HEADER T-CELL SURFACE GLYCOPROTEIN 30-JUL-92 3CD4 COMPND CD4 (N-TERMINAL FRAGMENT CONSISTING OF RESIDUES 1-182) SOURCE HUMAN (HOMO SAPIENS) RECOMBINANT FORM EXPRESSED IN SOURCE 2 CHINESE HAMSTER (CRICETULUS GRISEUS) OVARY CELLS AUTHOR T.P.J.GARRETT,J.WANG,Y.YAN,S.C.HARRISON REVDAT 1 31-OCT-93 3CD4 0 SPRSDE 15-OCT-93 3CD4 2CD4 JRNL AUTH T.P.J.GARRETT,J.WANG,Y.YAN,J.LIU,S.C.HARRISON JRNL TITL REFINEMENT AND ANALYSIS OF THE FIRST TWO DOMAINS JRNL TITL 2 OF HUMAN CD4 JRNL REF TO BE PUBLISHED JRNL REFN 353 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.WANG,Y.YAN,T.P.J.GARRETT,J.LIU,D.RODGERS, REMARK 1 AUTH 2 R.L.GARLICK,G.E.TARR,Y.HUSAIN,E.L.REINHERZ, REMARK 1 AUTH 3 S.C.HARRISON REMARK 1 TITL ATOMIC STRUCTURE OF A FRAGMENT OF HUMAN CD4 REMARK 1 TITL 2 CONTAINING TWO IMMUNOGLOBULIN-LIKE DOMAINS REMARK 1 REF NATURE V. 348 411 1990 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 REMARK 2 REMARK 2 RESOLUTION. 2.2 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM X-PLOR REMARK 3 AUTHORS BRUNGER REMARK 3 R VALUE 0.197 REMARK 3 RMSD BOND DISTANCES 0.015 ANGSTROMS REMARK 3 RMSD BOND ANGLES 2.42 DEGREES REMARK 3 REMARK 3 AN OVERALL ANISOTROPIC THERMAL FACTOR WAS REFINED USING REMARK 3 X-PLOR AND THE DIFFERENCE IN SEMI AXES WAS DELTA B = REMARK 3 10.8 ANGSTROMS SQUARED. REMARK 4 REMARK 4 FRAGMENTS OF CD4 WERE OBTAINED FROM TWO SOURCES (1 - 182 REMARK 4 EXPRESSED IN CHINESE HAMSTER OVARY (CHO) CELLS AND REMARK 4 MET + 1 - 183 EXPRESSED IN ESCHERICHIA COLI) AND BOTH REMARK 4 CRYSTALLIZED IN THE THREE POSSIBLE CRYSTAL FORMS. DATA REMARK 4 WERE COLLECTED FOR A SECOND CRYSTAL FORM (SPACE GROUP C2, REMARK 4 A = 80.15, B = 32.14, C = 75.98, BETA = 103.08) FROM REMARK 4 CRYSTALS OF E. COLI DERIVED PROTEIN AND THAT STRUCTURE WAS REMARK 4 SOLVED BY MOLECULAR REPLACEMENT. DENSITY AVERAGING BETWEEN REMARK 4 THE TWO FORMS, USING DATA TO 3.0 ANGSTROMS RESOLUTION AND REMARK 4 CARRIED OUT AS DESCRIBED IN P. J. BJORKMAN ET AL., NATURE, REMARK 4 V. 329, P. 506, (1987), GAVE SIGNIFICANT PHASE IMPROVEMENT, REMARK 4 AND MAPS CALCULATED WITH THOSE PHASES SUBSTANTIALLY REMARK 4 ACCELERATED COMPLETION OF THE REFINEMENT OF THE STRUCTURE REMARK 4 PRESENTED IN THIS ENTRY. REMARK 5 REMARK 5 THE LAST AMINO ACID OBSERVABLE IN THE ELECTRON DENSITY IS REMARK 5 178. THE FOUR C-TERMINAL RESIDUES COULD NOT BE FOUND. REMARK 6 REMARK 6 THE SIDE CHAINS OF RESIDUES 72 AND 73 HAVE BEEN INCLUDED REMARK 6 IN TWO ALTERNATE CONFORMATIONS AND THE SIDE CHAIN OF REMARK 6 RESIDUE 43 HAS BEEN INCLUDED AT 0.5 OCCUPANCY. THE REMARK 6 ELECTRON DENSITY SUGGESTS THAT RESIDUE 43 MAY HAVE MORE REMARK 6 THAN TWO ALTERNATE