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Database: PDB
Entry: 6EYJ
LinkDB: 6EYJ
Original site: 6EYJ 
HEADER    CELL ADHESION                           13-NOV-17   6EYJ              
TITLE     E-SELECTIN LECTIN, EGF-LIKE AND TWO SCR DOMAINS COMPLEXED WITH        
TITLE    2 GLYCOMIMETIC LIGAND NV354                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E-SELECTIN;                                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CD62 ANTIGEN-LIKE FAMILY MEMBER E,ENDOTHELIAL LEUKOCYTE     
COMPND   5 ADHESION MOLECULE 1,ELAM-1,LEUKOCYTE-ENDOTHELIAL CELL ADHESION       
COMPND   6 MOLECULE 2,LECAM2;                                                   
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SELE, ELAM1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: CHO;                                    
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1                                  
KEYWDS    CELL ADHESION, CELL-ADHESION MOLECULE, C-TYPE LECTIN, INFLAMMATION,   
KEYWDS   2 LEUKOCYTE, GLYCOMIMETIC, CATCH-BOND                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.P.JAKOB,P.ZIHLMANN,R.C.PRESTON,N.VARGA,B.ERNST,T.MAIER              
REVDAT   1   21-NOV-18 6EYJ    0                                                
JRNL        AUTH   N.VARGA,P.ZIHLMANN,R.C.PRESTON,R.P.JAKOB,T.MAIER,B.ERNST     
JRNL        TITL   E-SELECTIN LECTIN WITH DIFFERENT GLYCOMIMETIC LIGANDS        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.22                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 33972                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : FREE R-VALUE                   
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.221                          
REMARK   3   R VALUE            (WORKING SET)  : 0.219                          
REMARK   3   FREE R VALUE                      : 0.259                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.860                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1650                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 17                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.20                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.27                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 97.41                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2888                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2671                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2756                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2663                   
REMARK   3   BIN FREE R VALUE                        : 0.2837                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.57                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 132                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4358                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 284                                     
REMARK   3   SOLVENT ATOMS            : 252                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 12.48320                                             
REMARK   3    B22 (A**2) : -3.90060                                             
REMARK   3    B33 (A**2) : -8.58260                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.18620                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.370               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.286               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.216               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.280               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.216               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4792   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 6564   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2172   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 134    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 680    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4792   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 682    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 5302   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.12                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.40                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.89                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|1 - A|52 }                                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -14.2179  -52.8042   79.8190           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2593 T22:   -0.0897                                    
