Skip to Content

HEADER    CELL ADHESION PROTEIN                   03-JUN-94   1ESL      1ESL   2  

download here the glyco-file =>   

 

 

COMPND    E-SELECTIN (LECTIN AND EGF DOMAINS, RESIDUES 1 - 157)         1ESL   3

 

 

COMPND   2 (FORMERLY KNOWN AS ELAM-1)                                   1ESL   4

 

 

SOURCE    HUMAN (HOMO SAPIENS) RECOMBINANT FORM EXPRESSED IN CHO CELLS  1ESL   5

 

 

AUTHOR    B.J.GRAVES,R.L.CROWTHER                                       1ESL   6

 

 

REVDAT   1   31-AUG-94 1ESL    0                                        1ESL   7

 

 

JRNL        AUTH   B.J.GRAVES,R.L.CROWTHER,C.CHANDRAN,J.M.RUMBERGER,    1ESL   8

 

 

JRNL        AUTH 2 S.LI,K.-S.HUANG,D.H.PRESKY,P.C.FAMILLETTI,           1ESL   9

 

 

JRNL        AUTH 3 B.A.WOLITZKY,D.K.BURNS                               1ESL  10

 

 

JRNL        TITL   INSIGHT INTO E-SELECTIN(SLASH)LIGAND INTERACTION     1ESL  11

 

 

JRNL        TITL 2 FROM THE CRYSTAL STRUCTURE AND MUTAGENESIS OF THE    1ESL  12

 

 

JRNL        TITL 3 LEC(SLASH)EGF DOMAINS                                1ESL  13

 

 

JRNL        REF    NATURE                        V. 367   532 1994      1ESL  14

 

 

JRNL        REFN   ASTM NATUAS  UK ISSN 0028-0836                 0006  1ESL  15

 

 

REMARK   1                                                              1ESL  16

 

 

REMARK   1 REFERENCE 1                                                  1ESL  17

 

 

REMARK   1  AUTH   S.H.LI,D.K.BURNS,J.M.RUMBERGER,D.H.PRESKY,           1ESL  18

 

 

REMARK   1  AUTH 2 V.L.WILKINSON,M.ANOSTARIO JUNIOR,B.A.WOLITZKY,       1ESL  19

 

 

REMARK   1  AUTH 3 C.R.NORTON,P.C.FAMILLETTI,K.J.KIM,                   1ESL  20

 

 

REMARK   1  AUTH 4 A.L.GOLDSTEIN,D.C.COX,K.-S.HUANG                     1ESL  21

 

 

REMARK   1  TITL   CONSENSUS REPEAT DOMAINS OF E-SELECTIN ENHANCE       1ESL  22

 

 

REMARK   1  TITL 2 LIGAND BINDING                                       1ESL  23

 

 

REMARK   1  REF    J.BIOL.CHEM.                  V. 269  4431 1994      1ESL  24

 

 

REMARK   1  REFN   ASTM JBCHA3  US ISSN 0021-9258                 0071  1ESL  25

 

 

REMARK   2                                                              1ESL  26

 

 

REMARK   2 RESOLUTION. 2.0  ANGSTROMS.                                  1ESL  27

 

 

REMARK   3                                                              1ESL  28

 

 

REMARK   3 REFINEMENT.                                                  1ESL  29

 

 

REMARK   3   PROGRAM                    X-PLOR                          1ESL  30

 

 

REMARK   3   AUTHORS                    BRUNGER                         1ESL  31

 

 

REMARK   3   R VALUE (3 SIGMA CUTOFF)   0.164                           1ESL  32

 

 

REMARK   3   R VALUE (USING ALL DATA)   0.173                           1ESL  33

 

 

REMARK   3   RMSD BOND DISTANCES        0.010  ANGSTROMS                1ESL  34

 

 

REMARK   3   RMSD BOND ANGLES           2.60   DEGREES                  1ESL  35

 

 

REMARK   3   FREE R-FACTOR (F>3*SIGMA)  0.239                           1ESL  36

 

 

REMARK   3   FREE R-FACTOR (ALL DATA)   0.249                           1ESL  37

 

 

REMARK   3                                                              1ESL  38

 

 

REMARK   3   NUMBER OF REFLECTIONS      13718                           1ESL  39

 

 

REMARK   3   RESOLUTION RANGE      10.0 - 2.0  ANGSTROMS                1ESL  40

 

 

REMARK   3   DATA CUTOFF                3.     SIGMA(F)                 1ESL  41

 

 

