GenomeNet

Database: PDB
Entry: 3NAZ
LinkDB: 3NAZ
Original site: 3NAZ 
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION (2.5MCL): 10.0 MG/ML    
REMARK 280  TVNIR, 0.05M TRIS-HCL, PH7.2. RESERVOIR SOLUTION (2.5MCL): 1.26M    
REMARK 280  TRI-SODIUM CITRATE DIHYDRATE, 0.09M HEPES/NAOH, 10% V/V GLYCEROL,   
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 278.0K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3                           
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       97.49000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       97.49000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       97.49000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       97.49000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       97.49000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       97.49000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       97.49000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       97.49000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       97.49000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       97.49000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       97.49000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       97.49000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       97.49000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       97.49000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       97.49000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       97.49000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       97.49000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       97.49000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 99840 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 95710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1467.0 KCAL/MOL                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  0.000000  1.000000      -97.49000            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000       97.49000            
REMARK 350   BIOMT3   2  0.000000 -1.000000  0.000000      194.98000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000       97.49000            
REMARK 350   BIOMT2   3  0.000000  0.000000 -1.000000      194.98000            
REMARK 350   BIOMT3   3  1.000000  0.000000  0.000000       97.49000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B1307  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1031  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1208  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1269  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B1221  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B1061  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B1317  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1266  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B1316  LIES ON A SPECIAL POSITION.                          
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 456    CE   NZ                                             
REMARK 470     LYS B 456    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B  83   CD    GLU B  83   OE1     0.068                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  91       48.96    -84.41                                   
REMARK 500    SER A  95     -155.33   -114.53                                   
REMARK 500    GLU A 112      133.14   -178.78                                   
REMARK 500    ARG A 117     -169.77   -128.33                                   
REMARK 500    THR A 178       55.49   -119.97                                   
REMARK 500    MET A 199       -5.57     71.12                                   
REMARK 500    ASN A 222      -41.30   -136.01                                   
REMARK 500    LEU A 225       64.70     33.54                                   
REMARK 500    VAL A 250      -62.78    -95.45                                   
REMARK 500    PHE A 281      -59.05   -130.06                                   
REMARK 500    CYS A 305       56.85   -155.71                                   
REMARK 500    ASP A 343       63.86     60.45                                   
REMARK 500    HIS A 361       71.95     11.39                                   
REMARK 500    MET A 384       69.28   -150.86                                   
REMARK 500    MET A 406       55.32   -152.64                                   
REMARK 500    CYS A 411      -46.48   -138.84                                   
REMARK 500    HIS A 415       72.01   -105.40                                   
REMARK 500    ASN A 492       73.54   -164.46                                   
REMARK 500    ALA B  91       49.53    -81.94                                   
REMARK 500    SER B  95     -154.58   -114.45                                   
REMARK 500    GLU B 112      133.75   -178.46                                   
REMARK 500    ARG B 117     -167.16   -129.87                                   
REMARK 500    ASP B 163       83.96   -150.31                                   
REMARK 500    GLN B 175       58.46    -98.89                                   
REMARK 500    MET B 199       -3.20     73.70                                   
REMARK 500    ASN B 222      -42.28   -134.25                                   
REMARK 500    LEU B 225       70.02     32.44                                   
REMARK 500    VAL B 250      -63.01    -99.81                                   
