>gi|126608|sp|P00698.1|LYSC_CHICK RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; AltName: Full=Allergen Gal d IV; AltName: Allergen=Gal d 4; Flags: Precursor [Gallus gallus] >gi|193506635|pdb|3B6L|A Chain A, Crystal Structure Of Lysozyme Folded In Sds And 2-Methyl-2, 4-Pentanediol >gi|198443193|pdb|3B72|A Chain A, Crystal Structure Of Lysozyme Folded In Sds And 2-Methyl-2, 4-Pentanediol >gi|401871290|pdb|3TMU|A Chain A, X-Ray Radiation Damage To Hewl Crystals Soaked In 100mm Sodium Nitrate (Undosed) >gi|401871291|pdb|3TMV|A Chain A, X-Ray Radiation Damage To Hewl Crystals Soaked In 100mm Sodium Nitrate (Dose0.12mgy) >gi|401871292|pdb|3TMW|A Chain A, X-Ray Radiation Damage To Hewl Crystals Soaked In 100mm Sodium Nitrate (Undosed) >gi|401871293|pdb|3TMX|A Chain A, X-Ray Radiation Damage To Hewl Crystals Soaked In 100mm Sodium Nitrate (Dose1.9mgy) >gi|636665615|pdb|4CJ2|A Chain A, Crystal Structure Of Hewl In Complex With Affitin H4 >gi|636665616|pdb|4CJ2|B Chain B, Crystal Structure Of Hewl In Complex With Affitin H4 >gi|212276|gb|AAA48943.1| lysozyme ( [Gallus gallus] >gi|18419437|gb|AAL69327.1| egg white lysozyme [Gallus gallus] >gi|220899143|gb|ACL81757.1| lysozyme [Gallus sonneratii] >gi|220899145|gb|ACL81758.1| lysozyme [Gallus sonneratii] >gi|220899147|gb|ACL81759.1| lysozyme [Gallus lafayetii] >gi|220899149|gb|ACL81760.1| lysozyme [Gallus lafayetii] >gi|220899151|gb|ACL81761.1| lysozyme [Gallus gallus] >gi|220899153|gb|ACL81762.1| lysozyme [Gallus gallus]
MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRW
WCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157831887|pdb|1LSY|A Chain A, Crystal Structure Of The Mutant D52s Hen Egg White Lysozyme With An Oligosaccharide Product >gi|157831888|pdb|1LSZ|A Chain A, Crystal Structure Of The Mutant D52s Hen Egg White Lysozyme With An Oligosaccharide Product
MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTSYGILQINSRW
WCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|220898867|gb|ACL81619.1| lysozyme [Gallus gallus]
MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCVAKFESNFNTQATNRNTDGSTDFGILQINSRW
WCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|45384212|ref|NP_990612.1| lysozyme C precursor [Gallus gallus] >gi|63581|emb|CAA23711.1| unnamed protein product [Gallus gallus]
MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCVAKFESNFNTQATNRNTDGSTDYGILQINSRW
WCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMSAWVAWRNRCKGTDVQAWIRGCRL
>gi|220898771|gb|ACL81571.1| lysozyme [Gallus gallus] >gi|220898773|gb|ACL81572.1| lysozyme [Gallus gallus] >gi|220898777|gb|ACL81574.1| lysozyme [Gallus gallus] >gi|220898779|gb|ACL81575.1| lysozyme [Gallus gallus] >gi|220898781|gb|ACL81576.1| lysozyme [Gallus gallus] >gi|220898783|gb|ACL81577.1| lysozyme [Gallus gallus] >gi|220898785|gb|ACL81578.1| lysozyme [Gallus gallus] >gi|220898787|gb|ACL81579.1| lysozyme [Gallus gallus] >gi|220898789|gb|ACL81580.1| lysozyme [Gallus gallus] >gi|220898793|gb|ACL81582.1| lysozyme [Gallus gallus] >gi|220898797|gb|ACL81584.1| lysozyme [Gallus gallus] >gi|220898801|gb|ACL81586.1| lysozyme [Gallus gallus] >gi|220898803|gb|ACL81587.1| lysozyme [Gallus gallus] >gi|220898805|gb|ACL81588.1| lysozyme [Gallus gallus] >gi|220898807|gb|ACL81589.1| lysozyme [Gallus gallus] >gi|220898809|gb|ACL81590.1| lysozyme [Gallus gallus] >gi|220898811|gb|ACL81591.1| lysozyme [Gallus gallus] >gi|220898813|gb|ACL81592.1| lysozyme [Gallus gallus] >gi|220898815|gb|ACL81593.1| lysozyme [Gallus gallus] >gi|220898817|gb|ACL81594.1| lysozyme [Gallus gallus] >gi|220898821|gb|ACL81596.1| lysozyme [Gallus gallus] >gi|220898823|gb|ACL81597.1| lysozyme [Gallus gallus] >gi|220898825|gb|ACL81598.1| lysozyme [Gallus gallus] >gi|220898827|gb|ACL81599.1| lysozyme [Gallus gallus] >gi|220898829|gb|ACL81600.1| lysozyme [Gallus gallus] >gi|220898831|gb|ACL81601.1| lysozyme [Gallus gallus] >gi|220898833|gb|ACL81602.1| lysozyme [Gallus gallus] >gi|220898835|gb|ACL81603.1| lysozyme [Gallus gallus] >gi|220898837|gb|ACL81604.1| lysozyme [Gallus gallus] >gi|220898841|gb|ACL81606.1| lysozyme [Gallus gallus] >gi|220898843|gb|ACL81607.1| lysozyme [Gallus gallus] >gi|220898845|gb|ACL81608.1| lysozyme [Gallus gallus] >gi|220898847|gb|ACL81609.1| lysozyme [Gallus gallus] >gi|220898849|gb|ACL81610.1| lysozyme [Gallus gallus] >gi|220898857|gb|ACL81614.1| lysozyme [Gallus gallus] >gi|220898865|gb|ACL81618.1| lysozyme [Gallus gallus] >gi|220898869|gb|ACL81620.1| lysozyme [Gallus gallus] >gi|220898873|gb|ACL81622.1| lysozyme [Gallus gallus] >gi|220898877|gb|ACL81624.1| lysozyme [Gallus gallus] >gi|220898881|gb|ACL81626.1| lysozyme [Gallus gallus] >gi|220898885|gb|ACL81628.1| lysozyme [Gallus gallus] >gi|220898889|gb|ACL81630.1| lysozyme [Gallus gallus] >gi|220898891|gb|ACL81631.1| lysozyme [Gallus gallus] >gi|220898893|gb|ACL81632.1| lysozyme [Gallus gallus] >gi|220898895|gb|ACL81633.1| lysozyme [Gallus gallus] >gi|220898897|gb|ACL81634.1| lysozyme [Gallus gallus] >gi|220898899|gb|ACL81635.1| lysozyme [Gallus gallus] >gi|220898901|gb|ACL81636.1| lysozyme [Gallus gallus] >gi|220898905|gb|ACL81638.1| lysozyme [Gallus gallus] >gi|220898907|gb|ACL81639.1| lysozyme [Gallus gallus] >gi|220898909|gb|ACL81640.1| lysozyme [Gallus gallus] >gi|220898913|gb|ACL81642.1| lysozyme [Gallus gallus] >gi|220898915|gb|ACL81643.1| lysozyme [Gallus gallus] >gi|220898917|gb|ACL81644.1| lysozyme [Gallus gallus] >gi|220898919|gb|ACL81645.1| lysozyme [Gallus gallus] >gi|220898921|gb|ACL81646.1| lysozyme [Gallus gallus] >gi|220898923|gb|ACL81647.1| lysozyme [Gallus gallus] >gi|220898925|gb|ACL81648.1| lysozyme [Gallus gallus] >gi|220898927|gb|ACL81649.1| lysozyme [Gallus gallus] >gi|220898929|gb|ACL81650.1| lysozyme [Gallus gallus] >gi|220898931|gb|ACL81651.1| lysozyme [Gallus gallus] >gi|220898933|gb|ACL81652.1| lysozyme [Gallus gallus] >gi|220898937|gb|ACL81654.1| lysozyme [Gallus gallus] >gi|220898941|gb|ACL81656.1| lysozyme [Gallus gallus] >gi|220898945|gb|ACL81658.1| lysozyme [Gallus gallus] >gi|220898949|gb|ACL81660.1| lysozyme [Gallus gallus] >gi|220898951|gb|ACL81661.1| lysozyme [Gallus gallus] >gi|220898953|gb|ACL81662.1| lysozyme [Gallus gallus] >gi|220898955|gb|ACL81663.1| lysozyme [Gallus gallus] >gi|220898957|gb|ACL81664.1| lysozyme [Gallus gallus] >gi|220898959|gb|ACL81665.1| lysozyme [Gallus gallus] >gi|220898961|gb|ACL81666.1| lysozyme [Gallus gallus] >gi|220898963|gb|ACL81667.1| lysozyme [Gallus gallus] >gi|220898965|gb|ACL81668.1| lysozyme [Gallus gallus] >gi|220898969|gb|ACL81670.1| lysozyme [Gallus gallus] >gi|220898971|gb|ACL81671.1| lysozyme [Gallus gallus] >gi|220898973|gb|ACL81672.1| lysozyme [Gallus gallus] >gi|220898975|gb|ACL81673.1| lysozyme [Gallus gallus] >gi|220898977|gb|ACL81674.1| lysozyme [Gallus gallus] >gi|220898979|gb|ACL81675.1| lysozyme [Gallus gallus] >gi|220898981|gb|ACL81676.1| lysozyme [Gallus gallus] >gi|220898983|gb|ACL81677.1| lysozyme [Gallus gallus] >gi|220898985|gb|ACL81678.1| lysozyme [Gallus gallus] >gi|220898989|gb|ACL81680.1| lysozyme [Gallus gallus] >gi|220898991|gb|ACL81681.1| lysozyme [Gallus gallus] >gi|220898993|gb|ACL81682.1| lysozyme [Gallus gallus] >gi|220898995|gb|ACL81683.1| lysozyme [Gallus gallus] >gi|220898997|gb|ACL81684.1| lysozyme [Gallus gallus] >gi|220898999|gb|ACL81685.1| lysozyme [Gallus gallus] >gi|220899003|gb|ACL81687.1| lysozyme [Gallus gallus] >gi|220899005|gb|ACL81688.1| lysozyme [Gallus gallus] >gi|220899007|gb|ACL81689.1| lysozyme [Gallus gallus] >gi|220899009|gb|ACL81690.1| lysozyme [Gallus gallus] >gi|220899013|gb|ACL81692.1| lysozyme [Gallus gallus] >gi|220899017|gb|ACL81694.1| lysozyme [Gallus gallus] >gi|220899019|gb|ACL81695.1| lysozyme [Gallus gallus] >gi|220899023|gb|ACL81697.1| lysozyme [Gallus gallus] >gi|220899027|gb|ACL81699.1| lysozyme [Gallus gallus] >gi|220899029|gb|ACL81700.1| lysozyme [Gallus gallus] >gi|220899031|gb|ACL81701.1| lysozyme [Gallus gallus] >gi|220899033|gb|ACL81702.1| lysozyme [Gallus gallus] >gi|220899037|gb|ACL81704.1| lysozyme [Gallus gallus] >gi|220899039|gb|ACL81705.1| lysozyme [Gallus gallus] >gi|220899041|gb|ACL81706.1| lysozyme [Gallus gallus] >gi|220899051|gb|ACL81711.1| lysozyme [Gallus gallus] >gi|220899053|gb|ACL81712.1| lysozyme [Gallus gallus] >gi|220899055|gb|ACL81713.1| lysozyme [Gallus gallus] >gi|220899057|gb|ACL81714.1| lysozyme [Gallus gallus] >gi|220899063|gb|ACL81717.1| lysozyme [Gallus gallus] >gi|220899067|gb|ACL81719.1| lysozyme [Gallus gallus] >gi|220899071|gb|ACL81721.1| lysozyme [Gallus gallus] >gi|220899073|gb|ACL81722.1| lysozyme [Gallus gallus] >gi|220899075|gb|ACL81723.1| lysozyme [Gallus gallus] >gi|220899077|gb|ACL81724.1| lysozyme [Gallus gallus] >gi|220899079|gb|ACL81725.1| lysozyme [Gallus gallus] >gi|220899081|gb|ACL81726.1| lysozyme [Gallus gallus] >gi|220899083|gb|ACL81727.1| lysozyme [Gallus gallus] >gi|220899085|gb|ACL81728.1| lysozyme [Gallus gallus] >gi|220899087|gb|ACL81729.1| lysozyme [Gallus gallus] >gi|220899091|gb|ACL81731.1| lysozyme [Gallus gallus] >gi|220899093|gb|ACL81732.1| lysozyme [Gallus gallus] >gi|220899095|gb|ACL81733.1| lysozyme [Gallus gallus] >gi|220899097|gb|ACL81734.1| lysozyme [Gallus gallus] >gi|220899099|gb|ACL81735.1| lysozyme [Gallus gallus] >gi|220899103|gb|ACL81737.1| lysozyme [Gallus gallus] >gi|220899105|gb|ACL81738.1| lysozyme [Gallus gallus] >gi|220899107|gb|ACL81739.1| lysozyme [Gallus gallus] >gi|220899109|gb|ACL81740.1| lysozyme [Gallus gallus] >gi|220899111|gb|ACL81741.1| lysozyme [Gallus gallus] >gi|220899115|gb|ACL81743.1| lysozyme [Gallus gallus] >gi|220899117|gb|ACL81744.1| lysozyme [Gallus gallus] >gi|220899119|gb|ACL81745.1| lysozyme [Gallus gallus] >gi|220899121|gb|ACL81746.1| lysozyme [Gallus gallus] >gi|220899123|gb|ACL81747.1| lysozyme [Gallus gallus] >gi|220899125|gb|ACL81748.1| lysozyme [Gallus gallus] >gi|220899127|gb|ACL81749.1| lysozyme [Gallus gallus] >gi|220899129|gb|ACL81750.1| lysozyme [Gallus gallus]
MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDSGILQINSRW
WCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|220898775|gb|ACL81573.1| lysozyme [Gallus gallus] >gi|220898791|gb|ACL81581.1| lysozyme [Gallus gallus] >gi|220898795|gb|ACL81583.1| lysozyme [Gallus gallus] >gi|220898799|gb|ACL81585.1| lysozyme [Gallus gallus] >gi|220898819|gb|ACL81595.1| lysozyme [Gallus gallus] >gi|220898839|gb|ACL81605.1| lysozyme [Gallus gallus] >gi|220898851|gb|ACL81611.1| lysozyme [Gallus gallus] >gi|220898853|gb|ACL81612.1| lysozyme [Gallus gallus] >gi|220898855|gb|ACL81613.1| lysozyme [Gallus gallus] >gi|220898859|gb|ACL81615.1| lysozyme [Gallus gallus] >gi|220898861|gb|ACL81616.1| lysozyme [Gallus gallus] >gi|220898863|gb|ACL81617.1| lysozyme [Gallus gallus] >gi|220898871|gb|ACL81621.1| lysozyme [Gallus gallus] >gi|220898875|gb|ACL81623.1| lysozyme [Gallus gallus] >gi|220898879|gb|ACL81625.1| lysozyme [Gallus gallus] >gi|220898883|gb|ACL81627.1| lysozyme [Gallus gallus] >gi|220898887|gb|ACL81629.1| lysozyme [Gallus gallus] >gi|220898903|gb|ACL81637.1| lysozyme [Gallus gallus] >gi|220898911|gb|ACL81641.1| lysozyme [Gallus gallus] >gi|220898935|gb|ACL81653.1| lysozyme [Gallus gallus] >gi|220898939|gb|ACL81655.1| lysozyme [Gallus gallus] >gi|220898943|gb|ACL81657.1| lysozyme [Gallus gallus] >gi|220898947|gb|ACL81659.1| lysozyme [Gallus gallus] >gi|220898967|gb|ACL81669.1| lysozyme [Gallus gallus] >gi|220898987|gb|ACL81679.1| lysozyme [Gallus gallus] >gi|220899001|gb|ACL81686.1| lysozyme [Gallus gallus] >gi|220899011|gb|ACL81691.1| lysozyme [Gallus gallus] >gi|220899015|gb|ACL81693.1| lysozyme [Gallus gallus] >gi|220899021|gb|ACL81696.1| lysozyme [Gallus gallus] >gi|220899025|gb|ACL81698.1| lysozyme [Gallus gallus] >gi|220899035|gb|ACL81703.1| lysozyme [Gallus gallus] >gi|220899043|gb|ACL81707.1| lysozyme [Gallus gallus] >gi|220899045|gb|ACL81708.1| lysozyme [Gallus gallus] >gi|220899047|gb|ACL81709.1| lysozyme [Gallus gallus] >gi|220899049|gb|ACL81710.1| lysozyme [Gallus gallus] >gi|220899059|gb|ACL81715.1| lysozyme [Gallus gallus] >gi|220899061|gb|ACL81716.1| lysozyme [Gallus gallus] >gi|220899065|gb|ACL81718.1| lysozyme [Gallus gallus] >gi|220899069|gb|ACL81720.1| lysozyme [Gallus gallus] >gi|220899089|gb|ACL81730.1| lysozyme [Gallus gallus] >gi|220899101|gb|ACL81736.1| lysozyme [Gallus gallus] >gi|220899113|gb|ACL81742.1| lysozyme [Gallus gallus]
MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCVAKFESNFNTQATNRNTDGSTDSGILQINSRW
WCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|220899131|gb|ACL81751.1| lysozyme [Bambusicola thoracica] >gi|220899133|gb|ACL81752.1| lysozyme [Bambusicola thoracica]
MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFKTHATIRNTDGSTHYGILQINSRW
WCNDGKTPGSRNLCNFPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|2851416|sp|P00701.2|LYSC_COTJA RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor
MRSLLVLVLCFLPLAALGKVYGRCELAAAMKRHGLDKYQGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRW
WCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDVHGMNAWVAWRNRCKGTDVNAWIRGCRL
>gi|326911544|ref|XP_003202118.1| PREDICTED: lysozyme C-like [Meleagris gallopavo] >gi|126619|sp|P00703.2|LYSC_MELGA RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Meleagris gallopavo]
MRSLLILVLCFLPLAALGKVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRW
WCNDGRTPGSKNLCNIPCSALLSSDITASVNCAKKIASGGNGMNAWVAWRNRCKGTDVHAWIRGCRL
>gi|220899139|gb|ACL81755.1| lysozyme [Gallus varius] >gi|220899141|gb|ACL81756.1| lysozyme [Gallus varius]
MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFKTHATTRNTDGNTHYGILQINSRW
WCNDGKTPGSRNLCNVPRSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|220899135|gb|ACL81753.1| lysozyme [Francolinus pondicerianus interpositus] >gi|220899137|gb|ACL81754.1| lysozyme [Francolinus pondicerianus interpositus]
MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFGSNFKTHATTRNTDGSTYYGIPQINSRW
WCNDGRTPGSRNLCNFPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|547878|sp|P00702.2|LYSC_PHACO RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Phasianus colchicus colchicus]
MRSLLILVLCFLPLAAPGKVYGRCELAAAMKRMGLDNYRGYSLGNWVCAAKFESNFNTGATNRNTDGSTDYGILQINSRW
WCNDGRTPGSKNLCHIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRKHCKGTDVNVWIRGCRL
>gi|67408|pir||LZFER lysozyme (EC 3.2.1.17) c precursor [validated] - ring-necked pheasant (tentative sequence)
MRSLLILVLCFLPLAAPGKVYGRCELAAAMKRMGLDNYRGYSLGNWVCAAKFESNFNTGATNRNTDGSTDYGILQINSRW
WCNDGRTPGSKNLCHIPCSALLSSDITASVNCAKKIVSDGDGMNAWVAWRKHCKGTDVNVWIRGCRL
>gi|157831881|pdb|1LSG|A Chain A, Three-Dimensional Structure Of The Platelet Integrin Recognition Segment Of The Fibrinogen Gamma Chain Obtained By Carrier Protein-Driven Crystallization
MKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIP
CSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRLQQHHLGGAKQAGDV
>gi|375314811|gb|AFA52017.1| hen egg white lysozyme [Cloning vector pQRBL]
MKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIP
CSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|672886452|pdb|4MWN|A Chain A, Triclinic Hewl Co-crystallised With Cisplatin, Studied At A Data Collection Temperature Of 294k
AKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIP
CSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|229916|pdb|1FDL|Y Chain Y, Crystallographic Refinement Of The Three-Dimensional Structure Of The Fab D1.3-Lysozyme Complex At 2.5- Angstroms Resolution >gi|230143|pdb|1LZH|A Chain A, The Structures Of The Monoclinic And Orthorhombic Forms Of Hen Egg-White Lysozyme At 6 Angstroms Resolution. >gi|230144|pdb|1LZH|B Chain B, The Structures Of The Monoclinic And Orthorhombic Forms Of Hen Egg-White Lysozyme At 6 Angstroms Resolution. >gi|230872|pdb|3HFM|Y Chain Y, Structure Of An Antibody-Antigen Complex. Crystal Structure Of The HyHEL-10 Fab-Lysozyme Complex >gi|443222|pdb|1RCM|A Chain A, Crystal Structure Of A Ubiquitin-Dependent Degradation Substrate: A Three-Disulfide Form Of Lysozyme >gi|443223|pdb|1RCM|B Chain B, Crystal Structure Of A Ubiquitin-Dependent Degradation Substrate: A Three-Disulfide Form Of Lysozyme >gi|443468|pdb|3LYT|A Chain A, Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambient Temperatures >gi|443469|pdb|3LYT|B Chain B, Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambient Temperatures >gi|443498|pdb|4LYT|A Chain A, Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambient Temperatures >gi|443499|pdb|4LYT|B Chain B, Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambient Temperatures >gi|515216|pdb|1LYS|A Chain A, X-Ray Structure Of A Monoclinic Form Of Hen Egg-White Lysozyme Crystallized At 313k. Comparison Of Two Independent Molecules >gi|515217|pdb|1LYS|B Chain B, X-Ray Structure Of A Monoclinic Form Of Hen Egg-White Lysozyme Crystallized At 313k. Comparison Of Two Independent Molecules >gi|576328|pdb|1VFB|C Chain C, Bound Water Molecules And Conformational Stabilization Help Mediate An Antigen-Antibody Association >gi|1065172|pdb|1MLC|E Chain E, Monoclonal Antibody Fab D44.1 Raised Against Chicken Egg- White Lysozyme Complexed With Lysozyme >gi|1065173|pdb|1MLC|F Chain F, Monoclonal Antibody Fab D44.1 Raised Against Chicken Egg- White Lysozyme Complexed With Lysozyme >gi|1311198|pdb|5LYM|A Chain A, Studies Of Monoclinic Hen Egg White Lysozyme. Iv. X-Ray Refinement At 1.8 Angstrom Resolution And A Comparison Of The Variable Regions In The Polymorphic Forms >gi|1311199|pdb|5LYM|B Chain B, Studies Of Monoclinic Hen Egg White Lysozyme. Iv. X-Ray Refinement At 1.8 Angstrom Resolution And A Comparison Of The Variable Regions In The Polymorphic Forms >gi|1633111|pdb|1UCO|A Chain A, Hen Egg-White Lysozyme, Low Humidity Form >gi|1633112|pdb|1UCO|B Chain B, Hen Egg-White Lysozyme, Low Humidity Form >gi|1942789|pdb|1KIP|C Chain C, Fv Mutant Y(B 32)a (Vh Domain) Of Mouse Monoclonal Antibody D1.3 Complexed With Hen Egg White Lysozyme >gi|1942792|pdb|1KIQ|C Chain C, Fv Mutant Y(B 101)f (Vh Domain) Of Mouse Monoclonal Antibody D1.3 Complexed With Hen Egg White Lysozyme >gi|1942795|pdb|1KIR|C Chain C, Fv Mutant Y(A 50)s (Vl Domain) Of Mouse Monoclonal Antibody D1.3 Complexed With Hen Egg White Lysozyme >gi|2392449|pdb|1MEL|L Chain L, Crystal Structure Of A Camel Single-Domain Vh Antibody Fragment In Complex With Lysozyme >gi|2392450|pdb|1MEL|M Chain M, Crystal Structure Of A Camel Single-Domain Vh Antibody Fragment In Complex With Lysozyme >gi|3212565|pdb|1LKR|A Chain A, Monoclinic Hen Egg White Lysozyme Iodide >gi|3212566|pdb|1LKR|B Chain B, Monoclinic Hen Egg White Lysozyme Iodide >gi|3891491|pdb|1LCN|A Chain A, Monoclinic Hen Egg White Lysozyme, Thiocyanate Complex >gi|3891492|pdb|1LCN|B Chain B, Monoclinic Hen Egg White Lysozyme, Thiocyanate Complex >gi|4139796|pdb|1B2K|A Chain A, Structural Effects Of Monovalent Anions On Polymorphic Lysozyme Crystals >gi|4139797|pdb|1B2K|B Chain B, Structural Effects Of Monovalent Anions On Polymorphic Lysozyme Crystals >gi|4558137|pdb|1BVK|C Chain C, Humanized Anti-Lysozyme Fv Complexed With Lysozyme >gi|4558140|pdb|1BVK|F Chain F, Humanized Anti-Lysozyme Fv Complexed With Lysozyme >gi|5107604|pdb|1LZ8|A Chain A, Lysozyme Phased On Anomalous Signal Of Sulfurs And Chlorines >gi|5107605|pdb|1LZ9|A Chain A, Anomalous Signal Of Solvent Bromines Used For Phasing Of Lysozyme >gi|5542485|pdb|1QTK|A Chain A, Crystal Structure Of Hew Lysozyme Under Pressure Of Krypton (55 Bar) >gi|5821932|pdb|1C10|A Chain A, Crystal Structure Of Hew Lysozyme Under Pressure Of Xenon (8 Bar) >gi|6729692|pdb|1B0D|A Chain A, Structural Effects Of Monovalent Anions On Polymorphic Lysozyme Crystals >gi|6729748|pdb|1BVX|A Chain A, The 1.8 A Structure Of Gel Grown Tetragonal Hen Egg White Lysozyme >gi|6729751|pdb|1BWH|A Chain A, The 1.8 A Structure Of Ground Control Grown Tetragonal Hen Egg White Lysozyme >gi|6729752|pdb|1BWI|A Chain A, The 1.8 A Structure Of Microbatch Oil Drop Grown Tetragonal Hen Egg White Lysozyme >gi|6729753|pdb|1BWJ|A Chain A, The 1.8 A Structure Of Microgravity Grown Tetragonal Hen Egg White Lysozyme >gi|6980518|pdb|1DQJ|C Chain C, Crystal Structure Of The Anti-Lysozyme Antibody Hyhel-63 Complexed With Hen Egg White Lysozyme >gi|6980775|pdb|1DPW|A Chain A, Structure Of Hen Egg-White Lysozyme In Complex With Mpd >gi|6980776|pdb|1DPX|A Chain A, Structure Of Hen Egg-White Lysozyme >gi|9257052|pdb|1F0W|A Chain A, Crystal Structure Of Orthorhombic Lysozyme Grown At Ph 6.5 >gi|9257053|pdb|1F10|A Chain A, Crystal Structure Of Orthorhombic Lysozyme Grown At Ph 6.5 At 88% Relative Humidity >gi|9955193|pdb|1C08|C Chain C, Crystal Structure Of Hyhel-10 Fv-Hen Lysozyme Complex >gi|11513612|pdb|1G7H|C Chain C, Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3(Vlw92a) >gi|11513615|pdb|1G7I|C Chain C, Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3 (Vlw92f) >gi|11513618|pdb|1G7J|C Chain C, Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3 (Vlw92h) >gi|11513622|pdb|1G7L|C Chain C, Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3 (Vlw92s) >gi|11513625|pdb|1G7M|C Chain C, Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3 (Vlw92v) >gi|13096765|pdb|1HF4|A Chain A, Structural Effects Of Monovalent Anions On Polymorphic Lysozyme Crystals >gi|13096766|pdb|1HF4|B Chain B, Structural Effects Of Monovalent Anions On Polymorphic Lysozyme Crystals >gi|14278673|pdb|1QIO|A Chain A, Specific Chemical And Structural Damage Caused By Intense Synchrotron Radiation To Hen Egg White Lysozyme >gi|14719746|pdb|1JA2|A Chain A, Binding Of N-Acetylglucosamine To Chicken Egg Lysozyme: A Powder Diffraction Study >gi|14719747|pdb|1JA4|A Chain A, Binding Of N-Acetylglucosamine To Chicken Egg Lysozyme: A Powder Diffraction Study >gi|14719748|pdb|1JA6|A Chain A, Binding Of N-Acetylglucosamine To Chicken Egg Lysozyme: A Powder Diffraction Study >gi|14719749|pdb|1JA7|A Chain A, Binding Of N-Acetylglucosamine To Chicken Egg Lysozyme: A Powder Diffraction Study >gi|15825790|pdb|1IEE|A Chain A, Structure Of Tetragonal Hen Egg White Lysozyme At 0.94 A From Crystals Grown By The Counter-Diffusion Method >gi|15826220|pdb|1IC4|Y Chain Y, Crystal Structure Of Hyhel-10 Fv Mutant(Hd32a)-Hen Lysozyme Complex >gi|15826223|pdb|1IC5|Y Chain Y, Crystal Structure Of Hyhel-10 Fv Mutant(Hd99a)-Hen Lysozyme Complex >gi|15826226|pdb|1IC7|Y Chain Y, Crystal Structure Of Hyhel-10 Fv Mutant(Hd32a99a)-Hen Lysozyme Complex >gi|16974891|pdb|1JIS|A Chain A, Crystal Structure Of Tetragonal Lysozyme Grown At Ph 4.6 >gi|16974892|pdb|1JIT|A Chain A, Crystal Structure Of Tetragonal Lysozyme Grown In Presence 30% Trehalose >gi|16974893|pdb|1JIY|A Chain A, Crystal Structure Of Tetragonal Lysozyme Grown In Presence 20% Sorbitol >gi|16974894|pdb|1JJ0|A Chain A, Crystal Structure Of Tetragonal Lysozyme Grown In Presence Of 30% Sucrose >gi|16974895|pdb|1JJ1|A Chain A, Crystal Structure Of Orthorhombic Lysozyme Grown At Ph 4.6 In Presence Of 5% Sorbitol >gi|16974896|pdb|1JJ3|A Chain A, Crystal Structure Of Monoclinic Lysozyme Grown At Ph 4.6 >gi|16974897|pdb|1JJ3|B Chain B, Crystal Structure Of Monoclinic Lysozyme Grown At Ph 4.6 >gi|16974944|pdb|1JTO|L Chain L, Degenerate Interfaces In Antigen-Antibody Complexes >gi|16974945|pdb|1JTO|M Chain M, Degenerate Interfaces In Antigen-Antibody Complexes >gi|17943062|pdb|1JTT|L Chain L, Degenerate Interfaces In Antigen-Antibody Complexes >gi|18655908|pdb|1H87|A Chain A, Gadolinium Derivative Of Tetragonal Hen Egg-White Lysozyme At 1.7 A Resolution >gi|21730251|pdb|1GWD|A Chain A, Tri-Iodide Derivative Of Hen Egg-White Lysozyme >gi|24987598|pdb|1LJ3|A Chain A, Crystal Structure Of Monoclinic Lysozyme Grown At Ph 4.6 >gi|24987599|pdb|1LJ3|B Chain B, Crystal Structure Of Monoclinic Lysozyme Grown At Ph 4.6 >gi|24987600|pdb|1LJ4|A Chain A, Crystal Structure Of Monoclinic Lysozyme Grown At Ph 4.6 >gi|24987601|pdb|1LJ4|B Chain B, Crystal Structure Of Monoclinic Lysozyme Grown At Ph 4.6 >gi|24987602|pdb|1LJE|A Chain A, Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 10% Sucrose >gi|24987603|pdb|1LJE|B Chain B, Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 10% Sucrose >gi|24987604|pdb|1LJF|A Chain A, Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 10% Sucrose >gi|24987605|pdb|1LJF|B Chain B, Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 10% Sucrose >gi|24987606|pdb|1LJG|A Chain A, Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 5% Glycerol >gi|24987607|pdb|1LJG|B Chain B, Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 5% Glycerol >gi|24987608|pdb|1LJH|A Chain A, Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 5% Glycerol >gi|24987609|pdb|1LJH|B Chain B, Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 5% Glycerol >gi|24987610|pdb|1LJI|A Chain A, Crystal Structure Of Monoclinic Lysozyme Grown In Presence 10% Sorbitol >gi|24987611|pdb|1LJI|B Chain B, Crystal Structure Of Monoclinic Lysozyme Grown In Presence 10% Sorbitol >gi|24987612|pdb|1LJJ|A Chain A, Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 10% Trehalose >gi|24987613|pdb|1LJJ|B Chain B, Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 10% Trehalose >gi|24987614|pdb|1LJK|A Chain A, Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 15% Trehalose >gi|24987615|pdb|1LJK|B Chain B, Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 15% Trehalose >gi|28373421|pdb|1J1O|Y Chain Y, Crystal Structure Of Hyhel-10 Fv Mutant Ly50f Complexed With Hen Egg White Lysozyme >gi|28373424|pdb|1J1P|Y Chain Y, Crystal Structure Of Hyhel-10 Fv Mutant Ls91a Complexed With Hen Egg White Lysozyme >gi|28373427|pdb|1J1X|Y Chain Y, Crystal Structure Of Hyhel-10 Fv Mutant Ls93a Complexed With Hen Egg White Lysozyme >gi|29726214|pdb|1GPQ|C Chain C, Structure Of Ivy Complexed With Its Target, Hewl >gi|29726215|pdb|1GPQ|D Chain D, Structure Of Ivy Complexed With Its Target, Hewl >gi|30749559|pdb|1N4F|A Chain A, Para-Arsanilate Derivative Of Hen Egg-White Lysozyme >gi|30750168|pdb|1UC0|A Chain A, Crystal Structure Of Wild-Type Hen-Egg White Lysozyme Singly Labeled With 2',3'-Epoxypropyl Beta-Glycoside Of N-Acetyllactosamine >gi|31615673|pdb|1NDM|C Chain C, Crystal Structure Of Fab Fragment Of Antibody Hyhel-26 Complexed With Lysozyme >gi|31616035|pdb|2CDS|A Chain A, Lysozyme >gi|34809779|pdb|1PS5|A Chain A, Structure Of The Monoclinic C2 Form Of Hen Egg-White Lysozyme At 2.0 Angstroms Resolution >gi|42543878|pdb|1UUZ|C Chain C, Ivy:a New Family Of Protein >gi|42543879|pdb|1UUZ|D Chain D, Ivy:a New Family Of Protein >gi|46015071|pdb|1P2C|C Chain C, Crystal Structure Analysis Of An Anti-Lysozyme Antibody >gi|46015074|pdb|1P2C|F Chain F, Crystal Structure Analysis Of An Anti-Lysozyme Antibody >gi|46015774|pdb|1SF4|A Chain A, Binding Of N,n'-diacetylchitobiose To Hew Lysozyme: