HEADER IMMUNOGLOBULIN 17-JAN-91 6FAB 6FAB 2 COMPND ANTIGEN-BINDING FRAGMENT OF THE MURINE ANTI-PHENYLARSONATE 6FAB 3 COMPND 2 ANTIBODY 36-71, "FAB 36-71" 6FAB 4 SOURCE MOUSE (MUS $MUSCULUS) 6FAB 5 AUTHOR R.K.STRONG,D.R.ROSE,G.A.PETSKO,J.SHARON,M.N.MARGOLIES 6FAB 6 REVDAT 2 15-MAY-95 6FABA 1 SEQRES 6FABA 1 REVDAT 1 15-JAN-93 6FAB 0 6FAB 7 REMARK 1 6FAB 8 REMARK 1 REFERENCE 1 6FAB 9 REMARK 1 AUTH R.K.STRONG,R.CAMPBELL,D.R.ROSE,G.A.PETSKO,J.SHARON, 6FAB 10 REMARK 1 AUTH 2 M.N.MARGOLIES 6FAB 11 REMARK 1 TITL THREE-*DIMENSIONAL STRUCTURE OF MURINE 6FAB 12 REMARK 1 TITL 2 ANTI-P-AZOPHENYLARSONATE FAB 36-71. 1. X-RAY 6FAB 13 REMARK 1 TITL 3 CRYSTALLOGRAPHY, SITE-DIRECTED MUTAGENESIS, AND 6FAB 14 REMARK 1 TITL 4 MODELING OF THE COMPLEX WITH HAPTEN 6FAB 15 REMARK 1 REF BIOCHEMISTRY V. 30 3739 1991 6FAB 16 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 6FAB 17 REMARK 1 REFERENCE 2 6FAB 18 REMARK 1 AUTH R.K.STRONG,G.A.PETSKO,J.SHARON,M.N.MARGOLIES 6FAB 19 REMARK 1 TITL THREE-*DIMENSIONAL STRUCTURE OF MURINE 6FAB 20 REMARK 1 TITL 2 ANTI-P-AZOPHENYLARSONATE FAB 36-71. 2. STRUCTURAL 6FAB 21 REMARK 1 TITL 3 BASIS OF HAPTEN BINDING AND IDIOTYPY 6FAB 22 REMARK 1 REF BIOCHEMISTRY V. 30 3749 1991 6FAB 23 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 6FAB 24 REMARK 1 REFERENCE 3 6FAB 25 REMARK 1 AUTH D.R.ROSE,R.K.STRONG,M.N.MARGOLIES,M.L.GEFTER, 6FAB 26 REMARK 1 AUTH 2 G.A.PETSKO 6FAB 27 REMARK 1 TITL CRYSTAL STRUCTURE OF THE ANTIGEN-BINDING FRAGMENT 6FAB 28 REMARK 1 TITL 2 OF THE MURINE ANTI-ARSONATE MONOCLONAL ANTIBODY 6FAB 29 REMARK 1 TITL 3 36-71 AT 2.9 ANGSTROMS RESOLUTION 6FAB 30 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 87 338 1990 6FAB 31 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 6FAB 32 REMARK 2 6FAB 33 REMARK 2 RESOLUTION. 1.9 ANGSTROMS. 6FAB 34 REMARK 3 6FAB 35 REMARK 3 REFINEMENT. 6FAB 36 REMARK 3 PROGRAM PROLSQ; XPLOR 6FAB 37 REMARK 3 AUTHORS KONNERT, HENDRICKSON; BRUNGER 6FAB 38 REMARK 3 R VALUE 0.209 6FAB 39 REMARK 3 RMSD BOND DISTANCES 0.019 ANGSTROMS 6FAB 40 REMARK 3 RMSD BOND ANGLES 3.99 DEGREES 6FAB 41 REMARK 4 6FAB 42 REMARK 4 REGIONS OF POOR ELECTRON DENSITY OCCUR FOR RESIDUES L 40, 6FAB 43 REMARK 4 L 53, L 214, H 42 - H 43, AND H 135 - H 142. THE SIDE 6FAB 44 REMARK 4 CHAIN OF RESIDUE H 102 IS ALSO IN PARTIAL DENSITY. THE 6FAB 45 REMARK 4 POOR QUALITY OF THE ELECTRON DENSITY FOR RESIDUES H 135 - 6FAB 46 REMARK 4 H 142 SUGGESTS THAT THIS REGION IS HIGHLY FLEXIBLE. 6FAB 47 REMARK 5 6FABA 2 REMARK 5 CORRECT NUMBER OF RESIDUES ON SEQRES RECORDS FOR CHAIN H. 6FABA 3 REMARK 5 15-MAY-95. 