET    4   K 5 TYR C 212  SER C 217  1  O  LEU C 216   N  SER C 126           
SHEET    5   K 5 VAL C 290  THR C 292 -1  O  VAL C 291   N  LEU C 213           
SHEET    1   L 3 ASP C 220  PRO C 222  0                                        
SHEET    2   L 3 PHE C 398  ASN C 400 -1  O  ALA C 399   N  PHE C 221           
SHEET    3   L 3 ARG C 352  PHE C 353  1  N  PHE C 353   O  PHE C 398           
SHEET    1   M 2 GLU C 245  LYS C 246  0                                        
SHEET    2   M 2 PHE C 283  SER C 284 -1  O  SER C 284   N  GLU C 245           
SHEET    1   N 2 LYS C 257  VAL C 261  0                                        
SHEET    2   N 2 LEU C 266  VAL C 272 -1  O  THR C 267   N  ALA C 260           
SHEET    1   O 2 VAL C 375  VAL C 377  0                                        
SHEET    2   O 2 VAL C 380  VAL C 382 -1  O  VAL C 382   N  VAL C 375           
SHEET    1   P 5 VAL D 176  VAL D 178  0                                        
SHEET    2   P 5 PHE D 149  VAL D 154  1  N  ILE D 152   O  PHE D 177           
SHEET    3   P 5 ILE D 123  VAL D 129  1  N  ILE D 127   O  CYS D 151           
SHEET    4   P 5 TYR D 212  SER D 217  1  O  LEU D 216   N  SER D 126           
SHEET    5   P 5 VAL D 290  THR D 292 -1  O  VAL D 291   N  LEU D 213           
SHEET    1   Q 3 ASP D 220  PRO D 222  0                                        
SHEET    2   Q 3 PHE D 398  ASN D 400 -1  O  ALA D 399   N  PHE D 221           
SHEET    3   Q 3 ARG D 352  PHE D 353  1  N  PHE D 353   O  PHE D 398           
SHEET    1   R 2 THR D 244  LYS D 246  0                                        
SHEET    2   R 2 PHE D 283  GLY D 285 -1  O  SER D 284   N  GLU D 245           
SHEET    1   S 2 LYS D 257  VAL D 261  0                                        
SHEET    2   S 2 LEU D 266  VAL D 272 -1  O  ILE D 271   N  ARG D 258           
SHEET    1   T 2 VAL D 375  VAL D 377  0                                        
SHEET    2   T 2 VAL D 380  VAL D 382 -1  O  VAL D 382   N  VAL D 375           
SSBOND   1 CYS A   59    CYS A  413                          1555   1555  2.07  
SSBOND   2 CYS A  100    CYS A  172                          1555   1555  2.11  
SSBOND   3 CYS A  151    CYS A  199                          1555   1555  2.14  
SSBOND   4 CYS A  235    CYS B  235                          1555   1555  2.03  
SSBOND   5 CYS A  372    CYS A  381                          1555   1555  2.09  
SSBOND   6 CYS B  100    CYS B  172                          1555   1555  2.07  
SSBOND   7 CYS B  151    CYS B  199                          1555   1555  2.12  
SSBOND   8 CYS B  372    CYS B  381                          1555   1555  2.08  
SSBOND   9 CYS C   59    CYS C  413                          1555   1555  2.07  
SSBOND  10 CYS C  100    CYS C  172                          1555   1555  2.10  
SSBOND  11 CYS C  151    CYS C  199                          1555   1555  2.14  
SSBOND  12 CYS C  235    CYS D  235                          1555   1555  2.02  
SSBOND  13 CYS C  372    CYS C  381                          1555   1555  2.06  
SSBOND  14 CYS D  100    CYS D  172                          1555   1555  2.08  
SSBOND  15 CYS D  151    CYS D  199                          1555   1555  2.12  
SSBOND  16 CYS D  372    CYS D  381                          1555   1555  2.11  
LINK         ND2 ASN A  58                 C1  NAG A 588     1555   1555  1.45  
LINK         ND2 ASN A  95                 C1  NAG E   1     1555   1555  1.44  
LINK         ND2 ASN B  58                 C1  NAG B 592     1555   1555  1.45  
LINK         ND2 ASN C  58                 C1  NAG C 593     1555   1555  1.45  
LINK         ND2 ASN C  95                 C1  NAG F   1     1555   1555  1.44  
LINK         ND2 ASN D  58                 C1  NAG D 597     1555   1555  1.45  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.44  
LINK         O6  NAG E   1                 C1  FUC E   3     1555   1555  1.44  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.44  
LINK         O6  NAG F   1                 C1  FUC F   3     1555   1555  1.45  
LINK         O   ALA A 170                NA    NA A 586     1555   1555  2.42  
LINK         O   PHE A 173                NA    NA A 586     1555   1555  2.44  
LINK         O   VAL A 176                NA    NA A 586     1555   1555  2.41  
LINK         O   HOH A 438                NA    NA A 586     1555   1555  2.40  
LINK         O   HOH A 484                NA    NA A 586     1555   1555  2.32  
LINK         O   HOH C  29                NA    NA C 587     1555   1555  2.21  
LINK         O   ALA C 170                NA    NA C 587     1555   1555  2.41  
LINK         O   PHE C 173                NA    NA C 587     1555   1555  2.44  
LINK         O   VAL C 176                NA    NA C 587     1555   1555  2.42  
CISPEP   1 ASN A  400    LYS A  401          0         4.80                     
CISPEP   2 ASN B  400    LYS B  401          0        -1.10                     
CISPEP   3 ASN C  400    LYS C  401          0         5.25                     
CISPEP   4 ASN D  400    LYS D  401          0        -1.58                     
CRYST1   73.874  101.020  136.612  90.00  93.42  90.00 P 1 21 1      8          
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      0.013537  0.000000  0.000808        0.00000                         
SCALE2      0.000000  0.009899  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007333        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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