A Powder Diffraction Study >gi|46015775|pdb|1SF6|A Chain A, Binding Of N,N',N"-Triacetylchitotriose To Hew Lysozyme: A Powder Diffraction Study >gi|46015776|pdb|1SF7|A Chain A, Binding Of Tetra-N-Acetylchitotetraose To Hew Lysozyme: A Powder Diffraction Study >gi|46015778|pdb|1SFB|A Chain A, Binding Of Penta-N-Acetylchitopentaose To Hew Lysozyme: A Powder Diffraction Study >gi|46015779|pdb|1SFG|A Chain A, Binding Of Hexa-N-Acetylchitohexaose: A Powder Diffraction Study >gi|47169220|pdb|1UA6|Y Chain Y, Crystal Structure Of Hyhel-10 Fv Mutant Sfsf Complexed With Hen Egg White Lysozyme Complex >gi|47169430|pdb|1V7T|A Chain A, Triclinic Lysozyme With Low Solvent Content Obtained By Phase Transition >gi|47169431|pdb|1V7T|B Chain B, Triclinic Lysozyme With Low Solvent Content Obtained By Phase Transition >gi|48425893|pdb|1VDP|A Chain A, The Crystal Structure Of The Monoclinic Form Of Hen Egg White Lysozyme At 1.7 Angstroms Resolution In Space >gi|48425894|pdb|1VDP|B Chain B, The Crystal Structure Of The Monoclinic Form Of Hen Egg White Lysozyme At 1.7 Angstroms Resolution In Space >gi|48425895|pdb|1VDQ|A Chain A, The Crystal Structure Of The Orthorhombic Form Of Hen Egg White Lysozyme At 1.5 Angstroms Resolution >gi|48425896|pdb|1VDS|A Chain A, The Crystal Structure Of The Tetragonal Form Of Hen Egg White Lysozyme At 1.6 Angstroms Resolution In Space >gi|48425897|pdb|1VDT|A Chain A, The Crystal Structure Of The Tetragonal Form Of Hen Egg White Lysozyme At 1.7 Angstroms Resolution Under Basic Conditions In Space >gi|48425902|pdb|1VED|A Chain A, The Crystal Structure Of The Orthorhombic Form Of Hen Egg White Lysozyme At 1.9 Angstroms Resolution In Space >gi|52695548|pdb|1SQ2|L Chain L, Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor (nar) Variable Domain In Complex With Lysozyme >gi|52695647|pdb|1T6V|L Chain L, Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor (nar) Variable Domain In Complex With Lysozyme >gi|52695649|pdb|1T6V|M Chain M, Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor (nar) Variable Domain In Complex With Lysozyme >gi|55670850|pdb|1XFP|L Chain L, Crystal Structure Of The Cdr2 Germline Reversion Mutant Of Cab-lys3 In Complex With Hen Egg White Lysozyme >gi|56966684|pdb|1W6Z|A Chain A, High Energy Tetragonal Lysozyme X-ray Structure >gi|58177224|pdb|1WTM|A Chain A, X-Ray Structure Of Hew Lysozyme Orthorhombic Crystal Formed In The Earth's Magnetic Field >gi|58177225|pdb|1WTN|A Chain A, The Structure Of Hew Lysozyme Orthorhombic Crystal Growth Under A High Magnetic Field >gi|60593440|pdb|1RI8|B Chain B, Crystal Structure Of The Camelid Single Domain Antibody 1d2l19 In Complex With Hen Egg White Lysozyme >gi|60593442|pdb|1RJC|B Chain B, Crystal Structure Of The Camelid Single Domain Antibody Cab-Lys2 In Complex With Hen Egg White Lysozyme >gi|61680684|pdb|1YIK|A Chain A, Structure Of Hen Egg White Lysozyme Soaked With Cu-Cyclam >gi|61680685|pdb|1YIL|A Chain A, Structure Of Hen Egg White Lysozyme Soaked With Cu2- Xylylbicyclam >gi|62738107|pdb|1VAT|A Chain A, Iodine Derivative Of Hen Egg-White Lysozyme >gi|62738108|pdb|1VAU|A Chain A, Xenon Derivative Of Hen Egg-White Lysozyme >gi|66361153|pdb|1YQV|Y Chain Y, The Crystal Structure Of The Antibody Fab Hyhel5 Complex With Lysozyme At 1.7a Resolution >gi|71042052|pdb|1YKX|X Chain X, Effect Of Alcohols On Protein Hydration >gi|71042053|pdb|1YKY|X Chain X, Effect Of Alcohols On Protein Hydration >gi|71042054|pdb|1YKZ|X Chain X, Effect Of Alcohols On Protein Hydration >gi|71042055|pdb|1YL0|X Chain X, Effect Of Alcohols On Protein Hydration >gi|71042056|pdb|1YL1|X Chain X, Effect Of Alcohols On Protein Hydration >gi|71042165|pdb|1Z55|A Chain A, Effect Of Alcohols On Protein Hydration >gi|73535277|pdb|1T3P|A Chain A, Half-Sandwich Arene Ruthenium(Ii)-Enzyme Complex >gi|73536160|pdb|2A7D|A Chain A, On The Routine Use Of Soft X-Rays In Macromolecular Crystallography, Part Iii- The Optimal Data Collection Wavelength >gi|73536162|pdb|2A7F|A Chain A, On The Routine Use Of Soft X-Rays In Macromolecular Crystallography, Part Iii- The Optimal Data Collection Wavelength >gi|75765481|pdb|1XGP|C Chain C, Structure For Antibody Hyhel-63 Y33a Mutant Complexed With Hen Egg Lysozyme >gi|75765484|pdb|1XGQ|C Chain C, Structure For Antibody Hyhel-63 Y33v Mutant Complexed With Hen Egg Lysozyme >gi|75765487|pdb|1XGR|C Chain C, Structure For Antibody Hyhel-63 Y33i Mutant Complexed With Hen Egg Lysozyme >gi|75765490|pdb|1XGT|C Chain C, Structure For Antibody Hyhel-63 Y33l Mutant Complexed With Hen Egg Lysozyme >gi|75765493|pdb|1XGU|C Chain C, Structure For Antibody Hyhel-63 Y33f Mutant Complexed With Hen Egg Lysozyme >gi|78101077|pdb|1ZMY|L Chain L, Cabbcii-10 Vhh Framework With Cdr Loops Of Cablys3 Grafted On It And In Complex With Hen Egg White Lysozyme >gi|78101078|pdb|1ZMY|M Chain M, Cabbcii-10 Vhh Framework With Cdr Loops Of Cablys3 Grafted On It And In Complex With Hen Egg White Lysozyme >gi|78101618|pdb|2BLX|A Chain A, Hewl Before A High Dose X-Ray "burn" >gi|78101619|pdb|2BLY|A Chain A, Hewl After A High Dose X-Ray "burn" >gi|83753118|pdb|1HC0|A Chain A, Structure Of Lysozyme With Periodate >gi|83754039|pdb|2AUB|A Chain A, Lysozyme Structure Derived From Thin-Film-Based Crystals >gi|83754937|pdb|2D6B|A Chain A, Novel Bromate Species Trapped Within A Protein Crystal >gi|85544073|pdb|2A6U|A Chain A, Ph Evolution Of Tetragonal Hewl At 4 Degrees Celcius. >gi|93278622|pdb|1ZV5|L Chain L, Crystal Structure Of The Variable Domain Of The Camelid Heavy-Chain Antibody D2-L29 In Complex With Hen Egg White Lysozyme >gi|93278625|pdb|1ZVH|L Chain L, Crystal Stucture Of The Vhh Domain D2-L24 In Complex With Hen Egg White Lysozyme >gi|93278629|pdb|1ZVY|B Chain B, Crystal Structure Of The Vhh D3-l11 In Complex With Hen Egg White Lysozyme >gi|93278991|pdb|2C8O|A Chain A, Lysozyme (1sec) And Uv Lasr Excited Fluorescence >gi|93278992|pdb|2C8P|A Chain A, Lysozyme (60sec) And Uv Laser Excited Fluorescence >gi|93279480|pdb|2FBB|A Chain A, Crystal Structure Analysis Of Hexagonal Lysozyme >gi|99032133|pdb|2F2N|A Chain A, Triclinic Hen Egg Lysozyme Cross-linked By Glutaraldehyde >gi|99032137|pdb|2F30|A Chain A, Triclinic Cross-Linked Lysozyme Soaked With 4.5m Urea >gi|99032152|pdb|2F4A|A Chain A, Triclinic Cross-linked Lysozyme Soaked With Thiourea 1.5m >gi|99032153|pdb|2F4G|A Chain A, Triclinic Cross-Linked Lysozyme Soaked In Bromoethanol 1m >gi|112490403|pdb|2D4I|A Chain A, Monoclinic Hen Egg-White Lysozyme Crystallized At Ph4.5 Form Heavy Water Solution >gi|112490404|pdb|2D4I|B Chain B, Monoclinic Hen Egg-White Lysozyme Crystallized At Ph4.5 Form Heavy Water Solution >gi|112490406|pdb|2D4J|A Chain A, Transformed Monoclinic Crystal Of Hen Egg-White Lysozyme From A Heavy Water Solution >gi|112490408|pdb|2D4K|A Chain A, Monoclinic Hen Egg-White Lysozyme Crystallized At 313k >gi|112490409|pdb|2D4K|N Chain N, Monoclinic Hen Egg-White Lysozyme Crystallized At 313k >gi|112490429|pdb|2D91|A Chain A, Structure Of Hyper-Vil-Lysozyme >gi|114793537|pdb|2BPU|A Chain A, The Kedge Holmium Derivative Of Hen Egg-White Lysozyme At High Resolution From Single Wavelength Anomalous Diffraction >gi|114794494|pdb|2HS7|A Chain A, Multipattern Rietveld Refinement With Protein Powder Data: An Approach To Higher Resolution >gi|114794495|pdb|2HS9|A Chain A, Multipattern Rietveld Refinement With Protein Powder Data: An Approach To Higher Resolution >gi|114794503|pdb|2HSO|A Chain A, Multipattern Rietveld Refinement With Protein Powder Data: An Approach To Higher Resolution >gi|116666784|pdb|2B5Z|A Chain A, Hen Lysozyme Chemically Glycosylated >gi|119389068|pdb|2CGI|A Chain A, Siras Structure Of Tetragonal Lysosyme Using Derivative Data Collected At The High Energy Remote Holmium Kedge >gi|122920551|pdb|2I6Z|A Chain A, X-Ray Diffraction Studies Of Adducts Between Anticancer Platinum Drugs And Hen Egg White Lysozyme >gi|126030258|pdb|2DQC|Y Chain Y, Crystal Structure Of Hyhel-10 Fv Mutant(Hy33f) Complexed With Hen Egg Lysozyme >gi|126030261|pdb|2DQD|Y Chain Y, Crystal Structure Of Hyhel-10 Fv Mutant (Hy50f) Complexed With Hen Egg Lysozyme >gi|126030264|pdb|2DQE|Y Chain Y, Crystal Structure Of Hyhel-10 Fv Mutant (Hy53a) Complexed With Hen Egg Lysozyme >gi|126030267|pdb|2DQF|C Chain C, Crystal Structure Of Hyhel-10 Fv Mutant (Y33ay53a) Complexed With Hen Egg Lysozyme >gi|126030270|pdb|2DQF|F Chain F, Crystal Structure Of Hyhel-10 Fv Mutant (Y33ay53a) Complexed With Hen Egg Lysozyme >gi|126030273|pdb|2DQG|Y Chain Y, Crystal Structure Of Hyhel-10 Fv Mutant (Hy53f) Complexed With Hen Egg Lysozyme >gi|126030276|pdb|2DQH|Y Chain Y, Crystal Structure Of Hyhel-10 Fv Mutant (Hy58a) Complexed With Hen Egg Lysozyme >gi|126030279|pdb|2DQI|Y Chain Y, Crystal Structure Of Hyhel-10 Fv Mutant (Ly50a) Complexed With Hen Egg Lysozyme >gi|126030282|pdb|2DQJ|Y Chain Y, Crystal Structure Of Hyhel-10 Fv (Wild-Type) Complexed With Hen Egg Lysozyme At 1.8a Resolution >gi|134104341|pdb|2G4P|A Chain A, Anomalous Substructure Of Lysozyme At Ph 4.5 >gi|134104342|pdb|2G4Q|A Chain A, Anomalous Substructure Of Lysozyme At Ph 8.0 >gi|134104486|pdb|2I25|L Chain L, Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor Pbla8 Variable Domain In Complex With Lysozyme >gi|134104488|pdb|2I25|M Chain M, Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor Pbla8 Variable Domain In Complex With Lysozyme >gi|134104490|pdb|2I26|L Chain L, Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor Ancestral Variable Domain In Complex With Lysozyme >gi|134104492|pdb|2I26|M Chain M, Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor Ancestral Variable Domain In Complex With Lysozyme >gi|134104494|pdb|2I26|Q Chain Q, Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor Ancestral Variable Domain In Complex With Lysozyme >gi|146387197|pdb|2YVB|A Chain A, High Resolution X-ray Crystal Structure Of Tetragonal Hen Egg White Lysozyme >gi|146387243|pdb|2EPE|A Chain A, Crystal Structure Analysis Of Hen Egg White Lysozyme Grown By Capillary Method >gi|146387510|pdb|2H9J|A Chain A, Structure Of Hen Egg White Lysozyme Soaked With Ni2- Xylylbicyclam >gi|146387511|pdb|2H9K|A Chain A, Structure Of Hen Egg White Lysozyme Soaked With Ni-Cyclam >gi|149242090|pdb|2HTX|A Chain A, Crystal Structure Analysis Of Hen Egg White Lysozyme Crosslinked By Polymerized Glutaraldehyde In Acidic Environment >gi|149242091|pdb|2HU1|A Chain A, Crystal Structure Analysis Of Hen Egg White Lyszoyme >gi|157829624|pdb|193L|A Chain A, The 1.33 A Structure Of Tetragonal Hen Egg White Lysozyme >gi|157829625|pdb|194L|A Chain A, The 1.40 A Structure Of Spacehab-01 Hen Egg White Lysozyme >gi|157829924|pdb|1AKI|A Chain A, The Structure Of The Orthorhombic Form Of Hen Egg-White Lysozyme At 1.5 Angstroms Resolution >gi|157830155|pdb|1AZF|A Chain A, Chicken Egg White Lysozyme Crystal Grown In Bromide Solution >gi|157830296|pdb|1BGI|A Chain A, Orthorhombic Lysozyme Crystallized At High Temperature (310k) >gi|157830322|pdb|1BHZ|A Chain A, Low Temperature Middle Resolution Structure Of Hen Egg White Lysozyme From Masc Data >gi|157831312|pdb|1HEL|A Chain A, Structural And Thermodynamic Analysis Of Compensating Mutations Within The Core Of Chicken Egg White Lysozyme >gi|157831320|pdb|1HEW|A Chain A, Refinement Of An Enzyme Complex With Inhibitor Bound At Partial Occupancy. Hen Egg-White Lysozyme And Tri-N-Acetylchitotriose At 1.75 Angstroms Resolution >gi|157831389|pdb|1HSW|A Chain A, Lysozyme (Mucopeptide N-Acetylmuramyl Hydrolase) >gi|157831390|pdb|1HSX|A Chain A, Lysozyme Grown At Basic Ph And Its Low Humidity Variant >gi|157831568|pdb|1JPO|A Chain A, Low Temperature Orthorhombic Lysozyme >gi|157831840|pdb|1LKS|A Chain A, Hen Egg White Lysozyme Nitrate >gi|157831846|pdb|1LMA|A Chain A, Protein Hydration And Water Structure: X-Ray Analysis Of A Closely Packed Protein Crystal With Very Low Solvent Content >gi|157831859|pdb|1LPI|A Chain A, Hew Lysozyme: Trp...Na Cation-Pi Interaction >gi|157831875|pdb|1LSA|A Chain A, The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water >gi|157831876|pdb|1LSB|A Chain A, The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water >gi|157831877|pdb|1LSC|A Chain A, The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water >gi|157831878|pdb|1LSD|A Chain A, The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water >gi|157831879|pdb|1LSE|A Chain A, The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water >gi|157831880|pdb|1LSF|A Chain A, The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water >gi|157831906|pdb|1LYO|A Chain A, Cross-Linked Lysozyme Crystal In Neat Water >gi|157831909|pdb|1LYZ|A Chain A, Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme >gi|157831915|pdb|1LZA|A Chain A, Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg-White Lysozyme Complexes And Their Hydrolytic Activity >gi|157831916|pdb|1LZB|A Chain A, Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg- White Lysozyme Complexes And Their Hydrolytic Activity >gi|157831917|pdb|1LZC|A Chain A, Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg- White Lysozyme Complexes And Their Hydrolytic Activity >gi|157831922|pdb|1LZT|A Chain A, Refinement Of Triclinic Lysozyme >gi|157833676|pdb|1RFP|A Chain A, Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains >gi|157834081|pdb|1UIG|A Chain A, Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains >gi|157834082|pdb|1UIH|A Chain A, Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains >gi|157834233|pdb|1XEI|A Chain A, The Crystal Structures Of Lysozyme At Very Low Levels Of Hydration >gi|157834234|pdb|1XEJ|A Chain A, The Crystal Structures Of Lysozyme At Very Low Levels Of Hydration >gi|157834235|pdb|1XEK|A Chain A, The Crystal Structures Of Lysozyme At Very Low Levels Of Hydration >gi|157835094|pdb|2HU3|A Chain A, Parent Structure Of Hen Egg White Lysozyme Grown In Acidic Ph 4.8. Refinement For Comparison With Crosslinked Molecules Of Lysozyme >gi|157835095|pdb|2HUB|A Chain A, Structure Of Hen Egg-White Lysozyme Determined From Crystals Grown In Ph 7.5 >gi|157835326|pdb|2LYM|A Chain A, Crystal Structure Of Hen Egg-White Lysozyme At A Hydrostatic Pressure Of 1000 Atmospheres >gi|157835327|pdb|2LYO|A Chain A, Cross-Linked Chicken Lysozyme Crystal In 90% Acetonitrile- Water >gi|157835328|pdb|2LYZ|A Chain A, Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme >gi|157835330|pdb|2LZH|A Chain A, The Structures Of The Monoclinic And Orthorhombic Forms Of Hen Egg-White Lysozyme At 6 Angstroms Resolution. >gi|157835332|pdb|2LZT|A Chain A, Refinement Of Triclinic Lysozyme. Ii. The Method Of Stereochemically Restrained Least-Squares >gi|157836840|pdb|3LYM|A Chain A, Crystal Structure Of Hen Egg-White Lysozyme At A Hydrostatic Pressure Of 1000 Atmospheres >gi|157836841|pdb|3LYO|A Chain A, Cross-Linked Chicken Lysozyme Crystal In 95% Acetonitrile- Water >gi|157836842|pdb|3LYZ|A Chain A, Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme >gi|157836845|pdb|3LZT|A Chain A, Refinement Of Triclinic Lysozyme At Atomic Resolution >gi|157836964|pdb|4LYM|A Chain A, Crystal Structure Of Low Humidity Tetragonal Lysozyme At 2.1-Angstroms Resolution. Variability In Hydration Shell And Its Structural Consequences >gi|157836965|pdb|4LYO|A Chain A, Cross-Linked Chicken Lysozyme Crystal In Neat Acetonitrile, Then Back-Soaked In Water >gi|157836966|pdb|4LYZ|A Chain A, Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme >gi|157836968|pdb|4LZT|A Chain A, Atomic Resolution Refinement Of Triclinic Hew Lysozyme At 295k >gi|157837051|pdb|5LYT|A Chain A, Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambient Temperatures >gi|157837052|pdb|5LYZ|A Chain A, Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme >gi|157837108|pdb|6LYT|A Chain A, Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambient Temperatures >gi|157837109|pdb|6LYZ|A Chain A, Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme >gi|157837147|pdb|7LYZ|A Chain A, Protein Model Building By The Use Of A Constrained- Restrained Least-Squares Procedure >gi|157837177|pdb|8LYZ|A Chain A, An X-Ray Study Of The Structure And Binding Properties Of Iodine-Inactivated Lysozyme >gi|157874504|pdb|1E8L|A Chain A, Nmr Solution Structure Of Hen Lysozyme >gi|157878058|pdb|1GXV|2 Chain 2, Solution Structure Of Lysozyme At Low And High Pressure >gi|157878060|pdb|1GXX|A Chain A, Solution Structure Of Lysozyme At Low And High Pressure >gi|158431177|pdb|2VB1|A Chain A, Hewl At 0.65 Angstrom Resolution >gi|162329969|pdb|2Q0M|X Chain X, Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein >gi|170292142|pdb|2EIZ|C Chain C, Crystal Structure Of Humanized Hyhel-10 Fv Mutant(hw47y)-hen Lysozyme Complex >gi|170292443|pdb|2Z12|A Chain A, Structure Of The Transformed Monoclinic Lysozyme By Controlled Dehydration >gi|170292444|pdb|2Z18|A Chain A, Phase Transition Of Monoclinic Lysozyme Crystal Soaked In A 10% Nacl Solution >gi|170292445|pdb|2Z19|A Chain A, Phase Transition Of Monoclinic Lysozyme Crystal Soaked In A Saturated Nacl Solution >gi|170784957|pdb|2EKS|C Chain C, Crystal Structure Of Humanized Hyhel-10 Fv-Hen Lysozyme Complex >gi|171848758|pdb|2PC2|A Chain A, Lysozyme Cocrystallized With Tris-Dipicolinate Eu Complex >gi|178847402|pdb|2YSS|C Chain C, Crystal Structure Of Humanized Hyhel-10 Fv Mutant(Hq39kw47y)-Hen Lysozyme Complex >gi|190016419|pdb|3D9A|C Chain C, High Resolution Crystal Structure Structure Of Hyhel10 Fab Complexed To Hen Egg Lysozyme >gi|208435584|pdb|2ZQ3|A Chain A, The Crystal Structure Of The Orthorhombic Form Of Hen Egg White Lysozyme At 1.6 Angstroms Resolution >gi|208435585|pdb|2ZQ4|A Chain A, The Crystal Structure Of The Orthorhombic Form Of Hen Egg White Lysozyme At 2.0 Angstroms Resolution >gi|210060866|pdb|2W1L|A Chain A, The Interdependence Of Wavelength, Redundancy And Dose In Sulfur Sad Experiments: 0.979 A Wavelength 991 Images Data >gi|210061006|pdb|3E3D|A Chain A, Structure Of Hen Egg White Lysozyme With The Magic Triangle I3c >gi|210061083|pdb|3EXD|A Chain A, Sulfur-Sad Phased Hewl Crystal >gi|211939074|pdb|2W1M|A Chain A, The Interdependence Of Wavelength, Redundancy And Dose In Sulfur Sad Experiments: 2.070 A Wavelength With 2theta 30 Degrees Data >gi|211939075|pdb|2W1X|A Chain A, The Interdependence Of Wavelength, Redundancy And Dose In Sulfur Sad Experiments: 1.284 A Wavelength 360 Images Data >gi|215261103|pdb|2W1Y|A Chain A, The Interdependence Of Wavelength, Redundancy And Dose In Sulfur Sad Experiments: 1.540 A Wavelength 180 Images Data >gi|218766896|pdb|3F6Z|A Chain A, Crystal Structure Of Pseudomonas Aeruginosa Mlic In Complex With Hen Egg White Lysozyme >gi|218766898|pdb|3F6Z|C Chain C, Crystal Structure Of Pseudomonas Aeruginosa Mlic In Complex With Hen Egg White Lysozyme >gi|222143022|pdb|2ZNW|Y Chain Y, Crystal Structure Of Scfv10 In Complex With Hen Egg Lysozyme >gi|222143024|pdb|2ZNW|Z Chain Z, Crystal Structure Of Scfv10 In Complex With Hen Egg Lysozyme >gi|222143026|pdb|2ZNX|Y Chain Y, 5-fluorotryptophan Incorporated Scfv10 Complexed To Hen Egg Lysozyme >gi|222143028|pdb|2ZNX|Z Chain Z, 5-fluorotryptophan Incorporated Scfv10 Complexed To Hen Egg Lysozyme >gi|223673880|pdb|2ZYP|A Chain A, X-Ray Structure Of Hen Egg-White Lysozyme With Poly(Allyl Amine) >gi|241913321|pdb|3G3A|B Chain B, Structure Of A Lamprey Variable Lymphocyte Receptor In Complex With A Protein Antigen >gi|241913323|pdb|3G3A|D Chain D, Structure Of A Lamprey Variable Lymphocyte Receptor In Complex With A Protein Antigen >gi|241913325|pdb|3G3A|F Chain F, Structure Of A Lamprey Variable Lymphocyte Receptor In Complex With A Protein Antigen >gi|241913327|pdb|3G3A|H Chain H, Structure Of A Lamprey Variable Lymphocyte Receptor In Complex With A Protein Antigen >gi|241913329|pdb|3G3B|B Chain B, Structure Of A Lamprey Variable Lymphocyte Receptor Mutant In Complex With A Protein Antigen >gi|241913331|pdb|3G3B|D Chain D, Structure Of A Lamprey Variable Lymphocyte Receptor Mutant In Complex With A Protein Antigen >gi|241913333|pdb|3G3B|F Chain F, Structure Of A Lamprey Variable Lymphocyte Receptor Mutant In Complex With A Protein Antigen >gi|241913335|pdb|3G3B|H Chain H, Structure Of A Lamprey Variable Lymphocyte Receptor Mutant In Complex With A Protein Antigen >gi|281500700|pdb|3A67|Y Chain Y, Crystal Structure Of Hyhel-10 Fv Mutant Ln31d Complexed With White Lysozyme >gi|281500703|pdb|3A6B|Y Chain Y, Crystal Structure Of Hyhel-10 Fv Mutant Ln32d Complexed With White Lysozyme >gi|281500706|pdb|3A6C|Y Chain Y, Crystal Structure Of Hyhel-10 Fv Mutant Ln92d Complexed With White Lysozyme >gi|288965533|pdb|3KAM|A Chain A, Hen Egg White Lysozyme Derivatized With Rhenium(I) Diaquatricarbonyl Cation >gi|290789911|pdb|3A8Z|A Chain A, Crystal Structure Of Hen Egg White Lysozyme >gi|290789912|pdb|3A90|A Chain A, Crystal Structure Of Hen Egg White Lysozyme Soaked With 1mm Rhcl3 >gi|290789913|pdb|3A91|A Chain A, Crystal Structure Of Hen Egg White Lysozyme Soaked With 5mm Rhcl3 >gi|290789914|pdb|3A92|A Chain A, Crystal Structure Of Hen Egg White Lysozyme Soaked With 10mm Rhcl3 >gi|290789915|pdb|3A93|A Chain A, Crystal Structure Of Hen Egg White Lysozyme Soaked With 30mm Rhcl3 >gi|290789916|pdb|3A94|A Chain A, Crystal Structure Of Hen Egg White Lysozyme Soaked With 100mm Rhcl3 >gi|290789917|pdb|3A95|A Chain A, Crystal Structure Of Hen Egg White Lysozyme Soaked With 100mm Rhcl3 At Ph3.8 >gi|290789918|pdb|3A96|A Chain A, Crystal Structure Of Hen Egg White Lysozyme Soaked With 100mm Rhcl3 At Ph2.2 >gi|291463760|pdb|3M3U|A Chain A, Effect Of Temperature On Tryptophan Fluorescence In Lysozyme Crystals >gi|298508304|pdb|3A34|A Chain A, Effect Of Ariginine On Lysozyme >gi|299856772|pdb|3M18|B Chain B, Crystal Structure Of Variable Lymphocyte Receptor Vlra.R2.1 In Complex With Hen Egg Lysozyme >gi|302566072|pdb|3IJU|A Chain A, Chicken Egg White Lysozyme By Highly Ordered Apa (Anodic Porous Alumina) Nanotemplate Crystallization Method >gi|302566073|pdb|3IJV|A Chain A, Chicken Egg White Lysozyme By Classical Hanging Drop Vapour Diffusion Method >gi|312597037|pdb|2XBR|A Chain A, Raman Crystallography Of Hen White Egg Lysozyme - Low X-Ray Dose (0.2 Mgy) >gi|312597038|pdb|2XBS|A Chain A, Raman Crystallography Of Hen White Egg Lysozyme - High X- Ray Dose (16 Mgy) >gi|313754056|pdb|2XTH|A Chain A, K2ptbr6 Binding To Lysozyme >gi|315364362|pdb|2X0A|A Chain A, Mpd-Lysozyme Structure At 55.5 Kev Using A Trixxel Csi-Asi Based Digital Imager And The New Esrf U22 Undulator Source At Id15 >gi|320089688|pdb|2XJW|A Chain A, Lysozyme-Co Releasing Molecule Adduct >gi|322812501|pdb|3P4Z|A Chain A, Time-Dependent And Protein-Directed In Situ Growth Of Gold Nanoparticles In A Single Crystal Of Lysozyme >gi|322812504|pdb|3P64|A Chain A, Time-Dependent And Protein-Directed In Situ Growth Of Gold Nanoparticles In A Single Crystal Of Lysozyme >gi|322812505|pdb|3P65|A Chain A, Time-Dependent And Protein-Directed In Situ Growth Of Gold Nanoparticles In A Single Crystal Of Lysozyme >gi|322812506|pdb|3P66|A Chain A, Time-Dependent And Protein-Directed In Situ Growth Of Gold Nanoparticles In A Single Crystal Of Lysozyme >gi|322812507|pdb|3P68|A Chain A, Time-Dependent And Protein-Directed In Situ Growth Of Gold Nanoparticles In A Single Crystal Of Lysozyme >gi|323462842|pdb|3AJN|A Chain A, Structural Basis Of Glycine Amide On Suppression Of Protein Aggregation By High Resolution X-Ray Analysis >gi|326634180|pdb|3AGG|G Chain G, X-Ray Analysis Of Lysozyme In The Absence Of Arg >gi|326634181|pdb|3AGH|A Chain A, X-Ray Analysis Of Lysozyme In The Presence Of 200 Mm Arg >gi|326634182|pdb|3AGI|A Chain A, High Resolution X-Ray Analysis Of Arg-Lysozyme Complex In The Presence Of 500 Mm Arg >gi|327200550|pdb|3AW6|A Chain A, Crystal Structure Of Tetragonal Hen Egg White Lysozyme At 84.2% Relative Humidity >gi|327200551|pdb|3AW7|A Chain A, Crystal Structure Of Tetragonal Hen Egg White Lysozyme At 71.9% Relative Humidity >gi|333361483|pdb|3RNX|A Chain A, Crystal Structure Of Lysozyme In 30% Ethanol >gi|333944640|pdb|3RW8|A Chain A, Crystal Structure Of Lysozyme In 40% Ethanol >gi|333944645|pdb|3RZ4|A Chain A, Hen Egg-White Lysozyme In Hepes Buffer At Ph 7.5 >gi|335892269|pdb|3N9A|A Chain A, Mite-Y Lysozyme: Vegemite >gi|335892270|pdb|3N9C|A Chain A, Mite-Y Lysozyme: Marmite >gi|335892271|pdb|3N9E|A Chain A, Mite-Y Lysozyme: Promite >gi|340708138|pdb|3RT5|X Chain X, Lysozyme In 30% Propanol >gi|340780277|pdb|2YBH|A Chain A, Nitrate X-Ray Induced Reduction On Hewl Crystals (2.31 Mgy). >gi|340780278|pdb|2YBI|A Chain A, Nitrate X-Ray Induced Reduction On Hewl Crystals (6.62 Mgy) >gi|340780279|pdb|2YBJ|A Chain A, Nitrate X-Ray Induced Reduction On Hewl Crystals (12.31 Mgy) >gi|340780280|pdb|2YBL|A Chain A, Nitrate X-Ray Induced Reduction On Hewl Crystals (17.9 Mgy) >gi|340780281|pdb|2YBM|A Chain A, Nitrate X-Ray Induced Reduction On Hewl Crystals (23.3 Mgy) >gi|340780282|pdb|2YBN|A Chain A, Nitrate X-Ray Induced Reduction On Hewl Crystals (28.6 Mgy) >gi|340780283|pdb|2YDG|A Chain A, Ascorbate Co-Crystallized Hewl. >gi|344189852|pdb|3T6U|A Chain A, Crystal Structure Of Lysozyme In 40% Sucrose >gi|345101063|pdb|3SP3|A Chain A, Lysozyme In 20% Sucrose >gi|345101119|pdb|9LYZ|A Chain A, X-Ray Crystallography Of The Binding Of The Bacterial Cell Wall Trisaccharide Nam-Nag-Nam To Lysozyme >gi|358009560|pdb|3RU5|A Chain A, Silver Metallated Hen Egg White Lysozyme At 1.35 A >gi|358440267|pdb|4A7D|A Chain A, X-Ray Crystal Structure Of Hewl Flash-Cooled At High Pressure >gi|365813422|pdb|4A8A|M Chain M, Asymmetric Cryo-Em Reconstruction Of E. Coli Degq 12-Mer In Complex With Lysozyme >gi|371927616|pdb|3ULR|A Chain A, Lysozyme Contamination Facilitates Crystallization Of A Hetero- Trimericcortactin:arg:lysozyme Complex >gi|371927807|pdb|4A8B|M Chain M, Symmetrized Cryo-Em Reconstruction Of E. Coli Degq 12-Mer In Complex With Lysozymes >gi|371927808|pdb|4A8B|N Chain N, Symmetrized Cryo-Em Reconstruction Of E. Coli Degq 12-Mer In Complex With Lysozymes >gi|371927809|pdb|4A8B|O Chain O, Symmetrized Cryo-Em Reconstruction Of E. Coli Degq 12-Mer In Complex With Lysozymes >gi|371927810|pdb|4A8B|P Chain P, Symmetrized Cryo-Em Reconstruction Of E. Coli Degq 12-Mer In Complex With Lysozymes >gi|371927811|pdb|4A8B|Q Chain Q, Symmetrized Cryo-Em Reconstruction Of E. Coli Degq 12-Mer In Complex With Lysozymes >gi|371927812|pdb|4A8B|R Chain R, Symmetrized Cryo-Em Reconstruction Of E. Coli Degq 12-Mer In Complex With Lysozymes >gi|372466859|pdb|3QE8|A Chain A, Crystal Structure Analysis Of Lysozyme-Bound Fac-[re(Co)3(H2o)(Im)]+ >gi|372466860|pdb|3QE8|B Chain B, Crystal Structure