REMARK   3     T33:   -0.1406 T12:    0.0761                                    
REMARK   3     T13:   -0.0380 T23:   -0.0768                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    9.1645 L22:    3.4916                                    
REMARK   3     L33:    3.9414 L12:   -4.3259                                    
REMARK   3     L13:   -2.1315 L23:    1.1045                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2648 S12:   -0.3476 S13:   -0.2836                     
REMARK   3     S21:   -0.1984 S22:    0.0732 S23:    0.1802                     
REMARK   3     S31:   -0.2966 S32:   -0.4181 S33:    0.1916                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|53 - A|115 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):  -17.3631  -42.2551   87.3866           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0907 T22:    0.0370                                    
REMARK   3     T33:    0.1080 T12:    0.1559                                    
REMARK   3     T13:   -0.0460 T23:   -0.0928                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.7340 L22:    2.0432                                    
REMARK   3     L33:    7.4436 L12:   -1.3699                                    
REMARK   3     L13:    0.5975 L23:    2.3472                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0726 S12:   -0.3325 S13:    0.4730                     
REMARK   3     S21:   -0.3386 S22:   -0.1664 S23:    0.3194                     
REMARK   3     S31:   -1.0634 S32:   -0.2681 S33:    0.0938                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { A|116 - A|167 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   13.1857  -66.3442   76.9954           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3896 T22:   -0.1036                                    
REMARK   3     T33:    0.4012 T12:    0.0439                                    
REMARK   3     T13:    0.0017 T23:    0.0527                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    7.7062 L22:    2.0239                                    
REMARK   3     L33:    0.7059 L12:   -5.4244                                    
REMARK   3     L13:   -0.1517 L23:    0.3677                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0822 S12:   -0.1297 S13:   -0.2208                     
REMARK   3     S21:    0.1755 S22:   -0.0123 S23:   -0.0917                     
REMARK   3     S31:   -0.0870 S32:    0.1928 S33:    0.0945                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { A|168 - A|218 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   37.5237  -77.2349   78.4086           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.4270 T22:   -0.0207                                    
REMARK   3     T33:    0.3398 T12:    0.0712                                    
REMARK   3     T13:    0.0684 T23:    0.2303                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   10.4039 L22:    0.0000                                    
REMARK   3     L33:    0.4578 L12:   -3.4975                                    
REMARK   3     L13:    3.3771 L23:    1.0027                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0509 S12:   -0.1061 S13:   -0.0595                     
REMARK   3     S21:    0.0269 S22:    0.0560 S23:    0.2876                     
REMARK   3     S31:    0.0267 S32:    0.3409 S33:   -0.0051                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { A|219 - A|280 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   72.3941  -90.5511   77.0689           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3981 T22:   -0.2842                                    
REMARK   3     T33:    0.5096 T12:    0.0617                                    
REMARK   3     T13:    0.0950 T23:    0.1812                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   12.3672 L22:    8.4119                                    
REMARK   3     L33:    3.8578 L12:   -0.0867                                    
REMARK   3     L13:    3.1553 L23:    2.9391                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2356 S12:   -0.3439 S13:   -1.2190                     
REMARK   3     S21:   -0.0599 S22:    0.3805 S23:   -1.6401                     
REMARK   3     S31:    0.3191 S32:   -0.0139 S33:   -0.6161                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { B|1 - B|52 }                                         