REMARK 500    PHE B 281      -58.65   -124.71                                   
REMARK 500    CYS B 299      -34.45   -130.90                                   
REMARK 500    CYS B 305       52.10   -151.34                                   
REMARK 500    HIS B 361       69.10     14.73                                   
REMARK 500    MET B 384       69.67   -152.83                                   
REMARK 500    MET B 406       55.28   -152.54                                   
REMARK 500    CYS B 411      -47.09   -136.69                                   
REMARK 500    HIS B 415       71.20   -109.83                                   
REMARK 500    ASN B 492       77.03   -164.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR B  68        23.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     HEC A  605                                                       
REMARK 610     NO2 A  609                                                       
REMARK 610     HEC B  605                                                       
REMARK 610     NO2 B  609                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC B 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NO2 B 609   N                                                      
REMARK 620 2 HEC B 601   NA   89.2                                              
REMARK 620 3 HEC B 601   NB   88.3  89.4                                        
REMARK 620 4 HEC B 601   NC   91.6 179.2  90.8                                  
REMARK 620 5 HEC B 601   ND   90.6  90.7 178.9  89.1                            
REMARK 620 6 LYS B 188   NZ  173.7  91.7  97.9  87.5  83.2                      
REMARK 620 7 HOH B1205   O     5.6  83.6  87.7  97.2  91.3 172.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC A 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NO2 A 609   N                                                      
REMARK 620 2 HEC A 601   NA   95.8                                              
REMARK 620 3 HEC A 601   NB   87.8  89.0                                        
REMARK 620 4 HEC A 601   NC   84.6 179.6  91.0                                  
REMARK 620 5 HEC A 601   ND   90.9  91.1 178.7  88.8                            
REMARK 620 6 LYS A 188   NZ  173.2  90.1  95.7  89.4  85.6                      
REMARK 620 7 HOH A1175   O    14.1  81.7  87.7  98.7  91.0 171.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC B 608  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  18   NE2                                                    
REMARK 620 2 HEC B 608   NA   92.0                                              
REMARK 620 3 HEC B 608   NB   90.6  90.9                                        
REMARK 620 4 HEC B 608   NC   87.4 179.3  88.7                                  
REMARK 620 5 HEC B 608   ND   88.5  89.2 179.1  91.2                            
REMARK 620 6 HIS B  44   NE2 178.0  89.8  90.2  90.8  90.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC A 608  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  18   NE2                                                    
REMARK 620 2 HEC A 608   NA   93.2                                              
REMARK 620 3 HEC A 608   NB   88.6  90.4                                        
REMARK 620 4 HEC A 608   NC   86.3 179.3  89.2                                  
REMARK 620 5 HEC A 608   ND   90.3  89.9 179.0  90.5                            
REMARK 620 6 HIS A  44   NE2 174.6  92.1  90.5  88.4  90.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC B 606  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 234   NE2                                                    
REMARK 620 2 HEC B 606   NA   86.1                                              
REMARK 620 3 HEC B 606   NB   91.0  90.9                                        
REMARK 620 4 HEC B 606   NC   93.8 179.7  89.4                                  
REMARK 620 5 HEC B 606   ND   89.3  89.7 179.4  90.0                            
REMARK 620 6 HIS B  39   NE2 175.7  90.7  91.9  89.4  87.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC A 606  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  39   NE2                                                    
REMARK 620 2 HEC A 606   NA   91.8                                              
REMARK 620 3 HEC A 606   NB   88.4  90.7                                        
REMARK 620 4 HEC A 606   NC   88.2 179.6  89.7                                  
REMARK 620 5 HEC A 606   ND   90.7  89.3 179.1  90.3                            
REMARK 620 6 HIS A 234   NE2 177.7  87.9  89.3  92.1  91.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC B 605  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 415   NE2                                                    
REMARK 620 2 HEC B 605   NA   94.4                                              
REMARK 620 3 HEC B 605   NB   87.6  88.5                                        
REMARK 620 4 HEC B 605   NC   85.9 179.5  91.2                                  
REMARK 620 5 HEC B 605   ND   91.5  91.3 179.1  89.1                            
REMARK 620 6 HIS B 372   NE2 175.6  86.8  96.7  92.9  84.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC B 604  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 491   NE2                                                    
REMARK 620 2 HEC B 604   NA   91.8                                              
REMARK 620 3 HEC B 604   NB   86.7  90.8                                        
