源代码如下:
import java.util.*;
import java.io.*;
public class Test {
public static void main(String[] args) throws IOException{
//Map <String,String> map=new TreeMap();
FileInputStream fr=new FileInputStream(new File( "E:\\JAVA\\project\\workspace\\File\\temp\\endnote "));
List <String> list=new ArrayList <String> ();
Iterator <String> it=list.iterator();
fr.skip(5);
int len=fr.read();
while(len!=-1){
int i=0;
if(len==37){
byte[] buff=new byte[10000];
fr.skip(2);
while((len=fr.read())!=10){
buff[i]=(byte)len;
i++;
}
String a=new String(buff);//buff-wrong,被后面的覆盖
System.out.println(a+ ' ');
list.add(a);
}else {
len=fr.read();
continue;
}
len=fr.read();
}
while(it.hasNext()){
System.out.println(it.next()+ ' ');
}
}
}
endote的内容如下:
%A Fukui, Kenji
%A Kosaka, Hiromichi
%A Kuramitsu, Seiki
%A Masui, Ryoji
%T Nuclease activity of the MutS homologue MutS2 from Thermus thermophilus is confined to the Smr domain
%0 Journal Article
%D 2007
%J Nucl. Acids Res.
%R 10.1093/nar/gkl735
%P gkl735
%V
%N
%U http://nar.oxfordjournals.org/cgi/content/abstract/gkl735v1
%8 January 10, 2007
%X MutS homologues are highly conserved enzymes engaged in DNA mismatch repair (MMR), meiotic recombination and other DNA modifications. Genome sequencing projects have revealed that bacteria and plants possess a MutS homologue, MutS2. MutS2 lacks the mismatch-recognition domain of MutS, but contains an extra C-terminal region called the small MutS-related (Smr) domain. Sequences homologous to the Smr domain are annotated as proteins of unknown function ' in various organisms ranging from bacteria to human. Although recent in vivo studies indicate that MutS2 plays an important role in recombinational events, there had been only limited characterization of the biochemical function of MutS2 and the Smr domain. We previously established that Thermus thermophilus MutS2 (ttMutS2) possesses endonuclease activity. In this study, we report that a Smr-deleted ttMutS2 mutant retains the dimerization, ATPase and DNA-binding activities, but has no endonuclease activity. Furthermore, the Smr domain alone was stable and functional in binding and incising DNA. It is noteworthy that an endonuclease activity is associated with a MutS homologue, which is generally thought to recognize specific DNA structures.