REMARK   3    ORIGIN FOR THE GROUP (A):    5.2700  -51.2507   59.9256           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2167 T22:   -0.2977                                    
REMARK   3     T33:   -0.1407 T12:   -0.0383                                    
REMARK   3     T13:   -0.0304 T23:    0.1354                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    9.3481 L22:    3.2186                                    
REMARK   3     L33:    3.0856 L12:    2.8803                                    
REMARK   3     L13:   -2.0186 L23:   -0.0666                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1425 S12:    0.0457 S13:    0.1607                     
REMARK   3     S21:    0.2919 S22:   -0.1662 S23:   -0.3496                     
REMARK   3     S31:   -0.1304 S32:    0.0246 S33:    0.0237                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { B|53 - B|115 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):    8.5288  -40.0409   53.6483           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0374 T22:   -0.2643                                    
REMARK   3     T33:    0.0499 T12:   -0.0259                                    
REMARK   3     T13:    0.0797 T23:    0.1327                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.0315 L22:    5.4054                                    
REMARK   3     L33:    7.8467 L12:    0.9011                                    
REMARK   3     L13:   -1.1812 L23:   -0.6674                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.3841 S12:    0.2387 S13:    0.8302                     
REMARK   3     S21:    0.3484 S22:   -0.1718 S23:    0.0308                     
REMARK   3     S31:   -1.3003 S32:   -0.2117 S33:   -0.2122                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: { B|116 - B|167 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -22.1718  -65.1554   60.7764           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2830 T22:   -0.2058                                    
REMARK   3     T33:    0.4721 T12:   -0.0588                                    
REMARK   3     T13:   -0.0221 T23:    0.0462                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   12.9702 L22:    1.2791                                    
REMARK   3     L33:    0.3103 L12:    5.8571                                    
REMARK   3     L13:    1.1830 L23:    0.2752                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0582 S12:   -0.0347 S13:   -0.6111                     
REMARK   3     S21:   -0.0710 S22:    0.0873 S23:    0.1074                     
REMARK   3     S31:   -0.0828 S32:   -0.1798 S33:   -0.1455                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: { B|168 - B|218 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -46.5701  -75.5701   57.8292           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2997 T22:   -0.1823                                    
REMARK   3     T33:    0.4508 T12:   -0.0584                                    
REMARK   3     T13:    0.0216 T23:   -0.0292                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.2574 L22:    0.0000                                    
REMARK   3     L33:    0.2084 L12:    1.2473                                    
REMARK   3     L13:    1.7700 L23:    0.0489                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0117 S12:   -0.4772 S13:   -0.5143                     
REMARK   3     S21:   -0.1403 S22:   -0.2215 S23:   -0.4642                     
REMARK   3     S31:    0.0070 S32:   -0.1933 S33:    0.2098                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: { B|219 - B|280 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -81.5180  -89.0114   56.4812           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1564 T22:   -0.1971                                    
REMARK   3     T33:    0.5098 T12:   -0.0427                                    
REMARK   3     T13:    0.0939 T23:   -0.0138                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   10.5731 L22:    9.0205                                    
REMARK   3     L33:    4.6886 L12:    0.5220                                    
REMARK   3     L13:    5.4958 L23:    0.1564                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0588 S12:    0.1694 S13:   -1.0967                     
REMARK   3     S21:    0.1337 S22:    0.1863 S23:    1.5164                     
