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Database: PDB
Entry: 6EYI
LinkDB: 6EYI
Original site: 6EYI 
HEADER    CELL ADHESION                           13-NOV-17   6EYI              
TITLE     E-SELECTIN LECTIN, EGF-LIKE AND TWO SCR DOMAINS COMPLEXED WITH        
TITLE    2 GLYCOMIMETIC LIGAND BW69669                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E-SELECTIN;                                                
COMPND   3 CHAIN: A;                                                            
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_ORGAN: OVARY;                                      
SOURCE   9 EXPRESSION_SYSTEM_CELL: CHO;                                         
SOURCE  10 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 6EYI    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.    2.04 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) : 2.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 21493                          
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)  : 0.225                          
REMARK   3   R VALUE            (WORKING SET)  : 0.224                          
REMARK   3   FREE R VALUE                      : 0.237                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.580                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 985                            
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               : 11                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.04                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.14                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 89.31                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2645                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2573                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2529                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2569                   
REMARK   3   BIN FREE R VALUE                        : 0.2661                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.39                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 116                      
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            : 2179                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 141                                     
REMARK   3   SOLVENT ATOMS            : 127                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 52.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -16.79330                                            
REMARK   3    B22 (A**2) : -0.75060                                             
REMARK   3    B33 (A**2) : 17.54390                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.05720                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.380               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.214               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.165               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.211               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.165               
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      : 0.931                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2393   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3276   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1085   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 67     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 340    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2393   ; 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   : 328    ; 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   : 2741   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.08                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.30                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.79                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|4 - A|31 }                                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -16.3571  -15.9011   37.3155           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2239 T22:   -0.1943                                    
REMARK   3     T33:   -0.1996 T12:   -0.0901                                    
REMARK   3     T13:    0.0397 T23:    0.0574                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    9.0118 L22:   10.6180                                    
REMARK   3     L33:    7.9879 L12:    1.7812                                    
REMARK   3     L13:   -1.0752 L23:    0.1464                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2143 S12:   -0.3895 S13:    0.2796                     
REMARK   3     S21:    0.2668 S22:   -0.0829 S23:   -0.0789                     
REMARK   3     S31:   -0.3658 S32:   -0.2842 S33:   -0.1314                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|32 - A|115 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):  -17.0613  -29.5139   37.1267           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1392 T22:   -0.2796                                    
REMARK   3     T33:   -0.0357 T12:   -0.1037                                    
REMARK   3     T13:   -0.0390 T23:    0.1497                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    6.7650 L22:    2.2120                                    
REMARK   3     L33:    3.3005 L12:    1.5797                                    
REMARK   3     L13:   -1.7653 L23:   -0.5111                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1387 S12:   -0.2918 S13:   -1.0911                     
REMARK   3     S21:    0.3048 S22:   -0.2681 S23:   -0.4779                     
REMARK   3     S31:    0.4665 S32:   -0.1093 S33:    0.1294                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { A|116 - A|167 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   -8.7196   -6.1423    7.8448           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.2771 T22:   -0.1664                                    
REMARK   3     T33:   -0.2108 T12:   -0.0465                                    
REMARK   3     T13:    0.0145 T23:    0.0648                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8208 L22:    2.0484                                    
REMARK   3     L33:    9.2048 L12:    1.0783                                    
REMARK   3     L13:   -1.4172 L23:   -5.7578                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0055 S12:    0.1709 S13:    0.0135                     
REMARK   3     S21:   -0.0755 S22:    0.1806 S23:    0.3447                     
REMARK   3     S31:   -0.5528 S32:   -0.0526 S33:   -0.1861                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { A|168 - A|218 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   -9.1853    4.6162  -16.6594           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1247 T22:   -0.1335                                    
REMARK   3     T33:   -0.2753 T12:   -0.0227                                    
REMARK   3     T13:    0.0333 T23:    0.0561                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4552 L22:    0.0000                                    
REMARK   3     L33:    8.3554 L12:    0.1689                                    
REMARK   3     L13:    0.3971 L23:    0.1229                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1196 S12:    0.2963 S13:    0.0528                     
REMARK   3     S21:    0.4342 S22:    0.0148 S23:    0.2422                     
REMARK   3     S31:    0.1456 S32:   -0.4078 S33:   -0.1344                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { A|219 - A|280 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   -6.2947   17.9987  -51.6970           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0910 T22:   -0.2929                                    
REMARK   3     T33:   -0.3193 T12:    0.0219                                    
REMARK   3     T13:    0.1314 T23:    0.0700                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.4608 L22:    9.1516                                    
REMARK   3     L33:    7.7654 L12:    1.8764                                    
REMARK   3     L13:    3.7545 L23:   -1.8074                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.3858 S12:    0.1393 S13:    0.2960                     
REMARK   3     S21:   -1.0701 S22:    0.5710 S23:   -0.2921                     
REMARK   3     S31:   -1.0993 S32:   -0.0154 S33:   -0.1852                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6EYI 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_1200007437.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-11                          
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) : 0.99999                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21493                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.14800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.84900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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   (%): 56.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
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: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       46.79500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.47000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       46.79500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       36.47000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 KCAL/MOL                         
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 405  LIES ON A SPECIAL POSITION.                          