6FABA 4 SEQRES 1 L 214 ASP ILE GLN MET THR GLN ILE PRO SER SER LEU SER ALA 6FAB 48 SEQRES 2 L 214 SER LEU GLY ASP ARG VAL SER ILE SER CYS ARG ALA SER 6FAB 49 SEQRES 3 L 214 GLN ASP ILE ASN ASN PHE LEU ASN TRP TYR GLN GLN LYS 6FAB 50 SEQRES 4 L 214 PRO ASP GLY THR ILE LYS LEU LEU ILE TYR PHE THR SER 6FAB 51 SEQRES 5 L 214 ARG SER GLN SER GLY VAL PRO SER ARG PHE SER GLY SER 6FAB 52 SEQRES 6 L 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU 6FAB 53 SEQRES 7 L 214 GLU GLN GLU ASP ILE ALA THR TYR PHE CYS GLN GLN GLY 6FAB 54 SEQRES 8 L 214 ASN ALA LEU PRO ARG THR PHE GLY GLY GLY THR LYS LEU 6FAB 55 SEQRES 9 L 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE 6FAB 56 SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA 6FAB 57 SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP 6FAB 58 SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN 6FAB 59 SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS 6FAB 60 SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR 6FAB 61 SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU 6FAB 62 SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER 6FAB 63 SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS 6FAB 64 SEQRES 1 H 222 GLU VAL GLN LEU GLN GLN SER GLY VAL GLU LEU VAL ARG 6FABA 5 SEQRES 2 H 222 ALA GLY SER SER VAL LYS MET SER CYS LYS ALA SER GLY 6FABA 6 SEQRES 3 H 222 TYR THR PHE THR SER ASN GLY ILE ASN TRP VAL LYS GLN 6FABA 7 SEQRES 4 H 222 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TYR ASN ASN 6FABA 8 SEQRES 5 H 222 PRO GLY ASN GLY TYR ILE ALA TYR ASN GLU LYS PHE LYS 6FABA 9 SEQRES 6 H 222 GLY LYS THR THR LEU THR VAL ASP LYS SER SER SER THR 6FABA 10 SEQRES 7 H 222 ALA TYR MET GLN LEU ARG SER LEU THR SER GLU ASP SER 6FABA 11 SEQRES 8 H 222 ALA VAL TYR PHE CYS ALA ARG SER GLU TYR TYR GLY GLY 6FABA 12 SEQRES 9 H 222 SER TYR LYS PHE ASP TYR TRP GLY GLN GLY THR THR LEU 6FABA 13 SEQRES 10 H 222 THR VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR 6FABA 14 SEQRES 11 H 222 PRO LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER MET 6FABA 15 SEQRES 12 H 222 VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU 6FABA 16 SEQRES 13 H 222 PRO VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER 6FABA 17 SEQRES 14 H 222 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU 6FABA 18 SEQRES 15 H 222 TYR THR LEU SER SER SER VAL THR VAL PRO SER SER PRO 6FABA 19 SEQRES 16 H 222 ARG PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO 6FABA 20 SEQRES 17 H 222 ALA SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG 6FABA 21 SEQRES 18 H 222 ASP 6FABA 22 FTNOTE 1 6FAB 83 FTNOTE 1 RESIDUES PRO L 8, PRO L 95, PRO L 141, PRO H 155, 6FAB 84 FTNOTE 1 PRO H 157, AND PRO H 197 ARE CIS PROLINES. 6FAB 85 FORMUL 3 HOH *70(H2 O1) 6FAB 86 HELIX 1 H1 SER L 121 GLY L 128 1 6FAB 87 HELIX 2 H2 ASP L 184 GLU L 187 1 6FAB 88 HELIX 3 H3 TYR H 94 ARG H 98 1 6FAB 89 SSBOND 1 CYS L 23 CYS L 88 6FAB 90 SSBOND 2 CYS L 134 CYS L 194 6FAB 91 SSBOND 3 CYS H 22 CYS H 96 6FAB 92 SSBOND 4 CYS H 148 CYS H 203 6FAB 93 CRYST1 67.130 73.050 46.780 90.00 104.48 90.00 P 21 2 6FAB 94 ORIGX1 1.000000 0.000000 0.000000 0.00000 6FAB 95 ORIGX2 0.000000 1.000000 0.000000 0.00000 6FAB 96 ORIGX3 0.000000 0.000000 1.000000 0.00000 6FAB 97 SCALE1 0.014896 0.000000 0.003847 0.00000 6FAB 98 SCALE2 0.000000 0.013689 0.000000 0.00000 6FAB 99 SCALE3 0.000000 0.000000 0.022078 0.00000 6FAB 100