REMARK   3     S31:    0.2475 S32:   -0.2620 S33:   -0.2451                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6EYJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-NOV-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200007439.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00003                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DIALS                              
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33972                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.220                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.18000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
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: 4C16                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M CACL2, 0.1 M MOPS PH 6.2, 11-14%    
REMARK 280  PEG8000, AFTER MICROSEEDING, VAPOR DIFFUSION, SITTING DROP,         
REMARK 280  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       35.52000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   SG   CYS B   234     SG   CYS B   247              1.67            
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  29      -79.58    -96.22                                   
REMARK 500    GLN A  30      106.42     73.46                                   
REMARK 500    TYR A  48     -160.74     69.38                                   
REMARK 500    LYS A  86      156.28     64.71                                   
REMARK 500    SER A 128       19.35     57.43                                   
REMARK 500    ASN A 139     -129.60   -158.62                                   
REMARK 500    HIS A 167       23.68     83.73                                   
REMARK 500    ASN A 244       -4.12     90.60                                   
REMARK 500    ALA B  28     -100.24   -110.79                                   
REMARK 500    ILE B  29       99.98    -22.84                                   
REMARK 500    TYR B  48     -167.27     66.58                                   
REMARK 500    LYS B  86      155.44     65.32                                   
REMARK 500    SER B 128       16.56     58.36                                   
REMARK 500    ASN B 139     -130.17   -158.10                                   
REMARK 500    HIS B 167       21.47     83.11                                   
REMARK 500    TYR B 181      129.43    -39.62                                   
REMARK 500    ASN B 244       -5.64     91.51                                   
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                              CA A 309  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  80   OE1                                                    
REMARK 620 2 ASN A  82   OD1  68.4                                              
REMARK 620 3 GLU A  88   OE1 136.8  79.4                                        
REMARK 620 4 ASN A 105   OD1  67.6 131.0 149.5                                  
REMARK 620 5 ASP A 106   O   129.3 153.7  74.9  74.6                            
REMARK 620 6 ASP A 106   OD1  72.1  93.8  82.4  92.5  77.1                      
REMARK 620 7 C5H A 308   OBB  67.2  70.6 128.0  73.4 131.4 139.4                
REMARK 620 8 C5H A 308   OBD 128.9 114.2  90.0  79.1  72.0 149.2  66.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 309  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  80   OE1                                                    
REMARK 620 2 ASN B  82   OD1  72.6                                              
REMARK 620 3 GLU B  88   OE1 140.2  81.1                                        
REMARK 620 4 ASN B 105   OD1  67.3 138.0 139.5                                  
REMARK 620 5 ASP B 106   O   127.6 143.8  64.7  74.8                            
REMARK 620 6 ASP B 106   OD1  73.4  90.9  77.7  89.4  71.3                      
REMARK 620 7 C5H B 308   OBB  69.8  74.8 131.2  80.1 137.0 143.1                
REMARK 620 8 C5H B 308   OBD 134.2 118.4  84.6  83.3  71.7 143.0  71.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue C5H A 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 309                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue C5H B 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 309                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 305 bound   
REMARK 800  to ASN A 4                                                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 306 bound   
REMARK 800  to ASN A 124                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 302 bound   
REMARK 800  to ASN A 139                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 303 bound   
REMARK 800  to ASN A 158                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 304 bound   