REMARK 620 4 HEC B 604   NC   89.9 178.4  89.5                                  
REMARK 620 5 HEC B 604   ND   92.5  89.5 179.2  90.2                            
REMARK 620 6 HIS B 383   NE2 178.7  87.6  92.2  90.8  88.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC A 605  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 415   NE2                                                    
REMARK 620 2 HEC A 605   NA   92.9                                              
REMARK 620 3 HEC A 605   NB   86.6  88.4                                        
REMARK 620 4 HEC A 605   NC   87.9 179.2  91.6                                  
REMARK 620 5 HEC A 605   ND   92.8  91.4 179.3  88.7                            
REMARK 620 6 HIS A 372   NE2 178.9  87.0  94.5  92.2  86.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC A 604  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 491   NE2                                                    
REMARK 620 2 HEC A 604   NA   90.1                                              
REMARK 620 3 HEC A 604   NB   85.6  89.6                                        
REMARK 620 4 HEC A 604   NC   91.5 178.3  90.2                                  
REMARK 620 5 HEC A 604   ND   94.0  90.8 179.5  89.4                            
REMARK 620 6 HIS A 383   NE2 174.4  87.9  89.1  90.5  91.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC A 603  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 119   NE2                                                    
REMARK 620 2 HEC A 603   NA   88.8                                              
REMARK 620 3 HEC A 603   NB   94.5  90.5                                        
REMARK 620 4 HEC A 603   NC   90.0 178.8  89.6                                  
REMARK 620 5 HEC A 603   ND   85.4  89.9 179.5  90.0                            
REMARK 620 6 HIS A 300   NE2 178.8  92.4  85.0  88.9  95.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC B 603  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 300   NE2                                                    
REMARK 620 2 HEC B 603   NA   92.4                                              
REMARK 620 3 HEC B 603   NB   85.4  90.1                                        
REMARK 620 4 HEC B 603   NC   88.7 178.8  90.5                                  
REMARK 620 5 HEC B 603   ND   94.5  90.6 179.3  88.8                            
REMARK 620 6 HIS B 119   NE2 179.4  88.2  94.9  90.8  85.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC B 602  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 398   NE2                                                    
REMARK 620 2 HEC B 602   NA   88.9                                              
REMARK 620 3 HEC B 602   NB   87.0  90.7                                        
REMARK 620 4 HEC B 602   NC   92.9 178.1  89.1                                  
REMARK 620 5 HEC B 602   ND   91.6  89.4 178.6  90.9                            
REMARK 620 6 HIS B 231   NE2 179.0  91.3  94.0  86.9  87.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC A 602  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 231   NE2                                                    
REMARK 620 2 HEC A 602   NA   88.8                                              
REMARK 620 3 HEC A 602   NB   94.3  90.9                                        
REMARK 620 4 HEC A 602   NC   89.4 178.2  89.2                                  
REMARK 620 5 HEC A 602   ND   87.0  88.7 178.6  91.3                            
REMARK 620 6 HIS A 398   NE2 176.5  89.9  89.0  91.8  89.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC A 607  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  70   NE2                                                    
REMARK 620 2 HEC A 607   NA   91.3                                              
REMARK 620 3 HEC A 607   NB   89.6  91.8                                        
REMARK 620 4 HEC A 607   NC   87.6 178.9  88.5                                  
REMARK 620 5 HEC A 607   ND   90.5  88.7 179.5  91.0                            
REMARK 620 6 HIS A  30   NE2 177.2  90.7  88.5  90.3  91.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC B 607  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  70   NE2                                                    
REMARK 620 2 HEC B 607   NA   91.4                                              
REMARK 620 3 HEC B 607   NB   88.7  92.4                                        
REMARK 620 4 HEC B 607   NC   88.0 179.2  87.1                                  
REMARK 620 5 HEC B 607   ND   91.5  88.4 179.2  92.1                            
REMARK 620 6 HIS B  30   NE2 175.5  90.3  87.1  90.3  92.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 610  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 302   OE2                                                    
REMARK 620 2 GLN A 360   OE1 129.3                                              
REMARK 620 3 LYS A 358   O    94.0  84.0                                        
REMARK 620 4 TYR A 303   O    88.9  98.2 174.2                                  
REMARK 620 5 GLU A 302   OE1  54.8  74.7  93.7  92.1                            
REMARK 620 6 HOH A 962   O    77.5 151.9  86.1  89.5 132.2                      
REMARK 620 7 HOH A 866   O   151.9  78.8  89.1  86.0 152.9  74.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 611  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO A 116   O                                                      
