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