REMARK 800  to ASN A 178                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 301 bound   
REMARK 800  to ASN A 182                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 307 bound   
REMARK 800  to ASN A 244                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 305 bound   
REMARK 800  to ASN B 4                                                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 306 bound   
REMARK 800  to ASN B 124                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 302 bound   
REMARK 800  to ASN B 139                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 303 bound   
REMARK 800  to ASN B 158                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 304 bound   
REMARK 800  to ASN B 178                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 301 bound   
REMARK 800  to ASN B 182                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 307 bound   
REMARK 800  to ASN B 244                                                        
DBREF  6EYJ A    1   280  UNP    P16581   LYAM2_HUMAN     22    301             
DBREF  6EYJ B    1   280  UNP    P16581   LYAM2_HUMAN     22    301             
SEQRES   1 A  280  TRP SER TYR ASN THR SER THR GLU ALA MET THR TYR ASP          
SEQRES   2 A  280  GLU ALA SER ALA TYR CYS GLN GLN ARG TYR THR HIS LEU          
SEQRES   3 A  280  VAL ALA ILE GLN ASN LYS GLU GLU ILE GLU TYR LEU ASN          
SEQRES   4 A  280  SER ILE LEU SER TYR SER PRO SER TYR TYR TRP ILE GLY          
SEQRES   5 A  280  ILE ARG LYS VAL ASN ASN VAL TRP VAL TRP VAL GLY THR          
SEQRES   6 A  280  GLN LYS PRO LEU THR GLU GLU ALA LYS ASN TRP ALA PRO          
SEQRES   7 A  280  GLY GLU PRO ASN ASN ARG GLN LYS ASP GLU ASP CYS VAL          
SEQRES   8 A  280  GLU ILE TYR ILE LYS ARG GLU LYS ASP VAL GLY MET TRP          
SEQRES   9 A  280  ASN ASP GLU ARG CYS SER LYS LYS LYS LEU ALA LEU CYS          
SEQRES  10 A  280  TYR THR ALA ALA CYS THR ASN THR SER CYS SER GLY HIS          
SEQRES  11 A  280  GLY GLU CYS VAL GLU THR ILE ASN ASN TYR THR CYS LYS          
SEQRES  12 A  280  CYS ASP PRO GLY PHE SER GLY LEU LYS CYS GLU GLN ILE          
SEQRES  13 A  280  VAL ASN CYS THR ALA LEU GLU SER PRO GLU HIS GLY SER          
SEQRES  14 A  280  LEU VAL CYS SER HIS PRO LEU GLY ASN PHE SER TYR ASN          
SEQRES  15 A  280  SER SER CYS SER ILE SER CYS ASP ARG GLY TYR LEU PRO          
SEQRES  16 A  280  SER SER MET GLU THR MET GLN CYS MET SER SER GLY GLU          
SEQRES  17 A  280  TRP SER ALA PRO ILE PRO ALA CYS ASN VAL VAL GLU CYS          
SEQRES  18 A  280  ASP ALA VAL THR ASN PRO ALA ASN GLY PHE VAL GLU CYS          
SEQRES  19 A  280  PHE GLN ASN PRO GLY SER PHE PRO TRP ASN THR THR CYS          
SEQRES  20 A  280  THR PHE ASP CYS GLU GLU GLY PHE GLU LEU MET GLY ALA          
SEQRES  21 A  280  GLN SER LEU GLN CYS THR SER SER GLY ASN TRP ASP ASN          
SEQRES  22 A  280  GLU LYS PRO THR CYS LYS ALA                                  
SEQRES   1 B  280  TRP SER TYR ASN THR SER THR GLU ALA MET THR TYR ASP          
SEQRES   2 B  280  GLU ALA SER ALA TYR CYS GLN GLN ARG TYR THR HIS LEU          
SEQRES   3 B  280  VAL ALA ILE GLN ASN LYS GLU GLU ILE GLU TYR LEU ASN          
SEQRES   4 B  280  SER ILE LEU SER TYR SER PRO SER TYR TYR TRP ILE GLY          
SEQRES   5 B  280  ILE ARG LYS VAL ASN ASN VAL TRP VAL TRP VAL GLY THR          
SEQRES   6 B  280  GLN LYS PRO LEU THR GLU GLU ALA LYS ASN TRP ALA PRO          
SEQRES   7 B  280  GLY GLU PRO ASN ASN ARG GLN LYS ASP GLU ASP CYS VAL          
SEQRES   8 B  280  GLU ILE TYR ILE LYS ARG GLU LYS ASP VAL GLY MET TRP          
SEQRES   9 B  280  ASN ASP GLU ARG CYS SER LYS LYS LYS LEU ALA LEU CYS          
SEQRES  10 B  280  TYR THR ALA ALA CYS THR ASN THR SER CYS SER GLY HIS          
SEQRES  11 B  280  GLY GLU CYS VAL GLU THR ILE ASN ASN TYR THR CYS LYS          
SEQRES  12 B  280  CYS ASP PRO GLY PHE SER GLY LEU LYS CYS GLU GLN ILE          
SEQRES  13 B  280  VAL ASN CYS THR ALA LEU GLU SER PRO GLU HIS GLY SER          
SEQRES  14 B  280  LEU VAL CYS SER HIS PRO LEU GLY ASN PHE SER TYR ASN          
SEQRES  15 B  280  SER SER CYS SER ILE SER CYS ASP ARG GLY TYR LEU PRO          
SEQRES  16 B  280  SER SER MET GLU THR MET GLN CYS MET SER SER GLY GLU          
SEQRES  17 B  280  TRP SER ALA PRO ILE PRO ALA CYS ASN VAL VAL GLU CYS          
SEQRES  18 B  280  ASP ALA VAL THR ASN PRO ALA ASN GLY PHE VAL GLU CYS          
SEQRES  19 B  280  PHE GLN ASN PRO GLY SER PHE PRO TRP ASN THR THR CYS          
SEQRES  20 B  280  THR PHE ASP CYS GLU GLU GLY PHE GLU LEU MET GLY ALA          
