HEADER GROWTH FACTOR 20-OCT-93 2TGI 2TGI 2 COMPND TRANSFORMING GROWTH FACTOR-BETA TWO (TGF-B2) 2TGI 3 SOURCE HUMAN (HOMO SAPIENS) RECOMBINANT FORM 2TGI 4 AUTHOR S.DAOPIN,D.R.DAVIES 2TGI 5 REVDAT 1 31-JAN-94 2TGI 0 2TGI 6 JRNL AUTH S.DAOPIN,K.A.PIEZ,Y.OGAWA,D.R.DAVIES 2TGI 7 JRNL TITL CRYSTAL STRUCTURE OF TRANSFORMING GROWTH 2TGI 8 JRNL TITL 2 FACTOR-BETA2: AN UNUSUAL FOLD FOR THE 2TGI 9 JRNL TITL 3 SUPERFAMILY 2TGI 10 JRNL REF SCIENCE V. 257 369 1992 2TGI 11 JRNL REFN ASTM SCIEAS US ISSN 0036-8075 038 2TGI 12 REMARK 1 2TGI 13 REMARK 1 REFERENCE 1 2TGI 14 REMARK 1 AUTH S.DAOPIN,M.LI,D.R.DAVIES 2TGI 15 REMARK 1 TITL CRYSTAL STRUCTURE OF TGF-BETA2 REFINED AT 1.8 2TGI 16 REMARK 1 TITL 2 ANGSTROMS RESOLUTION 2TGI 17 REMARK 1 REF PROTEINS.STRUCT.,FUNCT., V. 17 176 1993 2TGI 18 REMARK 1 REF 2 GENET. 2TGI 19 REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 867 2TGI 20 REMARK 2 2TGI 21 REMARK 2 RESOLUTION. 1.8 ANGSTROMS. 2TGI 22 REMARK 3 2TGI 23 REMARK 3 REFINEMENT. 2TGI 24 REMARK 3 PROGRAM TNT 2TGI 25 REMARK 3 AUTHORS TRONRUD,TEN EYCK,MATTHEWS 2TGI 26 REMARK 3 R VALUE 0.173 2TGI 27 REMARK 3 RMSD BOND DISTANCES 0.017 ANGSTROMS 2TGI 28 REMARK 3 RMSD BOND ANGLES 2.28 DEGREES 2TGI 29 REMARK 3 2TGI 30 REMARK 3 RESOLUTION RANGE 8. - 1.8 ANGSTROMS 2TGI 31 REMARK 3 2TGI 32 REMARK 3 NUMBER OF PROTEIN ATOMS 890 2TGI 33 REMARK 3 NUMBER OF SOLVENT ATOMS 58 2TGI 34 REMARK 4 2TGI 35 REMARK 4 A DIMER OF TGF-BETA 2 CAN BE GENERATED BY THE 2TGI 36 REMARK 4 CRYSTALLOGRAPHIC SYMMETRY OPERATOR: 2TGI 37 REMARK 4 (-X, -X+Y, -Z+2/3). 2TGI 38 REMARK 5 2TGI 39 REMARK 5 THERE IS AN *SSBOND* BETWEEN CYS 77 AND ITS SYMMETRY 2TGI 40 REMARK 5 RELATED COUNTERPART. 2TGI 41 SEQRES 1 112 ALA LEU ASP ALA ALA TYR CYS PHE ARG ASN VAL GLN ASP 2TGI 42 SEQRES 2 112 ASN CYS CYS LEU ARG PRO LEU TYR ILE ASP PHE LYS ARG 2TGI 43 SEQRES 3 112 ASP LEU GLY TRP LYS TRP ILE HIS GLU PRO LYS GLY TYR 2TGI 44 SEQRES 4 112 ASN ALA ASN PHE CYS ALA GLY ALA CYS PRO TYR LEU TRP 2TGI 45 SEQRES 5 112 SER SER ASP THR GLN HIS SER ARG VAL LEU SER LEU TYR 2TGI 46 SEQRES 6 112 ASN THR ILE ASN PRO GLU ALA SER ALA SER PRO CYS CYS 2TGI 47 SEQRES 7 112 VAL SER GLN ASP LEU GLU PRO LEU THR ILE LEU TYR TYR 2TGI 48 SEQRES 8 112 ILE GLY LYS THR PRO LYS ILE GLU GLN LEU SER ASN MET 2TGI 49 SEQRES 9 112 ILE VAL LYS SER CYS LYS CYS SER 2TGI 50 FTNOTE 1 2TGI 51 FTNOTE 1 RESIDUE PRO 36 IS A CIS PROLINE. 2TGI 52 FTNOTE 2 2TGI 53 FTNOTE 2 RESIDUES 92 - 96 ARE ILL-DEFINED IN THE ELECTRON DENSITY. 2TGI 54 FTNOTE 2 MAP. 2TGI 55 FORMUL 2 HOH *58(H2 O1) 2TGI 56 HELIX 1 A1 ALA 4 PHE 8 1 2TGI 57 HELIX 2 A2 PHE 24 LEU 28 1 2TGI 58 HELIX 3 A3 HIS 58 TYR 65 1 2TGI 59 SHEET 1 S1 2 CYS 15 ARG 18 0 2TGI 60 SHEET 2 S1 2 ASN 42 ALA 45 -1 N ALA 45 O CYS 16 2TGI 61 SHEET 1 S2 2 LEU 20 ASP 23 0 2TGI 62 SHEET 2 S2 2 LYS 37 ALA 41 -1 N ALA 41 O LEU 20 2TGI 63 SHEET 1 S3 2 CYS 77 SER 80 0 2TGI 64 SHEET 2 S3 2 CYS 109 SER 112 -1 O SER 112 N CYS 77 2TGI 65 SHEET 1 S4 2 ASP 82 GLU 84 0 2TGI 66 SHEET 2 S4 2 MET 104 LYS 107 -1 N LYS 107 O ASP 82 2TGI 67 SHEET 1 S5 2 PRO 85 TYR 91 0 2TGI 68 SHEET 2 S5 2 PRO 96 SER 102 -1 O LEU 101 N LEU 86 2TGI 69 TURN 1 T1 ILE 92 THR 95 92O N95 2TGI 70 SSBOND 1 CYS 7 CYS 16 2TGI 71 SSBOND 2 CYS 15 CYS 78 2TGI 72 SSBOND 3 CYS 44 CYS 109 2TGI 73 SSBOND 4 CYS 48 CYS 111 2TGI 74 CRYST1 60.600 60.600 75.300 90.00 90.00 120.00 P 32 2 1 6 2TGI 75 ORIGX1 1.000000 0.000000 0.000000 0.00000 2TGI 76 ORIGX2 0.000000 1.000000 0.000000 0.00000 2TGI 77 ORIGX3 0.000000 0.000000 1.000000 0.00000 2TGI 78 SCALE1 0.016502 0.009527 0.000000 0.00000 2TGI 79 SCALE2 0.000000 0.019054 0.000000 0.00000 2TGI 80 SCALE3 0.000000 0.000000 0.013280 0.00000 2TGI 81