REMARK 620 2 GOL A 613   O3  110.1                                              
REMARK 620 3 HEC A 603   O2A  79.6 162.7                                        
REMARK 620 4 HOH A1029   O   108.2  79.9  83.5                                  
REMARK 620 5 HOH A 908   O   149.1  91.7  85.5  96.7                            
REMARK 620 6 HOH A 925   O    69.7  85.9 111.2 163.9  91.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 610  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN B 360   OE1                                                    
REMARK 620 2 LYS B 358   O    85.8                                              
REMARK 620 3 TYR B 303   O    95.5 178.0                                        
REMARK 620 4 GLU B 302   OE2 126.7  93.5  87.0                                  
REMARK 620 5 GLU B 302   OE1  74.5  91.8  90.0  52.3                            
REMARK 620 6 HOH B 990   O   149.3  89.8  88.4  83.8 136.1                      
REMARK 620 7 HOH B 893   O    80.1  91.2  87.5 153.1 154.1  69.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 611  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO B 116   O                                                      
REMARK 620 2 GOL B 613   O1  111.6                                              
REMARK 620 3 HEC B 603   O1A  82.1 159.0                                        
REMARK 620 4 HEC B 604   O1A 130.6  74.9  84.2                                  
REMARK 620 5 HOH B1059   O   104.0  79.6  81.7  26.9                            
REMARK 620 6 HOH B 936   O   147.8  91.7  82.9  75.6 101.8                      
REMARK 620 7 HOH B 953   O    70.2  85.0 115.2 155.2 160.2  90.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO2 A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 610                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 611                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO2 A 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO2 A 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO2 B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 610                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 611                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO2 B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO2 B 617                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4L38   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4L3X   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4L3Z   RELATED DB: NDB                                   
DBREF  4L3Y A    5   523  UNP    L0DSL2   L0DSL2_THIND    33    551             
DBREF  4L3Y B    5   523  UNP    L0DSL2   L0DSL2_THIND    33    551             
SEQADV 4L3Y VAL A  524  UNP  L0DSL2              EXPRESSION TAG                 
SEQADV 4L3Y VAL B  524  UNP  L0DSL2              EXPRESSION TAG                 
SEQRES   1 A  520  ASN LEU LYS PRO VAL ASP ALA MET GLN CYS PHE ASP CYS          
SEQRES   2 A  520  HIS THR GLN ILE GLU ASP MET HIS THR VAL GLY LYS HIS          
SEQRES   3 A  520  ALA THR VAL ASN CYS VAL HIS CYS HIS ASP ALA THR GLU          
SEQRES   4 A  520  HIS VAL GLU THR ALA SER SER ARG ARG MET GLY GLU ARG          
SEQRES   5 A  520  PRO VAL THR ARG MET ASP LEU GLU ALA CYS ALA THR CYS          
SEQRES   6 A  520  HIS THR ALA GLN PHE ASN SER PHE VAL GLU VAL ARG HIS          
SEQRES   7 A  520  GLU SER HIS PRO ARG LEU GLU LYS ALA THR PRO THR SER          
SEQRES   8 A  520  ARG SER PRO MET PHE ASP LYS LEU ILE ALA GLY HIS GLY          
SEQRES   9 A  520  PHE ALA PHE GLU HIS ALA GLU PRO ARG SER HIS ALA PHE          
SEQRES  10 A  520  MET LEU VAL ASP HIS PHE VAL VAL ASP ARG ALA TYR GLY          
SEQRES  11 A  520  GLY ARG PHE GLN PHE LYS ASN TRP GLN LYS VAL THR ASP          
SEQRES  12 A  520  GLY MET GLY ALA VAL ARG GLY ALA TRP THR VAL LEU THR          
SEQRES  13 A  520  ASP ALA ASP PRO GLU SER SER ASP GLN ARG ARG PHE LEU          
SEQRES  14 A  520  SER GLN THR ALA THR ALA ALA ASN PRO VAL CYS LEU ASN          
SEQRES  15 A  520  CYS LYS THR GLN ASP HIS ILE LEU ASP TRP ALA TYR MET          
SEQRES  16 A  520  GLY ASP GLU HIS GLU ALA ALA LYS TRP SER ARG THR SER          
SEQRES  17 A  520  GLU VAL VAL GLU PHE ALA ARG ASP LEU ASN HIS PRO LEU          
SEQRES  18 A  520  ASN CYS PHE MET CYS HIS ASP PRO HIS SER ALA GLY PRO          
SEQRES  19 A  520  ARG VAL VAL ARG ASP GLY LEU ILE ASN ALA VAL VAL ASP          
SEQRES  20 A  520  ARG GLY LEU GLY THR TYR PRO HIS ASP PRO VAL LYS SER          
SEQRES  21 A  520  GLU GLN GLN GLY MET THR LYS VAL THR PHE GLN ARG GLY          
SEQRES  22 A  520  ARG GLU ASP PHE ARG ALA ILE GLY LEU LEU ASP THR ALA          
SEQRES  23 A  520  ASP SER ASN VAL MET CYS ALA GLN CYS HIS VAL GLU TYR          
SEQRES  24 A  520  ASN CYS ASN PRO GLY TYR GLN LEU SER ASP GLY SER ARG          
SEQRES  25 A  520  VAL GLY MET ASP ASP ARG ARG ALA ASN HIS PHE PHE TRP          
SEQRES  26 A  520  ALA ASN VAL PHE ASP TYR LYS GLU ALA ALA GLN GLU ILE          
SEQRES  27 A  520  ASP PHE PHE ASP PHE ARG HIS ALA THR THR GLY ALA ALA          
SEQRES  28 A  520  LEU PRO LYS LEU GLN HIS PRO GLU ALA GLU THR PHE TRP          
SEQRES  29 A  520  GLY SER VAL HIS GLU ARG ASN GLY VAL ALA CYS ALA ASP          
SEQRES  30 A  520  CYS HIS MET PRO LYS VAL GLN LEU GLU ASN GLY LYS VAL          
SEQRES  31 A  520  TYR THR SER HIS SER GLN ARG THR PRO ARG ASP MET MET          
SEQRES  32 A  520  GLY GLN ALA CYS LEU ASN CYS HIS ALA GLU TRP THR GLU          