Analysis Of Lysozyme-Bound Fac-[re(Co)3(H2o)(Im)]+ >gi|372466868|pdb|3QNG|A Chain A, Crystal Structure Analysis Of Lysozyme-Bound Fac-[re(Co)3(L-Serine)] >gi|379318265|pdb|3ATN|A Chain A, Glycine Ethyl Ester Shielding On The Aromatic Surfaces Of Lysozyme: Implication For Suppression Of Protein Aggregation >gi|379318266|pdb|3ATO|A Chain A, Glycine Ethyl Ester Shielding On The Aromatic Surfaces Of Lysozyme: Implication For Suppression Of Protein Aggregation >gi|385252041|pdb|4DD0|A Chain A, Eval Processed Hewl, Cisplatin Aqueous Glycerol >gi|385252042|pdb|4DD1|A Chain A, Eval Processed Hewl, Cisplatin Aqueous Paratone >gi|385252043|pdb|4DD1|B Chain B, Eval Processed Hewl, Cisplatin Aqueous Paratone >gi|385252044|pdb|4DD2|A Chain A, Eval Processed Hewl, Carboplatin Aqueous Glycerol >gi|385252045|pdb|4DD3|A Chain A, Eval Processed Hewl, Carboplatin Aqueous Paratone >gi|385252046|pdb|4DD4|A Chain A, Eval Processed Hewl, Cisplatin Dmso Glycerol >gi|385252047|pdb|4DD6|A Chain A, Eval Processed Hewl, Cisplatin Dmso Paratone >gi|385252048|pdb|4DD7|A Chain A, Eval Processed Hewl, Carboplatin Dmso Glycerol >gi|385252049|pdb|4DD9|A Chain A, Eval Processed Hewl, Carboplatin Dmso Paratone >gi|385252050|pdb|4DDA|A Chain A, Eval Processed Hewl, Nag >gi|385252051|pdb|4DDB|A Chain A, Eval Processed Hewl, Cisplatin Dmso Paratone Ph 6.5 >gi|385252052|pdb|4DDC|A Chain A, Eval Processed Hewl, Cisplatin Dmso Nag Silicone Oil >gi|385252053|pdb|4DDC|B Chain B, Eval Processed Hewl, Cisplatin Dmso Nag Silicone Oil >gi|386783092|pdb|3AZ4|A Chain A, Crystal Structure Of Co/o-hewl >gi|386783093|pdb|3AZ5|A Chain A, Crystal Structure Of Pt/o-hewl >gi|386783094|pdb|3AZ6|A Chain A, Crystal Structure Of Co/t-hewl >gi|386783095|pdb|3AZ7|A Chain A, Crystal Structure Of Pt/t-hewl >gi|390981189|pdb|4ET8|A Chain A, Hen Egg-White Lysozyme Solved From 40 Fs Free-Electron Laser Pulse Data >gi|390981190|pdb|4ET9|A Chain A, Hen Egg-White Lysozyme Solved From 5 Fs Free-Electron Laser Pulse Data >gi|390981191|pdb|4ETA|A Chain A, Lysozyme, Room Temperature, 400 Kgy Dose >gi|390981192|pdb|4ETB|A Chain A, Lysozyme, Room Temperature, 200 Kgy Dose >gi|390981193|pdb|4ETC|A Chain A, Lysozyme, Room Temperature, 24 Kgy Dose >gi|390981194|pdb|4ETD|A Chain A, Lysozyme, Room-Temperature, Rotating Anode, 0.0026 Mgy >gi|390981195|pdb|4ETE|A Chain A, Lysozyme, Room-Temperature, Rotating Anode, 0.0021 Mgy >gi|395759327|pdb|4AGA|A Chain A, Hofmeister Effects Of Ionic Liquids In Protein Crystallization: Direct And Water-Mediated Interactions >gi|400261223|pdb|4E3U|A Chain A, Crystal Structure Of Hen Egg White Lysozyme Cryoprotected In Proline >gi|401871480|pdb|4B49|A Chain A, 1.15 A Structure Of Lysozyme Crystallized Without 2-Methyl- 2,4-Pentanediol >gi|401871481|pdb|4B4E|A Chain A, 1.00 A Structure Of Lysozyme Crystallized With (r)-2-methyl-2,4-pentanediol >gi|401871482|pdb|4B4I|A Chain A, 1.20 A Structure Of Lysozyme Crystallized With (S)-2-Methyl-2,4-Pentanediol >gi|401871483|pdb|4B4J|A Chain A, 1.25 A Structure Of Lysozyme Crystallized With (rs)-2-methyl-2,4-pentanediol >gi|404312871|pdb|4DT3|A Chain A, Crystal Structure Of Zinc-charged Lysozyme >gi|409973768|pdb|4B0D|A Chain A, Crystal Structure Of Hen Egg White Lysozyme From An Auto Harvested Crystal >gi|409974059|pdb|4H1P|A Chain A, Use Of Europium For Sad Phasing At The Cu K Alpha Wavelength >gi|410375168|pdb|3EMS|A Chain A, Effect Of Ariginine On Lysozyme >gi|410562525|pdb|4AXT|A Chain A, Crystal Structure Of Hen Egg White Lysozyme From An Auto Harvested Crystal, Control Experiment >gi|411024302|pdb|4G49|A Chain A, Room Temperature X-ray Diffraction Of Cisplatin Binding To Hewl In Aqueous Media After 15 Months Of Crystal Storage >gi|411024303|pdb|4G4A|A Chain A, Room Temperature X-ray Diffraction Studies Of Cisplatin Binding To Hewl In Dmso Media After 14 Months Of Crystal Storage >gi|411024304|pdb|4G4B|A Chain A, Room Temperature X-ray Diffraction Study Of Cisplatin Binding To Hewl In Dmso Media With Nag After 7 Months Of Crystal Storage >gi|411024305|pdb|4G4C|A Chain A, Room Temperature X-ray Diffraction Study Of Carboplatin Binding To Hewl In Dmso Media After 13 Months Of Crystal Storage >gi|411024306|pdb|4G4H|A Chain A, 100k X-ray Diffraction Study Of Carboplatin Binding To Hewl In Dmso Media After 13 Months Of Crystal Storage >gi|414145440|pdb|4BAD|A Chain A, Hen Egg-White Lysozyme Structure In Complex With The Europium Tris-Hydroxymethyltriazoledipicolinate Complex At 1.35 A Resolution. >gi|414145441|pdb|4BAF|A Chain A, Hen Egg-white Lysozyme Structure In Complex With The Europium Tris-hydroxyethyltriazoledipicolinate Complex At 1.51 A Resolution. >gi|414145443|pdb|4BAP|A Chain A, Hen Egg-White Lysozyme Structure In Complex With The Europium Tris-Hydroxyethylcholinetriazoledipicolinate Complex At 1.21 A Resolution. >gi|433286628|pdb|3ZEK|A Chain A, Hen Egg-White Lysozyme Structure Determined At Room Temperature By In-Situ Diffraction In Chipx >gi|436408836|pdb|4GCB|A Chain A, 100k X-ray Diffraction Study Of A 6-fold Molar Excess Of A Cisplatin/carboplatin Mixture Binding To Hewl >gi|436408837|pdb|4GCC|A Chain A, Room Temperature X-ray Diffraction Study Of A 6-fold Molar Excess Of A Cisplatin/carboplatin Mixture Binding To Hewl, Dataset 1 >gi|436408838|pdb|4GCD|A Chain A, Room Temperature X-ray Diffraction Study Of A 6-fold Molar Excess Of A Cisplatin/carboplatin Mixture Binding To Hewl, Dataset 2 >gi|436408839|pdb|4GCE|A Chain A, Room Temperature X-ray Diffraction Study Of A 6-fold Molar Excess Of A Cisplatin/carboplatin Mixture Binding To Hewl, Dataset 3 >gi|436408840|pdb|4GCF|A Chain A, Room Temperature X-ray Diffraction Study Of A 6-fold Molar Excess Of A Cisplatin/carboplatin Mixture Binding To Hewl, Dataset 4 >gi|442570372|pdb|3VFX|A Chain A, Lysozyme Dimer >gi|442570373|pdb|3VFX|B Chain B, Lysozyme Dimer >gi|442570578|pdb|4D9Z|A Chain A, Lysozyme At 318k >gi|442570839|pdb|4HP0|A Chain A, Crystal Structure Of Hen Egg White Lysozyme In Complex With Gn3-m >gi|442570840|pdb|4HPI|A Chain A, Crystal Structure Of Hen Egg White Lysozyme Complex With Gn2-m >gi|443428081|pdb|4DC4|A Chain A, Lysozyme Trimer >gi|443428082|pdb|4DC4|B Chain B, Lysozyme Trimer >gi|443428083|pdb|4DC4|C Chain C, Lysozyme Trimer >gi|444302028|pdb|3TXB|A Chain A, Hewl Co-crystallization With Cisplatin In Aqueous Media With Glycerol As The Cryoprotectant >gi|444302029|pdb|3TXD|A Chain A, Hewl Co-crystallization With Carboplatin In Aqueous Media With Glycerol As The Cryoprotectant >gi|444302030|pdb|3TXE|A Chain A, Hewl Co-crystallization With Carboplatin In Aqueous Media With Paratone As The Cryoprotectant >gi|444302031|pdb|3TXF|A Chain A, Hewl Co-crystallization With Cisplatin In Dmso Media With Glycerol As The Cryoprotectant >gi|444302032|pdb|3TXG|A Chain A, Hewl Co-crystallization With Cisplatin In Dmso Media With Paratone As The Cryoprotectant >gi|444302033|pdb|3TXH|A Chain A, Hewl Co-crystallization With Carboplatin In Dmso Media With Glycerol As The Cryoprotectant >gi|444302034|pdb|3TXI|A Chain A, Hewl Co-crystallization With Carboplatin In Dmso Media With Paratone As The Cryoprotectant >gi|444302035|pdb|3TXJ|A Chain A, Hewl Co-crystallization With Nag With Silicone Oil As The Cryoprotectant >gi|444302036|pdb|3TXK|A Chain A, Hewl Co-crystallization With Cisplatin In Dmso Media With Paratone As The Cryoprotectant At Ph 6.5 >gi|448262382|pdb|4B1A|A Chain A, Crystal Structure Of Lysozyme With Keggin Molecule >gi|474453357|pdb|4J1A|A Chain A, X-ray Structure Of The Adduct Between Hen Egg White Lysozyme And Aziru (green Crystal) >gi|474453358|pdb|4J1B|A Chain A, X-ray Structure Of The Adduct Between Hen Egg White Lysozyme And Aziru (black Crystal) >gi|480311992|pdb|4EOF|A Chain A, Lysozyme In The Presence Of Arginine >gi|499142048|pdb|4H8X|A Chain A, Radiation Damage Study Of Lysozyme - 0.07 Mgy >gi|499142049|pdb|4H8Y|A Chain A, Radiation Damage Study Of Lysozyme- 0.14 Mgy >gi|499142050|pdb|4H8Z|A Chain A, Radiation Damage Study Of Lysozyme - 0.21 Mgy >gi|499142051|pdb|4H90|A Chain A, Radiation Damage Study Of Lysozyme - 0.28 Mgy >gi|499142052|pdb|4H91|A Chain A, Radiation Damage Study Of Lysozyme - 0.35 Mgy >gi|499142053|pdb|4H92|A Chain A, Radiation Damage Study Of Lysozyme- 0.42 Mgy >gi|499142054|pdb|4H93|A Chain A, Radiation Damage Study Of Lysozyme - 0.49 Mgy >gi|499142055|pdb|4H94|A Chain A, Radiation Damage In Lysozyme - 0.56 Mgy >gi|499142056|pdb|4H9A|A Chain A, Radiation Damage Study Of Lysozyme - 0.63 Mgy >gi|499142057|pdb|4H9B|A Chain A, Radiation Damage Study Of Lysozyme - 0.70 Mgy >gi|499142058|pdb|4H9C|A Chain A, Radiation Damage Study Of Lysozyme - 0.77 Mgy >gi|499142059|pdb|4H9E|A Chain A, Radiation Damage Study Of Lysozyme - 0.84 Mgy >gi|499142060|pdb|4H9F|A Chain A, Radiation Damage Study Of Lysozyme - 0.91 Mgy >gi|499142061|pdb|4H9H|A Chain A, Radiation Damage Study Of Lysozyme - 0.98 Mgy >gi|499142062|pdb|4H9I|A Chain A, Radiation Damage Study Of Lysozyme - 1.05 Mgy >gi|499142069|pdb|4HTK|A Chain A, Mitigation Of X-ray Damage In Macromolecular Crystallography By Submicrometer Line Focusing; Total Dose 2.17 X 10e+12 X-ray Photons >gi|499142070|pdb|4HTN|A Chain A, Mitigation Of X-ray Damage In Macromolecular Crystallography By Submicrometer Line Focusing; Total Dose 1.32 X 10e+12 X-ray Photons >gi|499142071|pdb|4HTQ|A Chain A, Mitigation Of X-ray Damage In Macromolecular Crystallography By Submicrometer Line Focusing; Total Dose 6.70 X 10e+11 X-ray Photons >gi|520728634|pdb|4FJR|A Chain A, Mode Of Interaction Of Merocyanine 540 With Hew Lysozyme >gi|530537449|pdb|4GLA|A Chain A, Obody Nl8 Bound To Hen Egg-white Lysozyme >gi|530537450|pdb|4GLA|B Chain B, Obody Nl8 Bound To Hen Egg-white Lysozyme >gi|532137753|pdb|4GLV|A Chain A, Obody Am3l09 Bound To Hen Egg-white Lysozyme >gi|532137755|pdb|4GLV|C Chain C, Obody Am3l09 Bound To Hen Egg-white Lysozyme >gi|532137757|pdb|4GLV|E Chain E, Obody Am3l09 Bound To Hen Egg-white Lysozyme >gi|532137759|pdb|4GLV|G Chain G, Obody Am3l09 Bound To Hen Egg-white Lysozyme >gi|532137763|pdb|4GN3|A Chain A, Obody Am1l10 Bound To Hen Egg-white Lysozyme >gi|532137765|pdb|4GN3|C Chain C, Obody Am1l10 Bound To Hen Egg-white Lysozyme >gi|532137767|pdb|4GN3|E Chain E, Obody Am1l10 Bound To Hen Egg-white Lysozyme >gi|532137769|pdb|4GN3|G Chain G, Obody Am1l10 Bound To Hen Egg-white Lysozyme >gi|532137771|pdb|4GN3|I Chain I, Obody Am1l10 Bound To Hen Egg-white Lysozyme >gi|532137773|pdb|4GN3|K Chain K, Obody Am1l10 Bound To Hen Egg-white Lysozyme >gi|532137775|pdb|4GN3|M Chain M, Obody Am1l10 Bound To Hen Egg-white Lysozyme >gi|532137777|pdb|4GN3|O Chain O, Obody Am1l10 Bound To Hen Egg-white Lysozyme >gi|532137779|pdb|4GN3|Q Chain Q, Obody Am1l10 Bound To Hen Egg-white Lysozyme >gi|532137782|pdb|4GN4|A Chain A, Obody Am2ep06 Bound To Hen Egg-white Lysozyme >gi|532137785|pdb|4GN5|C Chain C, Obody Am3l15 Bound To Hen Egg-white Lysozyme >gi|532137786|pdb|4GN5|D Chain D, Obody Am3l15 Bound To Hen Egg-white Lysozyme >gi|550545055|pdb|4LGK|A Chain A, X-ray Structure Of The Adduct Between Hen Egg White Lysozyme And Au2phen, A Dinuclear Gold(iii) Complex With -dioxo Bridges Linking The Two Metal Centers >gi|550545056|pdb|4LFX|A Chain A, X-ray Structure Of The Adduct Between Hen Egg White Lysozyme And Auoxo6, A Dinuclear Gold(iii) Complex With -dioxo Bridges Linking The Two Metal Centers >gi|550545057|pdb|4LFP|A Chain A, X-ray Structure Of The Adduct Between Hen Egg White Lysozyme And A Homoleptic Gold(i) Complex With The Saccharynate Ligand >gi|554793261|pdb|4BS7|A Chain A, Hen Egg-white Lysozyme Structure Determined At Room Temperature By In-situ Diffraction And Sad Phasing In Chipx >gi|554793470|pdb|4HSF|A Chain A, Lysozyme With Arginine At 318k >gi|554793864|pdb|4N8Z|A Chain A, In Situ Lysozyme Crystallized On A Mitegen Micromesh With Benzamidine Ligand >gi|557803995|pdb|3J4G|A Chain A, Structure Of Lysozyme Solved By Microed To 2.9 A >gi|558704952|pdb|4HV1|A Chain A, Laser-induced Microfragmentation Of Lysozyme Crystals Allows X-ray Nanodiffraction Characterization Of Individual Domains (lb4) >gi|558704953|pdb|4HV2|A Chain A, Laser-induced Microfragmentation Of Lysozyme Crystals Allows X-ray Nanodiffraction Characterization Of Individual Domains (lb5) >gi|558704974|pdb|4I8S|A Chain A, Hen Lysozyme Protein Crystallization Via Standard Hanging Drop Vapor Diffusion >gi|560189177|pdb|4N5R|A Chain A, Hen Egg-white Lysozyme Phased Using Free-electron Laser Data >gi|564730994|pdb|4IAS|A Chain A, Hew Lysozyme By Langmuir- Blodgett Modified Vapour Diffusion >gi|564730995|pdb|4IAT|A Chain A, Hew Lysozyme By Langmuir- Blodgett Modified Vapour Diffusion >gi|564731161|pdb|4M6D|A Chain A, Crystal Structure Of The Aptamer Minf-lysozyme Complex. >gi|564731163|pdb|4M6D|C Chain C, Crystal Structure Of The Aptamer Minf-lysozyme Complex. >gi|564731165|pdb|4M6D|E Chain E, Crystal Structure Of The Aptamer Minf-lysozyme Complex. >gi|564731167|pdb|4M6D|G Chain G, Crystal Structure Of The Aptamer Minf-lysozyme Complex. >gi|564731169|pdb|4M6D|I Chain I, Crystal Structure Of The Aptamer Minf-lysozyme Complex. >gi|564731171|pdb|4M6D|K Chain K, Crystal Structure Of The Aptamer Minf-lysozyme Complex. >gi|567755486|pdb|4M4O|A Chain A, Crystal Structure Of The Aptamer Mine-lysozyme Complex >gi|568786542|pdb|4II8|A Chain A, Lysozyme With Benzyl Alcohol >gi|586500055|pdb|3W6A|A Chain A, Crystal Structure Of Cross-linked Tetragonal Hen Egg White Lysozyme Soaked Wiht 5mm [ru(benzene)cl2]2 >gi|586500209|pdb|4J7V|A Chain A, Crystal Structure Of Cross-linked Hen Egg White Lysozyme Soaked With 5mm [ru(benzene)cl2]2 >gi|597960345|pdb|4NY5|A Chain A, X-ray Structure Of The Adduct Formed Between Hen Egg White Lysozyme And Nami-a >gi|609412597|pdb|4P2E|A Chain A, Acoustic Transfer Of Protein Crystals From Agar Pedestals To Micromeshes For High Throughput Screening Of Heavy Atom Derivatives >gi|641389832|pdb|4KXI|A Chain A, Crystallographic Study Of The Complex Of Ni(ii) Schiff Base Complex And Hew Lysozyme >gi|641389877|pdb|4NEB|A Chain A, Previously De-ionized Hew Lysozyme Batch Crystallized In 0.5 M Mncl2 >gi|641389882|pdb|4NFV|A Chain A, Previously De-ionized Hew Lysozyme Batch Crystallized In 1.1 M Mncl2 >gi|641389883|pdb|4NG1|A Chain A, Previously De-ionized Hew Lysozyme Batch Crystallized In 1.9 M Cscl >gi|641389884|pdb|4NG8|A Chain A, Dialyzed Hew Lysozyme Batch Crystallized In 1.9 M Cscl And Collected At 100 K. >gi|641389885|pdb|4NGI|A Chain A, Previously De-ionized Hew Lysozyme Crystallized In 1.0 M Rbcl And Collected At 125k >gi|641389886|pdb|4NGJ|A Chain A, Dialyzed Hew Lysozyme Batch Crystallized In 1.0 M Rbcl And Collected At 100 K >gi|641389887|pdb|4NGK|A Chain A, Previously De-ionized Hew Lysozyme Batch Crystallized In 0.2 M Cocl2 >gi|641389888|pdb|4NGL|A Chain A, Previously De-ionized Hew Lysozyme Batch Crystallized In 0.6 M Cocl2 >gi|641389889|pdb|4NGO|A Chain A, Previously De-ionized Hew Lysozyme Batch Crystallized In 1.0 M Cocl2 >gi|641389890|pdb|4NGV|A Chain A, Previously De-ionized Hew Lysozyme Batch Crystallized In 0.5 M Ybcl3 >gi|641389891|pdb|4NGW|A Chain A, Dialyzed Hew Lysozyme Batch Crystallized In 0.5 M Ybcl3 And Collected At 100 K >gi|641389892|pdb|4NGY|A Chain A, Dialyzed Hew Lysozyme Batch Crystallized In 0.75 M Ybcl3 And Collected At 100 K >gi|641389893|pdb|4NGZ|A Chain A, Previously De-ionized Hew Lysozyme Crystallized In 0.5 M Ybcl3/30% (v/v) Glycerol And Collected At 125k >gi|641390195|pdb|4QEQ|A Chain A, High Resolution Structure Of Egg White Lysozyme >gi|645985751|pdb|4MR1|A Chain A, X-ray Structure Of The Adduct Between Hen Egg White Lysozyme And Cis- Diamminediiodoplatinum(ii) >gi|651207677|pdb|4O34|A Chain A, Room Temperature Macromolecular Serial Crystallography Using Synchrotron Radiation >gi|657232135|pdb|4OOO|A Chain A, X-ray Structure Of The Lysozyme Derivative Of Tetrakis(acetato) Chlorido Diruthenium(ii,iii) Complex >gi|662702078|pdb|4C3W|A Chain A, Vanadium(iv)-picolinate Complexed With Lysozyme >gi|662702540|pdb|4TUN|A Chain A, Crystal Structure Of Chicken Egg White Lysozyme Adduct With Organophosphorus Pesticide Monochrotophos >gi|662702541|pdb|4TUN|B Chain B, Crystal Structure Of Chicken Egg White Lysozyme Adduct With Organophosphorus Pesticide Monochrotophos >gi|667484844|pdb|4LT0|A Chain A, Hewl Co-crystallized With Carboplatin In Non-nacl Conditions: Crystal 1 Processed Using The Eval Software Package >gi|667484845|pdb|4LT1|A Chain A, Hewl Co-crystallised With Carboplatin In Non-nacl Conditions: Crystal 1 Processed Using The Xds Software Package >gi|667484846|pdb|4LT2|A Chain A, Hewl Co-crystallized With Carboplatin In Non-nacl Conditions: Crystal 2 Processed Using The Eval Software Package >gi|667484847|pdb|4LT3|A Chain A, Hewl Co-crystallized With Carboplatin In Non-nacl Conditions: Crystal 2 Processed Using The Xds Software Package >gi|672883245|pdb|3WPJ|A Chain A, Spatiotemporal Development Of Soaked Protein Crystal; Native >gi|672883246|pdb|3WPK|A Chain A, Spatiotemporal Development Of Soaked Protein Crystal; 750 Sec >gi|672883247|pdb|3WPL|A Chain A, Spatiotemporal Development Of Soaked Protein Crystal; 2510 Sec >gi|672883248|pdb|3WU7|A Chain A, Spatiotemporal Development Of Soaked Protein Crystal; Derivative 250 Sec >gi|672883249|pdb|3WU8|A Chain A, Spatiotemporal Development Of Soaked Protein Crystal; Derivative 1080 Sec >gi|672883250|pdb|3WU9|A Chain A, Spatiotemporal Development Of Soaked Protein Crystal; Derivative 1580 Sec >gi|672883251|pdb|3WUA|A Chain A, Spatiotemporal Development Of Soaked Protein Crystal; Derivative 3610 Sec >gi|672883667|pdb|4QGZ|A Chain A, X-ray Structure Of The Adduct Formed Between Hen Egg White Lysozyme And Trans-dimethylamine Methylamine Dichlorido Platinum(ii) >gi|672886232|pdb|3J6K|A Chain A, 2.5a Structure Of Lysozyme Solved By Microed >gi|672886451|pdb|4MWM|A Chain A, Triclinic Hewl Co-crystallised With Cisplatin, Studied At A Data Collection Temperature Of 200k
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157831315|pdb|1HEO|A Chain A, Structural And Thermodynamic Analysis Of Compensating Mutations Within The Core Of Chicken Egg White Lysozyme
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGVLQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|576405|pdb|2IFF|Y Chain Y, Structure Of An Antibody-Lysozyme Complex: Effect Of A Conservative Mutation
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGKTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157831313|pdb|1HEM|A Chain A, Structural And Thermodynamic Analysis Of Compensating Mutations Within The Core Of Chicken Egg White Lysozyme
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITATVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|15988034|pdb|1IR8|A Chain A, Im Mutant Of Lysozyme
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQMNSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|15988033|pdb|1IR7|A Chain A, Im Mutant Of Lysozyme
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNMPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|15988035|pdb|1IR9|A Chain A, Im Mutant Of Lysozyme
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKMVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157831318|pdb|1HER|A Chain A, Structural And Thermodynamic Analysis Of Compensating Mutations Within The Core Of Chicken Egg White Lysozyme
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNSQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|15826593|pdb|1H6M|A Chain A, Covalent Glycosyl-Enzyme Intermediate Of Hen Egg White Lysozyme >gi|288562779|pdb|2WAR|A Chain A, Hen Egg White Lysozyme E35q Chitopentaose Complex
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFQSNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|262367842|pdb|3A3Q|A Chain A, Structure Of N59d Hen Egg-white Lysozyme In Complex With (glcnac)3 >gi|262367843|pdb|3A3R|X Chain X, Structure Of N59d Hen Egg-white Lysozyme
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQIDSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157831653|pdb|1KXW|A Chain A, Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains
KVFGRCELAAAMKRHGLDNYRGYSLGDWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|229157|prf||630460A lysozyme
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGDGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|14278672|pdb|1IOT|A Chain A, Stabilization Of Hen Egg White Lysozyme By A Cavity-Filling Mutation
KVFGRCELAAALKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157831314|pdb|1HEN|A Chain A, Structural And Thermodynamic Analysis Of Compensating Mutations Within The Core Of Chicken Egg White Lysozyme
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGVLQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITATVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|10120552|pdb|1FLQ|A Chain A, Hen Egg White Lysozyme Mutant With Alanine Substituted For Glycine
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKATDVQAWIRGCRL
>gi|10120556|pdb|1FN5|A Chain A, Hen Egg White Lysozyme Mutant With Alanine Substituted For Glycine
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDASTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|10120554|pdb|1FLW|A Chain A, Hen Egg White Lysozyme Mutant With Alanine Substituted For Glycine
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPASRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|10120555|pdb|1FLY|A Chain A, Hen Egg White Lysozyme Mutant With Alanine Substituted For Glycine
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDANGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|10120553|pdb|1FLU|A Chain A, Hen Egg White Lysozyme Mutant With Alanine Substituted For Glycine
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDARTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157831655|pdb|1KXY|A Chain A, Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains
KVFGRCELAAAMKRHGLNNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|325053940|pdb|3OJP|A Chain A, D52n Mutant Of Hen Egg White Lysozyme (Hewl)
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTNYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|47169429|pdb|1V7S|A Chain A, Triclinic Hen Lysozyme Crystallized At 313k From A D2o Solution
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRX
>gi|14278671|pdb|1IOS|A Chain A, Stabilization Of Hen Egg White Lysozyme By A Cavity-Filling Mutation
KVFGRCELAAAFKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|29726608|pdb|1NBZ|C Chain C, Crystal Structure Of Hyhel-63 Complexed With Hel Mutant K97a
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKAIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|29726605|pdb|1NBY|C Chain C, Crystal Structure Of Hyhel-63 Complexed With Hel Mutant K96a
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAAKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157831918|pdb|1LZD|A Chain A, Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg-White Lysozyme Complexes And Their Hydrolytic Activity >gi|157831919|pdb|1LZE|A Chain A, Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg- White Lysozyme Complexes And Their Hydrolytic Activity
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRYWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157831317|pdb|1HEQ|A Chain A, Structural And Thermodynamic Analysis Of Compensating Mutations Within The Core Of Chicken Egg White Lysozyme
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNSQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITATVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157878404|pdb|1IO5|A Chain A, Hydrogen And Hydration Of Hen Egg-White Lysozyme Determined By Neutron Diffraction >gi|157879213|pdb|1LZN|A Chain A, Neutron Structure Of Hen Egg-White Lysozyme
XVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|31615670|pdb|1NDG|C Chain C, Crystal Structure Of Fab Fragment Of Antibody Hyhel-8 Complexed With Its Antigen Lysozyme
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSAWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|325053941|pdb|3OK0|A Chain A, E35a Mutant Of Hen Egg White Lysozyme (Hewl)
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFASNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|14278670|pdb|1IOR|A Chain A, Stabilization Of Hen Egg White Lysozyme By A Cavity-Filling Mutation
KVFGRCELAAALKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGIFQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157831316|pdb|1HEP|A Chain A, Structural And Thermodynamic Analysis Of Compensating Mutations Within The Core Of Chicken Egg White Lysozyme
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNSQATNRNTDGSTDYGVLQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITATVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|3212285|pdb|1A2Y|C Chain C, Hen Egg White Lysozyme, D18a Mutant, In Complex With Mouse Monoclonal Antibody D1.3
KVFGRCELAAAMKRHGLANYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157831920|pdb|1LZG|A Chain A, Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg- White Lysozyme Complexes And Their Hydrolytic Activity
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRFWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|345100466|pdb|1AT6|A Chain A, Hen Egg White Lysozyme With A Isoaspartate Residue
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSXGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157831884|pdb|1LSN|A Chain A, Thermal Stability Determinants Of Chicken Egg-White Lysozyme Core Mutants: Hydrophobicity, Packing Volume And Conserved Buried Water Molecules
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITAAVNCAKKIVSNGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|14278669|pdb|1IOQ|A Chain A, Stabilization Of Hen Egg White Lysozyme By A Cavity-Filling Mutation
KVFGRCELAAAFKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGIFQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157834077|pdb|1UIC|A Chain A, Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains
KVFGRCELAAAMKRAGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157831654|pdb|1KXX|A Chain A, Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains
KVFGRCELAAAMKRHGLNNYRGYSLGDWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|2811089|sp|P00700.2|LYSC_COLVI RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C [Colinus virginianus] >gi|1065191|pdb|1BQL|Y Chain Y, Structure Of An Anti-Hel Fab Fragment Complexed With Bobwhite Quail Lysozyme >gi|1633239|pdb|1DKK|A Chain A, Bobwhite Quail Lysozyme With Nitrate >gi|1633240|pdb|1DKK|B Chain B, Bobwhite Quail Lysozyme With Nitrate >gi|157830834|pdb|1DKJ|A Chain A, Bobwhite Quail Lysozyme
