问一个数组的问题
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.