SEQRES  33 A  520  ASP GLN ALA LEU TYR ALA ILE ASP TYR ILE LYS ASN TYR          
SEQRES  34 A  520  THR HIS GLY LYS ILE VAL LYS SER GLU TYR TRP LEU ALA          
SEQRES  35 A  520  LYS MET ILE ASP LEU PHE PRO VAL ALA LYS ARG ALA GLY          
SEQRES  36 A  520  VAL SER GLU ASP VAL LEU ASN GLN ALA ARG GLU LEU HIS          
SEQRES  37 A  520  TYR ASP ALA HIS LEU TYR TRP GLU TRP TRP THR ALA GLU          
SEQRES  38 A  520  ASN SER VAL GLY PHE HIS ASN PRO ASP GLN ALA ARG GLU          
SEQRES  39 A  520  SER LEU MET THR SER ILE SER LYS SER LYS GLU ALA VAL          
SEQRES  40 A  520  SER LEU LEU ASN ASP ALA ILE ASP ALA GLN VAL ALA VAL          
SEQRES   1 B  520  ASN LEU LYS PRO VAL ASP ALA MET GLN CYS PHE ASP CYS          
SEQRES   2 B  520  HIS THR GLN ILE GLU ASP MET HIS THR VAL GLY LYS HIS          
SEQRES   3 B  520  ALA THR VAL ASN CYS VAL HIS CYS HIS ASP ALA THR GLU          
SEQRES   4 B  520  HIS VAL GLU THR ALA SER SER ARG ARG MET GLY GLU ARG          
SEQRES   5 B  520  PRO VAL THR ARG MET ASP LEU GLU ALA CYS ALA THR CYS          
SEQRES   6 B  520  HIS THR ALA GLN PHE ASN SER PHE VAL GLU VAL ARG HIS          
SEQRES   7 B  520  GLU SER HIS PRO ARG LEU GLU LYS ALA THR PRO THR SER          
SEQRES   8 B  520  ARG SER PRO MET PHE ASP LYS LEU ILE ALA GLY HIS GLY          
SEQRES   9 B  520  PHE ALA PHE GLU HIS ALA GLU PRO ARG SER HIS ALA PHE          
SEQRES  10 B  520  MET LEU VAL ASP HIS PHE VAL VAL ASP ARG ALA TYR GLY          
SEQRES  11 B  520  GLY ARG PHE GLN PHE LYS ASN TRP GLN LYS VAL THR ASP          
SEQRES  12 B  520  GLY MET GLY ALA VAL ARG GLY ALA TRP THR VAL LEU THR          
SEQRES  13 B  520  ASP ALA ASP PRO GLU SER SER ASP GLN ARG ARG PHE LEU          
SEQRES  14 B  520  SER GLN THR ALA THR ALA ALA ASN PRO VAL CYS LEU ASN          
SEQRES  15 B  520  CYS LYS THR GLN ASP HIS ILE LEU ASP TRP ALA TYR MET          
SEQRES  16 B  520  GLY ASP GLU HIS GLU ALA ALA LYS TRP SER ARG THR SER          
SEQRES  17 B  520  GLU VAL VAL GLU PHE ALA ARG ASP LEU ASN HIS PRO LEU          
SEQRES  18 B  520  ASN CYS PHE MET CYS HIS ASP PRO HIS SER ALA GLY PRO          
SEQRES  19 B  520  ARG VAL VAL ARG ASP GLY LEU ILE ASN ALA VAL VAL ASP          
SEQRES  20 B  520  ARG GLY LEU GLY THR TYR PRO HIS ASP PRO VAL LYS SER          
SEQRES  21 B  520  GLU GLN GLN GLY MET THR LYS VAL THR PHE GLN ARG GLY          
SEQRES  22 B  520  ARG GLU ASP PHE ARG ALA ILE GLY LEU LEU ASP THR ALA          
SEQRES  23 B  520  ASP SER ASN VAL MET CYS ALA GLN CYS HIS VAL GLU TYR          
SEQRES  24 B  520  ASN CYS ASN PRO GLY TYR GLN LEU SER ASP GLY SER ARG          
SEQRES  25 B  520  VAL GLY MET ASP ASP ARG ARG ALA ASN HIS PHE PHE TRP          
SEQRES  26 B  520  ALA ASN VAL PHE ASP TYR LYS GLU ALA ALA GLN GLU ILE          
SEQRES  27 B  520  ASP PHE PHE ASP PHE ARG HIS ALA THR THR GLY ALA ALA          
SEQRES  28 B  520  LEU PRO LYS LEU GLN HIS PRO GLU ALA GLU THR PHE TRP          
SEQRES  29 B  520  GLY SER VAL HIS GLU ARG ASN GLY VAL ALA CYS ALA ASP          
SEQRES  30 B  520  CYS HIS MET PRO LYS VAL GLN LEU GLU ASN GLY LYS VAL          
SEQRES  31 B  520  TYR THR SER HIS SER GLN ARG THR PRO ARG ASP MET MET          
SEQRES  32 B  520  GLY GLN ALA CYS LEU ASN CYS HIS ALA GLU TRP THR GLU          
SEQRES  33 B  520  ASP GLN ALA LEU TYR ALA ILE ASP TYR ILE LYS ASN TYR          
SEQRES  34 B  520  THR HIS GLY LYS ILE VAL LYS SER GLU TYR TRP LEU ALA          
SEQRES  35 B  520  LYS MET ILE ASP LEU PHE PRO VAL ALA LYS ARG ALA GLY          
SEQRES  36 B  520  VAL SER GLU ASP VAL LEU ASN GLN ALA ARG GLU LEU HIS          
SEQRES  37 B  520  TYR ASP ALA HIS LEU TYR TRP GLU TRP TRP THR ALA GLU          
SEQRES  38 B  520  ASN SER VAL GLY PHE HIS ASN PRO ASP GLN ALA ARG GLU          
SEQRES  39 B  520  SER LEU MET THR SER ILE SER LYS SER LYS GLU ALA VAL          
SEQRES  40 B  520  SER LEU LEU ASN ASP ALA ILE ASP ALA GLN VAL ALA VAL          
HET    HEC  A 601      43                                                       
HET    HEC  A 602      43                                                       
HET    HEC  A 603      43                                                       
HET    HEC  A 604      43                                                       
HET    HEC  A 605      38                                                       
HET    HEC  A 606      43                                                       
HET    HEC  A 607      43                                                       
HET    HEC  A 608      43                                                       
HET    NO2  A 609       2                                                       
HET     CA  A 610       1                                                       
HET     CA  A 611       1                                                       
HET    MPD  A 612       8                                                       
HET    GOL  A 613       7                                                       
HET    GOL  A 614       6                                                       
HET    GOL  A 615       7                                                       
HET    SO4  A 616       5                                                       
HET    NO2  A 617       3                                                       
HET    NO2  A 618       3                                                       
HET    HEC  B 601      43                                                       