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNSQATNRNTDGSTDYGVLQINSRWWCNDGKTPGSRNLCNIPC
SALLSSDITATVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|327200728|pdb|3QY4|A Chain A, Crystallization And In Situ Data Collection Of Lysozyme Using The Crystal Former
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSSNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRA
>gi|157834078|pdb|1UID|A Chain A, Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains
KVFGRCELAAAMKRFGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157831883|pdb|1LSM|A Chain A, Thermal Stability Determinants Of Chicken Egg-White Lysozyme Core Mutants: Hydrophobicity, Packing Volume And Conserved Buried Water Molecules
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGLLQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITATVNCAKKIVSSGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157834079|pdb|1UIE|A Chain A, Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains
KVFGRCELAAAMKRGGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|126617|sp|P00699.1|LYSC_LOPCA RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNSQATNRNTDGSTDYGVLQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITATVNCAKKIVSDGNGMNAWVAWRNRCKGTDVHAWIRGCRL
>gi|157834080|pdb|1UIF|A Chain A, Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains
KVFGRCELAAAMKRVGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157830068|pdb|1AT5|A Chain A, Hen Egg White Lysozyme With A Succinimide Residue
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSXXNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|47117003|sp|Q7LZP9.1|LYSC_LOPIM RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C >gi|47117004|sp|Q7LZQ0.1|LYSC_CATWA RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C
KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVHAWIRGCRL
>gi|157834075|pdb|1UIA|A Chain A, Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains >gi|157834076|pdb|1UIB|A Chain A, Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains
KVFGRCELAAAMKGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSA
LLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|157835197|pdb|2IHL|A Chain A, Lysozyme (e.c.3.2.1.17) (japanese Quail)
KVYGRCELAAAMKRHGLDKYQGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDVHGMNAWVAWRNRCKGTDVNAWIRGCRL
>gi|157829560|pdb|132L|A Chain A, Structural Consequences Of Reductive Methylation Of Lysine Residues In Hen Egg White Lysozyme: An X-Ray Analysis At 1.8 Angstroms Resolution
XVFGRCELAAAMXRHGLDNYRGYSLGNWVCAAXFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAXKIVSDGNGMNAWVAWRNRCXGTDVQAWIRGCRL
>gi|48428233|sp|Q7LZI3.1|LYSC_TRASA RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C
KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSGGSGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|126624|sp|P19849.1|LYSC_PAVCR RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase >gi|226587|prf||1603217A lysozyme
KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDRNGMNAWVAWRNRCKGTDVHAWIRGCRL
>gi|126609|sp|P22910.1|LYSC_CHRAM RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C >gi|86143|pir||JH0212 lysozyme (EC 3.2.1.17) - golden pheasant (tentative sequence)
KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCHIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVNAWTRGCRL
>gi|514703587|ref|XP_005008937.1| PREDICTED: lysozyme C-1-like isoform X2 [Anas platyrhynchos]
MKALLTLVFCLLPLAAQGKVYSRCELAAAMKRLGLDNYRGYSLGNWVCAANYESGFNTQATNRNTDGSTDYGILQINSRW
WCDDGKTPRSKNACGIPCSVLLRSDITEAVRCAKRIVSDGNGMNAWVAWRNRCRGTDVSKWIRGCRL
>gi|47117009|sp|Q7LZT2.1|LYSC_TRATE RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase
KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSGGNGMSAWVAWRNRCKGTDVHAWIRGCRL
>gi|11514088|pdb|1DZB|X Chain X, Crystal Structure Of Phage Library-Derived Single-Chain Fv Fragment 1f9 In Complex With Turkey Egg-White Lysozyme >gi|11514090|pdb|1DZB|Y Chain Y, Crystal Structure Of Phage Library-Derived Single-Chain Fv Fragment 1f9 In Complex With Turkey Egg-White Lysozyme >gi|17943065|pdb|1JTP|L Chain L, Degenerate Interfaces In Antigen-Antibody Complexes >gi|17943066|pdb|1JTP|M Chain M, Degenerate Interfaces In Antigen-Antibody Complexes >gi|21466104|pdb|1LJN|A Chain A, Crystal Structure Of Tuekey Egg Lysozyme Complex With Di-N- Acetylchitobiose At 1.19a Resolution >gi|47169223|pdb|1UAC|Y Chain Y, Crystal Structure Of Hyhel-10 Fv Mutant Sfsf Complexed With Turkey White Lysozyme >gi|62738427|pdb|1XFT|A Chain A, Synchrotron X-Ray Powder Diffraction Study Of Hexagonal Turkey Egg-White Lysozyme >gi|157829565|pdb|135L|A Chain A, X-Ray Structure Of Monoclinic Turkey Egg Lysozyme At 1.3 Angstroms Resolution >gi|157831544|pdb|1JEF|A Chain A, Turkey Lysozyme Complex With (glcnac)3 >gi|157831570|pdb|1JSE|A Chain A, Full-Matrix Least-Squares Refinement Of Turkey Lysozyme >gi|157831923|pdb|1LZY|A Chain A, X-Ray Structure Of Turkey Egg Lysozyme Complex With Di-N- Acetylchitobiose. Recognition And Binding Of Alpha-Anomeric Form >gi|157833926|pdb|1TEW|A Chain A, Structure Of Hexagonal Turkey Egg White Lysozyme At 1.65 Angstroms Resolution >gi|157835329|pdb|2LZ2|A Chain A, The Three Dimensional Structure Of Turkey Egg White Lysozyme At 2.2 Angstroms Resolution >gi|157836843|pdb|3LZ2|A Chain A, Structure Determination Of Turkey Egg White Lysozyme Using Laue Diffraction
KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCNIPC
SALLSSDITASVNCAKKIASGGNGMNAWVAWRNRCKGTDVHAWIRGCRL
>gi|126620|sp|P00704.2|LYSC_NUMME RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C [Numida meleagris] >gi|999692|pdb|1FBI|X Chain X, Crystal Structure Of A Cross-Reaction Complex Between Fab F9.13.7 And Guinea-Fowl Lysozyme >gi|999695|pdb|1FBI|Y Chain Y, Crystal Structure Of A Cross-Reaction Complex Between Fab F9.13.7 And Guinea-Fowl Lysozyme
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNSQATNRNTDGSTDYGVLQINSRWWCNDGRTPGSRNLCNIPC
SALQSSDITATANCAKKIVSDGNGMNAWVAWRKHCKGTDVRVWIKGCRL
>gi|157831333|pdb|1HHL|A Chain A, The Three-Dimensional Structure Of Pheasant And Guinea-Fowl Egg Lysozymes
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNSQATNRNTDGSTDYGVLQINSRWWCNDGRTPGSRNLCNIPC
SALQSSDITATANCAKKIVSDGDGMNAWVAWRKHCKGTDVRVWIKGCRL
>gi|442943|pdb|1GHL|A Chain A, The Three-Dimensional Structure Of Pheasant And Guinea-Fowl Egg Lysozymes >gi|442944|pdb|1GHL|B Chain B, The Three-Dimensional Structure Of Pheasant And Guinea-Fowl Egg Lysozymes
GKVYGRCELAAAMKRMGLDNYRGYSLGNWVCAAKFESNFNTGATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCHIP
CSALLSSDITASVNCAKKIVSDGNGMNAWVAWRKHCKGTDVNVWIRGCRL
>gi|126618|sp|P24364.1|LYSC_LOPLE RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase >gi|242016|gb|AAB20837.1| lysozyme [Lophura leucomelana=kalij pheasant, egg-white, Peptide, 129 aa]
KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKYESNFNTHATNRNTDGSTDYGILQINSRWWCNDGKTPGSRNLCHIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVSVWTRGCRL
>gi|126592|sp|P00705.1|LYSC1_ANAPL RecName: Full=Lysozyme C-1; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor
MKALLTLVFCLLPLAAQGKVYSRCELAAAMKRLGLDNYRGYSLGNWVCAANYESGFNTQATNRNTDGSTDYGILQINSRW
WCDNGKTPRSKNACGIPCSVLLRSDITEAVRCAKRIVSDGDGMNAWVAWRNRCRGTDVSKWIRGCRL
>gi|126655|sp|P24533.1|LYSC_SYRRE RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase
KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCHISC
SALLSSDITASVNCAKKIVSDRNGMNAWVAWRNRCKGTDVNAWIRGCRL
>gi|742827|prf||2011187A lysozyme
KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDTIASVNCAKKIVSDGNGMNAWVAWRKRCKGTDVNAWTRGCRL
>gi|1346475|sp|P49663.1|LYSC_PHAVE RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase
GKVYGRCELAAAMKRMGLDNYRGYSLGNWVCAAKFESNFNTGATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCHIP
CSALLSSDITASVNCAKKIVSDGDGMNAWVAWRKHCKGTDVNVWIRGCRL
>gi|8928169|sp|P81711.1|LYSC_SYRSO RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; AltName: Full=CPL >gi|560594|gb|AAB31830.1| lysozyme [copper pheasants, egg white, Peptide, 129 aa]
KVYGRCELAAAMKRLGLDNFRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDTIASVNCAKKIVSDGNGMNAWVAWRKRCKGTDVNAWTRGCRL
>gi|494223|pdb|1JHL|A Chain A, Three-Dimensional Structure Of A Heteroclitic Antigen- Antibody Cross-Reaction Complex
KVYGRCELAAAMKRMGLDNYRGYSLGNWVCAAKFESNFNTGATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCHIPC
SALLSSDITASVNCAKKIVSDGDGMNAWVAWRKHCKGTDVNVWIRGCRL
>gi|403399454|sp|G3XDT7.1|LYSC_DRONO RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Dromaius novaehollandiae] >gi|350276100|dbj|BAL03621.1| lysozyme c precursor [Dromaius novaehollandiae] >gi|350276102|dbj|BAL03622.1| lysozyme c precursor [Dromaius novaehollandiae]
MKFFLILGFCLLPLIAQGKVFQRCELAAAMKKHGLSNYRGYSLGHWVCAAKYESNFNTAAINRNRDGSSDYGILQINSRW
WCNDGRTSGAKNLCKISCSALLSSDITASVNCAKRVVSDKNGMNAWVAWRNHCKGRDVSQWIRGCRV
>gi|157831911|pdb|1LZ2|A Chain A, Crystallographic Study Of Turkey Egg-White Lysozyme And Its Complex With A Disaccharide
KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTNGSTDYGILQINSRWWCDNGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIASGGDGMNAWVAWRNRCKGTDVHAWIRGCRL
>gi|350276104|dbj|BAL03623.1| lysozyme c precursor [Struthio camelus]
MKSLLILGFCLLPLVAQGKIYERCELAAAMKRLGLDNFRGYSLGHWVCAAKFESGFDTRAINRNRDGSTDYGILQINSRW
WCNDGRTSRAKNACNISCSALLSSDITASVNCAKRVVSDKNGMNAWKAWKKHCKGRDVSQWIRGCRL
>gi|47117006|sp|Q7LZQ2.1|LYSC_AIXSP RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C
KVYERCELAAAMKRLGLDNYRGYSLGNWVCAAKYESNFNTQATNRNTDGSTDYGILEINSRWWCNDGKTPGAKNVCGIPC
SVLLRSDITEAVKCAKRIVSDGNGMNAWVAWRNRCKGTDVSRWIRGCRL
>gi|47117007|sp|Q7LZQ3.1|LYSC_CRAFA RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C
KIYTRCELAAAMKRYGLDNYQGYSLGNWVCAARYESNYNTQATNRNSDGSTDYGILQINSRWWCNDGKTPGTRNLCHISC
SALMGADIAPSVRCAKKIVSDGNGMNAWVAWRKHCKGTDVSKWIKDCKL
>gi|350714|prf||0802160A lysozyme DL1
KVYSRCELAAAMKRLGLDNYRGYSLGNWVCAANYESGFNTQATNRNTDGSTDYGILQINSRWWCDNGKTPRSKNACGIPC
SVLLRSDITEAVRCAKRIVSDGDGMNAWVAWRNRCRGTDVSKWIRGCRL
>gi|126595|sp|P00706.1|LYSC3_ANAPL RecName: Full=Lysozyme C-3; AltName: Full=1,4-beta-N-acetylmuramidase
KVYERCELAAAMKRLGLDNYRGYSLGNWVCAANYESSFNTQATNRNTDGSTDYGILEINSRWWCDNGKTPRAKNACGIPC
SVLLRSDITEAVKCAKRIVSDGDGMNAWVAWRNRCKGTDVSRWIRGCRL
>gi|126622|sp|P00707.1|LYSC_ORTVE RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C
KIYKRCELAAAMKRYGLDNYRGYSLGNWVCAARYESNYNTQATNRNSNGSTDYGILQINSRWWCNDGRTPGTKNLCHISC
SALMGADIAPSVRCAKRIVSDGDGMNAWVAWRKHCKGTDVSTWIKDCKL
>gi|350715|prf||0802160B lysozyme DL3
KVYSRCELAAAMKRLGLDNYRGYSLGNWVCAANYESGFNTQATNRNTDGSTDYGILQINSRWWCDNGKTPRSKNACGIRC
SVLLRSDITEAVRCAKRIVSDGDGMNAWVAWRNRCRGTDVSKWIRGCRL
>gi|564256312|ref|XP_006267124.1| PREDICTED: lysozyme C-like [Alligator mississippiensis]
MLLKMKALIFLGFFLLPLAAHEKVYERCELAAAMKKLGLANIPGYSLGEWVCTARYESNFNTNAINHNSDGSTDYGILQI
NSRWWCNDGKTPGAKNACRIQCTELMKPDITATVKCAKRIVKDPQGMNAWVAWKKYCKGKDVSKWIKGCKL
>gi|564256314|ref|XP_006267125.1| PREDICTED: lysozyme C-like isoform X1 [Alligator mississippiensis]
MKALIFLEFFFLPLAAHGKIYERCELAAAMNRLGLANIPGYSLGDWVCTARYESNYNTSAMNYNPGDRSTDYGILQINSR
WWCNDGKTPRAKNVCRIQCTELLQPDITVAVNCAKRIVRDPQGMSAWVAWRNHCKGTDVSRFIRDCKLWGKKKELGV
>gi|530567142|ref|XP_005280098.1| PREDICTED: lysozyme C-like [Chrysemys picta bellii]
MKALLILGLFLLPMVAHGKVYGRCELARAMKRLGLDGYRGYSLGHWVCTAKYESNFNTGATNYNRGDKSTDYGIFQINSR
WWCNDGKTPKAKNACGIRCSGLLTSDITASVKCAKRVVRDPNGMGAWVAWKKYCKGKDVSKWISDCKL
>gi|557288695|ref|XP_006027021.1| PREDICTED: lysozyme C-like [Alligator sinensis]
MKALIFLELFLLPLAAHGKIYERCELAAAMNRLGLANIPGYSLGDWVCTARYESNYNTSAMNYNPGDRSTDYGILQINSH
WWCNDGKTPRAKNVCRIQCTELLQPDITVAVNCAKRIVRDPQGMSAWVAWRNHCKGTDVSRFIRDCKLWGKKKS
>gi|558155397|ref|XP_006121640.1| PREDICTED: lysozyme C-like [Pelodiscus sinensis]
MKILLILGLVLLPLAAPGKIYEQCELAREFKRHGMDGYHGYSLGDWVCTAKHESNFNTAATNYNRGDQSTDYGILQINSR
WWCNDGKTPKAKNACGIECSELLKADITAAVNCAKRIVRDPNGMGAWVAWTKYCKGKDVSQWIKGCKL
>gi|259016325|sp|Q7LZQ1.3|LYSC_TRISI RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; AltName: Full=Softshell turtle lysozyme C; Short=SSTL >gi|149241704|pdb|2GV0|A Chain A, The Structure Of The Orthorhombic Form Of Soft-Shelled Turtle Lysozyme At 1.9 Angstroms Resolution
GKIYEQCELAREFKRHGMDGYHGYSLGDWVCTAKHESNFNTAATNYNRGDQSTDYGILQINSRWWCNDGKTPKAKNACGI
ECSELLKADITAAVNCAKRIVRDPNGMGAWVAWTKYCKGKDVSQWIKGCKL
>gi|530567140|ref|XP_005280097.1| PREDICTED: lysozyme C-like [Chrysemys picta bellii]
MKALLILGFLLLPLAAHGKIYERCELARAMKRLGLDGYRGYSLGHWVCTANYESGFNTGATNYNRGDQSTDYGILQINSR
WWCNDGKTPRAKNACGIQCGELLTADITASVNCAKRVVRDPNGMGAWVAWTKNCKGRDVSPWIRGCGL
>gi|530567135|ref|XP_005280095.1| PREDICTED: lysozyme C isoform X1 [Chrysemys picta bellii]
MKALLILGFLLLPLAAHGKIYERCELARAMKRLGLDGYWGYSLGHWVCTARYESAFNTSATNYNPGDQSTDYGILQINSH
WWCNDGKTPGAKNACGIQCGELLTADITASVNCAKRVVRDPNGMGAWVAWTKNCKGRDVSPWIRGCGL
>gi|558155401|ref|XP_006121641.1| PREDICTED: lysozyme C-like [Pelodiscus sinensis]
MKALLILGLFLLPLAAHGKIYERCELARAMKRLGLDGYWGYSLGNWVCTARFESQFNTSATNYNRGDQSTDYGILQINSH
WWCNDGKTPGAKNACGIQCSDLLTADITNSVNCAKRVVRDPNGMAAWVAWTRNCKGRDVSQWIRGCGV
>gi|555949705|ref|XP_005887061.1| PREDICTED: lysozyme C, non-stomach isozyme-like [Bos mutus]
MKALLILGFLLFSVAVQGKVFERCELARTLKRFGMDNFRGISLANWMCLARWESNYNTQATNYNAGDQSTDYGIFQINSH
WWCNDGKTPGAVNACHLPCGALLQDDITQAVACAKRVVSDPQGIRAWVAWRSHCQNQDLTSYIQGCGV
>gi|595763342|ref|NP_001277843.1| lysozyme C, non-stomach isozyme-like precursor [Bubalus bubalis] >gi|94470493|gb|ABF20557.1| lysozyme [Bubalus bubalis]
MKALIILGLLLFSVAVQGKVFERCELARALKRFGMDNFRGISLANWMCLARWESSYNTRATNYNAGDRSTDYGIFQINSR
WWCNDGKTPGAVNACGIPCSVLLQDDITQAVACAKRVVSDPQGIRAWVAWRSHCQNQDLTSYIQGCGV
>gi|440913305|gb|ELR62770.1| Lysozyme C, non-stomach isozyme, partial [Bos mutus]
VKSRASSPGSAWRSGFSVNMKALLILGFLLFSVAVQGKVFERCELARTLKRFGMDNFRGISLANWMCLARWESNYNTQAT
NYNAGDQSTDYGIFQINSHWWCNDGKTPGAVNACHLPCGALLQDDITQAVACAKRVVSDPQGIRAWVAWRSHCQNQDLTS
YIQGCGV
>gi|451799064|gb|AGF69232.1| lysozyme precursor [Bos grunniens]
MKALLIVGFLLFLVAVQGKVFERCELARTLKRFGMDNFRGISLANWMCLARWESNYNTQATNYNAGDQSTDYGIFQINSH
WWCNDGKTPGAVNACHLPCGALLQDDVTQAVACAKRVVSDPQGIRAWVAWRSHCQNQDLTSYVQGCKV
>gi|557288697|ref|XP_006027022.1| PREDICTED: lysozyme C-like [Alligator sinensis]
MKALIFLELFLLLLTAHGKIYERCELAAAMKRLGLANIRGYTLGDWVCTAKYESNFNTNAINYNSGDGSTDYGILQINSR
WWCNDGKTPRAKNACRIQCSEFLKPDITAAINCAKRIVRDPQGMNAWMAWTRHCKGKYVSQYLKGCKL
>gi|564256316|ref|XP_006267126.1| PREDICTED: lysozyme C-like isoform X2 [Alligator mississippiensis]
MKALIFLELFLLLLTAHGKIYERCELAAAMNRLGLANIRGYTLGDWVCTARYESNYNTSAMNYNPGDRSTDYGILQINSR
WWCNDGKTPRAKNVCRIQCTELLQPDITVAVNCAKRIVRDPQGMSAWVAWRNHCKGTDVSRFIRDCKLWGKKKELGV
>gi|82124012|sp|P84492.1|LYSC_CHEMY RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C
KTYERCELARAMKRLGLDGYWGYSLGHWVCAAKYESNFNTGATNYNPGDQSTDYGILQINSRWWCNDGKTPRTKNACKIQ
CRELLTADITASVNCAKRVVRDPNGMGAWVAWTKNCKGRDVSPWIRDCGL
>gi|640912017|gb|AIA57285.1| lysozyme [Xenopus laevis]
MNSAVLILVGIFIFPATNGKLFERCELAGTMKKMGLDGYRGYSLPNWVCTAFFESSFYTDRTNFNRGDNSTDYGILQINS
RWWCNDDKTPRSHNACNINCRDLLSDDITQSVICAKRVVRDPQGMEAWVGWRNHCKGRDLSQWIKDCKLDILL
>gi|149632249|ref|XP_001511790.1| PREDICTED: lysozyme C [Ornithorhynchus anatinus]
MKPLFVLGLLVLPFLAHGKVFERCELARLLKRMGMDGYRGVSLPNWVCLANWESSFNTNAKNYNPGDGSTDYGIFQINSR
YWCNDGKTPRAVNACGISCNELLKDDITQAVRCAKRVVEDPQGIRAWVAWRNRCQGQDVSIWTRGCGV
>gi|49115630|gb|AAH72985.1| LOC443604 protein, partial [Xenopus laevis]
NSAVLILVGIFIFPATNGKLFERCELAGTMKKMGLDGYRGYSLPNWVCTAFFESSFYTDRTNFNRGDNSTDYGILQINSR
WWCNDDKTPRSHNACNINCRDLLSDDITQSVICAKRVVRDPQGMEAWVGWRNHCKGRDLSQWIKDCKLDILL
>gi|407971308|gb|AFU52840.1| lysozyme C [Taphozous melanopogon]
MKALFILGLLLISVTVQGKIYERCEFARTLKRLGMDGYKGISLANWVCLAKWESDYNTRATNYNPGDKSTDYGIFQINSH
YWCNDGKTPGAVNACHIPCSALLQDDISQAVACAKRVVSDPQGIRAWVAWRNRCQNQDLTQYIRGCGV
>gi|301618293|ref|XP_002938553.1| PREDICTED: lysozyme C, milk isozyme-like [Xenopus (Silurana) tropicalis]
MNSAVLFWGGIFIFTVTDGKVFERCELAGIMKKMGLDGYRGYSLPNWVCTAFFESSFYTDRTNFNRGDNSTDYGILQINS
RWWCNDNKTPGSHNACNINCRALLSDDITQSVICAKRVVRDPQGMEAWVGWRNHCKGRDLSQWIKDCKLDILP
>gi|591363181|ref|XP_007056495.1| PREDICTED: lysozyme C-like [Chelonia mydas]
MKALLILGLLLLPLAARGKTYERCELARAMKRFGLDGYRGYSLGHWVCTARYESNFNTGATNYNPGDQSTDYGILQINSR
LWCNDGKTPRTKNGCGIQCRELLTADITASVNCAKRVVRDPNGMGAWVAWTKNCKGRDVSPWIRDCGL
>gi|126339358|ref|XP_001362553.1| PREDICTED: lysozyme C-like [Monodelphis domestica]
MKVLILLGLVFLPMLAHGKVYERCELARILKQNGMDGYRGISLANWVCLAKWESNYNTRVTNYNSRDRSTDYGIFQINSR
YWCNDGKTPRAVNACGISCRDLLTDNISKAITCAKRVVRDPSGIRAWVAWRNRCQGKNLSSYIQGCRL
>gi|586457760|ref|XP_006859607.1| PREDICTED: lysozyme C [Chrysochloris asiatica]
MKALLILGFLFLSVSVQGKVYERCELARTMKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSR
YWCNDGKTPRAVNACGISCSVLLRDDITQAVTCAKRVVRDPQGIRAWVAWRNRCQNRDVSQYTRGCGV
>gi|126339144|ref|XP_001373446.1| PREDICTED: lysozyme C-like isoform X1 [Monodelphis domestica]
MKVLILLGLVFLPMLAHGKVYKRCELARVLKQNGMDGYRGNSVDNWVCLAKWESDFDTEATNYNPGDQSTNYGIFQINSH
YWCNDGKTPDAKNVCGISCRDLLTDNITQAVNCAKRVVHDPSGILAWKAWRNHCQGRDVSSYIQDCRL
>gi|404676|gb|AAA99863.1| lysozyme precursor [Bos taurus]
GLLLFSVAVQGKVFERCELARSLKRFGMDNFRGISLANWMCLARWESNYNTQATNYNAGDQSTDYGIFQINSHWWCNDGK
TPGAVNACHLPCGALLQDDITQAVACAKRVVSDPQGIRAWVAWRSHCQNQDLTSYIQGCGV
>gi|156119326|ref|NP_001095203.1| lysozyme C precursor [Macaca mulatta] >gi|544471266|ref|XP_005571565.1| PREDICTED: lysozyme C [Macaca fascicularis] >gi|266489|sp|P30201.1|LYSC_MACMU RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|38091|emb|CAA42796.1| lysozyme [Macaca mulatta] >gi|355564454|gb|EHH20954.1| Lysozyme C [Macaca mulatta]
MKAVIILGLVLLSVTVQGKIFERCELARTLKRLGLDGYRGISLANWVCLAKWESNYNTQATNYNPGDQSTDYGIFQINSH
YWCNNGKTPGAVNACHISCNALLQDNIADAVTCAKRVVSDPQGIRAWVAWRNHCQNRDVSQYVQGCGV
>gi|548465843|ref|XP_005680248.1| PREDICTED: lysozyme C, milk isozyme-like [Capra hircus]
MKALLILGLLLLSVAVQGKKFERCELARTLKRLGLDGYRGVSLANWMCLARWESNYNTRATNYNRGDKSTDYGIFQINSR
WWCNDGKTPRAVNACRIPCSALLKDDITQAVACAKRVVSDPQGIKAWVAWRNKCQNKDLRSYVKGCRV
>gi|166232900|sp|P85345.1|LYSC_AMYCA RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; AltName: Full=Asiatic softshell turtle lysozyme C; Short=ASTL
KIYEQCEAAREMKRLGLDGYDGYSLGDWVCTAKHESNFNTGATNYNRGDQSTDYGIFQINSRWWCNDGKTPNAKNACGIE
CSELLKADITAAVICAKRVVRDPNGMGAWVAWTKYCKGKDVSQWIKGCKL
>gi|118151442|ref|NP_001071627.1| lysozyme C, non-stomach isozyme precursor [Bos taurus] >gi|57015381|sp|P80189.4|LYSCN_BOVIN RecName: Full=Lysozyme C, non-stomach isozyme; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|86827403|gb|AAI12598.1| Lysozyme (renal amyloidosis) [Bos taurus] >gi|296487695|tpg|DAA29808.1| TPA: lysozyme C, non-stomach isozyme precursor [Bos taurus] >gi|326578942|gb|ADZ96001.1| lysozyme [Bos taurus]
MKALLILGLLLFSVAVQGKVFERCELARSLKRFGMDNFRGISLANWMCLARWESNYNTQATNYNAGDQSTDYGIFQINSH
WWCNDGKTPGAVNACHLPCGALLQDDITQAVACAKRVVSDPQGIRAWVAWRSHCQNQDLTSYIQGCGV
>gi|407971242|gb|AFU52807.1| lysozyme C [Chaerephon plicatus]
MKALFILGLFLLSVTVQGKVFERCELARTLKRLGLDGFRGVSLANWMCLARWESSYNTRATNYNPGSRSTDYGIFQINSR
YWCNDGKTPRAVNACHISCSALLQDDITQAVACAKRVVSDPQGIRAWVAWRNRCQNQDLTQYVRGCGV
>gi|126339136|ref|XP_001364061.1| PREDICTED: lysozyme C-like [Monodelphis domestica]
MKVLILLGLVFLPMLAHGKVYERCELARVLKQNGMDGFGGNSLADWVCLAKWESDYNTKATNYNPGDQSTDYGIFQINSH
YWCNDGKTPDAKNVCGISCRDLLTDNISKAITCAKRIVQDFQGIRAWVAWRNHCEGRDVSSYIRGCGL
>gi|307141|gb|AAA36188.1| lysozyme precursor (EC 3.2.1.17) [Homo sapiens]
MKALIVLGLVLLSVTVQGKVFERCELARTLKRLGMDGYRGMSLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSR
YWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|426224727|ref|XP_004006520.1| PREDICTED: lysozyme C, milk isozyme-like [Ovis aries]
MKALLILGLLLLSVAVQGKKFERCELARTLKRLGLDGYRGVSLANWMCLARWESNYNTRATNYNHGDKSTDYGIFQINSR
WWCNDGKTPRAVNACRIPCSALLKDDITQAVECAKRVVRDPQGIKAWVAWRNKCQNKDLRSYVKGCRV
>gi|162951912|ref|NP_001106112.1| lysozyme C precursor [Papio anubis] >gi|48428997|sp|P61629.1|LYSC_PAPAN RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|48428998|sp|P61630.1|LYSC_CERTO RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|1790931|gb|AAB41204.1| lysozyme c precursor [Cercocebus atys] >gi|1790937|gb|AAB41207.1| lysozyme c precursor [Papio anubis]
MKAVIILGLVLLSVTVQGKIFERCELARTLKRLGLDGYRGISLANWVCLAKWESDYNTQATNYNPGDQSTDYGIFQINSH
YWCNNGKTPGAVNACHISCNALLQDNIADAVTCAKRVVSDPQGIRAWVAWRNHCQNRDVSQYVQGCGV
>gi|54037756|sp|P67979.1|LYSC_TRAOB RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|54037757|sp|P67980.1|LYSC_TRAFR RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|1790947|gb|AAB41212.1| lysozyme c precursor [Trachypithecus francoisi] >gi|1790949|gb|AAB41213.1| lysozyme c precursor [Trachypithecus obscurus]
MRALIILGLVLLSVTVQGKIFERCELARTLKKLGLDGYKGVSLANWVCLAKWESGYNTEATNYNPGDESTDYGIFQINSR
YWCNNGKTPGAVDACHISCSALLQNNIADAVACAKRVVSDPQGIRAWVAWRNHCQNKDVSQYVKGCGV
>gi|4557894|ref|NP_000230.1| lysozyme C precursor [Homo sapiens] >gi|57114017|ref|NP_001009073.1| lysozyme C precursor [Pan troglodytes] >gi|397474616|ref|XP_003808770.1| PREDICTED: lysozyme C [Pan paniscus] >gi|48428995|sp|P61626.1|LYSC_HUMAN RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Homo sapiens] >gi|48428996|sp|P61628.1|LYSC_PANTR RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|54037754|sp|P61627.1|LYSC_PANPA RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|307140|gb|AAA59535.1| lysozyme precursor (EC 3.2.1.17) [Homo sapiens] >gi|307142|gb|AAA59536.1| lysozyme precursor (EC 3.2.1.17) [Homo sapiens] >gi|1790941|gb|AAB41209.1| lysozyme c precursor [Pan troglodytes] >gi|1790961|gb|AAB41214.1| lysozyme c precursor [Pan paniscus] >gi|13278744|gb|AAH04147.1| Lysozyme (renal amyloidosis) [Homo sapiens] >gi|119617626|gb|EAW97220.1| lysozyme (renal amyloidosis), isoform CRA_a [Homo sapiens] >gi|119617627|gb|EAW97221.1| lysozyme (renal amyloidosis), isoform CRA_a [Homo sapiens] >gi|119617628|gb|EAW97222.1| lysozyme (renal amyloidosis), isoform CRA_a [Homo sapiens] >gi|123982912|gb|ABM83197.1| lysozyme (renal amyloidosis) [synthetic construct] >gi|123997593|gb|ABM86398.1| lysozyme (renal amyloidosis) [synthetic construct] >gi|189053100|dbj|BAG34722.1| unnamed protein product [Homo sapiens] >gi|226201415|gb|ACO37637.1| lysozyme [Homo sapiens] >gi|649101272|gb|AIC49149.1| LYZ, partial [synthetic construct]
MKALIVLGLVLLSVTVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSR
YWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|126339409|ref|XP_001369349.1| PREDICTED: lysozyme C-like [Monodelphis domestica]
MKVLILLGLVFLPMLAHGKVYERCELARVLKRNGLHGFRSNSVADWVCLAKWESDYNTKATNYNPGDQSTDYGIFQINSH
YWCNDGKTPDAKNVCGISCRDLLTDNISKAITCAKRVVRDPSGIRAWVAWRNHCEGRDVSSYIRGCSL
>gi|525343342|ref|NP_001266591.1| lysozyme precursor [Gorilla gorilla] >gi|2497776|sp|P79179.1|LYSC_GORGO RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Gorilla gorilla gorilla] >gi|1790933|gb|AAB41205.1| lysozyme c precursor [Gorilla gorilla]
MKALIVLGLVLLSVMVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSR
YWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|118151378|ref|NP_001071297.1| lysozyme C, milk isozyme precursor [Bos taurus] >gi|75055545|sp|Q6B411.1|LYSM_BOVIN RecName: Full=Lysozyme C, milk isozyme; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|51012437|gb|AAT92538.1| milk lysozyme [Bos taurus] >gi|74267936|gb|AAI03298.1| Lysozyme 1 [Bos taurus] >gi|296487681|tpg|DAA29794.1| TPA: lysozyme 1 precursor [Bos taurus]
MKALLIVGLLLLSVAVQGKKFQRCELARTLKKLGLDGYRGVSLANWVCLARWESNYNTRATNYNRGDKSTDYGIFQINSR
WWCNDGKTPKAVNACRIPCSALLKDDITQAVACAKRVVRDPQGIKAWVAWRNKCQNRDLRSYVQGCRV
>gi|2497781|sp|P79847.1|LYSC_PYGNE RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|1790978|gb|AAB41217.1| lysozyme c precursor [Pygathrix nemaeus]
MKALIILGLVLLSVTVQGKIFERCELARTLKKLGLDGYKGVSLANWVCLAKWESGYNTEATNYNPGDESTDYGIFQINSR
YWCNNGKTPGAVDACHISCSALLQNNIADAVACAKRVVSDPQGVRAWVAWRNHCQNKDVSQYVKGCGV
>gi|550822083|ref|NP_001272640.1| serum lysozyme precursor [Capra hircus] >gi|260447259|gb|ACX37695.1| serum lysozyme [Capra hircus] >gi|260766474|gb|ACX50258.1| lysozyme [Capra hircus] >gi|582040376|gb|AHI42590.1| lysozyme [Ovis ammon]
MKALIILGLLLLSVAVQGKVFERCELARTLKRFGMDGFRGISLANWMCLARWESSYNTQATNYNSGDRSTDYGIFQINSH
WWCNDGKTPGAVNACHIPCSALLQDDITQAVACAKRVVSDPQGIRAWVAWRSHCQNQDLTSYIQGCGV
>gi|558550356|gb|AHA61787.1| lysozyme [Capra hircus]
MKALLILGLLLLSVAVQGKVFERCELARTLKRFGMDGFRGISLANWMCLARWESSYNTQATNYNSGDRSTDYGIFQINSH
WWCNDGKTPGAVNACHIPCSALLQDDITQAVACAKRVVSDPQGIRAWVAWRSHCQNQDLTSYIQGCGV
>gi|556745410|ref|XP_005968188.1| PREDICTED: lysozyme C, non-stomach isozyme-like [Pantholops hodgsonii]
MKALLILGLLLLSVAVQGKVFERCELARTLKRFGMDGFRGISLANWMCLARWESSYNTQATNYNSGDRSTDYGIFQINSR
WWCNDGKTPGAVNACRIPCSALLQDDITQAVACAKRVVSDPHGIRAWVAWRIHCQNQDLTSYIQGCGV
>gi|451799066|gb|AGF69233.1| lysozyme precursor [Ovis aries]
MKALLILGLLLLSVAVQGKKFERCELARTLKRLGLDGYRGVSLANWMCLARWESNYNTRATNYNRGDKSTDYGIFQINSR
WWCNDGKTPRAVNACRIPCSALLKDDITQAVECAKRVVRDPQGIKAWVAWRNKCQNKDLRSYVKGCTL
>gi|556722668|ref|XP_005957164.1| PREDICTED: lysozyme C, milk isozyme-like [Pantholops hodgsonii]
MLNTKSSSPWAPWTSGLSVNMKTLLILGLLLLSVAVQGKKFQRCELARTLKRLGLDGYKGVSLANWMCLARWESNYNTQA
TNYNRGDKSTDYGIFQINSRWWCNDGKTPKAVNACRIPCSALLKDDITQAVACAKRVVSDPQGIRAWVAWRNKCQNKDLR
SYVKGCGV
>gi|2497779|sp|P79811.1|LYSC_NASLA RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|1790984|gb|AAB41218.1| lysozyme c precursor [Nasalis larvatus]
MKALIILGLVLLSVTVQGKIFERCELARTLKKLGLDGYKGVSLANWVCLAKWESGYNTEATNYNPGDESTDYGIFQINSR
YWCNNGKTPGAVDACHISCSALLQNNIADAVACAKRVVSDPQGIRAWVAWRNHCQNRDVSQYVKGCGV
>gi|507929429|ref|XP_004675962.1| PREDICTED: lysozyme C [Condylura cristata]
MKAFLILGLLLFAITVQGKVFERCELARTLKRYGLDNFKGISLANWICLTKWESDYNTRAINYNPGSGSTDYGIFQINSR
YWCNDGKTPKAVNACGISCNVLLQDDITEAVKCAKRVVSDPQGIRAWVGWKNHCQNRDVSQYIRGCGV
>gi|112030802|gb|ABH88059.1| milk lysozyme [Bos indicus x Bos taurus]
MKALLIVGLLLLSVAVQGKKFQRCELARTLKKLGMDGYRGVSLANWVCLARWESNYNTRATNYNRGDKSTDYGIFQINSR
WWCNDGKTPKAVNACRIPCSALLKDDITQAVACAKRVVRDPQGIKAWVAWRNKCQNRDLRSYVQGCRV
>gi|225717284|gb|ACO14488.1| Lysozyme C II precursor [Esox lucius]
MRAVLVLLLVAVASAKVYDRCDLARRLKAAGMDGYYGNSLPNWVCLAKWESSYNTQATNRNTDGSTDYGIFQINSRWWCD
DGRTPRAKNGCGIRCSQLLTDDLTVAINCAKRVVRDPNGIGAWVAWRNRCKNRDLQSYVAGCGV
>gi|297692417|ref|XP_002823550.1| PREDICTED: lysozyme C [Pongo abelii] >gi|2497780|sp|P79239.1|LYSC_PONPY RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|1790939|gb|AAB41208.1| lysozyme c precursor [Pongo pygmaeus]
MKALIILGLVLLSVTVQSKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNPGDRSTDYGIFQINSR
YWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|483525634|gb|EOB09190.1| Lysozyme C-1, partial [Anas platyrhynchos]
MKALLTLVFCLLPLAAQGKVYSRCELAAAMKRLGLDNYRGYSLGNWVCAANYESGFNTQATNRNTDGSTDYGILQINSRW
WCDDGKTPRSKNACGIPCSGELS
>gi|54037755|sp|P67977.1|LYSC_SEMEN RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|54037772|sp|P67978.1|LYSC_TRAVT RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|38138|emb|CAA42795.1| lysozyme c [Semnopithecus entellus] >gi|1790972|gb|AAB41216.1| lysozyme c precursor [Trachypithecus vetulus]
