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