REMARK   3   PERCENT COMPLETION         99.8                            1ESL  42

 

 

REMARK   3                                                              1ESL  43

 

 

REMARK   3   NUMBER OF PROTEIN ATOMS                       1266         1ESL  44

 

 

REMARK   3   NUMBER OF SOLVENT ATOMS                        112         1ESL  45

 

 

REMARK   3                                                              1ESL  46

 

 

REMARK   3  THE STRUCTURE WAS FULLY REFINED USING X-PLOR, BUT DID NOT   1ESL  47

 

 

REMARK   3  EMPLOY THE ENGH & HUBER PARAMETERS.  REFINEMENT             1ESL  48

 

 

REMARK   3  STATISTICS, BROKEN DOWN IN RESOLUTION RANGES, ARE GIVEN IN  1ESL  49

 

 

REMARK   3  THE STRUCTURAL PAPER IN NATURE.                             1ESL  50

 

 

REMARK   4                                                              1ESL  51

 

 

REMARK   4 THE BIOCHEMICAL BACKGROUND FOR THIS PROTEIN IS GIVEN IN THE  1ESL  52

 

 

REMARK   4 PAPER CITED AS REFERENCE 1 ABOVE.  THE PROTEIN WAS           1ESL  53

 

 

REMARK   4 EXPRESSED IN A GLYCOSYLATED FORM IN CHO CELLS AND            1ESL  54

 

 

REMARK   4 ENZYMATICALLY DEGLYCOSYLATED WITH N-GLYCANASE.               1ESL  55

 

 

REMARK   5                                                              1ESL  56

 

 

REMARK   5 THERE ARE THREE ALPHA-HELICAL TWISTS IN THE STRUCTURE -      1ESL  57

 

 

REMARK   5 SEQUENCES IN WHICH THREE CONSECUTIVE RESIDUES HAVE HELICAL   1ESL  58

 

 

REMARK   5 MAIN CHAIN TORSION ANGLES.  TWO OF THESE (VAL 63 - THR 65    1ESL  59

 

 

REMARK   5 AND GLU 71 - ALA 73) ARE RIGHT-HANDED AND HAVE A HYDROGEN    1ESL  60

 

 

REMARK   5 BOND FROM THE CARBONYL OF THE RESIDUE PRIOR TO THE TRIAD TO  1ESL  61

 

 

REMARK   5 THE AMIDE NITROGEN OF THE RESIDUE JUST AFTER THE TRIPLET.    1ESL  62

 

 

REMARK   5 THE OTHER SEQUENCE (CYS 127 - GLY 129) IS LEFT-HANDED WITH   1ESL  63

 

 

REMARK   5 TWO HYDROGEN BONDS FROM O SER 126 TO N GLY 129 AND FROM      1ESL  64

 

 

REMARK   5 O CYS 127 TO N HIS 130.                                      1ESL  65

 

 

REMARK   6                                                              1ESL  66

 

 

REMARK   6 OF THE THREE CALCIUM IONS LOCATED IN THIS STRUCTURE ONLY     1ESL  67

 

 

REMARK   6 ONE, CA 160 (MCA2), IS BELIEVED TO BE PART OF THE NATIVE     1ESL  68

 

 

REMARK   6 STRUCTURE.  THE LIGANDS WHICH BIND TO THIS CALCIUM ARE       1ESL  69

 

 

REMARK   6 DESCRIBED ON THE SITE 1 (S1) RECORD.  THE OTHER TWO CALCIUM  1ESL  70

 

 

REMARK   6 IONS PROBABLY ARE PRESENT ONLY AS A RESULT OF THE HIGH       1ESL  71

 

 

REMARK   6 CALCIUM CONCENTRATION (0.2M) USED IN CRYSTALLIZATION.        1ESL  72

 

 

REMARK   7                                                              1ESL  73

 

 

REMARK   7 THREE WATER MOLECULES (HOH 260, HOH 266 AND HOH 318) HAVE    1ESL  74

 

 

REMARK   7 TEMPERATURE FACTORS ABOVE 60 A**2 BUT ALL THREE MAKE GOOD    1ESL  75

 

 

REMARK   7 HYDROGEN BONDING CONTACTS TO THE PROTEIN.                    1ESL  76

 

 

REMARK   8                                                              1ESL  77

 

 

REMARK   8 CROSS REFERENCE TO SEQUENCE DATABASE                         1ESL  78

 

 

REMARK   8 SWISS-PROT ENTRY NAME       PDB ENTRY CHAIN NAME