MKALTILGLVLLSVTVQGKIFERCELARTLKKLGLDGYKGVSLANWVCLAKWESGYNTEATNYNPGDESTDYGIFQINSR
YWCNNGKTPGAVDACHISCSALLQNNIADAVACAKRVVSDPQGIRAWVAWRNHCQNKDVSQYVKGCGV
>gi|332220818|ref|XP_003259554.1| PREDICTED: lysozyme C [Nomascus leucogenys]
MKALIILGLVLLSVTVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNPGDRSTDYGIFQINSR
YWCNDGKTPGAVNACHLSCNALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDLRQYIQGCGV
>gi|208966700|dbj|BAG73364.1| lysozyme [synthetic construct]
MKALIVLGLVLLSVTVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSR
YWCNDGKNPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|2497778|sp|P79806.1|LYSC_MIOTA RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|1790995|gb|AAB41220.1| lysozyme c precursor [Miopithecus talapoin]
MKAVIILGLVLLSVTVQGKIFERCELARTLKRLGLDGYRGISLANWVCLAKWESDYNTQATNYNPGDQSTDYGIFQINSH
YWCNNGKTPGAVNACHISCNALLQDNIADAVTCAKRVVRDPQGIRAWVAWRNHCHNRDVSQYVQGCGV
>gi|635066753|ref|XP_008002172.1| PREDICTED: lysozyme C [Chlorocebus sabaeus] >gi|48429001|sp|P61633.1|LYSC_CERAE RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|48429002|sp|P61634.1|LYSC_ERYPA RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|22807|emb|CAA42797.1| lysozyme [Chlorocebus aethiops] >gi|1791001|gb|AAB41221.1| lysozyme c precursor [Erythrocebus patas]
MKAVIILGLVLLSVTVQGKIFERCELARTLKRLGLDGYRGISLANWVCLAKWESGYNTQATNYNPGDQSTDYGIFQINSH
YWCNNGKTPGAVNACHISCNALLQDNIADAVTCAKRVVRDPQGIRAWVAWRNHCQNRDVSQYVQGCGV
>gi|2497771|sp|P79687.1|LYSC_ALLNI RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|1790989|gb|AAB41219.1| lysozyme c precursor [Allenopithecus nigroviridis]
MKAVIILGLVLLSVTVQGKIFERCELARTLKRLGLDGYRGISLANWVCLAKWESDYNTQATNYNPGDQSTDYGIFQINSH
YWCNNGKTPGAVNACRISCNALLQDNIADAVTCAKRVVRDPQGIRAWVAWRNHCQNRDVSQYVQGCGV
>gi|147907363|ref|NP_001091116.1| lysozyme C precursor [Ovis aries] >gi|94470497|gb|ABF20559.1| lysozyme [Ovis aries]
MKALIILGLLLLSVAVQAKVFERCELARTLKRFGMDGFRGISLANWMCLARWESSYNTQATNYNSGDRSTDYGIFQINSH
WWCNDGKTPGAVNACHIPCSALLQDDITQAVACAKRVVSDPQGIRAWVAWRSHCQNQDLTSYIQGCGV
>gi|354507521|ref|XP_003515804.1| PREDICTED: lysozyme C-1 [Cricetulus griseus] >gi|344258644|gb|EGW14748.1| Lysozyme C [Cricetulus griseus]
MKAFLTLGFLLLSVTVQAKVYSRCEFARILKRHGMDGYRGISLANWVCLAQHESGFNTKATNYNPGPRSTDYGIFQINSK
YWCNNGKTPGAVNACGIPCSVLLQDDITQAIQCAKRVVRDPQGIRAWVAWRSYCQNRNLSQYVRGCRL
>gi|1002429|gb|AAC48683.1| lysozyme [Bos taurus]
MKALLILGLLLFSVAVQGKVFERCELARSLKRFGMDNFRGISLANWMCLARWESNYNTQATNYNAGDQSTDYGIFQINSH
WWCNDGKTPGAVNACHLPCGALLQDDITQAVACTKRDVSDPQGIRAWVAWRSHCQNQDLTSYIQGCGV
>gi|514703585|ref|XP_005008936.1| PREDICTED: lysozyme C-1-like isoform X1 [Anas platyrhynchos]
MKALLTLVFCLLPLAAQGKVYSRCELAAAMKRLGLDNYRGYSLGNWVCAANYESGFNTQATNRNTDGSTDYGILQINSRW
WCDDGKTPRSKNACGIPCSGELSFPRQYRDGLPFHIPIANEQRLVAASALETLPYRVQTHPSPFQKGGLHRGRAHVRGKH
FFTAGTVFPCLPVLLFLE
>gi|209733732|gb|ACI67735.1| Lysozyme C II precursor [Salmo salar] >gi|221221318|gb|ACM09320.1| Lysozyme C II precursor [Salmo salar]
MRAVVVLLLVAVASAKVYDRCELARALKAYGMDGYAGNSLPNWVCLSKWESSYNTQATNRNTDGSTDYGIFQINSRYWCD
DGRTPGAKNVCGIRCSQLLTDDITVAVSCAKRVVLDPNGIGAWVAWRLHCQNQDLRPYVDGCGV
>gi|625290467|ref|XP_007636994.1| PREDICTED: lysozyme C-1 [Cricetulus griseus]
MKAFLTLGFLLLSVTVQAKVYSRCEFARILKRHGMDGYRGISLANWVCLAQHESGFNTKATNYNPGPRSTDYGIFQINSK
YWCNNGKTPGAVNACGIPCSVLLQDDITQAIKCAKRVVRDPQGIRAWVAWRSYCQNRNLSQYVRGCRL
>gi|149715270|ref|XP_001494180.1| PREDICTED: lysozyme C, milk isozyme isoform 1 [Equus caballus] >gi|664756714|ref|XP_008535863.1| PREDICTED: lysozyme C [Equus przewalskii]
MKVLLTLGLLLLSVTVQGKVFERCELARTLKRLGLDGFRGVSLPNWVCLARWESNYNTRATNYNPGSQSTDYGIFQINSR
YWCNDGKTPRAVNACRIPCSALLQDDITQAVACAKRVVSDPQGIRAWVAWRNRCQNHDLTQYVKGCRV
>gi|636634401|gb|AIA09919.1| lysozyme [Xenopus laevis]
MKLFERCELAGTMKKMGLDGYRGYSLPNWVCTAFFESSFYTDRTNFNRGDNSTDYGILQINSRWWCNDDKTPRSHNACNI
NCRDLLSDDITQSVICAKRVVRDPQGMEAWVGWRNHCKGRDLSQWIKDCKLDILL
>gi|585659865|ref|XP_006886141.1| PREDICTED: lysozyme C [Elephantulus edwardii]
MKALLVLGVLFLSVTVQAKVYERCEFARILKREGMDGFHGISLANWMCLAKWESNYNTRATNYNPGDRSTDYGIFQINSR
WWCNDGKTPRAVNACRISCNTLLQDDVTQAIKCAKRVVSDPQGIRAWVAWRNRCQNRDLTEYIKNCGV
>gi|507648793|ref|XP_004632211.1| PREDICTED: lysozyme C-like [Octodon degus]
MKTLLLVGLVILSGTVQSKVFKRCELAKTLKAKGMDNYHGISLANWMCLAKAESDYNTQATNYNSGDQSTDYGIFQINSR
YWCNDGKTPGAVNACGIPCNALLNDDISQAVTCAKRVVQDPQGIRAWVGWKKNCQNKDLKPYINGCGV
>gi|299876|gb|AAB26394.1| lysozyme {EC 3.2.1.17} [cattle, kidney, Peptide, 130 aa]
KVFERCELARSLKRFGMDNFRGISLANWMCLARWESNYNTQATNYNAGDQSTDYGIFQINSHWWCNDGKTPGAVNACHLP
CGALLQDDITQAVACAKRVVSDPQGIRAWVAWRSHCQNQDLTSYIQGCGV
>gi|371915507|dbj|BAL44624.1| lysozyme C [Platichthys stellatus]
MRSLVFLLLVAVAGARVYERCELARVLKSQGMDGYRGNSLANWVCLSHGESNYNTRATNHNTDGSTDYGIFQINSRWWCN
NGQTATSNACNIRCSALLTDDISVAINCAKRVVQDPAGIGAWVAWRRNCRGRDLSSYLAGCRL
>gi|847820|gb|AAC63078.1| lysozyme precursor [Homo sapiens]
MKALIVLGLALLSVTVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSR
YWCNDGKTPGAVNACHLSCSALLQDNIADAAACAKRVVRDPQGVRAWAAWRNRCQDRDVRQYVQGCGV
>gi|533174996|ref|XP_005400871.1| PREDICTED: lysozyme C-like [Chinchilla lanigera]
MKSLIFLGLVLLSVTVQGKVFKRCELAKTLKAKGMDGYQGISLANWMCLAKAESNYNTQATNYNPGDKSTDYGIFQINSH
YWCNDGKTPGAVNACGVSCKALLQDDISQAVACAKRVVRDPQGIRAWVGWKNHCQNKDLKPYINGCGV
>gi|2497777|sp|P79180.1|LYSC_HYLLA RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|1790935|gb|AAB41206.1| lysozyme c precursor [Hylobates lar]
MKALIILGLVLLSVMVQAKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNPGDRSTDYGIFQINSR
YWCNDGKTPGAVNACHLSCNALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDLRQYIQGCGV
>gi|259157584|gb|ACV96861.1| lysozyme [Ovis aries]
MKALIILGLLLLSVAVQAKVFERCELARTLKRFGMDGFRGISLANWMCLTRWESSYNTQATNYNSGDRSTDYGIFQINSH
WWCNDGKTPGAVNACHIPCSALLQDDITQAVACAKRVVSDPQGIRAWVAWRSHCQNQDLTSYIQGCGV
>gi|602706673|ref|XP_007463616.1| PREDICTED: lysozyme C [Lipotes vexillifer]
MKAVLILGLLLLSVAVQGKIFERCELARTLKRLGLDGYKGVSLANWMCLAKWESNYNTQATNYNPGSRSTDYGIFQINSR
YWCNDGKTPGAHNACRMPCSALLKDDITEAVTCAKRVVRDPQGVRAWVAWRSHCQNQDLRRYVQGCGV
>gi|466068621|ref|XP_004281925.1| PREDICTED: lysozyme C [Orcinus orca]
MKAVLILGLLLLSVAVQGKTFERCELARTLKRLGLDGYRGVSLANWMCLAKWESNYNTQATNYNPGSRSTDYGIFQINSR
YWCNDGKTPRAHNACGMPCSALLKDDITDAVTCAKRVVRDPQGIRAWVAWRSHCQNQDLRTYVQGCRV
>gi|266487|sp|P80190.1|LYSCK_SHEEP RecName: Full=Lysozyme C, kidney isozyme; AltName: Full=1,4-beta-N-acetylmuramidase C [Ovis aries] >gi|299875|gb|AAB26393.1| lysozyme {EC 3.2.1.17} [sheep, kidney, Peptide, 130 aa]
KVFERCELARTLKRFGMDGFRGISLANWMCLARWESSYNTQATNYNSGDRSTDYGIFQINSHWWCNDGKTPGAVNACHIP
CSALLQDDITQAVACAKRVVSDPQGIRAWVAWRSHCQNQDLTSYIQGCGV
>gi|194272796|gb|ACF37258.1| c-type lysozyme [Oreochromis aureus]
MRSVFVFLLLITVASAKVFERCDWARKLKANGMDGYRGVSLANWVCLTKHESNYNTKATNRNTDGSTDFGIFQINSRWWC
NDRRINSANGCNIDCSVLLADDVTSATNCAKRIVREQGITAWVAWRNRCQGQDLRPYLSGCRL
>gi|555978544|ref|XP_005901210.1| PREDICTED: lysozyme C, milk isozyme-like [Bos mutus]
MKALLIVGLLLLSVAVQGKKFQRCELARTLKKLGLDGYRGVSLANWVCLARWESNYNTRATNYNRGDKSTDYGIFQINSR
WWCNDGKTPKAVNACRIPCSALLKDDITQAVACAKRVVRDPQGIKAWVAWRKKCQNRDLRSYVQGCGV
>gi|185132632|ref|NP_001118188.1| lysozyme C II precursor [Oncorhynchus mykiss] >gi|266485|sp|P11941.2|LYSC2_ONCMY RecName: Full=Lysozyme C II; AltName: Full=1,4-beta-N-acetylmuramidase C; AltName: Full=Lysozyme type II; Flags: Precursor [Oncorhynchus mykiss] >gi|12025453|gb|AAG45933.1|AF322106_1 lysozyme II precursor [Oncorhynchus mykiss] >gi|64184|emb|CAA42084.1| lysozyme [Oncorhynchus mykiss] >gi|17933433|gb|AAL48290.1| lysozyme type II [Oncorhynchus mykiss]
MRAVVVLLLVAVASAKVYDRCELARALKASGMDGYAGNSLPNWVCLSKWESSYNTQATNRNTDGSTDYGIFQINSRYWCD
DGRTPGAKNVCGIRCSQLLTADLTVAIRCAKRVVLDPNGIGAWVAWRLHCQNQDLRSYVAGCGV
>gi|27923806|sp|Q9TUN1.1|LYSC3_SHEEP RecName: Full=Lysozyme C-3; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Ovis aries] >gi|5802278|gb|AAD51637.1| lysozyme 3 [Ovis aries]
MKALVILGLLFLSVAVQGKVFERCELARTLKKLGLDDYKGVSLANWLCLSKWESGYNTKATNYNPGSESTDYGIFQINSK
WWCNDGKTPNAVDGCHVSCSALMENDIEKAVACAKHIVSEQGITAWVAWKSHCRVHDVSSYVEGCKL
>gi|11344949|gb|AAG34564.1|AF321519_1 lysozyme variant [Oncorhynchus mykiss]
MRAVVVLLLVAVASAKVYDRCELARALKASGMDGYAGNSLPNWVCLSKWESSYNTQATNRNTDGSTDYGIFQINSRYWCD
DGRTPGAKNVCGIHCSQLLTDDLTVAIRCAKRVVLDPNGIGAWVAWRLHCQNQDLRSYVAGCGV
>gi|440901569|gb|ELR52484.1| Lysozyme C, milk isozyme [Bos mutus]
MLNTKSSSPGQLGHLASVNMKALLIVGLLLLSVAVQGKKFQRCELARTLKKLGLDGYRGVSLANWVCLARWESNYNTRAT
NYNRGDKSTDYGIFQINSRWWCNDGKTPKAVNACRIPCSALLKDDITQAVACAKRVVRDPQGIKAWVAWRKKCQNRDLRS
YVQGCGV
>gi|348580753|ref|XP_003476143.1| PREDICTED: lysozyme C-like [Cavia porcellus]
MKAFLILGLLLLSVPIHGKIFERCELARALKRYGLDGYRGISLANWVCLARWESSYNTRATNYNPGDRSTDYGIFQINSR
YWCNDGKTPRAVNGCGISCNALLQDDITQAVNCAKRVVRDAQGIRAWVAWRNRCQNHDLTEYVRGCGV
>gi|157830202|pdb|1BB6|A Chain A, Lysozyme Complex With 4-Methyl-Umbelliferyl Chitotriose >gi|157830203|pdb|1BB7|A Chain A, Lysozyme Complex With 4-Methyl-Umbelliferyl Chitobiose >gi|157831847|pdb|1LMC|A Chain A, The Crystal Structure Of A Complex Between Bulgecin, A Bacterial Metabolite, And Lysozyme From The Rainbow Trout >gi|157831849|pdb|1LMN|A Chain A, The Refined Crystal Structure Of Lysozyme From The Rainbow Trout (Oncorhynchus Mykiss) >gi|157831850|pdb|1LMO|A Chain A, The Crystal Structures Of Three Complexes Between Chitooligosaccharides And Lysozyme From The Rainbow Trout >gi|157831851|pdb|1LMP|A Chain A, The Crystal Structures Of Three Complexes Between Chitooligosaccharides And Lysozyme From The Rainbow Trout >gi|157831852|pdb|1LMQ|A Chain A, The Crystal Structures Of Three Complexes Between Chitooligosaccharides And Lysozyme From The Rainbow Trout
KVYDRCELARALKASGMDGYAGNSLPNWVCLSKWESSYNTQATNRNTDGSTDYGIFQINSRYWCDDGRTPGAKNVCGIRC
SQLLTDDLTVAIRCAKRVVLDPNGIGAWVAWRLHCQNQDLRSYVAGCGV
>gi|505777208|ref|XP_004602715.1| PREDICTED: lysozyme C [Sorex araneus]
MKALLILGLVLLCVTVQGKVFERCELARTLKRLGMDGYRGVSLANWMCLTKWESDYNTRATNFNPGSGSTDYGIFQINSR
YWCNDGKTPGAKNACGISCSVLLKDDITQAVACAKRVVRDPQGIRAWVAWRNHCQNRDVSQYVRGCRV
>gi|558701393|gb|AHA85993.1| c-type lysozyme [Hucho taimen]
MRAVVVLLLVAVASAKVYDRCELARALKASGMDGYAGNSLPNWVCLSKWESSYNTQATNRNTDGSTDYGIFQINSRYWCD
DGRTPGAKNVCGIRCSQLLTDDLTVAIRCAKRVVLDPNGIGAWVAWRRYCQNRDLSSYVAGCGV
>gi|401063464|gb|AFP89959.1| lysozyme [Ovis aries]
MKALLILGLLLLSVAVQAKVFERCELARTLKRFGMDGFRGISLANWMCLARWESSYNTQATNYNSGDRSTDYGIFQINSH
WWCNDGKTSGAVNACHIPCSALLQDDITQAVACAKRVVSDPQGIRAWVAWRSHCQNQDLTSYIQGCGV
>gi|48428999|sp|P61631.1|LYSC_COLAN RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|48429000|sp|P61632.1|LYSC_COLGU RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|1790927|gb|AAB41202.1| lysozyme c precursor [Colobus guereza] >gi|1790967|gb|AAB41215.1| lysozyme c precursor [Colobus angolensis]
MKALIILGLVLLSVTVQGKIFERCELARTLKKLGLDGYKGVSLANWVCLAKWESGYNTDATNYNPGDESTDYGIFQINSR
YWCNNGKTPGAVNACHISCNALLQNNIADAVACAKRVVSDPQGIRAWVAWKKHCQNRDVSQYVEGCGV
>gi|525507200|ref|NP_001267639.1| lysozyme 3a precursor [Ovis aries] >gi|451799074|gb|AGF69237.1| lysozyme-2 precursor [Ovis aries]
MKALVILGLLFLSVAVQGKVFERCELARTLKKLGLDDYKGVSLANWLCLTKWESGYNTKATNYNPGSESTDYGIFQINSK
WWCNDGKTPNAVDGCHVSCSALMENDIEKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|537242707|gb|ERE87493.1| lysozyme C-like protein [Cricetulus griseus]
MKALLTLGFLLLSVTVQAKVYERCEFARTLKSHGMDGYRGISLANWVCLAQHESNYNTQATNYNRKDQSTDYGIFQINSR
YWCNDGKTPRAVNACGIPCSVLLQDDITQAIKCAKRVVRDPQGIRAWVAWRSYCQNRNLSQYVRGCRL
>gi|470618557|ref|XP_004317869.1| PREDICTED: lysozyme C-like [Tursiops truncatus]
MKAVLILGLLLLSVAVQGKTFERCELARTLKRLGLDGYRGVSLANWMCLAKWESNYNTQATNYNPGSRSTDYGIFQINSR
YWCNDGKTPRAHNACGIPCSALLKDDITDAVRCAKRVVRDPQGIRAWVAWRSHCQNQDLRTYVQGCGV
>gi|507636797|ref|XP_004700515.1| PREDICTED: lysozyme C-like [Echinops telfairi]
MKALLILGFLFLSVTVQGKVYERCELARRLKQLGMDGYKGISLANWMCLIKWESGYNTRVTNYNRGDKSTDYGIFQINSR
YWCNDGKTPRAVNACRISCNVLLQDDITQAVACAKRVVRDPQGIRAWVAWRNRCQNRDLTEYVRGCGV
>gi|556745407|ref|XP_005968187.1| PREDICTED: lysozyme C-2-like [Pantholops hodgsonii]
MLNSKSSSPWSVWTFDFSVNMKALIILGLLFLSVAVQGKVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESGYNTKA
TNYNPSSESTDYGIFQINSKWWCNDGKTPKAVDGCHVSCSELMENDITKAVACAKHIVSEQGITAWVAWKSHCRDHDVSS
YVEGCTL
>gi|354469545|ref|XP_003497189.1| PREDICTED: lysozyme C [Cricetulus griseus]
MKALLTLGFLLLSVTVQAKVYERCEFARTLKSHGMDSYRGISLANWVCLAQHESNYNTQATNYNRKDQSTDYGIFQINSR
YWCNDGKTPRAVNACGIPCSVLLQDDITQAMECAKRVVRDPQGIRAWVAWRSHCQNRDLTQYIRGCGV
>gi|595763495|ref|NP_001277817.1| uncharacterized protein LOC102414936 precursor [Bubalus bubalis] >gi|146149612|gb|ABQ02304.1| lysozyme [Bubalus bubalis]
MKALIILGFLFLSVAVQGKVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKATNYNPSSESTDYGIFQINSK
WWCNDGKTPNAVDGCHVSCSELMENDIAKAVACAKQIVSEQGITAWVAWKSHCRDHDVSSYIEGCTL
>gi|344266359|ref|XP_003405248.1| PREDICTED: lysozyme C-like [Loxodonta africana]
MRALLILGLLFLSGTVHGKVFERCELARTLKRHGLGGYRGISLANWVCLAKHESNYNTRATNYNPPDKSTDYGIFQINSR
YWCNDGKTPRAVNACGISCKALLQDDITQAIACAKRVVRDPQGIKAWVAWRNHCQNHDLTQYVRGCGV
>gi|532058963|ref|XP_005372167.1| PREDICTED: lysozyme C-2-like [Microtus ochrogaster]
MKALLTLGFLLLSVTVQAKVYERCEFARTLKRNGMDGYRGVSLANWVCLAQHESNYNTRATNYNPGDKSTDYGIFQINSR
YWCNDGKTPRAVNACGIPCSALLQDDITQAIQCAKRVVRDPQGIRAWVAWRNYCQNRDLTQYLRNCRL
>gi|625290469|ref|XP_007636995.1| PREDICTED: lysozyme C [Cricetulus griseus]
MKALLTLGFLLLSVTVQAKVYERCEFARTLKSHGMDGYRGISLANWVCLAQHESNYNTQATNYNRKDQSTDYGIFQINSR
YWCNDGKTPRAVNACGIPCSVLLQDDITQAIQCAKRVVRDPQGIRAWVAWRDYCRNRDLTQYIRGCGV
>gi|595763181|ref|NP_001277870.1| lysozyme C-1-like precursor [Bubalus bubalis] >gi|555976806|ref|XP_005900363.1| PREDICTED: lysozyme C-1-like [Bos mutus] >gi|94470495|gb|ABF20558.1| lysozyme [Bubalus bubalis]
MKALIILGFLFLSVAVQGKVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKATNYNPSSESTDYGIFQINSK
WWCNDGKTPNAVDGCHVSCSELMENDIAKAVACAKQIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|504141260|ref|XP_004583074.1| PREDICTED: lysozyme C [Ochotona princeps]
MKVLLILGMLLLSNTIQGKVFERCELAKTLKKFGMDGYKGISLPNWMCLAKWESSYNTKATNYNPGDKSTDYGIFQINSH
YWCNDGKTPKSVNACHIPCSALLQDDISQAVTCAKRVVSDPQGIRAWVAWRNHCQNRDLSEYTRGCGV
>gi|28849925|ref|NP_776529.1| lysozyme C-3 precursor [Bos taurus] >gi|27923798|sp|Q06284.2|LYSC3_BOVIN RecName: Full=Lysozyme C-3; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Bos taurus] >gi|163323|gb|AAA30632.1| lysozyme 3a precursor [Bos taurus] >gi|163334|gb|AAC37312.1| lysozyme [Bos taurus] >gi|296487682|tpg|DAA29795.1| TPA: lysozyme C-3 precursor [Bos taurus]
MKALIILGFLFLSVAVQGKVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKATNYNPSSESTDYGIFQINSK
WWCNDGKTPNAVDGCHVSCSELMENDIAKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVQGCTL
>gi|407971304|gb|AFU52838.1| lysozyme C [Scotomanes ornatus]
MKALLTLGLLLLSVAVQAKVYERCELARTLKRLGMDGYRGVSLANWMCLAKWESSYNTRATNYNPGDRSTDYGIFQINSR
YWCNDGKTPGAVNACGISCSVLLQDDITQAATCAKRVVRDPQGIRAWVAWRNRCQNQDVSQYIRGCGV
>gi|555976804|ref|XP_005900362.1| PREDICTED: lysozyme C-2-like [Bos mutus] >gi|555976808|ref|XP_005900364.1| PREDICTED: lysozyme C-2-like [Bos mutus] >gi|440902310|gb|ELR53116.1| Lysozyme C-2 [Bos mutus] >gi|558550358|gb|AHA61788.1| lysozyme [Capra hircus]
MKALIILGFLFLSVAVQGKVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKATNYNPSSESTDYGIFQINSK
WWCNDGKTPNAVDGCHVSCSELMENDIAKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|407971252|gb|AFU52812.1| lysozyme C [Ia io]
MKALLTLGLLLLSVNVQAKVYERCELARTLKRLGMDGYRGVSLANWMCLAKWESSYNTRATNYNPGDRSTDYGIFQINSR
YWCNDGKTPGAVNACGISCSVLLQDDITQAVTCAKRVVRDPQGIRAWVAWRNRCQNQDVSQYIRGCGV
>gi|440902311|gb|ELR53117.1| Lysozyme C-1 [Bos mutus]
MLNSKSSSPWSVWTFDFSVNMKALIILGFLFLSVAVQGKVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKA
TNYNPSSESTDYGIFQINSKWWCNDGKTPNAVDGCHVSCSELMENDIAKAVACAKQIVSEQGITAWVAWKSHCRDHDVSS
YVEGCTL
>gi|30794294|ref|NP_851342.1| lysozyme C-2 precursor [Bos taurus] >gi|27923797|sp|Q06283.2|LYSC2_BOVIN RecName: Full=Lysozyme C-2; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Bos taurus] >gi|163317|gb|AAA30629.1| lysozyme 2b precursor [Bos taurus] >gi|163332|gb|AAC37311.1| lysozyme [Bos taurus] >gi|296487679|tpg|DAA29792.1| TPA: lysozyme C-2 precursor [Bos taurus]
MKALVILGFLFLSVAVQGKVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKATNYNPSSESTDYGIFQINSK
WWCNDGKTPNAVDGCHVSCSELMENDIAKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|407971306|gb|AFU52839.1| lysozyme C [Scotomanes ornatus]
MKALLTLGLLLLSVAVQAKVYERCELARTLKRLGMDGYRGVSLANWMCLAKWESGYNTRATNYNPGSKSTDYGIFQINSR
YWCNDGKTPGAVNACGISCSVLLKDDITQAVTCAKRVVRDPQGIRAWVAWRNRCQNKNVSQYIKGCRL
>gi|27923799|sp|Q06285.2|LYSC1_BOVIN RecName: Full=Lysozyme C-1; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Bos taurus] >gi|163330|gb|AAC37310.1| lysozyme [Bos taurus] >gi|296487698|tpg|DAA29811.1| TPA: lysozyme C-1 precursor [Bos taurus] >gi|737858|prf||1923351A lysozyme
MKALIILGFLFLSVAVQGKVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKATNYNPGSESTDYGIFQINSK
WWCNDGKTPNAVDGCHVSCSELMENDIAKAVACAKQIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|291389539|ref|XP_002711370.1| PREDICTED: lysozyme C [Oryctolagus cuniculus]
MKALLILGLLLLSTTVQGKIYERCELARTLKKLGLDGYKGVSLANWMCLTKWESSYNTQATNYNPGDKSTDYGIFQINSR
YWCNDGKTPRAVNACHIPCSDLLKDDITQAVACAKRVVSDPQGIRAWVAWRNHCQSQDLTSYIQGCGV
>gi|407971254|gb|AFU52813.1| lysozyme C [Ia io]
MKALLTLGLLLLSVAVQAKVYERCELARTLKRLGMDGYKGVSLANWMCLAKWESSYNTQATNYNPGDRSTDYGIFQINSH
YWCNDGKTPGAVNACGISCSVLLQDDITQAVTCAKRVVRDPQGIRAWVAWRNRCQNQDVSQYIQGCGV
>gi|589920844|ref|XP_006973432.1| PREDICTED: lysozyme C-2-like [Peromyscus maniculatus bairdii]
MKALLSLGLLLLSVTVQAKVYERCEFARTLKSHGMDGYRGISLANWVCLAQHESSYNTRATNYNRGDQSTDYGIFQINSR
YWCNDGKTPRAVNACGIPCSALLLDDITQAIQCAKRVVRDPQGIRAWVAWRNHCQNRDLTQYLRNCRL
>gi|407971240|gb|AFU52806.1| lysozyme C [Barbastella beijingensis]
MKALLTLGLLLLSVAVQAKVYERCELARTLKRLGMDGYRGVSLANWVCLARWESSYNTRAQNYNPGDRSTDYGIFQINSR
YWCNDGKTPGAVNACSISCNVLLQDDITQAVTCAKRVVRDPQGIRAWVAWRNRCQNQDVTQYIRGCGV
>gi|594081410|ref|XP_006064329.1| PREDICTED: lysozyme C-2-like [Bubalus bubalis]
MLNSKSSSPWSVWTFDFSVNMKTLIILGFLFLSVAVQGKVFERCELARTLKKLGLDGYEGVSLANWLCLTKWESSYNTKA
TNYNPSSESTDYGIFQINSKWWCNDGKTPNAVDGCHVSCSELMENDIAKAVACAKHIVSEQGITAWVAWKSHCRDHDVSS
YVEGCTL
>gi|478510359|ref|XP_004429455.1| PREDICTED: lysozyme C-like [Ceratotherium simum simum]
MKALLTLGLLLLSVTVQGKVFERCELARTLKRLGLDGFRGVSLANWMCLAKWESGYNTRATNYNPPDRSTDYGIFQINSH
YWCNDGKTPGAVNACHIPCKALLQDDITQAVACAKRVVSDPQGIRAWVAWRSHCQNHDLTQYVQGCGV
>gi|591382866|ref|XP_007072695.1| PREDICTED: LOW QUALITY PROTEIN: lysozyme [Chelonia mydas]
MKVLLILGLFLLPLAARGKICERCELARAMKRLGLDGYQGYSLGHWVCTARYESNLNTRATHYNNPSRSTDCGIFQINSR
WXCNDGKTPRAKNGCGIQCHALLAADITARVNCTKRIVCASNGMRAWVVWKKYCRGRDVSWWIKGCKL
>gi|440902312|gb|ELR53118.1| hypothetical protein M91_04732 [Bos mutus]
MLNSKCGSPWSVWTFDFSVNMKALIILGFLFLSVAVQGKVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKA
TNYNPSSESTDYGIFQINSKWWCNDGKTPNAVDGCHVSCSELMENDIAKAVACAKHIVSEQGITAWVAWKSHCRDHDVSS
YVEGCTL
>gi|156138697|dbj|BAF75844.1| c-type lysozyme [Scophthalmus rhombus]
MRCLLFLLLVAVAGAKVFERCELARLLKSYGMNNYRGISLADWVCLSQWESSYNTRATNRNTDGSTDYGIFQINSRWWCN
NGQTPTSNACGISCSALLTDDVIAAIACAKRVVVDPNGIGAWVAWKSHCEGRDLSPYLAGCGV
>gi|122692317|ref|NP_001073808.1| lysozyme C-1 precursor [Bos taurus] >gi|163311|gb|AAA30626.1| lysozyme 1a precursor [Bos taurus] >gi|163313|gb|AAA30627.1| lysozyme 1b precursor [Bos taurus]
MKALIILGFLFLSVAVQGKVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKATNYNPGSESTDYGIFQINSK
WWCNDGKTPNAVDGCHVSCSELMENEIAKAVACAKQIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|548549340|ref|XP_005754847.1| PREDICTED: lysozyme C-like [Pundamilia nyererei]
MRSVFVFLLLITVASAKVFERCDWARKLKANGMDGYGGVSLANWVCLTKHESNYNTKATNRNTDGSTDFGIFQINSRWWC
NDRRIHSANGCNIDCNVLLTDDVTSAINCAKRIVREQGITAWVAWRTRCQGQDLRPYLSGCRL
>gi|344266355|ref|XP_003405246.1| PREDICTED: lysozyme C-like [Loxodonta africana]
MKALLILGLLFLSGTAQGKVFERCELARTLKRYGMDGFRGISLANWMCLTKWESDYNTQATNYNPGDKSTDYGIFQINSH
YWCNDGKTPRAVNACGISCYALLQDDITQAVACAKRVVSDPQGIRAWVAWRNHCQNHDVTQYIQGCGV
>gi|291389537|ref|XP_002711369.1| PREDICTED: lysozyme C [Oryctolagus cuniculus]
MKALLILGLLLLSTTVQGKIYERCELARTLKKLGLDGYKGVSLANWMCLTKWESGYNTQATNYNPGDKSTDYGIFQINSR
YWCNDGKTPRAVNACHIPCSDLLKDDITQAVACAKRVVSDPQGIRAWVAWKNHCQSQDLTSYIQGCGV
>gi|512863593|ref|XP_004890444.1| PREDICTED: lysozyme C-like isoform X1 [Heterocephalus glaber] >gi|512863597|ref|XP_004890445.1| PREDICTED: lysozyme C-like isoform X2 [Heterocephalus glaber] >gi|513027894|ref|XP_004875091.1| PREDICTED: lysozyme C-like [Heterocephalus glaber] >gi|351703706|gb|EHB06625.1| Lysozyme C [Heterocephalus glaber]
MKALLILGLLLLSVTIHGKIFERCELARTLKRFGLDGYRGISLPNWVCLARWESSYNTKATNYNPGDRSTDYGIFQINSH
YWCNDGKTPGAVNACGISCNALLQDDITEAVACAKRVVRDPQGIRAWVAWRHRCQNQDLTQYVRGCGV
>gi|532086134|ref|XP_005328788.1| PREDICTED: lysozyme C-like [Ictidomys tridecemlineatus]
MKAFLILGLLLLSVTVQGKVYGRCELARALKRLGMDGYRGISLANWVCLAKWESSYNTRATNYNPGSRSTDYGIFQINSR
YWCNDGKTPRAVNACGISCSALLQDDISQAVTCAKRVVRDPQGIRAWVAWRNRCQNRNLSQYIQGCGV
>gi|407971302|gb|AFU52837.1| lysozyme C [Scotophilus kuhlii]
MKALLTLGLLLLSVAVQAKIYERCELARTLKRLGMDGYKGVSLANWMCLAKWESSYNTQATNYNPGDKSTDYGIFQINSH
YWCNDGKTPRAVNACGISCSVLLQDDITQAVNCAKRVVRDPQGVRAWVAWRNRCQNQDVSQYTRGCGV
>gi|12084272|pdb|1GFR|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGARNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|126607|sp|P04421.2|LYSC_BOVIN RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor
MKALVILGFLFLSVAVQGKVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKATNYNPSSESTDYGIFQINSK
WWCNDGKTPNAVDGCHVSCRELMENDIAKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|6730356|pdb|1DI3|A Chain A, Role Of Amino Acid Residues At Turns In The Conformational Stability And Folding Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDGSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|472373134|ref|XP_004406042.1| PREDICTED: lysozyme C isoform 1 [Odobenus rosmarus divergens] >gi|472373136|ref|XP_004406043.1| PREDICTED: lysozyme C isoform 2 [Odobenus rosmarus divergens]
MKALLLLGLLLLSVTVQGKIFERCELARTLKRLGLAGFKGVSLANWMCLAKWESNYNTKATNYNPGSRSTDYGIFQINSR
YWCNDGKTPGAVNACHIPCSDLLKDDITEAVACAKRVVSDPNGVRAWVAWRAHCENQDVSQYIRNCGV
>gi|157831822|pdb|1LHJ|A Chain A, Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of Proline Mutants
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDGQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|348580421|ref|XP_003475977.1| PREDICTED: lysozyme C-like [Cavia porcellus]
MKALLLLGLLVLSVTVQGKVYKRCELARTLKRLGMDGYRGVSLANWMCLIKWESNYNTRVKNYNPESKSTDYGIFQINSR
YWCNDGKTPGAVNGCGISCNVLLQNDITKAVACAKRVVRDPQGIRAWVAWRNRCQNQDVSLYVRGCRV
>gi|126628|sp|P16973.1|LYSC_RABIT RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C
KIYERCELARTLKKLGLDGYKGVSLANWMCLAKWESSYNTRATNYNPGDKSTDYGIFQINSRYWCNDGKTPRAVNACHIP
CSDLLKDDITQAVACAKRVVSDPQGIRAWVAWRNHCQNQDLTPYIRGCGV
>gi|407971288|gb|AFU52830.1| lysozyme C [Nyctalus plancyi]
MKALLTLGLLLLSVAAQAKVYERCELARTLKRLGLDGYRGVSLANWMCLARWESSYNTRATNYNPGDRSTDYGIFQINSR
YWCNDGKTPRSVNACGISCNVLLQDDITQAVTCAKRVVRDPQGIRAWVAWRNRCQNRDVSQYVQGCGV
>gi|532086132|ref|XP_005328787.1| PREDICTED: lysozyme C-like [Ictidomys tridecemlineatus]
MKAFLILGLLLLSVTVQGKVFGRCELARALKRFGMDGYHRISLANWVCLAKWESSYNTRATNYNPGDQSTDYGIFQINSH
YWCNDGKTPGAVNACGISCNALLQDDISQAVTCAKRVVRDPQGIRAWVAWRNHCQNRDLTQYIQGCGV
>gi|11513935|pdb|1GE3|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQGRDVRQYVQGCGV
>gi|451799068|gb|AGF69234.1| lysozyme precursor [Capra hircus] >gi|558550354|gb|AHA61786.1| lysozyme [Capra hircus]
MKALIILGFLFLSVAVQGKVFERCELARTLKKLGLDDYKGVSLANWLCLTKWESGYNTKATNYNPGSESTDYGIFQINSK
WWCNDGKTPDAVDGCHVSCSELMENDIEKAVACAMHIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|594069048|ref|XP_006058439.1| PREDICTED: lysozyme C, milk isozyme-like [Bubalus bubalis]
MLNTKSSSPGQLGHLASVNMKALLIVGLLLLSVAVQGKKFERCELARTLKKLGLAGYKGVSLANWMCLARWESNYNTRAT
NYNRGDKSTDYGIFQINSRWWCNDGKTPRAVNACGIPCSALLKDDITQAVTCAKRVVRDPQGIRAWVAWRKKCQNRDLTS
YVKGCGV
>gi|325684009|gb|ADZ44620.1| c-type lysozyme [Oplegnathus fasciatus] >gi|332155264|dbj|BAK19960.1| lysozyme C [Oplegnathus fasciatus]
MRSLVFLLLVALASAKVYQRCEWARVLKNHGMDGYQGYSLANWVCLSQWESSYNTRAINHNTDGSTDYGILQINSRWWCD
DGRTQSSNACSIRCSELLTDDASVAINCAKRVARDPNGIKAWVAWRNHCQGRDLSPYLAGCGV
>gi|7305247|ref|NP_038618.1| lysozyme C-1 precursor [Mus musculus] >gi|126599|sp|P17897.1|LYZ1_MOUSE RecName: Full=Lysozyme C-1; AltName: Full=1,4-beta-N-acetylmuramidase C; AltName: Full=Lysozyme C type P; Flags: Precursor [Mus musculus] >gi|49676|emb|CAA35922.1| unnamed protein product [Mus musculus domesticus] >gi|38511912|gb|AAH61129.1| Lysozyme 1 [Mus musculus] >gi|148689889|gb|EDL21836.1| mCG3047 [Mus musculus]
MKALLTLGLLLLSVTAQAKVYNRCELARILKRNGMDGYRGVKLADWVCLAQHESNYNTRATNYNRGDRSTDYGIFQINSR
YWCNDGKTPRSKNACGINCSALLQDDITAAIQCAKRVVRDPQGIRAWVAWRTQCQNRDLSQYIRNCGV
>gi|157833921|pdb|1TDY|A Chain A, Dissection Of The Functional Role Of Structural Elements Of Tyrosine-63 In The Catalytic Action Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRWWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|530291167|gb|AGT17844.1| c-type lysozyme [Capra hircus]
MKALIILGLLCLSVAVQGKVFERCELARTLKKLGLDDYKGVSLANWLCLTKWESGYNTKATNYNPGSESTDYGIFQINSK
WWCNDGKTPDAVDGCHVSCSELMENDIEKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|163315|gb|AAA30628.1| lysozyme 2a precursor, partial [Bos taurus]
TLVILGFLFLSVAVQGKVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKATNYNPSSESTDYGIFQINSKWW
CNDGKTPNAVDGCHVSCSELMENDIAKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|344266357|ref|XP_003405247.1| PREDICTED: lysozyme C-like [Loxodonta africana]
MKALLILGLLFLCGTVHGKVFKRCELARTLKRHGLDGYRGISLANWVCLAKHESNYKTRTTNYNPGDKSTDYGIFQINSR
YWCNDGKTPNAVNACGISCYDLLQGDITQAVACAKRVVRDPQGIKAWVAWRKHCQNRDLTQYVRGCGV
>gi|558155218|ref|XP_006095525.1| PREDICTED: lysozyme C-like [Myotis lucifugus]
MKALLTLGLLLLSVAVRAKVYERCDLARTLKRLGMDGYRGVSLANWMCLAKWESSYNTRATNNNPGDKSTDYGIFQINSR
YWCNDGKTPGAVNACGIPCNDLLQDDITKAATCAKRVVKDPQGIKAWVAWRNHCQNKDVTQYTRGCGV
>gi|5821957|pdb|1C46|A Chain A, Mutant Human Lysozyme With Foreign N-Terminal Residues
GKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHL
SCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|566559935|ref|NP_001274495.1| lysozyme C-1-like precursor [Capra hircus] >gi|451799060|gb|AGF69230.1| lysozyme precursor [Capra hircus]
MKALVILGLLCLSVAVQGKVFERCELARTLKKLGLDDYKGVSLANWLCLTKWESGYNTKATNYNPGSESTDYGIFQINSK
WWCNDGKTPDAVDGCHVSCSELMENDIEKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|562882491|ref|XP_006168797.1| PREDICTED: lysozyme C-like [Tupaia chinensis]
MKAFLFLVLLLLSVTVQGKTFERCELAQILKRNGLDGYRGISLANWMCLAKWESDYDTRATNYNPGDQSTDYGIFQINSR
YWCNDGKTPGAVNACGISCNALLQDDISQAAACAKRVVKDPQGVRAWVAWRNHCQNQDISPYVRGCGI
>gi|126593|sp|P12067.1|LYSC1_PIG RecName: Full=Lysozyme C-1; AltName: Full=1,4-beta-N-acetylmuramidase C >gi|108438|pir||S10046 lysozyme (EC 3.2.1.17) - red deer
KVYDRCEFARILKKSGMDGYRGVSLANWVCLAKWESDFNTKAINRNVGSTDYGIFQINSRYWCNDGKTPKAVNACHISCK
VLLDDDLSQDIECAKRVVRDPQGIKAWVAWRTHCQNKDVSQYIRGCKL