HET    HEC  B 602      43                                                       
HET    HEC  B 603      43                                                       
HET    HEC  B 604      47                                                       
HET    HEC  B 605      39                                                       
HET    HEC  B 606      43                                                       
HET    HEC  B 607      43                                                       
HET    HEC  B 608      43                                                       
HET    NO2  B 609       2                                                       
HET     CA  B 610       1                                                       
HET     CA  B 611       1                                                       
HET    MPD  B 612       8                                                       
HET    GOL  B 613       7                                                       
HET    GOL  B 614       6                                                       
HET    SO4  B 615       5                                                       
HET    NO2  B 616       3                                                       
HET    NO2  B 617       3                                                       
HETNAM     HEC HEME C                                                           
HETNAM     NO2 NITRITE ION                                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  HEC    16(C34 H34 FE N4 O4)                                         
FORMUL  11  NO2    6(N O2 1-)                                                   
FORMUL  12   CA    4(CA 2+)                                                     
FORMUL  14  MPD    2(C6 H14 O2)                                                 
FORMUL  15  GOL    5(C3 H8 O3)                                                  
FORMUL  18  SO4    2(O4 S 2-)                                                   
FORMUL  38  HOH   *1211(H2 O)                                                   
HELIX    1   1 ASP A   10  ASP A   16  1                                   7    
HELIX    2   2 HIS A   18  THR A   26  1                                   9    
HELIX    3   3 ASN A   34  HIS A   37  5                                   4    
HELIX    4   4 ALA A   41  ALA A   48  1                                   8    
HELIX    5   5 LEU A   63  THR A   68  1                                   6    
HELIX    6   6 HIS A   70  GLU A   79  1                                  10    
HELIX    7   7 MET A   99  ALA A  105  1                                   7    
HELIX    8   8 HIS A  107  GLU A  112  5                                   6    
HELIX    9   9 SER A  118  ALA A  120  5                                   3    
HELIX   10  10 PHE A  121  VAL A  129  1                                   9    
HELIX   11  11 ASN A  141  THR A  146  5                                   6    
HELIX   12  12 ASP A  147  GLY A  154  1                                   8    
HELIX   13  13 GLY A  154  VAL A  158  1                                   5    
HELIX   14  14 ASN A  181  LYS A  188  5                                   8    
HELIX   15  15 ALA A  197  ASP A  201  5                                   5    
HELIX   16  16 GLU A  213  ASP A  220  1                                   8    
HELIX   17  17 ASN A  226  CYS A  230  5                                   5    
HELIX   18  18 ARG A  242  VAL A  250  1                                   9    
HELIX   19  19 ASP A  260  GLN A  267  1                                   8    
HELIX   20  20 ASP A  291  ALA A  297  1                                   7    
HELIX   21  21 ASP A  321  ARG A  323  5                                   3    
HELIX   22  22 ASN A  331  ASP A  343  1                                  13    
HELIX   23  23 PRO A  362  TRP A  368  1                                   7    
HELIX   24  24 SER A  370  ASN A  375  1                                   6    
HELIX   25  25 ALA A  378  MET A  384  1                                   7    
HELIX   26  26 THR A  402  ASP A  405  5                                   4    
HELIX   27  27 MET A  406  CYS A  411  1                                   6    
HELIX   28  28 THR A  419  ALA A  458  1                                  40    
HELIX   29  29 SER A  461  GLU A  485  1                                  25    
HELIX   30  30 ASN A  492  ALA A  523  1                                  32    
HELIX   31  31 ASP B   10  HIS B   18  1                                   9    
HELIX   32  32 HIS B   18  THR B   26  1                                   9    
HELIX   33  33 ASN B   34  HIS B   37  5                                   4    
HELIX   34  34 ALA B   41  ALA B   48  1                                   8    
HELIX   35  35 LEU B   63  THR B   68  1                                   6    
HELIX   36  36 HIS B   70  GLU B   79  1                                  10    
HELIX   37  37 MET B   99  ALA B  105  1                                   7    
HELIX   38  38 HIS B  107  GLU B  112  5                                   6    
HELIX   39  39 SER B  118  ALA B  120  5                                   3    
HELIX   40  40 PHE B  121  VAL B  129  1                                   9    
HELIX   41  41 ASN B  141  THR B  146  5                                   6    
HELIX   42  42 ASP B  147  GLY B  154  1                                   8    
HELIX   43  43 GLY B  154  VAL B  158  1                                   5    