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      106.62     33.85                                   
REMARK 500    TYR A  48     -159.00     67.54                                   
REMARK 500    LYS A  86      160.18     63.61                                   
REMARK 500    ASN A 139     -129.63   -160.85                                   
REMARK 500    HIS A 167       22.86     86.76                                   
REMARK 500    ASN A 244       -8.40     92.86                                   
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   OE2                                                    
REMARK 620 2 ASN A  82   OD1  68.6                                              
REMARK 620 3 GLU A  88   OE1 139.5  82.6                                        
REMARK 620 4 ASN A 105   OD1  59.0 123.0 153.9                                  
REMARK 620 5 ASP A 106   O   120.3 160.8  80.7  73.3                            
REMARK 620 6 ASP A 106   OD1  67.3  91.8  86.4  87.9  77.9                      
REMARK 620 7 C4Z A 308   OBG  68.8  75.6 131.8  66.3 122.9 135.9                
REMARK 620 8 C4Z A 308   OBF 124.7 118.9  93.7  78.5  71.7 149.1  62.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 311  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 168   O                                                      
REMARK 620 2 HOH A 429   O    65.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue C4Z 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 CA A 310                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 311                  
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                                                        
DBREF  6EYI A    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                                  
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    C4Z  A 308      40                                                       
HET     CA  A 309       1                                                       
HET     CA  A 310       1                                                       
HET     CA  A 311       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     C4Z (2~{R})-3-CYCLOHEXYL-2-[(2~{R},3~{S},4~{S},5~{R},                
HETNAM   2 C4Z  6~{R})-2-(HYDROXYMETHYL)-6-[(1~{R},2~{R})-2-[(2~{S},            
HETNAM   3 C4Z  3~{S},4~{R},5~{S},6~{S})-6-METHYL-3,4,5-                        
HETNAM   4 C4Z  TRIS(OXIDANYL)OXAN-2-YL]OXYCYCLOHEXYL]OXY-3,5-                  
HETNAM   5 C4Z  BIS(OXIDANYL)OXAN-4-YL]OXY-PROPANOIC ACID                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   2  NAG    7(C8 H15 N O6)                                               
FORMUL   9  C4Z    C27 H46 O13                                                  
FORMUL  10   CA    3(CA 2+)                                                     
FORMUL  13  HOH   *127(H2 O)                                                    
HELIX    1 AA1 THR A   11  ARG A   22  1                                  12    
HELIX    2 AA2 ASN A   31  LEU A   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  61   N  ARG A  54           
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  ASP A 250   N  PHE A 231           
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           
SSBOND   1 CYS A   19    CYS A  117                          1555   1555  2.05  
SSBOND   2 CYS A   90    CYS A  109                          1555   1555  2.05  
SSBOND   3 CYS A  122    CYS A  133                          1555   1555  2.04  
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  2.04  
SSBOND   9 CYS A  221    CYS A  265                          1555   1555  2.03  
SSBOND  10 CYS A  234    CYS A  247                          1555   1555  2.05  
SSBOND  11 CYS A  251    CYS A  278                          1555   1555  2.03  
LINK         ND2 ASN A   4                 C1  NAG A 305     1555   1555  1.44  
LINK         OE2 GLU A  80                CA    CA A 309     1555   1555  2.87  
LINK         OD1 ASN A  82                CA    CA A 309     1555   1555  2.50  
LINK         OE1 GLU A  88                CA    CA A 309     1555   1555  2.22  
LINK         OD2 ASP A  89                CA    CA A 310     1555   1555  2.99  
LINK         OD1 ASN A 105                CA    CA A 309     1555   1555  2.78  
LINK         O   ASP A 106                CA    CA A 309     1555   1555  2.46  
LINK         OD1 ASP A 106                CA    CA A 309     1555   1555  2.26  
LINK         ND2 ASN A 124                 C1  NAG A 306     1555   1555  1.43  
LINK         ND2 ASN A 139                 C1  NAG A 302     1555   1555  1.44  
LINK         ND2 ASN A 158                 C1  NAG A 303     1555   1555  1.43  
LINK         O   GLY A 168                CA    CA A 311     1555   1555  2.44  
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         OBG C4Z A 308                CA    CA A 309     1555   1555  2.73  
LINK         OBF C4Z A 308                CA    CA A 309     1555   1555  2.56  
LINK        CA    CA A 311                 O   HOH A 429     1555   1555  3.02  
CISPEP   1 GLU A   80    PRO A   81          0        -4.02                     
SITE     1 AC1 13 TYR A  48  GLU A  80  ASN A  82  GLN A  85                    
SITE     2 AC1 13 GLU A  88  GLU A  92  TYR A  94  ARG A  97                    
SITE     3 AC1 13 GLU A  98  ASN A 105  ASP A 106  GLU A 107                    
SITE     4 AC1 13  CA A 309                                                     
SITE     1 AC2  6 GLU A  80  ASN A  82  GLU A  88  ASN A 105                    
SITE     2 AC2  6 ASP A 106  C4Z A 308                                          
SITE     1 AC3  3 ASP A  87  ASP A  89  ASP A 222                               
SITE     1 AC4  2 GLY A 168  HOH A 429                                          
SITE     1 AC5  6 ASN A   4  ARG A  22  LEU A 151  GLU A 208                    
SITE     2 AC5  6 NAG A 302  HOH A 408                                          
SITE     1 AC6  3 GLU A  71  LYS A  74  ASN A 124                               
SITE     1 AC7  4 ASN A 139  TYR A 140  NAG A 305  HOH A 455                    
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 411  HOH A 414                    
SITE     3 AC8  9 HOH A 424                                                     
SITE     1 AC9  9 ASN A 178  VAL A 224  VAL A 232  GLU A 233                    
SITE     2 AC9  9 CYS A 234  PHE A 241  NAG A 303  HOH A 414                    
SITE     3 AC9  9 HOH A 443                                                     
SITE     1 AD1  1 ASN A 182                                                     
SITE     1 AD2  3 TYR A 193  ASN A 244  HOH A 444                               
CRYST1   93.590   72.940   52.520  90.00  94.16  90.00 C 1 2 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      0.010685  0.000000  0.000777        0.00000                         
SCALE2      0.000000  0.013710  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019091        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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