>gi|594695805|ref|XP_007195105.1| PREDICTED: lysozyme C [Balaenoptera acutorostrata scammoni]
MVILRTSEYPSSNIRKKTFKVSGPINGSCFPHVSKGGAARPLGEEGSEKMLNTRTSSAWSAWRSGFSVNMKAVLILGLLL
LSVAVQGKIFERCELARTLKRLGLDGFKGISLANWVCLAKWESSYNTRATNYNPGSRSTDYGIFQINSRYWCNDGKTPRA
SNGCHIHCSVLLKDDITEAVRCAKRVVQDPQGIKAWVAWRNRCQNQDLRSYVQGCGV
>gi|4930014|pdb|1CJ6|A Chain A, T11a Mutant Human Lysozyme
KVFERCELARALKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|564232691|ref|XP_006260721.1| PREDICTED: sperm acrosome membrane-associated protein 3-like [Alligator mississippiensis]
MKALALLPLFGCLIMANEAKVFSRCELAYKLQEAGMDGYEGYSLANWICMAFFESGFNTAAEDDNADGSTDYGIFQINSR
VWCNNHRSPTENLCYMPCTDLLSSDITDDIICAKRIVKDPKGMDAWEDWTMHCKGRDLSEWVDGCDL
>gi|407971298|gb|AFU52835.1| lysozyme C [Rousettus leschenaultii]
MKTLLILGLLLLSVTVQGKVFERCELARTLKRLGMDGFRGVSLANWVCLAKWESSYNTRATNYNPGSQSTDYGIFQINSR
YWCNDGKTPRAVNACRISCNALLQDDISQAVACAKRVVSDPQGIRAWVAWRNRCQNQDLTQYIKGCGV
>gi|407971300|gb|AFU52836.1| lysozyme C [Scotophilus kuhlii]
MKALLTLGLLLLSVAVQAKIYERCELARTLKRLGMDGYRGVSLANWMCLARWESSYNTRVTNYNPGDRSTDYGIFQINSR
YWCNDGKTPRAVNACGISCSVLLQDDITQAVNCAKRVVRDPQGVRAWVAWRNRCQNQDVSQYTRGCGV
>gi|558105455|ref|XP_006110751.1| PREDICTED: sperm acrosome membrane-associated protein 3-like [Pelodiscus sinensis]
MQGETVDLALNATYSCYESPREKGEKEGGTEVPHSLAKMKVLALLFLVSCLIMANEAKIFSRCELAYILHEEGLDGYEGY
SLANWICMAFFESGFNSAAEDDNADGSTDYGMFQINSRVWCNNYRSPTENLCHIPCTDLLSNDIADDIACAKRIVRDPQG
MDAWEDWTMHCKGRDLSEWVDGCDL
>gi|301773614|ref|XP_002922226.1| PREDICTED: lysozyme C-like [Ailuropoda melanoleuca]
MKALLLLGLLLLSITVQGKVFERCELARTLKRLGLAGFKGVSLANWVCLAKWESSYNTRATNYNPGSRSTDYGIFQINSR
YWCNDGKTPRAVNACRIPCSALLTDDITQAVACAKRVVSDPNGIRAWVAWRAHCENRDVSQYVRNCGV
>gi|302320875|gb|ADL16408.1| c-type lysozyme [Oryzias melastigma]
MKSLVLLLFVVGASARVFERCQWARLLKASGMDGYRGVSLANWVCLTKHESNFNTSSVNHNRDKSTDYGIFQINCRWWCN
DTQTPTANGCSIPCSALLTDNVDTAINCAKRVVRDPSGIAAWVAWRKYCKGQDVSSYIQGCGL
>gi|14278472|pdb|1GF3|A Chain A, Buried Polar Mutant Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADSVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157834217|pdb|1WQO|A Chain A, Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGFNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|7546189|pdb|1C7P|A Chain A, Crystal Structure Of Mutant Human Lysozyme With Four Extra Residues (Eaea) At The N-Terminal
EAEAKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNA
CHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|407971268|gb|AFU52820.1| lysozyme C [Murina leucogaster]
MKALLTLGLLLLSVAIQAKVYERCELARTLKRQGMDGYKGVSLANWMCLAQWESSYNTRATNYNPGDRSTDYGIFQINSR
YWCNDGKTPRAVNACGISCDALLQDDITQAITCAKRVVSDPQGIRAWVAWRNRCQNQDVSQYTQGCGV
>gi|6729883|pdb|1B7O|A Chain A, Verification Of Spmp Using Mutant Human Lysozymes
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESQYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|407971246|gb|AFU52809.1| lysozyme C [Cynopterus sphinx]
MKALLILGLLLLSVTIQGKVFKRCELARTLKKHGMDGFKGISLANWVCLVKWESSYNTRDTHYNPGSRSTDYGIFQINSR
YWCNDGKTPRAVNACHVSCNALMKDDITQAIACAKKVVSDTQGIRAWVAWRNHCQNKDLTRYVKGCRL
>gi|507648797|ref|XP_004632212.1| PREDICTED: lysozyme C-like [Octodon degus]
MKALFVLGLLVLSVTVQGKVYERCELARILKNLGMDGYHGVSLANWMCLAKWESDYNTKATNYNPGDESTDYGIFQINSR
YWCNNGRTPRAVNACGISCSALLQDNIAEAVTCAKRVVRDPQGIRAWMAWRSHCQNQDVAKYVQGCGV
>gi|11513937|pdb|1GE4|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQARDVRQYVQGCGV
>gi|157831823|pdb|1LHK|A Chain A, Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of Proline Mutants
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIAPAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157830185|pdb|1B7S|A Chain A, Verification Of Spmp Using Mutant Human Lysozymes
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGASNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|9955033|pdb|1GB8|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAMNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|407971274|gb|AFU52823.1| lysozyme C [Myotis ricketti]
MKALLTLGLLLLSVAVQAKVYERCELARTLKRLGMDGYRGVSLANWVCLARWESSYNTRATNYNPGDRSTDYGIFQINSR
YWCNDGKTPRAVNACGINCNVLLQDDITQAVTCAKRVVRDPQGIRAWVAWRNRCQNQDVSQYTRGCGV
>gi|17942573|pdb|1IP2|A Chain A, G48a Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAADRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|17942566|pdb|1IP7|A Chain A, G129a Human Lysozyme >gi|17942567|pdb|1IP7|B Chain B, G129a Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCAV
>gi|12084401|pdb|1GFH|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAYNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|667278696|ref|XP_008573453.1| PREDICTED: lysozyme C [Galeopterus variegatus]
MKALLLLGLLLLSVTVQGKIFERCELAKAMKRLGMDSYRGVSLANWMCLAKWESSYNTRATNYNPGDQSTDYGIFQINSH
YWCNDGKTPRAVNSCGISCNVLLQDDITKAAECAKKIVRDQGITAWVAWRNHCQNQDVSQYVRGCGV
>gi|557281796|ref|XP_006023845.1| PREDICTED: sperm acrosome membrane-associated protein 3-like [Alligator sinensis]
MKALALLPLFGCLIMSNEAKVFSRCELAYKLQEAGMDGYEGYSLANWICMAFFESGFNTAAEDDNADGSTDYGIFQINSR
VWCNNHRSPTENLCYMPCTDLLSSDITDDIICAKRIVKDPKGMDAWEDWTMHCKGRDLSEWVDGCDL
>gi|157832585|pdb|1OUH|A Chain A, Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V74a Mutant
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAANACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|12084403|pdb|1GFK|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGANNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|74136111|ref|NP_001027914.1| lysozyme C precursor [Takifugu rubripes] >gi|48428216|sp|P61944.1|LYSC_TAKRU RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Takifugu rubripes] >gi|38603664|dbj|BAD02933.1| chicken-type lysozyme [Takifugu rubripes]
MKIPVFLLLLALANAKVFQRCEWARVLKARGMDGYRGISLADWVCLSKWESQYNTNAINHNTDGSTDYGIFQINSRWWCN
DDRIPTRNACNIKCSALQTDDVTVAINCAKRVVSDPQGIRAWVAWNRHCQNRDLSAYIAGCGL
>gi|407088|emb|CAA53144.1| lysozyme [synthetic construct] >gi|34484362|gb|AAQ72808.1| lysozyme [synthetic construct]
MKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHL
SCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|4930015|pdb|1CJ7|A Chain A, T11v Mutant Human Lysozyme
KVFERCELARVLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|9955032|pdb|1GB7|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGALNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|478510361|ref|XP_004429456.1| PREDICTED: lysozyme C-like [Ceratotherium simum simum]
MKALLTLGLLLLSVTVQGKVIERCELARTMKRLGLDGFRGVSLANWMCLAKWESGYNTRATNYNPPDRSTDYGIFQINSH
YWCNDGKTPGAVNACHIPCKALLQDDITQAVACAKQIVTKQGLGAWVAWKKHCQHKDLTQYVKGCRL
>gi|296212336|ref|XP_002752792.1| PREDICTED: lysozyme C [Callithrix jacchus] >gi|2497772|sp|P79158.1|LYSC_CALJA RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|1790929|gb|AAB41203.1| lysozyme c precursor [Callithrix jacchus]
MKVLIILGLVLLSVMVQGKVFERCELARTLKRFGLDGYRGISLANWMCLAKWESDYNTRATNYNPGDQSTDYGIFQINSH
YWCNNGRTPGAVNACHISCNALLQDDITEAVACAKRVVRDPQGIRAWVAWKAHCQNRDVSQYVQGCGV
>gi|6730357|pdb|1DI4|A Chain A, Role Of Amino Acid Residues At Turns In The Conformational Stability And Folding Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCS
ALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|511858608|ref|XP_004752511.1| PREDICTED: lysozyme C [Mustela putorius furo] >gi|511958227|ref|XP_004797377.1| PREDICTED: lysozyme C [Mustela putorius furo]
MLNTEDCSPWSARRSGFPVNMKALLLLGILFLSVTVQGKVFERCELARTLKRLGLGGYRGVSLANWMCLAKWESNYNTKA
TNYNPGSRSTDYGIFQINSRYWCNDGKTPGAVNACGIPCSDLLKDDITQAVACAKRVVRDPNGIRAWVAWKAHCENRDVS
QYVRNCGV
>gi|12084402|pdb|1GFJ|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGADNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|6729705|pdb|1B5X|A Chain A, Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLA
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157834289|pdb|1YAN|A Chain A, Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of The Five Isoleucine To Valine Mutants
KVFERCELARTLKRLGMDGYRGVSLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|17942574|pdb|1IP1|A Chain A, G37a Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESAYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157832583|pdb|1OUF|A Chain A, Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V130a Mutant
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGA
>gi|9955034|pdb|1GB9|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAFNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|1065033|pdb|1LZS|A Chain A, Structural Changes Of The Active Site Cleft And Different Saccharide Binding Modes In Human Lysozyme Co-Crystallized With Hexa-N-Acetyl- Chitohexaose At Ph 4.0 >gi|1065034|pdb|1LZS|B Chain B, Structural Changes Of The Active Site Cleft And Different Saccharide Binding Modes In Human Lysozyme Co-Crystallized With Hexa-N-Acetyl- Chitohexaose At Ph 4.0 >gi|5107681|pdb|1RE2|A Chain A, Human Lysozyme Labelled With Two 2',3'-epoxypropyl Beta-glycoside Of N-acetyllactosamine >gi|15988350|pdb|1JWR|A Chain A, Crystal Structure Of Human Lysozyme At 100 K >gi|22218808|pdb|1IY3|A Chain A, Solution Structure Of The Human Lysozyme At 4 Degree C >gi|22218809|pdb|1IY4|A Chain A, Solution Structure Of The Human Lysozyme At 35 Degree C >gi|38492671|pdb|1OP9|B Chain B, Complex Of Human Lysozyme With Camelid Vhh Hl6 Antibody Fragment >gi|157831571|pdb|1JSF|A Chain A, Full-Matrix Least-Squares Refinement Of Human Lysozyme >gi|157831910|pdb|1LZ1|A Chain A, Refinement Of Human Lysozyme At 1.5 Angstroms Resolution. Analysis Of Non-Bonded And Hydrogen-Bond Interactions >gi|157831921|pdb|1LZR|A Chain A, Structural Changes Of The Active Site Cleft And Different Saccharide Binding Modes In Human Lysozyme Co-Crystallized With Hexa-N-Acetyl- Chitohexaose At Ph 4.0 >gi|157833668|pdb|1REM|A Chain A, Human Lysozyme With Man-B1,4-Glcnac Covalently Attached To Asp53 >gi|157833671|pdb|1REX|A Chain A, Native Human Lysozyme >gi|157833672|pdb|1REY|A Chain A, Human Lysozyme-N,N'-Diacetylchitobiose Complex >gi|157833673|pdb|1REZ|A Chain A, Human Lysozyme-N-Acetyllactosamine Complex >gi|159046750|pdb|1IWT|A Chain A, Crystal Structure Analysis Of Human Lysozyme At 113k. >gi|159046751|pdb|1IWU|A Chain A, Crystal Structure Analysis Of Human Lysozyme At 127k. >gi|159046752|pdb|1IWV|A Chain A, Crystal Structure Analysis Of Human Lysozyme At 147k. >gi|159046753|pdb|1IWW|A Chain A, Crystal Structure Analysis Of Human Lysozyme At 152k. >gi|159046754|pdb|1IWX|A Chain A, Crystal Structure Analysis Of Human Lysozyme At 161k. >gi|159046755|pdb|1IWY|A Chain A, Crystal Structure Analysis Of Human Lysozyme At 170k. >gi|159046756|pdb|1IWZ|A Chain A, Crystal Structure Analysis Of Human Lysozyme At 178k. >gi|215794704|pdb|3EBA|B Chain B, Cabhul6 Fglw Mutant (Humanized) In Complex With Human Lysozyme >gi|219689182|pdb|2ZIJ|A Chain A, Crystal Structure Of Human Lysozyme Expressed In E. Coli. >gi|219689183|pdb|2ZIK|A Chain A, Crystal Structure Of Human Lysozyme From Pichia Pastoris >gi|219689184|pdb|2ZIL|A Chain A, Crystal Structure Of Human Lysozyme From Urine >gi|253723297|pdb|2NWD|X Chain X, Structure Of Chemically Synthesized Human Lysozyme At 1 Angstrom Resolution >gi|270346492|pdb|3FE0|A Chain A, X-Ray Crystal Structure Of Wild Type Human Lysozyme In D2o >gi|353529987|pdb|2ZWB|A Chain A, Neutron Crystal Structure Of Wild Type Human Lysozyme In D2o >gi|550545696|pdb|4I0C|A Chain A, The Structure Of The Camelid Antibody Cabhul5 In Complex With Human Lysozyme >gi|550545697|pdb|4I0C|B Chain B, The Structure Of The Camelid Antibody Cabhul5 In Complex With Human Lysozyme >gi|667484857|pdb|4ML7|A Chain A, Crystal Structure Of Brucella Abortus Plic In Complex With Human Lysozyme >gi|667484859|pdb|4ML7|C Chain C, Crystal Structure Of Brucella Abortus Plic In Complex With Human Lysozyme >gi|208796|gb|AAA72819.1| lysozyme, partial [synthetic construct] >gi|1335210|emb|CAA32175.1| lysozyme [Homo sapiens]
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|407971248|gb|AFU52810.1| lysozyme C [Eonycteris spelaea]
MKALLILGLLLLSVTVQGKVYERCELARTLKRLGMDGFRGVSLANWVCLAKWESSYNTRATNYNPGSQSTDYGIFQINSR
YWCNDGKTPRAVNACHISCNALLQDDITQAVACAKRVVSDPQGIRAWVAWRNRCQNQDLTQYIKNCGV
>gi|157831824|pdb|1LHL|A Chain A, Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of Proline Mutants
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNPGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|426258555|ref|XP_004022875.1| PREDICTED: lysozyme C, milk isozyme-like [Ovis aries]
MKAVLILGLLLLSVTVQGKKFQKCELARTLKRLGLDGYKGFSLAKWMCLARWESNYNTRATNYNRGDKSTDYGIFQINSR
WWCNDGKTPRAVNACRIPCSDLLKDDITQAVASAKKVVSDPQDVRAWVAWRNKCQNQDLRSHLQGCGA
>gi|47213161|emb|CAG06232.1| unnamed protein product [Tetraodon nigroviridis]
MRHKVHSNGGAALAAPGRLASVRRLAAAAAMRTLVFLLLLAVASAKVYQRCELARVLKSQGMDGYRGISLANWVCLSKWE
SEYNTNAINHNTDGSTDYGIFQINSRWWCNNDVTPTSNGCNIKCRALLTDDISVAIACAKRVVRDPQGIRAWVAWRNRCQ
GRDLSGYVAGCGL
>gi|190610720|gb|ACE80211.1| lysozyme [Scophthalmus maximus]
MRCLLLLLLVAVAGAKVFERCEWARLLKRNGMSNYRGISLADWVCLSQWESSYNTRATNRNTDGSTDYGIFQINSRWWCD
NGQTPTSNACGISCSALLTDDVGAAIICAKHVVRDPNGIGAWVAWKRHCQGQDLSSYVAGCGV
>gi|157834288|pdb|1YAM|A Chain A, Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of The Five Isoleucine To Valine Mutants
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGVRAWVAWRNRCQNRDVRQYVQGCGV
>gi|220950|dbj|BAA00314.1| lysozyme [synthetic construct]
MKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACQL
SCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|13399625|pdb|1I1Z|A Chain A, Mutant Human Lysozyme (Q86d)
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLDDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|9955031|pdb|1GB6|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAINACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|554884155|ref|XP_005951763.1| PREDICTED: lysozyme C-like [Haplochromis burtoni]
MRSVFVFLLLITVASAKVFERCDWARKLKANGMDGYGGVSLANWVCLTKHESNYNTKATNRNTDGSTDFGIFQINSRWWC
NDRRIHSANGCNIDCNVLLTDDVTSAINCAKRIVREQGITAWVAWRARCQGQDLRPYLSGCGL
>gi|9955030|pdb|1GB5|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAGNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|548465845|ref|XP_005680249.1| PREDICTED: lysozyme C-1-like [Capra hircus]
MLNSKSGSPWSVWTLDFSVNMKALVILGLLCLSVAVQGKVFERCELARTLKKLGLDDYKGVSLANWLCLTKWESSYNTKA
TNYNPGSESTDYGIFQINSKWWCNDGKTPDAVDGCHVSCSELMENNIAKAVACAKQIVSEQGITAWVAWKSHCRDHDVSS
YVEGCTL
>gi|558155301|ref|XP_006095544.1| PREDICTED: lysozyme C [Myotis lucifugus]
MKALLTLGLLLLSVAVRAKVYERCDLARTLKRLGMDGYSGVSLANWMCLAKWESSYNTRATNNNPGDKSTDYGIFQINSR
YWCNDGKTPGAVNACGIPCNDLLQDDITKAATCAKRVVKDPQGIKAWVAWRNHCQNKDVTQYTRGCGV
>gi|157835053|pdb|2HEB|A Chain A, Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability
KVFERCELARTLKRLGMDGYRGASLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|612049935|ref|XP_007502944.1| PREDICTED: lysozyme C-like isoform X2 [Monodelphis domestica]
MLNGLWALAHGKVYKRCELARVLKQNGMDGYRGNSVDNWVCLAKWESDFDTEATNYNPGDQSTNYGIFQINSHYWCNDGK
TPDAKNVCGISCRDLLTDNITQAVNCAKRVVHDPSGILAWKAWRNHCQGRDVSSYIQDCRL
>gi|407971292|gb|AFU52832.1| lysozyme C [Pipistrellus abramus]
MKALLTLGLLLLSVAVQAKVYERCELARTLKRLGMDGYRGVSLANWMCLARWESSYNTRATNYNPGDRSTDYGIFQINSR
YWCNDGKTPRSSNACGISCNVLLQDDITQAVTCAKRVVRDPQGIRAWVAWRNRCQNRDLTQYVQGCGV
>gi|395537849|ref|XP_003770901.1| PREDICTED: lysozyme C [Sarcophilus harrisii]
MKVLLLLGFIFLPMAVHGKIFERCDFARRIKELGMDNYHRVSLANWVCLAKWESSFNTKARNYNPGDKSTDYGIFQTNSH
YWCDDGKTPHATNGCGYKCSELEEDNLIKAVKCAKKIVDQQGITAWVAWRNKCQGKDLSGYLKGCKL
>gi|2497782|sp|P79268.1|LYSC_SAGOE RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|1790943|gb|AAB41210.1| lysozyme c precursor [Saguinus oedipus]
MKVLILLGLVLLSVMVQGKVFERCELARTLKRLGLDGYRGISLANWMCLAKWESDYNTRATNYNPGDQSTDYGIFQINSH
YWCNNGRTPGAVNACHISCNALLQDDITEAVACAKRVVRDPQGIRAWVAWKAHCQNRDVSQYIQGCGV
>gi|9955036|pdb|1GBW|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWIAWRNRCQNRDVRQYVQGCGV
>gi|9955027|pdb|1GAZ|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KIFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157834218|pdb|1WQP|A Chain A, Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNFNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157834215|pdb|1WQM|A Chain A, Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQFVQGCGV
>gi|157833914|pdb|1TCY|A Chain A, Dissection Of The Functional Role Of Structural Elements Of Tyrosine-63 In The Catalytic Action Of Human Lysozyme >gi|157834220|pdb|1WQR|A Chain A, Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRFWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157834291|pdb|1YAP|A Chain A, Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of The Five Isoleucine To Valine Mutants
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQVNSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157834292|pdb|1YAQ|A Chain A, Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of The Five Isoleucine To Valine Mutants
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNVADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157834290|pdb|1YAO|A Chain A, Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of The Five Isoleucine To Valine Mutants
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGVFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|13399626|pdb|1I20|A Chain A, Mutant Human Lysozyme (A92d)
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADDVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|48428270|sp|Q9PU28.1|LYSC_PSEMX RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Scophthalmus maximus] >gi|6165445|emb|CAB59841.1| lysozyme precursor [Psetta maxima]
MRCLLLLLLVPVPGAKVFERCEWARLLKRNGMSNYRGISLADWVCLSQWESSYNTRATNRNTDGSTDYGIFQINSRWWCD
NGQTPTSNACGISCSALLTDDVGAAIICAKHVVRDPNGIGAWVAWKRHCQGQDLSSYVAGCGV
>gi|407971250|gb|AFU52811.1| lysozyme C [Hipposideros armiger]
MKSLLILGLLLLAATVQGKVFERCELARALKRMGMDGFKGISLPNWVCLAQWESSYNTQATNYNPGSKSTDYGIFQINSR
YWCNDGKTPKAVNACHISCNVLLQDDITQAVACAKRVVSDPQGIRAWVAWKNHCQNRDLTQYTRGCGV
>gi|157835322|pdb|2LHM|A Chain A, Crystal Structures Of The Apo-And Holomutant Human Lysozymes With An Introduced Ca2+ Binding Site >gi|157836837|pdb|3LHM|A Chain A, Crystal Structures Of The Apo-And Holomutant Human Lysozymes With An Introduced Ca2+ Binding Site
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLDDNIADDVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|407971264|gb|AFU52818.1| lysozyme C [Miniopterus fuliginosus]
MKALLILGLFLLSVAVQGKVYERCELARTLKRLGMDGFRGVKLADWVCLAKWESSYNTRATNYNPGSKSTDYGIFQINSR
YWCNDGKTPSTANACRISCNVLLQDDITQAVACAKRVVSDPQGIRAWVAWRNRCQNRDLTQYIQGCGV
>gi|6729884|pdb|1B7P|A Chain A, Verification Of Spmp Using Mutant Human Lysozymes
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACGLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|24987350|pdb|1IOC|A Chain A, Crystal Structure Of Mutant Human Lysozyme, Eaea-I56t
EAEAKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGTFQINSRYWCNDGKTPGAVNA
CHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|27923983|sp|P17607.2|LYSC1_SHEEP RecName: Full=Lysozyme C-1; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Ovis aries] >gi|5802272|gb|AAD51636.1| lysozyme 1 [Ovis aries] >gi|451799072|gb|AGF69236.1| lysozyme-1 precursor [Ovis aries]
MKALIILGLLCLSVAVQGKVFERCELARTLKELGLDGYKGVSLANWLCLTKWESSYNTKATNYNPGSESTDYGIFQINSK
WWCNDGKTPNAVDGCHVSCSELMENNIAKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCSL
>gi|407971266|gb|AFU52819.1| lysozyme C [Murina leucogaster]
MKALLTLGLLLLSVAVQAKVYERCELARTLKRLGMHGYRGVSLANWMCLARWESSYNTRATNYNPGDRSTDYGIFQINSR
YWCNDGKTPRAVNACGISCDALLQDDITQAATCAKRVVRDPQGIRAWVAWRNRCQNQDVSQYIRGCGV
>gi|157835340|pdb|2MEE|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQLNSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157835338|pdb|2MEB|A Chain A, Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGLFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157835052|pdb|2HEA|A Chain A, Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGARAWVAWRNRCQNRDVRQYVQGCGV
>gi|14278470|pdb|1GEZ|A Chain A, Buried Polar Mutant Human Lysozyme
KVFERCELSRTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|14278474|pdb|1GF5|A Chain A, Buried Polar Mutant Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACSKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|4388847|pdb|1B5Z|A Chain A, Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants >gi|4388848|pdb|1B5Z|B Chain B, Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CAALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|6729876|pdb|1B5U|A Chain A, Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutant
KVFERCELARTLKRLGMDGYRGIALANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|6729879|pdb|1B5Y|A Chain A, Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWEAGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|6729878|pdb|1B5W|A Chain A, Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINARYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|14278471|pdb|1GF0|A Chain A, Buried Polar Mutant Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLSKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|6729877|pdb|1B5V|A Chain A, Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRATDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|407971244|gb|AFU52808.1| lysozyme C [Cynopterus sphinx]
MKALLILGLLLLSVTIQGKVYERCEFARTLKRRGMDGFKGISLANWVCLAKWESSYNTRATNYNPGSRSTDYGIFQINSR
YWCNDGKTPQAVNACHISCNALLQDDITQAIECAKRVVSDPQGIRAWVAWRNHCQNQDLTQYIQGCGV
>gi|157835341|pdb|2MEF|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQMNSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|3402142|pdb|2MEC|A Chain A, Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions >gi|3402143|pdb|2MEC|B Chain B, Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGMFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|11513933|pdb|1GE2|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACALS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|641700567|ref|XP_008138834.1| PREDICTED: lysozyme C [Eptesicus fuscus]
MRAILIISLFSCFFAAYNAKVFSKCELARQLKAHGMDGFHGYSLANWVCMAQYESNFNTRAFNGKNSNGSSDYGLFQLNN
KWWCKDNKYPSENACNIMCSKFLDDNINDDINCIKRVVKDPNGMSAWVAWVNHCKNRDLSQYLAGCQL
>gi|9955028|pdb|1GB0|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KLFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|9955037|pdb|1GBX|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWLAWRNRCQNRDVRQYVQGCGV
>gi|9955038|pdb|1GBY|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWMAWRNRCQNRDVRQYVQGCGV
>gi|9955327|pdb|1GB2|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KMFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|7767015|pdb|1EQ4|A Chain A, Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme
KVFERCQLARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157831754|pdb|1LAA|A Chain A, X-Ray Structure Of Glu 53 Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTEYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|6980459|pdb|1D6Q|A Chain A, Human Lysozyme E102 Mutant Labelled With 2',3'-Epoxypropyl Glycoside Of N-Acetyllactosamine >gi|30750167|pdb|1UBZ|A Chain A, Crystal Structure Of Glu102-Mutant Human Lysozyme Doubly Labeled With 2',3'-Epoxypropyl Beta-Glycoside Of N-Acetyllactosamine
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVREPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|403271884|ref|XP_003927830.1| PREDICTED: lysozyme C [Saimiri boliviensis boliviensis]
MKVLIILGLVLLSVMVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESDYNTRATNYNPGDQSTDYGIFQINSH
YWCNNGRTPGAVNACHISCNALLQDDITQAVACAKRVVRDPQGIRAWVAWKAHCQNRDVSQYVQGCGV
>gi|2497783|sp|P79294.1|LYSC_SAISC RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|1790945|gb|AAB41211.1| lysozyme c precursor [Saimiri sciureus]
MKVLVILGLVLLSVMVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESDYNTRATNYNPGDQSTDYGIFQINSH
YWCNNGRTPGAVNACHISCNALLQDDITQAVACAKRVVRDPQGIRAWVAWKAHCQNRDVSQYVQGCGV
>gi|14278475|pdb|1GF6|A Chain A, Buried Polar Mutant Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRTVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157834219|pdb|1WQQ|A Chain A, Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDFGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157834216|pdb|1WQN|A Chain A, Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGFRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157831551|pdb|1JKA|A Chain A, Human Lysozyme Mutant With Glu 35 Replaced By Asp
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWDSGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|665505916|ref|NP_001287805.1| lysozyme precursor [Canis lupus familiaris] >gi|661492823|gb|AIE13825.1| lysozyme [Canis lupus familiaris]
MKTLLFLGLLLLSITVQGKIFERCELARTLKNLGLAGYKGVSLANWVCLAKWESNYNTRATNYNPGSKSTDYGIFQINSR
YWCNDGKTPRAVNACHISCSALLQDDITQAVACAKRVVSDPNGIRAWVAWRAHCENRDVSQYVRNCGV
>gi|4930017|pdb|1CJ9|A Chain A, T40v Mutant Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNVRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|4930023|pdb|1CKH|A Chain A, T70v Mutant Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKVPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|5107556|pdb|1CKG|A Chain A, T52v Mutant Human Lysozyme >gi|5107557|pdb|1CKG|B Chain B, T52v Mutant Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSVDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|4930021|pdb|1CKD|A Chain A, T43v Mutant Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRAVNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157835339|pdb|2MED|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQFNSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|6980458|pdb|1D6P|A Chain A, Human Lysozyme L63 Mutant Labelled With 2',3'-Epoxypropyl N,N'- Diacetylchitobiose >gi|157833905|pdb|1TBY|A Chain A, Dissection Of The Functional Role Of Structural Elements Of Tyrosine-63 In The Catalytic Action Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRLWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|3402139|pdb|2MEA|A Chain A, Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions >gi|3402140|pdb|2MEA|B Chain B, Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGFFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|14278476|pdb|1GF7|A Chain A, Buried Polar Mutant Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVTRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|14278473|pdb|1GF4|A Chain A, Buried Polar Mutant Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADATACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|253683451|ref|NP_001156629.1| c-type lysozyme precursor [Oryzias latipes] >gi|226821191|gb|ACO82287.1| c-type lysozyme [Oryzias latipes]
MKSLVFLLLVAGASAKVFERCQWARLLKAQGMDGYRGVSLANWVCLTQHESRFNTNAINHNRDGSTDYGIFQINSYWWCD
DGKTGRVNGCKIPCSALLSDSVGTAIACAKRIVQDPSGIAAWVAWRDHCRGRDVSSYIQGCGF
>gi|157832587|pdb|1OUJ|A Chain A, Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V99a Mutant