HELIX   44  44 ASN B  181  LYS B  188  5                                   8    
HELIX   45  45 ALA B  197  ASP B  201  5                                   5    
HELIX   46  46 GLU B  213  ASP B  220  1                                   8    
HELIX   47  47 ASN B  226  CYS B  230  5                                   5    
HELIX   48  48 ARG B  242  VAL B  250  1                                   9    
HELIX   49  49 ASP B  260  GLN B  267  1                                   8    
HELIX   50  50 ASP B  291  ALA B  297  1                                   7    
HELIX   51  51 ASP B  321  ASN B  325  5                                   5    
HELIX   52  52 ASN B  331  ILE B  342  1                                  12    
HELIX   53  53 PRO B  362  TRP B  368  1                                   7    
HELIX   54  54 SER B  370  ASN B  375  1                                   6    
HELIX   55  55 ALA B  378  MET B  384  1                                   7    
HELIX   56  56 THR B  402  ASP B  405  5                                   4    
HELIX   57  57 MET B  406  CYS B  411  1                                   6    
HELIX   58  58 THR B  419  ALA B  458  1                                  40    
HELIX   59  59 SER B  461  GLU B  485  1                                  25    
HELIX   60  60 ASN B  492  VAL B  524  1                                  33    
SHEET    1   A 2 HIS A  39  ASP A  40  0                                        
SHEET    2   A 2 VAL A  58  THR A  59 -1  O  VAL A  58   N  ASP A  40           
SHEET    1   B 2 PHE A 137  PHE A 139  0                                        
SHEET    2   B 2 LEU A 159  ASP A 161 -1  O  THR A 160   N  GLN A 138           
SHEET    1   C 3 ARG A 239  VAL A 240  0                                        
SHEET    2   C 3 GLU A 279  LEU A 287 -1  O  GLY A 285   N  VAL A 240           
SHEET    3   C 3 MET A 269  ARG A 276 -1  N  VAL A 272   O  ILE A 284           
SHEET    1   D 2 TYR A 303  CYS A 305  0                                        
SHEET    2   D 2 ASN A 325  PHE A 327 -1  O  HIS A 326   N  ASN A 304           
SHEET    1   E 2 GLY A 308  TYR A 309  0                                        
SHEET    2   E 2 ARG A 316  VAL A 317 -1  O  VAL A 317   N  GLY A 308           
SHEET    1   F 2 PHE A 347  ARG A 348  0                                        
SHEET    2   F 2 ALA A 355  LEU A 356 -1  O  LEU A 356   N  PHE A 347           
SHEET    1   G 2 HIS B  39  ASP B  40  0                                        
SHEET    2   G 2 VAL B  58  THR B  59 -1  O  VAL B  58   N  ASP B  40           
SHEET    1   H 2 PHE B 137  PHE B 139  0                                        
SHEET    2   H 2 LEU B 159  ASP B 161 -1  O  THR B 160   N  GLN B 138           
SHEET    1   I 3 ARG B 239  VAL B 240  0                                        
SHEET    2   I 3 GLU B 279  LEU B 287 -1  O  GLY B 285   N  VAL B 240           
SHEET    3   I 3 MET B 269  ARG B 276 -1  N  PHE B 274   O  ARG B 282           
SHEET    1   J 2 TYR B 303  ASN B 304  0                                        
SHEET    2   J 2 HIS B 326  PHE B 327 -1  O  HIS B 326   N  ASN B 304           
SHEET    1   K 2 GLY B 308  TYR B 309  0                                        
SHEET    2   K 2 ARG B 316  VAL B 317 -1  O  VAL B 317   N  GLY B 308           
SHEET    1   L 2 PHE B 347  ARG B 348  0                                        
SHEET    2   L 2 ALA B 355  LEU B 356 -1  O  LEU B 356   N  PHE B 347           
LINK        FE   HEC B 601                 N   NO2 B 609     1555   1555  1.85  
LINK        FE   HEC A 601                 N   NO2 A 609     1555   1555  1.86  
LINK         NE2 HIS B  18                FE   HEC B 608     1555   1555  1.88  
LINK         NE2 HIS A  18                FE   HEC A 608     1555   1555  1.89  
LINK         NZ  LYS B 188                FE   HEC B 601     1555   1555  1.90  
LINK         NE2 HIS B  44                FE   HEC B 608     1555   1555  1.90  
LINK         NE2 HIS B 234                FE   HEC B 606     1555   1555  1.90  
LINK         NZ  LYS A 188                FE   HEC A 601     1555   1555  1.90  
LINK         NE2 HIS B  39                FE   HEC B 606     1555   1555  1.90  
LINK         NE2 HIS A  44                FE   HEC A 608     1555   1555  1.91  
LINK         NE2 HIS A  39                FE   HEC A 606     1555   1555  1.92  
LINK         NE2 HIS A 234                FE   HEC A 606     1555   1555  1.93  
LINK         NE2 HIS B 415                FE   HEC B 605     1555   1555  1.93  
LINK         NE2 HIS B 491                FE   HEC B 604     1555   1555  1.94  
LINK         NE2 HIS A 415                FE   HEC A 605     1555   1555  1.94  
LINK         NE2 HIS A 491                FE   HEC A 604     1555   1555  1.95  
LINK         NE2 HIS A 119                FE   HEC A 603     1555   1555  1.95  
LINK         NE2 HIS B 300                FE   HEC B 603     1555   1555  1.95  
LINK         NE2 HIS A 372                FE   HEC A 605     1555   1555  1.95  
LINK         NE2 HIS B 119                FE   HEC B 603     1555   1555  1.95  
LINK         NE2 HIS B 383                FE   HEC B 604     1555   1555  1.95  
LINK         NE2 HIS A 383                FE   HEC A 604     1555   1555  1.96  
LINK         NE2 HIS B 372                FE   HEC B 605     1555   1555  1.96  
LINK         NE2 HIS B 398                FE   HEC B 602     1555   1555  1.96  
LINK         NE2 HIS A 231                FE   HEC A 602     1555   1555  1.96  
