HEADER COMPLEX (ANTIBODY-ANTIGEN) 27-AUG-90 1FDL 1FDL 2 COMPND IG*G1 FAB FRAGMENT (ANTI-LYSOZYME ANTIBODY D1.3, KAPPA) 1FDL 3 COMPND 2 - LYSOZYME (E.C.3.2.1.17) COMPLEX 1FDL 4 SOURCE MOUSE (MUS $MUSCULUS) FROM BALB/$C STRAIN AND 1FDL 5 SOURCE 2 HEN (GALLUS $GALLUS) EGG WHITE 1FDL 6 AUTHOR T.O.FISCHMANN,R.J.POLJAK 1FDL 7 REVDAT 1 15-OCT-91 1FDL 0 1FDL 8 JRNL AUTH T.O.FISCHMANN,G.A.BENTLEY,T.N.BHAT,G.BOULOT, 1FDL 9 JRNL AUTH 2 R.A.MARIUZZA,S.E.V.PHILLIPS,D.TELLO,R.J.POLJAK 1FDL 10 JRNL TITL CRYSTALLOGRAPHIC REFINEMENT OF THE 1FDL 11 JRNL TITL 2 THREE-DIMENSIONAL STRUCTURE OF THE 1FDL 12 JRNL TITL 3 FAB*D1.3-*LYSOZYME COMPLEX AT 2.5-*ANGSTROMS 1FDL 13 JRNL TITL 4 RESOLUTION 1FDL 14 JRNL REF J.BIOL.CHEM. V. 266 12915 1991 1FDL 15 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 071 1FDL 16 REMARK 1 1FDL 17 REMARK 2 1FDL 18 REMARK 2 RESOLUTION. 2.5 ANGSTROMS. 1FDL 19 REMARK 3 1FDL 20 REMARK 3 REFINEMENT. BY THE MOLECULAR DYNAMICS PROCEDURES OF A. 1FDL 21 REMARK 3 BRUENGER, J. KURIYAN, AND M. KARPLUS (PROGRAM "XPLOR"). 1FDL 22 REMARK 3 THE R VALUE IS 0.184. THE RMS DEVIATION FROM IDEALITY OF 1FDL 23 REMARK 3 THE BOND DISTANCES IS 0.013 ANGSTROMS. THE RMS DEVIATION 1FDL 24 REMARK 3 FROM IDEALITY OF THE BOND ANGLES IS 3.3 DEGREES. 1FDL 25 REMARK 4 1FDL 26 REMARK 4 CHAIN "L" REPRESENTS ANTIBODY LIGHT CHAIN RESIDUES. CHAIN 1FDL 27 REMARK 4 "H" REPRESENTS ANTIBODY HEAVY CHAIN RESIDUES. CHAIN "Y" 1FDL 28 REMARK 4 REPRESENTS LYSOZYME. 1FDL 29 SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO ALA SER LEU SER ALA 1FDL 30 SEQRES 2 L 214 SER VAL GLY GLU THR VAL THR ILE THR CYS ARG ALA SER 1FDL 31 SEQRES 3 L 214 GLY ASN ILE HIS ASN TYR LEU ALA TRP TYR GLN GLN LYS 1FDL 32 SEQRES 4 L 214 GLN GLY LYS SER PRO GLN LEU LEU VAL TYR TYR THR THR 1FDL 33 SEQRES 5 L 214 THR LEU ALA ASP GLY VAL PRO SER ARG PHE SER GLY SER 1FDL 34 SEQRES 6 L 214 GLY SER GLY THR GLN TYR SER LEU LYS ILE ASN SER LEU 1FDL 35 SEQRES 7 L 214 GLN PRO GLU ASP PHE GLY SER TYR TYR CYS GLN HIS PHE 1FDL 36 SEQRES 8 L 214 TRP SER THR PRO ARG THR PHE GLY GLY GLY THR LYS LEU 1FDL 37 SEQRES 9 L 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE 1FDL 38 SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA 1FDL 39 SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP 1FDL 40 SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN 1FDL 41 SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS 1FDL 42 SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR 1FDL 43 SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU 1FDL 44 SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER 1FDL 45 SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS 1FDL 46 SEQRES 1 H 218 GLN VAL GLN LEU LYS GLU SER GLY PRO GLY LEU VAL ALA 1FDL 47 SEQRES 2 H 218 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY 1FDL 48 SEQRES 3 H 218 PHE SER LEU THR GLY TYR GLY VAL ASN TRP VAL ARG GLN 1FDL 49 SEQRES 4 H 218 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY MET ILE TRP 1FDL 50 SEQRES 5 H 218 GLY ASP GLY ASN THR ASP TYR ASN SER ALA LEU LYS SER 1FDL 51 SEQRES 6 H 218 ARG LEU SER ILE SER LYS ASP ASN SER LYS SER GLN VAL 1FDL 52 SEQRES 7 H 218 PHE LEU LYS MET ASN SER LEU HIS THR ASP ASP THR ALA 1FDL 53 SEQRES 8 H 218 ARG TYR TYR CYS ALA ARG GLU ARG ASP TYR ARG LEU ASP 1FDL 54 SEQRES 9 H 218 TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER ALA 1FDL 55 SEQRES 10 H 218 SER THR THR PRO PRO SER VAL PHE PRO LEU ALA PRO GLY 1FDL 56 SEQRES 11 H 218 SER ALA ALA GLN THR ASN SER MET VAL THR LEU GLY CYS 1FDL 57 SEQRES 12 H 218 LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR 1FDL 58 SEQRES 13 H 218 TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE 1FDL 59 SEQRES 14 H 218 PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER 1FDL 60 SEQRES 15 H 218 SER VAL THR VAL PRO SER SER PRO ARG PRO SER GLU THR 1FDL 61 SEQRES 16 H 218 VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS 1FDL 62 SEQRES 17 H 218 VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS 1FDL 63 SEQRES 1 Y 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS 1FDL 64 SEQRES 2 Y 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY 1FDL 65 SEQRES 3 Y 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN 1FDL 66 SEQRES 4 Y 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP 1FDL 67 SEQRES 5 Y 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN 1FDL 68 SEQRES 6 Y 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE 1FDL 69 SEQRES 7 Y 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER 1FDL 70 SEQRES 8 Y 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY 1FDL 71 SEQRES 9 Y 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY 1FDL 72 SEQRES 10 Y 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU 1FDL 73 FTNOTE 1 1FDL 74 FTNOTE 1 RESIDUES PRO L 8, PRO L 95, PRO L 141, PRO H 150, PRO H 152 1FDL 75 FTNOTE 1 AND PRO H 192 ARE CIS PROLINES. 1FDL 76 SSBOND 1 CYS L 23 CYS L 88 1FDL 77 SSBOND 2 CYS L 134 CYS L 194 1FDL 78 SSBOND 3 CYS H 22 CYS H 95 1FDL 79 SSBOND 4 CYS H 143 CYS H 198 1FDL 80 SSBOND 5 CYS L 214 CYS H 218 1FDL 81 SSBOND 6 CYS Y 6 CYS Y 127 1FDL 82 SSBOND 7 CYS Y 30 CYS Y 115 1FDL 83 SSBOND 8 CYS Y 64 CYS Y 80 1FDL 84 SSBOND 9 CYS Y 76 CYS Y 94 1FDL 85 CRYST1 56.000 143.500 49.300 90.00 120.40 90.00 P 21 2 1FDL 86 ORIGX1 1.000000 0.000000 0.000000 0.00000 1FDL 87 ORIGX2 0.000000 1.000000 0.000000 0.00000 1FDL 88 ORIGX3 0.000000 0.000000 1.000000 0.00000 1FDL 89 SCALE1 0.017857 0.000000 0.010477 0.00000 1FDL 90 SCALE2 0.000000 0.006969 0.000000 0.00000 1FDL 91 SCALE3 0.000000 0.000000 0.023517 0.00000 1FDL 92