SEQRES  21 B  280  GLN SER LEU GLN CYS THR SER SER GLY ASN TRP ASP ASN          
SEQRES  22 B  280  GLU LYS PRO THR CYS LYS ALA                                  
HET    NAG  A 301      14                                                       
HET    NAG  A 302      14                                                       
HET    NAG  A 303      14                                                       
HET    NAG  A 304      14                                                       
HET    NAG  A 305      14                                                       
HET    NAG  A 306      14                                                       
HET    NAG  A 307      14                                                       
HET    C5H  A 308      43                                                       
HET     CA  A 309       1                                                       
HET    NAG  B 301      14                                                       
HET    NAG  B 302      14                                                       
HET    NAG  B 303      14                                                       
HET    NAG  B 304      14                                                       
HET    NAG  B 305      14                                                       
HET    NAG  B 306      14                                                       
HET    NAG  B 307      14                                                       
HET    C5H  B 308      43                                                       
HET     CA  B 309       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     C5H (2~{S})-3-CYCLOHEXYL-2-[(2~{R},3~{S},4~{S},5~{R},                
HETNAM   2 C5H  6~{R})-2-(HYDROXYMETHYL)-3,5-BIS(OXIDANYL)-6-[(1~{R},           
HETNAM   3 C5H  2~{R})-2-[(2~{R},3~{S},4~{R},5~{S},6~{R})-3,4,5-                
HETNAM   4 C5H  TRIS(OXIDANYL)-6-(TRIFLUOROMETHYL)OXAN-2-                       
HETNAM   5 C5H  YL]OXYCYCLOHEXYL]OXY-OXAN-4-YL]OXY-PROPANOIC ACID               
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  NAG    14(C8 H15 N O6)                                              
FORMUL  10  C5H    2(C27 H43 F3 O13)                                            
FORMUL  11   CA    2(CA 2+)                                                     
FORMUL  21  HOH   *252(H2 O)                                                    
HELIX    1 AA1 THR A   11  ARG A   22  1                                  12    
HELIX    2 AA2 ASN A   31  LEU A   42  1                                  12    
HELIX    3 AA3 THR B   11  ARG B   22  1                                  12    
HELIX    4 AA4 ASN B   31  LEU B   42  1                                  12    
SHEET    1 AA1 5 SER A   2  THR A   5  0                                        
SHEET    2 AA1 5 LEU A 114  THR A 119 -1  O  CYS A 117   N  ASN A   4           
SHEET    3 AA1 5 TYR A  49  VAL A  56  1  N  TRP A  50   O  LEU A 114           
SHEET    4 AA1 5 VAL A  59  TRP A  62 -1  O  VAL A  59   N  VAL A  56           
SHEET    5 AA1 5 LYS A  67  PRO A  68 -1  O  LYS A  67   N  TRP A  62           
SHEET    1 AA2 5 HIS A  25  LEU A  26  0                                        
SHEET    2 AA2 5 LEU A 114  THR A 119 -1  O  TYR A 118   N  HIS A  25           
SHEET    3 AA2 5 TYR A  49  VAL A  56  1  N  TRP A  50   O  LEU A 114           
SHEET    4 AA2 5 CYS A  90  ILE A  93 -1  O  ILE A  93   N  TYR A  49           
SHEET    5 AA2 5 TRP A 104  GLU A 107 -1  O  GLU A 107   N  CYS A  90           
SHEET    1 AA3 2 GLY A 131  GLU A 135  0                                        
SHEET    2 AA3 2 TYR A 140  CYS A 144 -1  O  THR A 141   N  VAL A 134           
SHEET    1 AA4 2 PHE A 148  SER A 149  0                                        
SHEET    2 AA4 2 GLN A 155  ILE A 156 -1  O  GLN A 155   N  SER A 149           
SHEET    1 AA5 3 GLY A 168  SER A 173  0                                        
SHEET    2 AA5 3 SER A 184  CYS A 189 -1  O  SER A 184   N  SER A 173           
SHEET    3 AA5 3 MET A 201  GLN A 202 -1  O  MET A 201   N  CYS A 185           
SHEET    1 AA6 2 TYR A 193  PRO A 195  0                                        
SHEET    2 AA6 2 CYS A 216  VAL A 218 -1  O  ASN A 217   N  LEU A 194           
SHEET    1 AA7 3 GLY A 230  GLU A 233  0                                        
SHEET    2 AA7 3 THR A 246  CYS A 251 -1  O  THR A 248   N  GLU A 233           
SHEET    3 AA7 3 SER A 262  GLN A 264 -1  O  LEU A 263   N  CYS A 247           
SHEET    1 AA8 2 GLU A 256  MET A 258  0                                        
SHEET    2 AA8 2 THR A 277  LYS A 279 -1  O  THR A 277   N  MET A 258           