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRAVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157832582|pdb|1OUE|A Chain A, Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V125a Mutant
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYAQGCGV
>gi|225831|prf||1314258A lysozyme
KIFERCELARTLKKLGLDGYKGVSLANWVCLAKWESGYNTEATNYNPGDESTDYGIFQINSRYWCNNGKTPGAVDACHIS
CSALLQNNIADAVACAKRVVSDPQGIRAWVAWRNHCQNKDVSQYVKGCGV
>gi|6729881|pdb|1B7M|A Chain A, Verification Of Spmp Using Mutant Human Lysozymes
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACMKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157832580|pdb|1OUC|A Chain A, Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V110a Mutant
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWAAWRNRCQNRDVRQYVQGCGV
>gi|17942570|pdb|1IP4|A Chain A, G72a Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPAAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157832579|pdb|1OUB|A Chain A, Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-ray Structure Of The V100a Mutant
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVARDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|17942571|pdb|1IP3|A Chain A, G68a Human Lysozyme >gi|17942572|pdb|1IP3|B Chain B, G68a Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDAKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157832584|pdb|1OUG|A Chain A, Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V2a Mutant
KAFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157832586|pdb|1OUI|A Chain A, Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V93a Mutant
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAAACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|17942568|pdb|1IP6|A Chain A, G127a Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQACGV
>gi|17942569|pdb|1IP5|A Chain A, G105a Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQAIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157832581|pdb|1OUD|A Chain A, Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V121a Mutant
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDARQYVQGCGV
>gi|593760417|ref|XP_007118936.1| PREDICTED: lysozyme C [Physeter catodon]
MKAVLILGLLLLSVTVQGKIFERCELARTLKRLGLDGYVGISLANWMCLARWESSYNTRATNYNPGSRSTDYGIFQINSR
YWCNDGKTPRAVNACHIPCSVLLKDDIAEAVKCAKRIVGDPQGIRAWVAWKNHCQNQDLRSYVQGCGV
>gi|9955029|pdb|1GB3|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KFFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157829563|pdb|134L|A Chain A, Role Of Arg 115 In The Catalytic Action Of Human Lysozyme. X-Ray Structure Of His 115 And Glu 115 Mutants
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNECQNRDVRQYVQGCGV
>gi|9955039|pdb|1GBZ|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWFAWRNRCQNRDVRQYVQGCGV
>gi|323462871|pdb|3LN2|A Chain A, Crystal Structure Of A Charge Engineered Human Lysozyme Variant >gi|323462872|pdb|3LN2|B Chain B, Crystal Structure Of A Charge Engineered Human Lysozyme Variant
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVDDPQGIRAWVAWRNHCQNRDVRQYVQGCGV
>gi|5821955|pdb|1C43|A Chain A, Mutant Human Lysozyme With Foreign N-Terminal Residues
MVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157829561|pdb|133L|A Chain A, Role Of Arg 115 In The Catalytic Action Of Human Lysozyme. X-Ray Structure Of His 115 And Glu 115 Mutants
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNHCQNRDVRQYVQGCGV
>gi|4930016|pdb|1CJ8|A Chain A, T40a Mutant Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNARATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|4930020|pdb|1CKC|A Chain A, T43a Mutant Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRAANYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|4930022|pdb|1CKF|A Chain A, T52a Mutant Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSADYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|3659958|pdb|1BB3|A Chain A, Human Lysozyme Mutant A96l >gi|3659959|pdb|1BB3|B Chain B, Human Lysozyme Mutant A96l >gi|3659962|pdb|1BB5|A Chain A, Human Lysozyme Mutant A96l Complexed With Chitotriose >gi|3659963|pdb|1BB5|B Chain B, Human Lysozyme Mutant A96l Complexed With Chitotriose
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACLKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|6729880|pdb|1B7L|A Chain A, Verification Of Spmp Using Mutant Human Lysozymes
KVFERCELARTLKRLGMDGYRGISLANWMCLLKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|12084397|pdb|1GF9|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KYFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|12084273|pdb|1GFT|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWYAWRNRCQNRDVRQYVQGCGV
>gi|122064294|sp|P85045.1|LYS_BUFAN RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor
SGKYISWEDSCSYLQLQKYERCELAKALKKGGLADFKGYSLENWICTAFHESGYNTASTNYNPPDKSTDYGIFQINSRWW
CNDYKTPRSKNTCNIDCKVLLGDDISPAIKCAKRVVSDPNGMGAWVAWKKYCKGKNLSQWTQGCKL
>gi|657594329|ref|XP_008301771.1| PREDICTED: lysozyme C [Stegastes partitus]
MRTLLVLFLVVVTGAEALERCAWAKILKNSGMDGYRGISLANWVCLTRWESNFNTGAINHNTDGSTDYGIFQINSRWWCT
DGKTPSANGCNIQCSALLTSNVAVAINCAKRVVRDPQGISAWVAWRNRCRNQDLSSYLAGCQL
>gi|14278467|pdb|1GEV|A Chain A, Buried Polar Mutant Human Lysozyme
KVFERCETARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157831857|pdb|1LOZ|A Chain A, Amyloidogenic Variant (i56t) Variant Of Human Lysozyme >gi|157832578|pdb|1OUA|A Chain A, Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The I56t Mutant >gi|299033|gb|AAB26052.1| lysozyme=amyloid fibril protein [human, Peptide Mutant, 130 aa]
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGTFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157835343|pdb|2MEH|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQTNSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|48428265|sp|Q9DD65.1|LYSC_PAROL RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Paralichthys olivaceus] >gi|11034661|dbj|BAB17215.1| chicken-type lysozyme [Paralichthys olivaceus] >gi|11275394|dbj|BAB18249.1| c-type lysozyme [Paralichthys olivaceus]
MRTLVVLLLVAVANARVYERCEWARLLRNQGMDGYRGISLANWVCLTEWESHYNTRATNHNTDGSTDYGIFQINSRWWCN
DSQTPTSNACNIRCSELLTDDVIVAIKCAKRVVRDPNGIGAWVAWRQHCQGQDLSSYLAGCGL
>gi|157835344|pdb|2MEI|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQYNSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|589920840|ref|XP_006973430.1| PREDICTED: lysozyme C-2-like [Peromyscus maniculatus bairdii]
MKALLSLGLFLLSVTVQAKVYERCEFARTLKSHGMDGYLGISLANWVCLAQHESNFNTRATNYNPGGQSTDYGIFQINSR
YWCNDGKTPRAVNACGISCSALLQDDITQAIQCAKRVVRDPQGIKAWVAWRSHCQNRDLTQYIRNCGV
>gi|5821956|pdb|1C45|A Chain A, Mutant Human Lysozyme With Foreign N-Terminal Residues
AVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|7767016|pdb|1EQ5|A Chain A, Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRNPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|7767021|pdb|1EQE|A Chain A, Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRNVRQYVQGCGV
>gi|50514025|pdb|1W08|A Chain A, Structure Of T70n Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKNPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|426224733|ref|XP_004006523.1| PREDICTED: lysozyme 1b precursor [Ovis aries]
MLNSKSGSPWSVWTFDFSVNMKALVILGLLCLSVAVQGKVFERCELARTLKELGLDGYKGVSLANWLCLTKWESSYNTKA
TNYNPGSESTDYGIFQINSKWWCNDGKTPNAVDGCHVSCSELMENNIAKAVACAKHIVSEQGITAWVAWKSHCRDHDVSS
YVEGCSL
>gi|157833900|pdb|1TAY|A Chain A, Dissection Of The Functional Role Of Structural Elements Of Tyrosine-63 In The Catalytic Action Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRAWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|55583782|sp|Q659U1.1|LYSC_PHOVI RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|55583783|sp|Q659U5.1|LYSC_HALGR RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|52075484|emb|CAH39859.1| lysozyme [Halichoerus grypus] >gi|52075492|emb|CAH39863.1| lysozyme [Phoca vitulina]
MKALLLLGLLLLSVTVQGKIFERCDLARTLKRLGLAGFKGVSLANWMCLAKWESNYNTKATNYNPGSRSTDYGIFQINSR
YWCNDGKTPRAVNACHIPCSDLLKDDITQAVACAKRVVSDPNGIRAWVAWRAHCENQDVSQYVRNCGV
>gi|157831908|pdb|1LYY|A Chain A, Amyloidogenic Variant (Asp67his) Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNHGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157835055|pdb|2HED|A Chain A, Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQANSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157835054|pdb|2HEC|A Chain A, Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGAFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157835057|pdb|2HEF|A Chain A, Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNAADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|269914120|ref|NP_999557.2| lysozyme C-3 precursor [Sus scrofa] >gi|2506829|sp|P12068.2|LYSC2_PIG RecName: Full=Lysozyme C-2; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|1143948|gb|AAB16862.1| lysozyme [Sus scrofa]
MKTLLVLALLLLSVSVQAKVYDRCEFARILKKSGMDGYRGVSLANWVCLAKWESDFNTKAINHNVGSTDYGIFQINSRYW
CNDGKTPKAVNACHISCKVLLDDDLSQDIECAKRVVRDPLGVKAWVAWRAHCQNKDVSQYIRGCKL
>gi|556722672|ref|XP_005957166.1| PREDICTED: lysozyme C, milk isozyme-like [Pantholops hodgsonii]
MKAVLILGLLLLSVTVQGKKFQKCELARTLKRLGLDGYKGISLAKWMCLARWESNYNTRATNYNHGDKSTDYGIFQINSR
WWCNDGKTPRAVKACCIPCSDLLKDDITQAVASAKKVVSDPQGVRAWVAWRNKCQNQDLRSHVQGCGV
>gi|507636801|ref|XP_004700516.1| PREDICTED: lysozyme C-like [Echinops telfairi]
MKVLLILGFLFLSVTVQGKVFKRCELAKRLKELRMDGYEGISLANWMCLIKWESSYNTQVKKHIRGKSSNYGIFQINSHY
WCNDGKTPRSRNACRVSCNALLKDDITQAVACAKEVVSRPQGIKGWVAWRNRCENRDLTQYVQGCGV
>gi|12084396|pdb|1GF8|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KSFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157831820|pdb|1LHH|A Chain A, Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of Proline Mutants
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWPAWRNRCQNRDVRQYVQGCGV
>gi|2506830|sp|P12069.2|LYSC3_PIG RecName: Full=Lysozyme C-3; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|1174173|gb|AAA86644.1| lysozyme [Sus scrofa]
MKTLLVLALLLLSVSVQAKVYDRCEFARILKKSGMDGYRGVSLANWVCLAKWESNFNTKATNYNPGSQSTDYGIFQINSR
YWCNDGKTPKAVNACHISCKVLLDDDLSQDIECAKRVVRDPQGIKAWVAWKAHCQNKDVSQYIRGCKL
>gi|12084400|pdb|1GFG|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KRFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|12084409|pdb|1INU|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWRAWRNRCQNRDVRQYVQGCGV
>gi|83972426|gb|ABC49680.1| c-type lysozyme [Solea senegalensis]
MKCLVFMLLVALSSAKVFERCEWARKLRSHGMDGVGGYNLANWVCLTKGESDYNTRATNRNTDGSIDYGIFQINSRYWCN
NGQGPTSNACGISCSELLKDDVTAAIRCVKRVVQDPNGIRAWVAWVRHCEGRDLSSYVRGCGV
>gi|13399627|pdb|1I22|A Chain A, Mutant Human Lysozyme (A83kQ86DA92D) >gi|13399628|pdb|1I22|B Chain B, Mutant Human Lysozyme (A83kQ86DA92D) >gi|13399629|pdb|1I22|C Chain C, Mutant Human Lysozyme (A83kQ86DA92D) >gi|13399630|pdb|1I22|D Chain D, Mutant Human Lysozyme (A83kQ86DA92D)
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSKLLDDNIADDVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157831553|pdb|1JKC|A Chain A, Human Lysozyme Mutant With Trp 109 Replaced By Phe
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAFVAWRNRCQNRDVRQYVQGCGV
>gi|157831552|pdb|1JKB|A Chain A, Human Lysozyme Mutant With Glu 35 Replaced By Ala
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWASGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|591379597|ref|XP_007064345.1| PREDICTED: sperm acrosome membrane-associated protein 3-like [Chelonia mydas] >gi|465968056|gb|EMP31617.1| Sperm acrosome membrane-associated protein 3 [Chelonia mydas]
MKALTLLSLLGCLITANEAKIFSRCELAYTLHEEGLDGYEGYSLANWICMAFFESGFNSAAEDDNADGSTDYGIFQINSR
VWCNNYRSPTENLCHIPCTDLLSNDITDDIVCAKRIVRDPQGMDAWEDWTMHCKGRDLSEWVDGCDL
>gi|11513931|pdb|1GE1|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFAINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157835342|pdb|2MEG|A Chain A, Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQSNSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|1827553|pdb|208L|A Chain A, Mutant Human Lysozyme C77a >gi|1827555|pdb|207L|A Chain A, Mutant Human Lysozyme C77a >gi|157831359|pdb|1HNL|A Chain A, Crystal Structure Of A Glutathionylated Human Lysozyme: A Folding Intermediate Mimic In The Formation Of A Disulfide Bond >gi|157831912|pdb|1LZ4|A Chain A, Enthalpic Destabilization Of A Mutant Human Lysozyme Lacking A Disulfide Bridge Between Cysteine-77 And Cysteine-95
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNAAHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|530594856|ref|XP_005291002.1| PREDICTED: sperm acrosome membrane-associated protein 3-like [Chrysemys picta bellii]
MKALTLLSLLGCLITANEAKIFSRCELAYMLHEEGLDGYEGYSLANWICMAFFESGFNSAAEDDNADGSTDYGIFQINSR
VWCNNYRSPTENLCHIPCTDLLSNDITDDIVCAKRIVRDPQGMDAWEDWTMHCKGRDLSEWVDGCDL
>gi|407971282|gb|AFU52827.1| lysozyme C [Myotis siligorensis]
MKALLTLGLLLLSVTVQAKVFERCDLARTLKRLGMDGYRGVSLANWMCLARWESSYNTRATNYNPGDRSTDYGIFQINSR
YWCNDGKTPRAVNACGINCNVLLQDDITQAVTCAKRVVRDPQGIRAWVAWRNRCQNQDVSQYTRGCGV
>gi|11513927|pdb|1GDX|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions
KVFERCELARTLKRLGMDGYAGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|6729885|pdb|1B7Q|A Chain A, Verification Of Spmp Using Mutant Human Lysozymes
KVFERCELARTLKRLGMDGYRGISLALWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|11513929|pdb|1GE0|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGGNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|12084274|pdb|1GFU|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWDAWRNRCQNRDVRQYVQGCGV
>gi|12084398|pdb|1GFA|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KDFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|9955035|pdb|1GBO|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWGAWRNRCQNRDVRQYVQGCGV
>gi|9256911|pdb|1GAY|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KGFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|6729882|pdb|1B7N|A Chain A, Verification Of Spmp Using Mutant Human Lysozymes
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWLSGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|670982810|ref|XP_008682500.1| PREDICTED: lysozyme C [Ursus maritimus]
MLNTEDNPPWSAQRSGFPVNMKALLLLGLLLLSITVQGKVFERCELARTLKRLGLAGFKGVSLANWVCLAKWESSYNTRA
TNYNPGSRSTDYGIFQINSRYWCNDGKTPRAVNACRISCSALLTDDITQAVACAKRVVSDPNGIRAWVAWRAHCENRDVS
QYVRNCGV
>gi|12084399|pdb|1GFE|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KNFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|12084275|pdb|1GFV|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWNAWRNRCQNRDVRQYVQGCGV
>gi|6980888|pdb|1B7R|A Chain A, Verification Of Spmp Using Mutant Human Lysozymes
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFGINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|586798150|ref|NP_001276996.1| lysozyme C precursor [Leptonychotes weddellii] >gi|55583781|sp|Q659U0.1|LYSC_LEPWE RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Leptonychotes weddellii] >gi|52075494|emb|CAH39864.1| lysozyme [Leptonychotes weddellii]
MKAPLLLGLLLLSVTVQGKVFERCDLARTLKRLGLAGFKGVSLANWMCLAKWESDYNTKATNYNPGSRSTDYGIFQINSR
YWCNDGKTPRAVNSCHIPCSDLLKDDITQAVACAKRVVSDPNGIRAWVAWRAHCENQDVSQYVRNCGV
>gi|11514208|pdb|1GDW|A Chain A, Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions
KVFERCELARTLKRLGMDGYGGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157835056|pdb|2HEE|A Chain A, Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQGNSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|533117666|ref|XP_005374355.1| PREDICTED: lysozyme C-like [Chinchilla lanigera]
MKALLILGLLLFSVTVQGKVYERCELARILKRLGMDGYHGISLANWMCLAKWESDYNTKATNYNPGDESTDYGIFQINSR
YWCNNGKTPKAVNACGISCEALLQNDIAEAVTCAKRVVRDPQGIRAWVAWRNHCQGRDLTQYVSGCGV
>gi|586537879|ref|XP_006923788.1| PREDICTED: lysozyme C [Pteropus alecto]
MKALLILGLLLLSVTIQGKIYERCEFARTLKRHGMDGFKGVSLANWVCLAKWESSYNTRATNYNRGDKSTDYGIFQINSR
YWCNDGKTPRAVNGCHVSCNALMNDDITQAIACAKTVVSDRQGIRAWVAWRNHCQNRDLTHYTQGCGV
>gi|166200970|gb|ABY84356.1| c-type lysozyme [Solea senegalensis]
MKCLVFMLLVALSSAKVFERCEWARKLRSHGMDGVGGYNLANWVCLTKGESDYNTRATNRNTDGSIDYGIFQMNSRYWCN
NGQGPTSNACGISCSELLKDDVTAAIRCVKRVVQDPNGIRAWVAWVRHCEGRDLSSYVRGCGV
>gi|532086130|ref|XP_005328786.1| PREDICTED: lysozyme C-like [Ictidomys tridecemlineatus]
MKAFLILGLLLLSVTVQGKVYGRCELARTLKRLGMDGYHGISLANWVCLAEWESSYNTRATNYNPGDQSTDYGIFQINSH
YWCNDGKTPRAVNACGISCNVLLQDDISQAVTCAKRVVRDPQGIRAWVAWRNHCQNRDLTQYIQGCGV
>gi|40254796|ref|NP_036903.2| lysozyme C-1 precursor [Rattus norvegicus] >gi|37231667|gb|AAH58490.1| Lysozyme 2 [Rattus norvegicus]
MKALLVLGFLLLSASVQAKIYERCEFARTLKRNGMSGYYGVSLADWVCLAQHESNYNTQARNYNPGDQSTDYGIFQINSR
YWCNDGKTPRAKNACGIPCSALLQDDITQAIQCAKRVVRDPQGIRAWVAWQRHCKNRDLSGYIRNCGV
>gi|157831821|pdb|1LHI|A Chain A, Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of Proline Mutants
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTGGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157831554|pdb|1JKD|A Chain A, Human Lysozyme Mutant With Trp 109 Replaced By Ala
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAAVAWRNRCQNRDVRQYVQGCGV
>gi|407971286|gb|AFU52829.1| lysozyme C [Myotis siligorensis]
MKALLTLGLLLLSVTVQAKVYERCELARTLQTLGMDGYSGVSLADWVCLAQWESSYNTQATNYNPGDSSTDYGIFQINSH
YWCDDGKTPGAVNACGIPCDALLQDDITQAITCAKRVVGDPQGISAWVAWRNHCQNQDLTQYTQGCGV
>gi|1708893|sp|P51782.1|LYSC_TRIVU RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|1143317|gb|AAB97109.1| lysozyme [Trichosurus vulpecula]
MKVLLLLGFIFCSMAAHGKRMERCEFARRIKQLHLDGYHQISLANWVCLAQWESGFDTKATNYNPGDQSTDYGILQINSH
YWCDDGKTPHAANECKVRCSELQEDDLVKAVNCAKKIVDQQGIRAWVAWRNKCEGKDLSKYLEGCHL
>gi|8928189|sp|P81709.1|LYSC2_CANFA RecName: Full=Lysozyme C, spleen isozyme; AltName: Full=1,4-beta-N-acetylmuramidase C >gi|684995|gb|AAB31795.1| type c lysozyme, alpha-lactalbumin, LZ {EC 3.2.1.17} [dogs, spleen, Peptide, 130 aa]
KIFERCELARTLKNLGLAGYKGVSLANWVCLAKWESNYNTRATNYNPGSKSTDYGIFQINSRYWCNDGKTPRAVNACHIS
CSALLQDDITQAVACAKRVVSDPNGIRAWVAWRAHCENRDVSQYVRNCGV
>gi|6730358|pdb|1DI5|A Chain A, Role Of Amino Acid Residues At Turns In The Conformational Stability And Folding Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|634883242|ref|XP_007951584.1| PREDICTED: lysozyme C [Orycteropus afer afer]
MKAILILGFLFLSVTVQGKVFEKCELARILKQNGMDGFRRISLANWMCLVTWESEYNTQATHYNRKDRSTDYGIFQINSR
YWCNDGKTPRAVNGCGISCRVLLQDDINQAIKCAKRVVSDPQGITAWRAWQDHCENRDLTQYIQGCGV
>gi|209973079|gb|ACJ03829.1| stomach lysozyme [Bos grunniens]
MKALIILGLLLLSVAVQGKKFQRCELARTLKKLGLDGYRGVSLANWVCLARWESNYNTRASNYNRRDKSTDYGIFQINSR
WWCNDGKTPKAVNACRIPCSALLKDDITQAVACAKRVVRDPQGIKAWVAWRKKVSKPRSQELC
>gi|407971290|gb|AFU52831.1| lysozyme C [Nyctalus plancyi]
MKALLTLGLLLLSVAVQAKVYERCELARTLKRLGLDGYRGVSLANWMCLAKWESDYNTRATNYNPGSKSTDYGIFQINSR
YWCNDGKTPKSVDACGISCSVLLQDDITQAVTCAKRVVRDPQGIRAWVAWKTHCQNKDLTQYVQGCGV
>gi|551843677|dbj|BAO02295.1| c-type lysozyme [Epinephelus akaara]
MRLVFLLLVAASAKVYQRCEWARLLKANGMDGYHGNSLADWVCLSQWESGYSTTATNHNSRGDGSTDYGIFQINSRWWCN
DGHTSPSANACGISCSELLTDDISKAINCAKRVVRDPQGIRAWVAWRNHCEGRDLSSYIAGCGV
>gi|385536|gb|AAB26912.1| lysozyme {beta-sheet domain} [human, Peptide Mutagenesis, 130 aa]
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHCS
ASALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|617627082|ref|XP_007528461.1| PREDICTED: lysozyme C [Erinaceus europaeus]
MKVLLVLGLLLLSITAQGKVWDRCELARYLKKAGMDGYRGVSLANWVCLAKWESDYNTRALNYNPGSRSTDYGIFQINSR
YWCNDGKTPRAVNACGIPCSVLLQDDISQAVQCAKRVVRDPQGIQAWVAWKKHCKNQNLTPYIQGCGV
>gi|410965082|ref|XP_003989081.1| PREDICTED: lysozyme C isoform X1 [Felis catus] >gi|586993049|ref|XP_006933947.1| PREDICTED: lysozyme C isoform X2 [Felis catus] >gi|586993051|ref|XP_006933948.1| PREDICTED: lysozyme C isoform X3 [Felis catus]
MKALLFLGLLLLSVTVQGKIFQRCELAKTLKRLGMDGFKGVSLATWVCVAKWESDYNTRATNYNPGSRSTDYGIFQINSR
YWCNDGKTPHAENACHVSCSELLQDNISQAVKCAKRVVSDPQGIKAWVAWKKHCQNKDVSQYVRNCGV
>gi|157834714|pdb|2BQM|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAANAAHLS
CSALLQDNIADAVAAAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|407971278|gb|AFU52825.1| lysozyme C [Myotis ricketti]
MKALLTLGLLLLSVAVQAKVYERCELARTLKRLGMDGYRGVNLADWVCLTQWESSYNTRATNYNPGDSSTDYGIFQINSH
YWCDDGKTPGAVNACGINCNVLLQDDITQAVTCAKRVVRDPQGISAWVAWRNHCQNQDVSQYTRGCGV
>gi|585432|sp|P00697.2|LYSC1_RAT RecName: Full=Lysozyme C-1; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|349089|gb|AAA41551.1| lysozyme [Rattus norvegicus]
MKALLVLGFLLLSASVQAKIYERCQFARTLKRNGMSGYYGVSLADWVCLAQHESNYNTQARNYNPGDQSTDYGIFQINSR
YWCNDGKTPRAKNACGIPCSALLQDDITQAIQCAKRVVRDPQGIRAWVAWQRHCKNRDLSGYIRNCGV
>gi|33088590|gb|AAP93336.1| human lysozyme [synthetic construct]
MRKKRRQRRRMKKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDG
KTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRGVRQYVQGCGV
>gi|407971260|gb|AFU52816.1| lysozyme C [Myotis adversus]
MKALLTLGLLLLSVAIQAKVYERCELARTLKRLGMDGYRGVSLADWVCLTQWESSYNTRATNYNPGDSSTDYGIFQINSH
YWCDDGKTPGAVNACGINCNVLLQDDITQAVTCAKRVVRDPQGISAWVAWRNHCQNKDLSQYTRGCGV
>gi|407971256|gb|AFU52814.1| lysozyme C [Myotis adversus]
MKALLTLGLLLLSVAVQAKVYERCELARTLKRLGMDGYRRVSLANWMCLARWESSYNTRATNYNPGDRSTDYGIFQINSR
YWCNDGKTPRAVNACGINCNVLLQDDITQAVTCAKRVVRDPQGIRAWVAWRNHCQNQDVSQYTRGCGV
>gi|157834704|pdb|2BQC|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGVSLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNAAHLS
CSALLQDNIADAVAAAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157831825|pdb|1LHM|A Chain A, The Crystal Structure Of A Mutant Lysozyme C77(Slash)95a With Increased Secretion Efficiency In Yeast >gi|157834702|pdb|2BQA|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNAAHLS
CSALLQDNIADAVAAAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157834712|pdb|2BQK|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNAAHLS
CSALLQDNIADAVAAAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGA
>gi|407971270|gb|AFU52821.1| lysozyme C [Murina leucogaster]
MKALLTLGLLLLSVAVQAKVYERCELARTLKRHGMDGYRGVSLANWLCLARWESSYSTRATNYNPKYGSTDYGIFQINSL
YWCNDGKTPRAVNNCGISCNALLQDDITQAIACAKRVVSDPQGIRAWVAWKDHCRNRDLTRYTRGCGV
>gi|3659960|pdb|1BB4|A Chain A, Human Lysozyme Double Mutant A96l, W109h >gi|3659961|pdb|1BB4|B Chain B, Human Lysozyme Double Mutant A96l, W109h
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACLKRVVRDPQGIRAHVAWRNRCQNRDVRQYVQGCGV
>gi|584070607|ref|XP_006755628.1| PREDICTED: lysozyme C, milk isozyme-like [Myotis davidii]
MRTILIISLLSCFFAAYNAKVFSKCELARQLKAHGMDGFHGYSLANWVCMAEHESSFNTRAFNGRNSNGSSDYGIFQLNN
QWWCKDNKYPSENACNIMCSKFLDDNISDDINCIKRVVRDPNGMSAWVAWVNHCRNKNLSQYLAGCQL
>gi|157831913|pdb|1LZ5|A Chain A, Structural And Functional Analyses Of The Arg-Gly-Asp Sequence Introduced Into Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVRGDSNA
CHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157834703|pdb|2BQB|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNAAHLS
CSALLQDNIADAVAAAKRVVRDPQGVRAWVAWRNRCQNRDVRQYVQGCGV
>gi|73996855|ref|XP_851313.1| PREDICTED: lysozyme C, milk isozyme-like [Canis lupus familiaris]
MRSILVITILSYFFVADEAKIFSKCELARKLKSMGMDGFHGYSLANWVCMAEYESNFNTQAFNGRNSNGSSDYGIFQLNS
KWWCKSNSHSSANACNIMCSKFLDDNIDDDIACAKRVVKDPNGMSAWVAWVKHCKGKDLSKYLASCNL
>gi|407971272|gb|AFU52822.1| lysozyme C [Megaderma lyra]
MKSLLILGLLLLSVTVQGKVYERCEFARALKRLGMDGFRGISLANWVCLAQWESSYNTRATNYNPGSKSTDYGIFQINSR
YWCNDGKTPKAVNGCRVSCNALLQDDITQAVACAKRVVSDPQGIRAWVAWKNHCQNRDLTQYIKDCGV
>gi|395850591|ref|XP_003797865.1| PREDICTED: lysozyme C [Otolemur garnettii]
MKTLLLLGLVLLSAPTQGKVYEKCELARTLKRMGMDGYHGISLANWMCLAKWESSYNTRAINYNAGDRSTDYGIFQINSR
YWCNDGKTPRAVNACGISCNALLQDDITQAVACAKRVVRDPQGIRAWVAWRNHCQNQDLSQYTRGCGV
>gi|74192892|dbj|BAE34954.1| unnamed protein product [Mus musculus]
MLSLVSQQLTQPPVTMKTLLTLGLLLLSVTAQAKVYERCEFARTLKRNGMAGYYGVSLADWVCLAQHESNYNTRATNYNR
GDQSTDYGIFQINSRYWCNDGKTPRAVNACGINCSALLQDDITAAIQCAKRVVRDPQGIRAWVAWRAHCQNRDLSQYIRN
CGV
>gi|407971262|gb|AFU52817.1| lysozyme C [Myotis adversus]
MKALLTLGFLLLSVAVQAKVYERCELARTLKTLGMDGYSGVSLADWVCLAQWESSYNTQAINSNPGDSTDYGIFQINSRY
WCDDGKTPGAVNACGINCNVLLQDDITQAVTCAKRVVGDPQGISAWVAWRNHCQNQDLTQYTQGCGV
>gi|157834706|pdb|2BQE|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQVNSRYWCNDGKTPGAVNAAHLS
CSALLQDNIADAVAAAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157834705|pdb|2BQD|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGVFQINSRYWCNDGKTPGAVNAAHLS
CSALLQDNIADAVAAAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|149066890|gb|EDM16623.1| rCG48637 [Rattus norvegicus]
MKALLVLGFLLLSASVQAKTYERCEFARTLKRNGMSGYYGVSLADWVCLAQHESNYNTQARNYNPGDQSTDYGIFQINSR
YWCNDGKTPRAKNACGIPCSALLQDDITQAIQCAKRVVRDPQGIRAWVAWQRHCQNRDLSGYIRNCGV
>gi|74140002|dbj|BAE31835.1| unnamed protein product [Mus musculus] >gi|74181507|dbj|BAE30022.1| unnamed protein product [Mus musculus]
MSQQLTQPPVTMKTLLTLGLLLLSVTAQAKVYERCEFARTLKRNGMAGYYGVSLADWVCLAQHESNYNTRATNYNRGDQS
TDYGIFQINSRYWCNDGKTPRAVNACGINCSALLQDDITAAIQCAKRVVRDPQGIRAWVAWRAHCQNRDLSQYIRNCGV
>gi|488587846|ref|XP_004479241.1| PREDICTED: lysozyme C [Dasypus novemcinctus]
MKALFILGLLLLSVTVQGKKYERCELARTLKSYGLDGFKGISLANWMCLARWESDYDTQAINFNPGDKSTDYGIFQINSR
YWCNDGKTPGAVNGCGISCNVLLQDDITQAVKCAERVVSDPQGIRAWVAWRIHCKNQDVTQYIQGCGV
>gi|8393739|ref|NP_059068.1| lysozyme C-2 precursor [Mus musculus] >gi|126598|sp|P08905.2|LYZ2_MOUSE RecName: Full=Lysozyme C-2; AltName: Full=1,4-beta-N-acetylmuramidase C; AltName: Full=Lysozyme C type M; Flags: Precursor [Mus musculus] >gi|387410|gb|AAA39473.1| lysozyme M [Mus musculus] >gi|12805219|gb|AAH02069.1| Lysozyme 2 [Mus musculus] >gi|32484357|gb|AAH54463.1| Lysozyme 2 [Mus musculus] >gi|74138214|dbj|BAE28595.1| unnamed protein product [Mus musculus] >gi|74151974|dbj|BAE32025.1| unnamed protein product [Mus musculus] >gi|74198153|dbj|BAE35253.1| unnamed protein product [Mus musculus] >gi|148689888|gb|EDL21835.1| mCG3049 [Mus musculus]
MKTLLTLGLLLLSVTAQAKVYERCEFARTLKRNGMAGYYGVSLADWVCLAQHESNYNTRATNYNRGDQSTDYGIFQINSR
YWCNDGKTPRAVNACGINCSALLQDDITAAIQCAKRVVRDPQGIRAWVAWRAHCQNRDLSQYIRNCGV
>gi|625229782|ref|XP_003515940.2| PREDICTED: lysozyme C-2-like [Cricetulus griseus]
MMGVKGCLNTVARLLWAAAELIPGNMKALLTLGFLLLSVTVQAKVYDRCEFARTLKSHGMDGFLGISLANWVCLAQHESS
FNTKATNYNPGSRSTDYGIFQINSKYWCNDGKTPGAVNACGISCSVLLQDDITQAIQCAKRVVRDPQGIRAWVAWKSHCQ
NRDLTQYIRGCGV
>gi|524963262|ref|XP_005081550.1| PREDICTED: lysozyme C-2-like [Mesocricetus auratus]
MKVLLILGFLLLSVTVQAKVYSRCEFARTLKSHGMDGYRGISLANWVCLAQHESGFNTGATNYNPGSRSTDYGIFQINSK
YWCNDGKTPGAVNACGIPCSALLKNDITQAIKCAKRIATSSQGLRAWVAWKAYCQNRNLSQYVRNCGV
>gi|407971276|gb|AFU52824.1| lysozyme C [Myotis ricketti]
MKALLTLGLLLLSVAVQAKVYERCDLARTLKRLGMDGHSGVKLADWVCLAKWESSYNTRATNHNRGDKSTDYGIFQINSR
YWCNDGKTPGAVNACGINCNDLLQDDITKAVTCAKRVVKDPQGIKAWVAWRNHCQNKDLTEYTRGCGV
>gi|122692323|ref|NP_001073805.1| lysozyme C, tracheal isozyme precursor [Bos taurus] >gi|27923800|sp|Q27996.1|LYSCT_BOVIN RecName: Full=Lysozyme C, tracheal isozyme; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor >gi|841212|gb|AAA85544.1| lysozyme [Bos taurus]