CONFORMATIONS. REMARK 7 REMARK 7 IN THE ELECTRON DENSITY MAP RESIDUES 20 - 23, 105 - 107 REMARK 7 AND 132 - 137 APPEAR DISORDERED AND THEIR POSITIONS ARE REMARK 7 UNRELIABLE. FOR RESIDUES 1, 40, 43, 87, 88, 89, AND 152 REMARK 7 SIDE CHAIN POSITIONS ARE SOMEWHAT UNCERTAIN AS INDICATED REMARK 7 BY LARGE B VALUES. REMARK 8 REMARK 8 RESIDUES 89 - 102 FORM ONE UNINTERRUPTED STRAND PASSING REMARK 8 FROM DOMAIN 1 TO DOMAIN 2. RESIDUES 89 - 98 FORM STRAND 2 REMARK 8 OF SHEET *S1* AND RESIDUES 99 - 103 FORM STRAND 1 OF SHEET REMARK 8 *S4*. SEQRES 1 182 LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL GLU SEQRES 2 182 LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN PHE SEQRES 3 182 HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY ASN SEQRES 4 182 GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU ASN SEQRES 5 182 ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN GLY SEQRES 6 182 ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU ASP SEQRES 7 182 SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS GLU SEQRES 8 182 GLU VAL GLN LEU LEU VAL PHE GLY LEU THR ALA ASN SER SEQRES 9 182 ASP THR HIS LEU LEU GLN GLY GLN SER LEU THR LEU THR SEQRES 10 182 LEU GLU SER PRO PRO GLY SER SER PRO SER VAL GLN CYS SEQRES 11 182 ARG SER PRO ARG GLY LYS ASN ILE GLN GLY GLY LYS THR SEQRES 12 182 LEU SER VAL SER GLN LEU GLU LEU GLN ASP SER GLY THR SEQRES 13 182 TRP THR CYS THR VAL LEU GLN ASN GLN LYS LYS VAL GLU SEQRES 14 182 PHE LYS ILE ASP ILE VAL VAL LEU ALA PHE GLN LYS ALA FORMUL 2 HOH *30(H2 O1) HELIX 1 H1 ARG 58 GLN 64 1 HELIX IS IRREGULAR SHEET 1 S1 6 LYS 2 GLY 6 0 SHEET 2 S1 6 GLN 89 PHE 98 1 O GLN 94 N VAL 4 SHEET 3 S1 6 ASP 80 VAL 86 -1 O ASP 80 N LEU 95 SHEET 4 S1 6 PHE 26 ASN 30 -1 O HIS 27 N GLU 85 SHEET 5 S1 6 LYS 35 GLN 40 -1 O LEU 37 N TRP 28 SHEET 6 S1 6 PHE 43 LYS 46 -1 O THR 45 N GLY 38 SHEET 1 S2 3 ASP 10 THR 15 0 SHEET 2 S2 3 GLY 65 LYS 72 -1 O LEU 69 N LEU 14 SHEET 3 S2 3 ARG 54 SER 57 -1 O ASP 56 N ILE 70 SHEET 1 S3 5 LEU 108 GLN 110 0 SHEET 2 S3 5 LYS 166 LEU 177 1 N LEU 177 O LEU 108 SHEET 3 S3 5 GLY 155 GLN 163 -1 O GLY 155 N ILE 174 SHEET 4 S3 5 SER 127 ARG 131 -1 O SER 127 N LEU 162 SHEET 5 S3 5 ILE 138 GLY 140 -1 O ILE 138 N CYS 130 SHEET 1 S4 3 GLY 99 ASN 103 0 SHEET 2 S4 3 SER 113 GLU 119 -1 N GLU 119 O GLY 99 SHEET 3 S4 3 LYS 142 VAL 146 -1 N VAL 146 O LEU 114 SSBOND 1 CYS 16 CYS 84 SSBOND 2 CYS 130 CYS 159 CRYST1 84.230 30.650 88.940 90.00 118.43 90.00 C 2 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 0.011872 0.000000 0.006427 0.00000 SCALE2 0.000000 0.032626 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012785 0.00000