SHEET    1 AA9 4 SER B   2  THR B   5  0                                        
SHEET    2 AA9 4 LEU B 114  THR B 119 -1  O  CYS B 117   N  ASN B   4           
SHEET    3 AA9 4 TYR B  49  VAL B  56  1  N  TRP B  50   O  LEU B 114           
SHEET    4 AA9 4 VAL B  59  TRP B  62 -1  O  VAL B  59   N  VAL B  56           
SHEET    1 AB1 5 HIS B  25  LEU B  26  0                                        
SHEET    2 AB1 5 LEU B 114  THR B 119 -1  O  TYR B 118   N  HIS B  25           
SHEET    3 AB1 5 TYR B  49  VAL B  56  1  N  TRP B  50   O  LEU B 114           
SHEET    4 AB1 5 CYS B  90  ILE B  93 -1  O  ILE B  93   N  TYR B  49           
SHEET    5 AB1 5 TRP B 104  GLU B 107 -1  O  GLU B 107   N  CYS B  90           
SHEET    1 AB2 2 GLY B 131  GLU B 135  0                                        
SHEET    2 AB2 2 TYR B 140  CYS B 144 -1  O  THR B 141   N  VAL B 134           
SHEET    1 AB3 2 PHE B 148  SER B 149  0                                        
SHEET    2 AB3 2 GLN B 155  ILE B 156 -1  O  GLN B 155   N  SER B 149           
SHEET    1 AB4 3 GLY B 168  SER B 173  0                                        
SHEET    2 AB4 3 SER B 184  CYS B 189 -1  O  SER B 184   N  SER B 173           
SHEET    3 AB4 3 MET B 201  GLN B 202 -1  O  MET B 201   N  CYS B 185           
SHEET    1 AB5 2 TYR B 193  PRO B 195  0                                        
SHEET    2 AB5 2 CYS B 216  VAL B 218 -1  O  ASN B 217   N  LEU B 194           
SHEET    1 AB6 3 GLY B 230  GLU B 233  0                                        
SHEET    2 AB6 3 THR B 246  CYS B 251 -1  O  THR B 248   N  GLU B 233           
SHEET    3 AB6 3 SER B 262  GLN B 264 -1  O  LEU B 263   N  CYS B 247           
SHEET    1 AB7 2 GLU B 256  MET B 258  0                                        
SHEET    2 AB7 2 THR B 277  LYS B 279 -1  O  THR B 277   N  MET B 258           
SSBOND   1 CYS A   19    CYS A  117                          1555   1555  2.05  
SSBOND   2 CYS A   90    CYS A  109                          1555   1555  2.04  
SSBOND   3 CYS A  122    CYS A  133                          1555   1555  2.05  
SSBOND   4 CYS A  127    CYS A  142                          1555   1555  2.04  
SSBOND   5 CYS A  144    CYS A  153                          1555   1555  2.05  
SSBOND   6 CYS A  159    CYS A  203                          1555   1555  2.03  
SSBOND   7 CYS A  172    CYS A  185                          1555   1555  2.05  
SSBOND   8 CYS A  189    CYS A  216                          1555   1555  2.05  
SSBOND   9 CYS A  221    CYS A  265                          1555   1555  2.03  
SSBOND  10 CYS A  234    CYS A  247                          1555   1555  2.04  
SSBOND  11 CYS A  251    CYS A  278                          1555   1555  2.04  
SSBOND  12 CYS B   19    CYS B  117                          1555   1555  2.04  
SSBOND  13 CYS B   90    CYS B  109                          1555   1555  2.04  
SSBOND  14 CYS B  122    CYS B  133                          1555   1555  2.04  
SSBOND  15 CYS B  127    CYS B  142                          1555   1555  2.04  
SSBOND  16 CYS B  144    CYS B  153                          1555   1555  2.06  
SSBOND  17 CYS B  159    CYS B  203                          1555   1555  2.03  
SSBOND  18 CYS B  172    CYS B  185                          1555   1555  2.05  
SSBOND  19 CYS B  189    CYS B  216                          1555   1555  2.04  
SSBOND  20 CYS B  221    CYS B  265                          1555   1555  2.01  
SSBOND  21 CYS B  251    CYS B  278                          1555   1555  2.04  
LINK         ND2 ASN A   4                 C1  NAG A 305     1555   1555  1.43  
LINK         OE1 GLU A  80                CA    CA A 309     1555   1555  2.79  
LINK         OD1 ASN A  82                CA    CA A 309     1555   1555  2.60  
LINK         OE1 GLU A  88                CA    CA A 309     1555   1555  2.38  
LINK         OD1 ASN A 105                CA    CA A 309     1555   1555  2.59  
LINK         O   ASP A 106                CA    CA A 309     1555   1555  2.53  
LINK         OD1 ASP A 106                CA    CA A 309     1555   1555  2.25  
LINK         ND2 ASN A 124                 C1  NAG A 306     1555   1555  1.43  
LINK         ND2 ASN A 139                 C1  NAG A 302     1555   1555  1.43  
LINK         ND2 ASN A 158                 C1  NAG A 303     1555   1555  1.44  
LINK         ND2 ASN A 178                 C1  NAG A 304     1555   1555  1.43  
LINK         ND2 ASN A 182                 C1  NAG A 301     1555   1555  1.43  
LINK         ND2 ASN A 244                 C1  NAG A 307     1555   1555  1.43  