MKALLILGLLLLSVAVQGKTFKRCELAKTLKNLGLAGYKGVSLANWMCLAKGESNYNTQAKNYNPGSKSTDYGIFQINSK
WWCNDGKTPKAVNGCGVSCSALLKDDITQAVACAKKIVSQQGITAWVAWKNKCRNRDLTSYVKGCGV
>gi|507636793|ref|XP_004700514.1| PREDICTED: lysozyme C-like [Echinops telfairi]
MKALLILGFLFLLVTIQGKVYERCELARRMKQLGMDGYERISLANWMCLARWESGYNTRATNYNRGDQSTDYGIFQINSR
YWCNDGKTPRAVNACGISCNVLLQDDITQAVACAKRVVRDPQGIRAWVAWRNRCQNRDLTEYVRGCGV
>gi|407971294|gb|AFU52833.1| lysozyme C [Pipistrellus abramus]
MKALLTLGLLLLSVAVQAKVYERCELARTLKNLGMDGYEGVSLANWMCLAKWESSYNTRATNYNPGSKSTDYGIFQINSR
YWCNDGKTPKSVDACHISCSVLLQDDITQAVACAKRVVRDPQGIRAWVAWRNHCQNRDLTQYVQGCGV
>gi|407971280|gb|AFU52826.1| lysozyme C [Myotis ricketti]
MKALLTLGFLLLSVAVQAKVYERCELARTLKTLGMDGYSGVSLADWVCLAQWESSYNTQAINSNPGDSTDYGIFQINSRY
WCDDGKTPGAVNACGINCNDLLKDDITKAVTCAKRVVGDPQGISAWVAWRNHCQNQDLTQYTQGCGV
>gi|558199799|ref|XP_006105225.1| PREDICTED: lysozyme C-1-like [Myotis lucifugus]
MKALLTLGLLLLSVAVRAKVYERCDLARTLKRLGMDGYRGVKLADWMCLARWESSYNTRATNYNRGDRSTDYGIFQINSR
YWCNDGRTPRAVNGCGINCDVLLQDDITKAATCAKRVVKDPQGIKAWVAWRNRCQNKDVTQYTRGCGV
>gi|472362721|ref|XP_004400944.1| PREDICTED: lysozyme C, milk isozyme-like [Odobenus rosmarus divergens]
MRSILIITLLSCFCAAYEAKVFSKCELARKLKTKGMDGYHGYSLANWVCMAQYESKFDTRAFNGRNTDGSKDYGIFQLNS
RWWCKNSNQPSANACNKTCNKFLDDNIDDDITCAKRVVRDPNGMSAWVAWVKHCKGKNLSRYLAGCRL
>gi|157831853|pdb|1LMT|A Chain A, Structure Of A Conformationally Constrained Arg-Gly-Asp Sequence Inserted Into Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVCRGDSC
NACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157834711|pdb|2BQJ|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNAAHLS
CSALLQDNIADAVAAAKRVVRDPQGIRAWVAWRNRCQNRDVRQYAQGCGV
>gi|478509461|ref|XP_004429008.1| PREDICTED: lysozyme C, milk isozyme-like [Ceratotherium simum simum]
MRSTLIISLLSCFFAAYEAKVFSKCELARKLKAQGMDGYRGYSLENWVCMAKYESNFNTKAFNGKNANGSSDYGLFQLNN
KWWCKDNNYSSSNACNIMCSELMDDNIDDDITCAKRVVRDPNGMSAWVAWVNHCKDKDLSKYLASCNL
>gi|157834709|pdb|2BQH|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNAAHLS
CSALLQDNIADAVAAAKRVVRDPQGIRAWAAWRNRCQNRDVRQYVQGCGV
>gi|157834713|pdb|2BQL|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KAFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNAAHLS
CSALLQDNIADAVAAAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157834710|pdb|2BQI|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNAAHLS
CSALLQDNIADAVAAAKRVVRDPQGIRAWVAWRNRCQNRDARQYVQGCGV
>gi|15825835|pdb|1QSW|A Chain A, Crystal Structure Analysis Of A Human Lysozyme Mutant W64c C65a >gi|15825836|pdb|1QSW|B Chain B, Crystal Structure Analysis Of A Human Lysozyme Mutant W64c C65a >gi|15825837|pdb|1QSW|C Chain C, Crystal Structure Analysis Of A Human Lysozyme Mutant W64c C65a >gi|15825838|pdb|1QSW|D Chain D, Crystal Structure Analysis Of A Human Lysozyme Mutant W64c C65a
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYCANDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|407971258|gb|AFU52815.1| lysozyme C [Myotis adversus]
MKALLTLGLLLLSVAVQAKVYERCDLARTLKRLGMDGHSGVKLADWVCLAKWESSYNTRATNHNRGDKSTDYGIFQINSR
YWCNDGKTPGGVNACGINCNDLLQDDITKAVTCAKRVVKDPQGIKAWVAWRNHCQNKDLSQYTRGCGV
>gi|34811083|pdb|1IX0|A Chain A, I59a-3ss Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQANSRYWCNDGKTPGAVNAAHLS
CSALLQDNIADAVAAAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157831914|pdb|1LZ6|A Chain A, Structural And Functional Analyses Of The Arg-Gly-Asp Sequence Introduced Into Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVTGRGDS
PANACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|555976802|ref|XP_005900361.1| PREDICTED: lysozyme C, intestinal isozyme-like [Bos mutus]
MKAVLILGLLLLSVTVQGKKFERCELARTLRRYGLDGYKGVSLANWMCLTYGESRYNTRVTNYNPGSKSTDYGIFQINSK
WWCNDGKTPKAVNGCGVSCSAMLKDDITQAVACAKKIVSRQGITAWVAWKNKCRNRDVSSYIQGCKL
>gi|548465935|ref|XP_005680291.1| PREDICTED: lysozyme C, milk isozyme-like [Capra hircus]
MKAVLILGLLLLSVTVRGKKFQKCELARTLKRLGLDGYKGVSLAKWMCLARWESNYNTRATNYNHGDKSTDYGIFQINSC
WWCNDGKTPRAVNACCIPRSNLLKDDITQAVASAKKVVSDPQGVRAWVAWRNKCQNQDLRSHLQGCRA
>gi|558137615|ref|XP_006091637.1| PREDICTED: LOW QUALITY PROTEIN: lysozyme C, milk isozyme-like [Myotis lucifugus]
MPKVFSKCELARQLKGHGMDGFHGYSLANWVCMAEHESSFDTRAFNGRNSNGSSDYGIFQINNKWWCKDNKHPSKNACNI
MCSKLLDDNISDDINCIKRVVRDPNGMSAWVAWVNHCKNKDLSQYLAGCQL
>gi|407971296|gb|AFU52834.1| lysozyme C [Rhinolophus ferrumequinum]
MKSLLILGLVLLSVTVQGKVYERCELARTLKRLGMDGFKGISLPNWVCLAQWESSYNTRATNYNPGSQSTDYGIFQINSR
YWCNDGKTPKAVNACGISCNVLLQDDITQAVKCAKRVVSDPQGIRAWVAWKNHCQNRDLTQYTKGCGV
>gi|564359375|ref|XP_006241454.1| PREDICTED: putative lysozyme C-2 isoform X1 [Rattus norvegicus] >gi|585435|sp|Q05820.1|LYSC2_RAT RecName: Full=Putative lysozyme C-2; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Rattus norvegicus] >gi|294585|gb|AAA41552.1| lysozyme [Rattus norvegicus] >gi|149066892|gb|EDM16625.1| rCG48647, isoform CRA_b [Rattus norvegicus]
MKALLVLGFLLLSASVQAKVFKHCELARILRSSALAGYRGVSLENWMCMAQHESNFDTEAINYNSTDQSTDYGIFQINSR
YWCNDGKTPRAVNACGIPCSALLQDDITQAIQCAKRVVRDPQGIRAWVAWQRHCQNRDLSGYIRNCGV
>gi|488597491|ref|XP_004483906.1| PREDICTED: lysozyme C, milk isozyme-like [Dasypus novemcinctus]
MKALLILGLLLLSATVRGKKFERCELARTLKRLGLGGFKGISLANWVCLIKWESNYNTRVTNYNRGDRSTDYGIFQINSR
YWCDDGKTPRAVNGCGISCNVLLQDDITQAVKCAKRVVSDPQGIKAWVAWRNRCQNKNLSQYVRGCGV
>gi|591311545|ref|XP_007082297.1| PREDICTED: lysozyme C isoform X1 [Panthera tigris altaica] >gi|591311547|ref|XP_007082298.1| PREDICTED: lysozyme C isoform X2 [Panthera tigris altaica] >gi|591311549|ref|XP_007082299.1| PREDICTED: lysozyme C isoform X3 [Panthera tigris altaica]
MKALLFLGLLLLSVTVQGKIFQRCELARTLKKLGMDGFKGVSLATWMCVAKWESDYNTRATNYNPGSRSTDYGIFQINSR
YWCNDGKTPRAENACHVSCSELLQDNISQAVKCAKRVVSDPQGIKAWVAWKTHCRNKDVSQYVRNCGV
>gi|388816923|gb|AFK78901.1| c-type lysozyme [Epinephelus coioides] >gi|388816925|gb|AFK78902.1| c-type lysozyme [Epinephelus coioides]
MRTLVVLLLVALASAKVYERCEWARLLKANGMDGFRGNSLADWVCLSQWESGYSTTATNHNRDGSTDYGIFQINSRWWCE
DGHTSPSVNACHISCSELLTDDVSKAINCAKRVVKDPNGIRAWVAWRLHCEGRDLSSYVAGCGV
>gi|440902309|gb|ELR53115.1| Lysozyme C, intestinal isozyme [Bos mutus]
MLNTKSSSPWSAWRSGFSVNMKAVLILGLLLLSVTVQGKKFERCELARTLRRYGLDGYKGVSLANWMCLTYGESRYNTRV
TNYNPGSKSTDYGIFQINSKWWCNDGKTPKAVNGCGVSCSAMLKDDITQAVACAKKIVSRQGITAWVAWKNKCRNRDVSS
YIQGCKL
>gi|163319|gb|AAA30630.1| lysozyme 2c precursor, partial [Bos taurus]
VKGKVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKATNYNPSSESTDYGIFQINSKWWCNDGKTPNAVDGC
HVSCSELMENDIAKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|429525222|gb|AFZ99003.1| calcium-binding lysosyme [Arctocephalus tropicalis]
MRSVLIITLLSCYCAAYEAKVFSKCELARKLKTKGMDGYHGYSLANWVCMAQYESKFNTQAFNGRNTDGSKDYGIFQLNS
RWWCKNSNQPSANACSKTCNKFLDDNIDDDITCAKRVVRDPNGMSAWVAWVKHCKGRNLSRYLAGCNL
>gi|56119082|ref|NP_001007806.1| lysozyme C, intestinal isozyme precursor [Bos taurus] >gi|75055544|sp|Q6B410.1|LYSI_BOVIN RecName: Full=Lysozyme C, intestinal isozyme; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Bos taurus] >gi|51012439|gb|AAT92539.1| intestinal lysozyme [Bos taurus] >gi|74268307|gb|AAI02282.1| Intestinal lysozyme [Bos taurus] >gi|296487684|tpg|DAA29797.1| TPA: lysozyme C, intestinal isozyme precursor [Bos taurus]
MKAVLILGLLLLSVTVQGKKFEKCELARTLRRYGLDGYKGVSLANWMCLTYGESRYNTRVTNYNPGSKSTDYGIFQINSK
WWCNDGKTPKAVNGCGVSCSAMLKDDITQAVACAKTIVSRQGITAWVAWKNKCRNRDVSSYIRGCKL
>gi|640816057|ref|XP_008064819.1| PREDICTED: lysozyme C [Tarsius syrichta]
MKALLILGLVLLSVTVQGKKWERCALARELKAKGMDNYAGVSLADWMCLSKWESDYNTRATNYNPGDKSTDYGIFQINSH
YWCEDGKTPKSVNACGIPCSALLQDDITQAVTCAKRVVRDPQGIKAWVGWKRHCQNKDLRSYIRGCGV
>gi|157834715|pdb|2BQN|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNAAHLS
CSALLQDNIADAAAAAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|165974|gb|AAA31562.1| lysozyme 4a precursor, partial [Ovis aries] >gi|165976|gb|AAA31563.1| lysozyme 4b precursor, partial [Ovis aries]
KVFERCELARTLKKLGLDDYKGVSLANWLCLTKWESGYNTKATNYNPGSESTDYGIFQINSKWWCNDGKTPNAVDGCHVS
CSALMENDIEKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|297466241|ref|XP_001252825.3| PREDICTED: lysozyme C, tracheal isozyme isoform X1 [Bos taurus] >gi|297474657|ref|XP_002687434.1| PREDICTED: lysozyme C, tracheal isozyme [Bos taurus] >gi|296487701|tpg|DAA29814.1| TPA: lysozyme 14D [Bos taurus]
MKALLILGLLLLSVAVQGKTFERCELARTLKNLGLAGYKGVSLANWMCLAKGESGYNTQAKNYSPGFKSTDYGIFQINSK
WWCNDGKTPKAVNGCGVSCSALLKDDITQAVACAKKIVSQLGLTAWVAWKNKCQNRDLTSYVQGCRV
>gi|642112580|emb|CDQ70012.1| unnamed protein product [Oncorhynchus mykiss]
MRAVVVLLLVAVASAKVYDRCELARALKASGMDGYAGNSLPNWVCLSKWESSYNTQATNRNTDGSTDYGIFQINSRYWCD
DGRTPGAKNVCGIRCSQLLTADLTVAIRCAKRVVLDPNGIGAW
>gi|21465677|pdb|1IVM|A Chain A, Solution Structure Of Mouse Lysozyme M
XVYERCEFARTLKRNGMAGYYGVSLADWVCLAQHESNYNTRATNYNRGDQSTDYGIFQINSRYWCNDGKTPRAVNACGIN
CSALLQDDITAAIQCAKRVVRDPQGIRAWVAWRAHCQNRDLSQYIRNCGV
>gi|642112579|emb|CDQ70011.1| unnamed protein product [Oncorhynchus mykiss]
MRAVVVLLLVAVASAKVYDRCELARALKASGMDGYAGNSLPNWVCLSKWESSYNTQATNRNTDGSTDYGIFQINSRYWCD
DGRTPGAKNVCGIHCSQLLTDDLTVAIRCAKRVVLDPNGIGAW
>gi|328677263|gb|AEB31354.1| lysozyme C, partial [Epinephelus bruneus]
MRGLVFLLLVALASAKVYERCEWARLLKANGMDGYHGNSLADWVCLSQWESGYSTTVTNHNRDGSTDYGIFQINSRWWCE
DGHTSRSANACSISCSELLTDDVSKAINCAKRVVRDPNGIRAWVAWRLHCEGRDLSSYVAGCGV
>gi|165970|gb|AAA31560.1| lysozyme 2a precursor, partial [Ovis aries]
KVFERCELARTLKELGLDGYKGVSLANWLCLTKWESSYNTKATNYNPGSESTDYGIFQINSKWWCNDGKTPNAVDGCHVS
CSALMENDIEKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|296487697|tpg|DAA29810.1| TPA: lysozyme C, tracheal isozyme precursor [Bos taurus]
MKALLILGLLLLSVAVQGKTFKRCELAKTLKNLGLAGYKGVSLANWMCLAEGESSYNTQAKNYNPGSKSTDYGIFQINSK
WWCNDGKTPKAVNGCGVSCSALLKDDITQAVACAKKIVSQQGITAWVAWTNKCRNRDLTSYVKGCGV
>gi|426224729|ref|XP_004006521.1| PREDICTED: lysozyme C, tracheal isozyme-like [Ovis aries]
MKALLILGLLVLSVAVQGKKFERCELARTLKKFGLAGYKGVSLANWMCLAYGESRYNTQAINYNPGSKSTDYGIFQINSK
WWCNDGKTPKAVNGCGVSCSALLKDDITQAVACAKKIVSQQGITAWVAWKNNCQNRDVTSYVKGCGV
>gi|165972|gb|AAA31561.1| lysozyme 3a precursor, partial [Ovis aries]
KVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESGYNTKATNYNPGSESTDYGIFQINSKWWCNDGKTPNAVDGCHVS
CSALMENDIEKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|189096084|pdb|2Z2F|A Chain A, X-Ray Crystal Structure Of Bovine Stomach Lysozyme
KVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKATNYNPSSESTDYGIFQINSKWWCNDGKTPNAVDGCHVS
CSELMENDIAKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|225794849|gb|ACO34809.1| C-type lysozyme [Perca flavescens]
MRCLVFLLFVALANAKVYERCEWARVLKNYGMDGYRGISLADWVCLSHRESNYNTAAINPYNTDGSIDYGIFQINSRWWC
NNGVTPTSNGCNIRCSELLTDNVRVAINCAKRVVRDPQGIGAWVAWRNHCKNRNLSSYVAGCGL
>gi|76692356|ref|XP_874528.1| PREDICTED: lysozyme C, tracheal isozyme [Bos taurus]
MKALLILGLLLLSVAVQGKTFKRCELARTLKNLGLAGYKGVSLADWMCLAKGESSYNTQAKNFNRGSQSTDYGIFQINSK
WWCNDGKTPNAVNGCGVSCSALLKDDITQAVACAKKIVSQQGITAWVAWKNKCRNRDLTSYVKGCGV
>gi|548465839|ref|XP_005680246.1| PREDICTED: lysozyme C, tracheal isozyme-like isoform X1 [Capra hircus]
MKALLILGLLVLSVAVQGKKFERCELARTLKKFGLAGYKGVSLANWMCLAYGESHYNTQAINYNPRSKSTDYGIFQINSK
WWCNDGKTPKAVNGCGVSCSALLKDDITQAVACAKKIVSQQGITAWVAWKNNCQNRDLTSYVKGCGV
>gi|594081404|ref|XP_006064326.1| PREDICTED: lysozyme C, intestinal isozyme-like [Bubalus bubalis]
MLNTKSSSPWSAWRSGFSVNMKAVLILGLLLLSVTVQGKKFEKCELARTLRRFGLDGYKGVSLANWMCLTYGESRYNTRV
TNYNPGSKSTDYGIFQINSKWWCNDGKTPKAVNGCGVSCSAMLKDDITQAVACAKTIVSRQGITAWVAWKNKCRNRDVSS
YIRGCKL
>gi|584026546|ref|XP_006807844.1| PREDICTED: lysozyme C-like [Neolamprologus brichardi] >gi|584026548|ref|XP_006807845.1| PREDICTED: lysozyme C-like [Neolamprologus brichardi]
MRSVFVFLLLITVASAQVFEKCAWARMLKANGMDGYGGVSLANWVCLTKHESNYNTKATNRNRNGSTDFGIFQINSRWWC
NDRSIQSANGCNIDCDVLLTDVTSAINCAKRIVRQQGITAWYAWRKHCQGQDLTSYLSGCRL
>gi|585437|sp|P37712.1|LYSC_CAMDR RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase [Camelus dromedarius]
KVWERCALARKLKELGMDGYRGVSLANWMCLTKWESDYNTDATNYNPSSESTDYGIFQINSRYWCNNGKTPHAVNGCGIN
CNVLLEDDITKAVQCAKRVVRDPQGVRAWVAWKNHCEGHDVEQYVEGCDL
>gi|556722670|ref|XP_005957165.1| PREDICTED: lysozyme C, tracheal isozyme-like [Pantholops hodgsonii]
MKALLILGLLVLSVAVQGKKFERCELARTLKKFGLAGYKGVSLANWMCLAYGESRYNTQAINYNPGSKSTDYGIFQINSK
WWCNDGKTPKAVNGCGVSCSALLKDDITQAVACAKKIVSQQGITAWVAWKNNCQNRDLTSYVKGCGV
>gi|484214|gb|AAA74656.1| lysozyme, partial [Sus scrofa]
KKSGMDGYRGVSLANWVCLAKWESDFNTKAINRNVGSTDYGIFQINSRYWCNDGKTPKAVNACHISCKVLLDDDLSQDIE
CAKRVVRDPQGIKAWVAWRTHCQNKDVSQYIRGCKL
>gi|471409833|ref|XP_004386489.1| PREDICTED: lysozyme C [Trichechus manatus latirostris]
MKALLILGLLFLSASVQGKIFERCEFARTLKRNGMGGYHGIRLADWVCLARWESSYNTKATNYNPGSKSTDYGIFQINSR
YWCNDGKTPGAVNACGISCNVLLQDDITQAIACAKRVVRDPQGIRAWVAWKKHCENQDLTQYIQGCGV
>gi|348580743|ref|XP_003476138.1| PREDICTED: lysozyme C-like [Cavia porcellus]
MKALLLLGLLVLSVTVQGKVYERCELARTLKRLGMDGYHGVSLANWMCLIKWESDYNTKATNYNPGDESTDYGIFQINSR
YWCNNGKTPDAVDACHISCSVLLEDNIAQAVACAKRVVRDPQGIRAWMGWRNHCENRDVSQYVSGCGV
>gi|297474659|ref|XP_002687436.1| PREDICTED: lysozyme C, tracheal isozyme isoform 1 [Bos taurus] >gi|296487702|tpg|DAA29815.1| TPA: lysozyme C, tracheal isozyme-like [Bos taurus]
MKALLILGLLLLSVAVQGKTFKRCELARTLKNLGLAGYKGVSLADWMCLAKGESSYNTQAKNFNRGSQSTDYGIFQINSK
WWCNDGKTPNAVNGCGVSCSALLKDDITQAVACAKKIVSQQGLTAWVAWKNNCRNRDLTSYVQGCGV
>gi|426224731|ref|XP_004006522.1| PREDICTED: lysozyme C, intestinal isozyme-like [Ovis aries]
MKALLILGLLLLSVTVQGKKFERCELARTLRRFGLDGYNGVSLANWMCLIYGESRYNTQVTNYNPGSKSTDYGIFQINSK
WWCNDGKTPRAVNGCGVSCSALLKDDITQAVACAKKIVSRQGITAWVAWKNNCRNRNVSSYIQGCKL
>gi|353251981|pdb|3ZVQ|A Chain A, Crystal Structure Of Proteolyzed Lysozyme
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTP
>gi|162586|gb|AAA30345.1| lysozyme 2 precursor, partial [Axis axis]
KVFERCELARTLKELGLDGYKGVSLANWLCLTKWESSYNTKATNYNPGSESTDYGIFQINSKWWCNDGKTPNAVDGCHVA
CSELMENDIAKAVACAKQIVREQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|585431|sp|P37713.1|LYSC1_CAPHI RecName: Full=Lysozyme C-1; AltName: Full=1,4-beta-N-acetylmuramidase C-1 [Capra hircus]
KVFERCELARTLKKLGLDDYKGVSLANWLCLTKWESGYNTKATNYNPGSESTDYGIFQINSKFWCNDGKTPDAVDGCHVS
CSELMENDIEKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|165964|gb|AAA31557.1| lysozyme 1a precursor, partial [Ovis aries] >gi|165966|gb|AAA31558.1| lysozyme 1b precursor, partial [Ovis aries] >gi|165968|gb|AAA31559.1| lysozyme 1c precursor, partial [Ovis aries]
KVFERCELARTLKELGLDGYKGVSLANWLCLTKWESSYNTKATNYNPGSESTDYGIFQINSKWWCNDGKTPNAVDGCHVS
CSELMENNIAKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCSL
>gi|111572535|gb|ABH10624.1| lysozyme [Felis catus]
RCELARTLKRLGMDGFKGVSLATWMCVAKWESDYNTRATNYNPGSRSTDYGIFQINSRYWCNDGKTPHAENACHVSCSEL
LQDNISQAVKCAKRVVSDPQGIKAWVAWKKHCQNKDVSQYVRNCGV
>gi|126606|sp|P12066.1|LYSC_AXIAX RecName: Full=Lysozyme C-1/C-2; AltName: Full=1,4-beta-N-acetylmuramidase C >gi|108439|pir||S07290 lysozyme (EC 3.2.1.17) - red deer >gi|162584|gb|AAA30344.1| lysozyme 1 precursor, partial [Axis axis]
KVFERCELARTLKELGLDGYKGVSLANWLCLTKWESSYNTKATNYNPGSESTDYGIFQINSKWWCDDGKTPNAVDGCHVA
CSELMENNIDKAVTCAKQIVREQGITAWVAWKSHCRGHDVSSYVEGCTL
>gi|9257149|pdb|1QQY|A Chain A, X-Ray Crystal Structure Analysis Of Canine Milk Lysozyme (Apo-Type)
MKIFSKCELARKLKSMGMDGFHGYSLANWVCMAEYESNFNTQAFNGRNSNGSSDYGIFQLNSKWWCKSNSHSSANACNIM
CSKFLDDNIDDDIACAKRVVKDPNGMSAWVAWVKHCKGKDLSKYLASCNL
>gi|13787134|pdb|1EL1|A Chain A, X-Ray Crystal Structure Analysis Of Canine Milk Lysozyme (Holo-Type) >gi|13787135|pdb|1EL1|B Chain B, X-Ray Crystal Structure Analysis Of Canine Milk Lysozyme (Holo-Type) >gi|20150098|pdb|1I56|A Chain A, Solution Structure Of Ca2+-Bound State Of Canine Milk Lysozyme
SKIFSKCELARKLKSMGMDGFHGYSLANWVCMAEYESNFNTQAFNGRNSNGSSDYGIFQLNSKWWCKSNSHSSANACNIM
CSKFLDDNIDDDIACAKRVVKDPNGMSAWVAWVKHCKGKDLSKYLASCNL
>gi|8928188|sp|P81708.1|LYSC1_CANFA RecName: Full=Lysozyme C, milk isozyme; AltName: Full=1,4-beta-N-acetylmuramidase C >gi|110591076|pdb|2CWI|A Chain A, X-Ray Crystal Structure Analysis Of Recombinant Wild-Type Canine Milk Lysozyme (Apo-Type) >gi|110591077|pdb|2CWI|B Chain B, X-Ray Crystal Structure Analysis Of Recombinant Wild-Type Canine Milk Lysozyme (Apo-Type) >gi|684994|gb|AAB31794.1| type c lysozyme, alpha-lactalbumin, LZ {EC 3.2.1.17} [dogs, milk, Peptide, 129 aa]
KIFSKCELARKLKSMGMDGFHGYSLANWVCMAEYESNFNTQAFNGRNSNGSSDYGIFQLNSKWWCKSNSHSSANACNIMC
SKFLDDNIDDDIACAKRVVKDPNGMSAWVAWVKHCKGKDLSKYLASCNL
>gi|585434|sp|P37714.1|LYSC2_CAPHI RecName: Full=Lysozyme C-2; AltName: Full=1,4-beta-N-acetylmuramidase C-2 [Capra hircus]
KVFERCELARTLKELGLDGYKGVSLANWLCLTKWESSYNTKATNYNPGSESTDYGIFQINSKFWCNDGKTPNAVDGCHVS
CSELMENNIAKAVACAKQIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|511919478|ref|XP_004778978.1| PREDICTED: lysozyme C, milk isozyme-like [Mustela putorius furo] >gi|511975930|ref|XP_004805908.1| PREDICTED: lysozyme C, milk isozyme-like [Mustela putorius furo]
MKSILIITLLSCFCAVYEAKIFSKCKLAHKLKTKGMDGYHGYSLADWVCMAQYESNFNTRAFNGKNANGSSDYGLFQLNS
KWWCKNSHHSSANACNIMCSKFLDDNINDDIVCAKRVVRDPKGMSAWMAWVKHCKGKDLSKYLASCKL
>gi|157834716|pdb|2BQO|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNAAHLS
CSALLQDNIADAVAAAKRAVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|157834708|pdb|2BQG|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNAAHLS
CSALLQDNIADAVAAAKRVARDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|556745452|ref|XP_005968208.1| PREDICTED: lysozyme C-2-like [Pantholops hodgsonii]
MLNSKSSSRWSAWRSGFSVNVRTVLILGLLLLSVTVQGKKFQRCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKA
TNYNPSSENTDYGIFQINSKWWCNDGKTPKAVEGCHVSHSELMENDIAKAVACAKKIVSEQGITVWVAGKSHCRGHDVSS
YVEGCTL
>gi|194211935|ref|XP_001491556.2| PREDICTED: lysozyme C, milk isozyme-like [Equus caballus] >gi|664759438|ref|XP_008537283.1| PREDICTED: lysozyme C, milk isozyme [Equus przewalskii]
MRSTLIISLLSCFFAVYEAKVFSKCELAHKLKAQEMDGFGGYSLANWVCMAEYESNFNTRAFNGKNANGSSDYGLFQLNN
KWWCKDNKRSSSNACNIMCSKLLDENIDDDISCAKRVVRDPKGMSAWKAWVKHCKDKDLSEYLASCNL
>gi|157834707|pdb|2BQF|A Chain A, Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNAAHLS
CSALLQDNVADAVAAAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>gi|344239914|gb|EGV96017.1| Lysozyme C-2 [Cricetulus griseus]
MKALLTLGFLLLSVTVQAKVYERCEFARTLKSHGMDSYRGISLANWVCLAQHESNYNTQATNYNRKDQSTDYGIFQINSR
YWCNDGKTPRAVNACGIPCSVLLQDDITQAMECAKRVVRDPQGIRAWYVGTWEGETVGCVDMCNLLQDDITQAMECAKRV
VRDPQGIRAWYVGTWEGETVGCVDMCRWHGEAIVKTEMSPSIFRAVESNRCALLLQLILSLYRYRSRNGKSHMFLDSPLD
KHDLNRNGQNVDCFLRGFMLTNVFIVLSKAIIFWLPRQQMLVTVV
>gi|161172303|pdb|2Z2E|A Chain A, Crystal Structure Of Canine Milk Lysozyme Stabilized Against Non-Enzymatic Deamidation >gi|161172304|pdb|2Z2E|B Chain B, Crystal Structure Of Canine Milk Lysozyme Stabilized Against Non-Enzymatic Deamidation
KIFSKCELARKLKSMGMDGFHGYSLANWVCMAEYESNFNTQAFQGRQSQGSSDYGIFQLNSKWWCKSQSHSSANACNIMC
SKFLDDNIDDDIACAKRVVKDPQGMSAWVAWVKHCKGKDLSKYLASCNL
>gi|9971739|gb|AAG10396.1|AF179305_1 lysozyme [Salmo salar] >gi|10047367|gb|AAG12207.1| lysozyme [Salmo salar]
GWLAGISLPNWVCLSKWELSYNTQATNRNTDGSTDYGIFQINSRYWCDDGRTPGAKNVCGIRCSQLLTDDITVAVSCAKR
VVLDPNGIGAWVAWRLHCQNQDLRSYVA
>gi|426226733|ref|XP_004007493.1| PREDICTED: lysozyme C-2-like [Ovis aries]
MLNSKSSSRWSAWRSGFSVNVRAVLILGLLLLSVTVQGKKFQRCELARTLKKLGLDGYKGVSLANWLCLTKWESGYNTKA
TNYNPSSENTDYGIFQINSKWWCNDGKTPKAVDGCHVSRSELMENDIAKAVTCAKKIVSEQGITVWVAGKSHCRDHDISS
YVEGCTL
>gi|591291297|ref|XP_007073017.1| PREDICTED: LOW QUALITY PROTEIN: lysozyme C, milk isozyme-like [Panthera tigris altaica]
MRSILIICLLGCFFAAYEAKIFXKCGLARKLKAEGMDGFHGYSLANWVCMAEHESNFNTQAFNGKNDNGSSDYGIFQINS
KWWCKNNSSPSANACNTMCSRFLDDNISDDITCAKRVVKDPNGMSAWVAWVRHCRYLASCNL
>gi|528904501|ref|XP_001790119.2| PREDICTED: lysozyme C-2 [Bos taurus] >gi|528949278|ref|XP_002687437.2| PREDICTED: lysozyme C-2 [Bos taurus]
MKALLILGLLLLSVPVQGKVFERCELAKTLKRLGMDGFRGVSLANWLCLTKWESSYNTKATNYNPSNESTDYGIYQINSK
WWCKTPKAVDGCPVSHSSLMGNDIAKAVACAKKIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|296487703|tpg|DAA29816.1| TPA: lysozyme-like [Bos taurus]
MKALLILGLLLLSVPVQGKVFERCELAKTLKRLGMDGFRGVSLANWLCLTKWESSYNTKATNYNPSNESTDYGIYQINSK
WWCKTPKAVDGCPVSHSKLMGNDIAKAVACAKKIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|548465937|ref|XP_005680292.1| PREDICTED: lysozyme C-2-like [Capra hircus]
MLHSKSSSHWSAWRSGFSVNVRAVLILGLLLLSVTVQGKKFQRCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKA
TNYNPSSENTDYGIFQINSKWWCNDGKTPKAVDGCHVSRSELMENDIATAVACAKKIASEQGITVWVAGKSHCRDHDISS
YVEGCTL
>gi|126614|sp|P11376.1|LYSC1_HORSE RecName: Full=Lysozyme C, milk isozyme; AltName: Full=1,4-beta-N-acetylmuramidase C >gi|157834937|pdb|2EQL|A Chain A, Crystallographic Studies Of A Calcium Binding Lysozyme From Equine Milk At 2.5 Angstroms Resolution
KVFSKCELAHKLKAQEMDGFGGYSLANWVCMAEYESNFNTRAFNGKNANGSSDYGLFQLNNKWWCKDNKRSSSNACNIMC
SKLLDENIDDDISCAKRVVRDPKGMSAWKAWVKHCKDKDLSEYLASCNL
>gi|625290465|ref|XP_007636993.1| PREDICTED: lysozyme C-2-like [Cricetulus griseus]
MKALLTLGFLLLSVTVQAKVYDRCEFARTLKSHGMDGFLGISLANWVCLAQHESSFNTKATNYNPGSRSTDYGIFQINSK
YWCNDGKTPGAVNACGISCSVLLQDDITQAIKCAKRVVRDPQGIRAWYVGTWEGETVGCVDMCSESS
>gi|301783675|ref|XP_002927250.1| PREDICTED: lysozyme C, milk isozyme-like [Ailuropoda melanoleuca]
MRSILIVTLLSCFWAVNEAKVFSKCELARKLKTMGMDGYHGQSLASWVCMAQYESNFNTQAFNGKNDNGSSDYGIFQLNN
KWWCKNGYRSSANGCGTTCSKFLDDDIDDDIICAKRVVRDPKGMSAWNAWVDHCQGRDLSKYLASCKL
>gi|671023826|ref|XP_008702739.1| PREDICTED: lysozyme C, milk isozyme-like [Ursus maritimus]
MRSILIITLLSCFWAVYEAKVFSKCELARKLKTMGMDGYHGQSLASWVCMAEHESRFNTRAFNGKNDNGSSDYGIFQLNN
KWWCKNGYRSSANGCGTTCSKFLDDDIDDDIICAKRVVRDPQGMSAWRAWVNNCQGRDLSKYLAGCKL
>gi|507649010|ref|XP_004632265.1| PREDICTED: lysozyme C-like [Octodon degus]
MDLERSQNGMLMSTALGVCLARWESSYNTGATNYNPGDRSTDYGIFQINSRYWCNDGKTPRAVNACGIPCSALLQDDITQ
AVNCAKRVVRDPQGIRAWVAWRNRCQNKDLTEYVRGCGV
>gi|126613|sp|P11375.1|LYSC_EQUAS RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C
KVFSKCELAHKLKAQEMDGFGGYSLANWVCMAEYESNFNTRAFNGKNANGSYDYGLFQLNSKWWCKDNKRSSSNACNIMC
SKLLDDNIDDDISCAKRVVRDPKGMSAWKAWVKHCKDKDLSEYLASCNL
>gi|524963338|ref|XP_005081588.1| PREDICTED: lysozyme C-1-like [Mesocricetus auratus]
MKALLTLGFLLLFVTVQAKVFDRCEFARTLKRHGMDGYRGVSLANWVCLAQHESGFNTKATNYNPGPRSTDYGIFQINSK
YWCNDGKTPRSVNACGIPCSGSAGPFTASLLLGNFSRVVAWKNRCQNRDLSQYIRNCGV
>gi|507533022|ref|XP_004650578.1| PREDICTED: lysozyme C [Jaculus jaculus]
MKALLPLGLLLLSVTVQGKVFERCELARTLKRAGMDGYRGISLANWVCLARWESNYNTRATNFNRGDQSTDYGIFQINSR
YWCNDGKTPRAVNGCGISCDDNIPINSVGRVAWRNRCQGRDLTEYVRGCGV
>gi|47197416|emb|CAF89297.1| unnamed protein product [Tetraodon nigroviridis]
VCLSKWESEYNTNAINHNTDGSTDYGIFQINSRWWCNNDVTPTSNGCNIKCRALLTDDISVAIACAKRVVRDPQGIRAWV
AWRNRCQGRDLSGYVAGCGL
>gi|440902313|gb|ELR53119.1| hypothetical protein M91_04733 [Bos mutus]
MVNSKSSSPWSVWRSGFSVSVKAVLILGLLLLSVTVQGKVIERCELARTLKKLGLDGYKGVRLCLTKWESGYNTKATNYN
PSNESTDYGIFQINSKWWCKTPKAADGCPVSHSKLMENDIAKAVACAKKIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
>gi|554523557|ref|XP_005856673.1| PREDICTED: lysozyme C [Myotis brandtii] >gi|521019879|gb|EPQ01667.1| Lysozyme C [Myotis brandtii]
MKALLTLGLLLLSVAVQAKVYERCELARTLKRRYSGSLANWMCLAKWESSYNTRATKYNPGDKSTDYAIFQINSHYWCNE
GKTPGGVNGCGIPCNVLLQDDITQAVTCAKRVVRDPQGIRAWYV
>gi|163321|gb|AAA30631.1| lysozyme 2d, partial [Bos taurus]
ASWLCLTKWESSYNTKATNYNPSSESTDYGIFQINSKWWCNDGKTPNAVDGCHVSCSELMENDIAKAVACAKHIVSEQGI
TAWVAWKSHCRDHDVSSYVEGCTL
>gi|353251982|pdb|3ZVQ|B Chain B, Crystal Structure Of Proteolyzed Lysozyme
SRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|323650262|gb|ADX97217.1| lysozyme c [Perca flavescens]
DWVLVLSKWESSYSTTAINHNTDGSTDYGIFQINSRWWCNDGLTPTKNACNINCRELLTDNVGVAINCAKRVVRDPAGIS
AWVGWRNHCQNRDLSSYLAGC
>gi|556745448|ref|XP_005968206.1| PREDICTED: lysozyme C-1-like, partial [Pantholops hodgsonii]
MKALVILGLLFLSVAVQGKVFERCELARTLKELGLDGYKGVSLANWLCLTKWESSYNTKATNYNPGSESTDYGIFQINSK
WWCNDGKTPDA
>gi|524963336|ref|XP_005081587.1| PREDICTED: lysozyme C-2-like [Mesocricetus auratus]
MKALLTLGLLLLSVTVQAMVYERCEFARTLKSHGMDGYLGIRLANWVCLAQHESGFNTQATNYNPGSRSNDYGIFQINSK
YWCNDGKTPRAVNACGIPCSEHLLMVLSSECSHENCSLAWKTHCQNRDLSQYVRNCGV
>gi|444514655|gb|ELV10638.1| 60S ribosomal protein L31 [Tupaia chinensis]
MKAFLFLVLLLLSVTVQGKTFERCELAQILKRNGLDGYRGISLANWMCLAKWESDYDTRATNYNPGDQSTDYGIFQINSR
YWCNDGKTPGAVNACGISCNVLCVPSLQLRPGRMTPAKKGGEKKKGRSAIEVVTREHTINIHKRIHGVGFKKRAPRALKE
IQKFAMKEMGTPDVRIDTRLNKAVWAKGIRNVPYRIHVWLSRKRNEEEDSPNKLYTLVTYVPVTTFKNLQTVNVDEN
>gi|281339058|gb|EFB14642.1| hypothetical protein PANDA_011184 [Ailuropoda melanoleuca]
MKALLLLGLLLLSITVQGKVFERCELARTLKRLGLAGFKGVSLANWVCLAKWESSYNTRATNYNPGSRSTDYGIFQINSR
YWCNDGKTPRAVNACRIPCS
>gi|327239790|gb|AEA39739.1| lysozyme C, partial [Epinephelus coioides]
RDGSTDYGIFQINSRWWCEDGHTSPSVNACHISCSELLTDDVSKAINCAKRVVGDPNGIRAWVAWRLHCEGRDLSSYVAG
CGV
>gi|524963334|ref|XP_005081586.1| PREDICTED: lysozyme C-like [Mesocricetus auratus]
MKALLALGFLLLSVTVQAMVYERCKFARTLKSHGMDGYLGISLANWVCLAEHESGFNTRATNYNPGPRSTDYGIFQINSK
YWCNDGKTPGAVNACGISCSGKTREV
>gi|4204093|gb|AAD10202.1| egg white lysozyme [Gallus gallus]
MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGN
>gi|281343728|gb|EFB19312.1| hypothetical protein PANDA_017018 [Ailuropoda melanoleuca]
KVFSKCELARKLKTMGMDGYHGQSLASWVCMAQYESNFNTQAFNGKNDNGSSDYGIFQLNNKWWCKNGYRSSANGCGTTC
S
>gi|625230600|ref|XP_007606447.1| PREDICTED: lysozyme C-2-like, partial [Cricetulus griseus] >gi|625230618|ref|XP_007606457.1| PREDICTED: lysozyme C-2-like, partial [Cricetulus griseus]
CLAQHESSFNTKATNYNPGSRSTDYGIFQINSKYWCNDGKTPGAVNACGISCSGKTRRV
>gi|18044585|gb|AAH19611.1| Lyz2 protein [Mus musculus]
GINCSALLQDDITAAIQCAKRVVRDPQGIRAWVAWRAHCQNRDLSQYIRNCGV
>gi|21628827|gb|AAM68947.1|AF294864_1 lysozyme [Trachypithecus pileatus] >gi|21628829|gb|AAM68948.1|AF294865_1 lysozyme [Trachypithecus geei] >gi|21628831|gb|AAM68949.1|AF294866_1 lysozyme [Trachypithecus phayrei] >gi|21628833|gb|AAM68950.1|AF294867_1 lysozyme [Trachypithecus phayrei] >gi|21628835|gb|AAM68951.1|AF294868_1 lysozyme [Trachypithecus cristatus] >gi|21628837|gb|AAM68952.1|AF294869_1 lysozyme [Trachypithecus francoisi] >gi|429845300|gb|AGA17173.1| lysozyme c precursor, partial [Trachypithecus phayrei crepuscula] >gi|429845302|gb|AGA17174.1| lysozyme c precursor, partial [Trachypithecus phayrei crepuscula] >gi|429845304|gb|AGA17175.1| lysozyme c precursor, partial [Trachypithecus phayrei crepuscula] >gi|429845306|gb|AGA17176.1| lysozyme c precursor, partial [Trachypithecus phayrei crepuscula] >gi|429845308|gb|AGA17177.1| lysozyme c precursor, partial [Trachypithecus phayrei shanicus] >gi|429845310|gb|AGA17178.1| lysozyme c precursor, partial [Trachypithecus phayrei shanicus] >gi|429845312|gb|AGA17179.1| lysozyme c precursor, partial [Trachypithecus phayrei shanicus] >gi|429845314|gb|AGA17180.1| lysozyme c precursor, partial [Trachypithecus phayrei shanicus] >gi|429845316|gb|AGA17181.1| lysozyme c precursor, partial [Trachypithecus germaini]
MRALIILGLVLLSVTVQGKIFERCELARTLKKLGLDGYKGVSLAN
>gi|21628823|gb|AAM68945.1|AF294862_1 lysozyme [Semnopithecus entellus] >gi|21628825|gb|AAM68946.1|AF294863_1 lysozyme [Trachypithecus johnii]
MKALTILGLVLLSVTVQGKIFERCELARTLKKLGLDGYKGVSLAN
