HEADER GROWTH FACTOR 01-DEC-91 1GMF COMPND GRANULOCYTE-MACROPHAGE COLONY-STIMULATING FACTOR SOURCE HUMAN (HOMO SAPIENS) RECOMBINANT FORM EXPRESSED IN SOURCE 2 (ESCHERICHIA COLI) AUTHOR P.A.KARPLUS,K.DIEDERICHS REVDAT 1 31-OCT-93 1GMF 0 JRNL AUTH K.DIEDERICHS,T.BOONE,P.A.KARPLUS JRNL TITL NOVEL FOLD AND PUTATIVE RECEPTOR BINDING SITE OF JRNL TITL 2 GRANULOCYTE-MACROPHAGE COLONY-STIMULATING FACTOR JRNL REF SCIENCE V. 254 1779 1991 JRNL REFN ASTM SCIEAS US ISSN 0036-8075 038 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.DIEDERICHS,S.JACQUES,T.BOONE,P.A.KARPLUS REMARK 1 TITL LOW-RESOLUTION STRUCTURE OF RECOMBINANT HUMAN REMARK 1 TITL 2 GRANULOCYTE-MACROPHAGE COLONY STIMULATING FACTOR REMARK 1 REF J.MOL.BIOL. V. 221 55 1991 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 2 REMARK 2 RESOLUTION. 2.4 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM X-PLOR REMARK 3 AUTHORS BRUNGER REMARK 3 R VALUE 0.205 REMARK 3 RMSD BOND DISTANCES 0.017 ANGSTROMS REMARK 3 RMSD BOND ANGLES 3.50 DEGREES REMARK 4 REMARK 4 THE PUTATIVE RECEPTOR BINDING SITES IN CHAINS *A* AND *B* REMARK 4 ARE PRESENTED AS SITES *REA* AND *REB*, RESPECTIVELY, ON REMARK 4 *SITE* RECORDS BELOW. REMARK 5 REMARK 5 RESIDUES 1 - 4 AND 124 - 127 ARE NOT SEEN IN THE ELECTRON REMARK 5 DENSITY MAP, PROBABLY DUE TO DISORDER. SEQRES 1 A 127 ALA PRO ALA ARG SER PRO SER PRO SER THR GLN PRO TRP SEQRES 2 A 127 GLU HIS VAL ASN ALA ILE GLN GLU ALA ARG ARG LEU LEU SEQRES 3 A 127 ASN LEU SER ARG ASP THR ALA ALA GLU MET ASN GLU THR SEQRES 4 A 127 VAL GLU VAL ILE SER GLU MET PHE ASP LEU GLN GLU PRO SEQRES 5 A 127 THR CYS LEU GLN THR ARG LEU GLU LEU TYR LYS GLN GLY SEQRES 6 A 127 LEU ARG GLY SER LEU THR LYS LEU LYS GLY PRO LEU THR SEQRES 7 A 127 MET MET ALA SER HIS TYR LYS GLN HIS CYS PRO PRO THR SEQRES 8 A 127 PRO GLU THR SER CYS ALA THR GLN ILE ILE THR PHE GLU SEQRES 9 A 127 SER PHE LYS GLU ASN LEU LYS ASP PHE LEU LEU VAL ILE SEQRES 10 A 127 PRO PHE ASP CYS TRP GLU PRO VAL GLN GLU SEQRES 1 B 127 ALA PRO ALA ARG SER PRO SER PRO SER THR GLN PRO TRP SEQRES 2 B 127 GLU HIS VAL ASN ALA ILE GLN GLU ALA ARG ARG LEU LEU SEQRES 3 B 127 ASN LEU SER ARG ASP THR ALA ALA GLU MET ASN GLU THR SEQRES 4 B 127 VAL GLU VAL ILE SER GLU MET PHE ASP LEU GLN GLU PRO SEQRES 5 B 127 THR CYS LEU GLN THR ARG LEU GLU LEU TYR LYS GLN GLY SEQRES 6 B 127 LEU ARG GLY SER LEU THR LYS LEU LYS GLY PRO LEU THR SEQRES 7 B 127 MET MET ALA SER HIS TYR LYS GLN HIS CYS PRO PRO THR SEQRES 8 B 127 PRO GLU THR SER CYS ALA THR GLN ILE ILE THR PHE GLU SEQRES 9 B 127 SER PHE LYS GLU ASN LEU LYS ASP PHE LEU LEU VAL ILE SEQRES 10 B 127 PRO PHE ASP CYS TRP GLU PRO VAL GLN GLU FTNOTE 1 FTNOTE 1 ASN 27 AND ASN 37 ARE HETEROGENEOUSLY GLYCOSYLATED IN THE FTNOTE 1 NATURAL PROTEIN. HELIX 1 AA TRP A 13 LEU A 28 1 HELIX 2 BA LEU A 55 GLN A 64 1 HELIX 3 CA LYS A 74 HIS A 87 1 HELIX 4 DA PHE A 103 VAL A 116 1 HELIX 5 EA GLY A 68 LEU A 73 5 NON-CONSERVED FEATURE OF FOLD HELIX 6 FA ALA A 33 MET A 36 1 HELIX 7 AB TRP B 13 LEU B 28 1 HELIX 8 BB LEU B 55 GLN B 64 1 HELIX 9 CB LYS B 74 HIS B 87 1 HELIX 10 DB PHE B 103 VAL B 116 1 HELIX 11 EB GLY B 68 LEU B 73 5 NON-CONSERVED FEATURE OF FOLD HELIX 12 FB ALA B 33 MET B 36 1 SHEET 1 S1 2 THR A 39 ILE A 43 0 SHEET 2 S1 2 THR A 98 THR A 102 -1 SHEET 1 S2 2 THR B 39 ILE B 43 0 SHEET 2 S2 2 THR B 98 THR B 102 -1 SSBOND 1 CYS A 54 CYS A 96 SSBOND 2 CYS A 88 CYS A 121 SSBOND 3 CYS B 54 CYS B 96 SSBOND 4 CYS B 88 CYS B 121 SITE 1 REA 14 GLU A 14 ASN A 17 ALA A 18 GLU A 21 SITE 2 REA 14 ARG A 24 LEU A 25 LYS A 72 LYS A 74 SITE 3 REA 14 GLY A 75 PRO A 76 THR A 78 MET A 79 SITE 4 REA 14 SER A 82 GLN A 86 SITE 1 REB 14 GLU B 14 ASN B 17 ALA B 18 GLU B 21 SITE 2 REB 14 ARG B 24 LEU B 25 LYS B 72 LYS B 74 SITE 3 REB 14 GLY B 75 PRO B 76 THR B 78 MET B 79 SITE 4 REB 14 SER B 82 GLN B 86 CRYST1 47.600 59.100 126.700 90.00 90.00 90.00 P 21 21 21 8 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 0.021008 0.000000 0.000000 0.00000 SCALE2 0.000000 0.016920 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007893 0.00000