LINK         ND2 ASN B   4                 C1  NAG B 305     1555   1555  1.44  
LINK         OE1 GLU B  80                CA    CA B 309     1555   1555  2.67  
LINK         OD1 ASN B  82                CA    CA B 309     1555   1555  2.56  
LINK         OE1 GLU B  88                CA    CA B 309     1555   1555  2.41  
LINK         OD1 ASN B 105                CA    CA B 309     1555   1555  2.54  
LINK         O   ASP B 106                CA    CA B 309     1555   1555  2.64  
LINK         OD1 ASP B 106                CA    CA B 309     1555   1555  2.43  
LINK         ND2 ASN B 124                 C1  NAG B 306     1555   1555  1.43  
LINK         ND2 ASN B 139                 C1  NAG B 302     1555   1555  1.43  
LINK         ND2 ASN B 158                 C1  NAG B 303     1555   1555  1.43  
LINK         ND2 ASN B 178                 C1  NAG B 304     1555   1555  1.44  
LINK         ND2 ASN B 182                 C1  NAG B 301     1555   1555  1.43  
LINK         ND2 ASN B 244                 C1  NAG B 307     1555   1555  1.43  
LINK         OBB C5H A 308                CA    CA A 309     1555   1555  2.63  
LINK         OBD C5H A 308                CA    CA A 309     1555   1555  2.28  
LINK         OBB C5H B 308                CA    CA B 309     1555   1555  2.43  
LINK         OBD C5H B 308                CA    CA B 309     1555   1555  2.21  
CISPEP   1 GLU A   80    PRO A   81          0        -5.92                     
CISPEP   2 GLU B   80    PRO B   81          0        -3.19                     
SITE     1 AC1 14 TYR A  48  GLU A  80  ASN A  82  ARG A  84                    
SITE     2 AC1 14 GLN A  85  GLU A  88  GLU A  92  TYR A  94                    
SITE     3 AC1 14 ARG A  97  ASN A 105  ASP A 106  GLU A 107                    
SITE     4 AC1 14  CA A 309  HOH A 419                                          
SITE     1 AC2  6 GLU A  80  ASN A  82  GLU A  88  ASN A 105                    
SITE     2 AC2  6 ASP A 106  C5H A 308                                          
SITE     1 AC3 13 TYR B  48  GLU B  80  ASN B  82  ARG B  84                    
SITE     2 AC3 13 GLN B  85  GLU B  88  GLU B  92  TYR B  94                    
SITE     3 AC3 13 ARG B  97  ASN B 105  ASP B 106  GLU B 107                    
SITE     4 AC3 13  CA B 309                                                     
SITE     1 AC4  6 GLU B  80  ASN B  82  GLU B  88  ASN B 105                    
SITE     2 AC4  6 ASP B 106  C5H B 308                                          
SITE     1 AC5  4 ASN A   4  ARG A  22  GLU A 208  NAG B 302                    
SITE     1 AC6  1 ASN A 124                                                     
SITE     1 AC7  3 ASN A 139  TYR A 140  NAG B 305                               
SITE     1 AC8  9 SER A 149  GLN A 155  ILE A 156  ASN A 158                    
SITE     2 AC8  9 PRO A 238  NAG A 304  HOH A 408  ASN B 158                    
SITE     3 AC8  9 NAG B 303                                                     
SITE     1 AC9 10 ASN A 178  VAL A 224  VAL A 232  GLU A 233                    
SITE     2 AC9 10 CYS A 234  PHE A 241  NAG A 303  HOH A 403                    
SITE     3 AC9 10 HOH A 446  NAG B 304                                          
SITE     1 AD1  1 ASN A 182                                                     
SITE     1 AD2  4 TYR A 193  TRP A 243  ASN A 244  HOH A 409                    
SITE     1 AD3  6 LEU A 151  NAG A 302  ASN B   4  ARG B  22                    
SITE     2 AD3  6 GLU B 208  HOH B 468                                          
SITE     1 AD4  1 ASN B 124                                                     
SITE     1 AD5  4 NAG A 305  ASN B 139  TYR B 140  HOH B 418                    
SITE     1 AD6  8 ASN A 158  NAG A 303  SER B 149  GLN B 155                    
SITE     2 AD6  8 ILE B 156  ASN B 158  PRO B 238  NAG B 304                    
SITE     1 AD7  9 GLU A 233  NAG A 304  ASN B 178  VAL B 224                    
SITE     2 AD7  9 VAL B 232  CYS B 234  PHE B 241  NAG B 303                    
SITE     3 AD7  9 HOH B 437                                                     
SITE     1 AD8  1 ASN B 182                                                     
SITE     1 AD9  3 TYR B 193  TRP B 243  ASN B 244                               
CRYST1   52.580   71.040   92.160  90.00  93.73  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      0.019019  0.000000  0.001240        0.00000                         
SCALE2      0.000000  0.014077  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010874        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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