HEADER ISOMERASE(PEPTIDYL-PROLYL CIS-TRANS) 30-JUN-92 2CPL COMPND CYCLOPHILIN A SOURCE HUMAN (HOMO SAPIENS) T CELL AUTHOR H.KE REVDAT 1 31-OCT-93 2CPL 0 JRNL AUTH H.KE JRNL TITL SIMILARITIES AND DIFFERENCES BETWEEN HUMAN JRNL TITL 2 CYCLOPHILIN A AND OTHER BETA-BARREL STRUCTURES. JRNL TITL 3 STRUCTURAL REFINEMENT AT 1.63 ANGSTROMS JRNL TITL 4 RESOLUTION JRNL REF J.MOL.BIOL. V. 228 539 1992 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH H.KE,L.D.ZYDOWSKY,J.LIU,C.T.WALSH REMARK 1 TITL CRYSTAL STRUCTURE OF RECOMBINANT HUMAN T CELL REMARK 1 TITL 2 CYCLOPHILIN A AT 2.5 ANGSTROMS RESOLUTION REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 88 9483 1991 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 REMARK 2 REMARK 2 RESOLUTION. 1.63 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM X-PLOR REMARK 3 AUTHORS BRUNGER REMARK 3 R VALUE 0.180 REMARK 3 RMSD BOND DISTANCES 0.013 ANGSTROMS REMARK 3 RMSD BOND ANGLES 2.50 DEGREES REMARK 4 REMARK 4 THE SHEET PRESENTED AS *A* ON SHEET RECORDS BELOW IS REMARK 4 ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS REMARK 4 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND REMARK 4 LAST STRANDS ARE IDENTICAL. SEQRES 1 165 MET VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP SEQRES 2 165 GLY GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA SEQRES 3 165 ASP LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU SEQRES 4 165 SER THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS SEQRES 5 165 PHE HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY SEQRES 6 165 ASP PHE THR ARG HIS ASN GLY THR GLY GLY LYS SER ILE SEQRES 7 165 TYR GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS SEQRES 8 165 HIS THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY SEQRES 9 165 PRO ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA SEQRES 10 165 LYS THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY SEQRES 11 165 LYS VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU SEQRES 12 165 ARG PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE SEQRES 13 165 THR ILE ALA ASP CYS GLY GLN LEU GLU FORMUL 2 HOH *119(H2 O1) HELIX 1 H1 PHE 25 VAL 29 5 HELIX 2 H2 PRO 30 THR 41 1 HELIX 3 H3 THR 119 ASP 123 5 HELIX 4 H4 GLY 135 MET 142 1 HELIX 5 H5 GLU 143 GLY 146 5 SHEET 1 A 9 PRO 4 ALA 11 0 SHEET 2 A 9 PRO 16 LEU 24 -1 SHEET 3 A 9 VAL 127 GLU 134 -1 SHEET 4 A 9 GLY 96 ALA 101 -1 SHEET 5 A 9 GLN 111 THR 116 -1 SHEET 6 A 9 MET 61 GLY 64 -1 SHEET 7 A 9 GLY 50 ILE 56 -1 SHEET 8 A 9 LYS 155 LEU 164 -1 SHEET 9 A 9 PRO 4 ALA 11 -1 TURN 1 T1 VAL 12 GLU 15 TURN 2 T2 GLY 42 GLY 45 TURN 3 T3 ILE 57 PHE 60 TURN 4 T4 SER 147 GLY 150 CRYST1 43.000 52.600 89.200 90.00 90.00 90.00 P 21 21 21 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 0.023256 0.000000 0.000000 0.00000 SCALE2 0.000000 0.019011 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011211 0.00000