LINK         NE2 HIS A  70                FE   HEC A 607     1555   1555  1.96  
LINK         NE2 HIS A 300                FE   HEC A 603     1555   1555  1.96  
LINK         NE2 HIS B 231                FE   HEC B 602     1555   1555  1.97  
LINK         NE2 HIS A 398                FE   HEC A 602     1555   1555  1.97  
LINK         NE2 HIS B  70                FE   HEC B 607     1555   1555  1.97  
LINK         NE2 HIS A  30                FE   HEC A 607     1555   1555  1.97  
LINK         NE2 HIS B  30                FE   HEC B 607     1555   1555  1.98  
LINK         OE2 GLU A 302                CA    CA A 610     1555   1555  2.32  
LINK         OE1 GLN A 360                CA    CA A 610     1555   1555  2.32  
LINK         O   PRO A 116                CA    CA A 611     1555   1555  2.32  
LINK         OE1 GLN B 360                CA    CA B 610     1555   1555  2.33  
LINK         O   PRO B 116                CA    CA B 611     1555   1555  2.33  
LINK         O   LYS A 358                CA    CA A 610     1555   1555  2.34  
LINK         O   LYS B 358                CA    CA B 610     1555   1555  2.34  
LINK         O   TYR B 303                CA    CA B 610     1555   1555  2.35  
LINK         O   TYR A 303                CA    CA A 610     1555   1555  2.35  
LINK         OE2 GLU B 302                CA    CA B 610     1555   1555  2.35  
LINK        CA    CA B 611                 O1  GOL B 613     1555   1555  2.35  
LINK        CA    CA A 611                 O3  GOL A 613     1555   1555  2.35  
LINK         OE1 GLU A 302                CA    CA A 610     1555   1555  2.39  
LINK         O1A HEC B 603                CA    CA B 611     1555   1555  2.55  
LINK         O2A HEC A 603                CA    CA A 611     1555   1555  2.56  
LINK         OE1 GLU B 302                CA    CA B 610     1555   1555  2.56  
LINK         O1ABHEC B 604                CA    CA B 611     1555   1555  2.90  
LINK        CA    CA B 611                 O   HOH B1059     1555   1555  1.87  
LINK        CA    CA A 611                 O   HOH A1029     1555   1555  2.20  
LINK        FE   HEC B 601                 O   HOH B1205     1555   1555  2.26  
LINK        FE   HEC A 601                 O   HOH A1175     1555   1555  2.27  
LINK        CA    CA A 611                 O   HOH A 908     1555   1555  2.39  
LINK        CA    CA B 611                 O   HOH B 936     1555   1555  2.40  
LINK        CA    CA A 610                 O   HOH A 962     1555   1555  2.44  
LINK        CA    CA B 610                 O   HOH B 990     1555   1555  2.48  
LINK        CA    CA B 610                 O   HOH B 893     1555   1555  2.48  
LINK        CA    CA A 610                 O   HOH A 866     1555   1555  2.55  
LINK        CA    CA B 611                 O   HOH B 953     1555   1555  2.62  
LINK        CA    CA A 611                 O   HOH A 925     1555   1555  2.66  
LINK         SG  CYS B 411                 CAB HEC B 605     1555   1555  1.62  
LINK         SG  CYS A 411                 CAB HEC A 605     1555   1555  1.63  
LINK         SG  CYS A 184                 CAB HEC A 601     1555   1555  1.64  
LINK         SG  CYS A 227                 CAB HEC A 602     1555   1555  1.65  
LINK         SG  CYS B 379                 CAB HEC B 604     1555   1555  1.65  
LINK         SG  CYS A  66                 CAB HEC A 607     1555   1555  1.66  
LINK         SG  CYS B  14                 CAB HEC B 608     1555   1555  1.66  
LINK         SG  CYS A  14                 CAB HEC A 608     1555   1555  1.66  
LINK         SG  CYS B 227                 CAB HEC B 602     1555   1555  1.66  
LINK         SG  CYS A 379                 CAB HEC A 604     1555   1555  1.67  
LINK         SG  CYS B 184                 CAB HEC B 601     1555   1555  1.67  
LINK         SG  CYS B  17                 CAC HEC B 608     1555   1555  1.68  
LINK         SG  CYS B  66                 CAB HEC B 607     1555   1555  1.69  
LINK         SG  CYS B 296                 CAB HEC B 603     1555   1555  1.70  
LINK         SG  CYS A 296                 CAB HEC A 603     1555   1555  1.70  
LINK         SG  CYS B  35                 CAB HEC B 606     1555   1555  1.70  
LINK         SG  CYS A  35                 CAB HEC A 606     1555   1555  1.70  
LINK         SG  CYS B 414                 CAC HEC B 605     1555   1555  1.70  
LINK         SG  CYS A 414                 CAC HEC A 605     1555   1555  1.70  
LINK         SG  CYS A  17                 CAC HEC A 608     1555   1555  1.71  
LINK         SG  CYS B  38                 CAC HEC B 606     1555   1555  1.71  
LINK         SG  CYS A 299                 CAC HEC A 603     1555   1555  1.72  
LINK         SG  CYS A  38                 CAC HEC A 606     1555   1555  1.72  
LINK         SG  CYS B 299                 CAC HEC B 603     1555   1555  1.72  
LINK         SG  CYS B 187                 CAC HEC B 601     1555   1555  1.73  
LINK         SG  CYS A 382                 CAC HEC A 604     1555   1555  1.74  
LINK         SG  CYS B 382                 CAC HEC B 604     1555   1555  1.75  
LINK         SG  CYS A 187                 CAC HEC A 601     1555   1555  1.75  
LINK         SG  CYS B 230                 CAC HEC B 602     1555   1555  1.76  
LINK         SG  CYS A  69                 CAC HEC A 607     1555   1555  1.77  
LINK         SG  CYS A 230                 CAC HEC A 602     1555   1555  1.78  
LINK         SG  CYS B  69                 CAC HEC B 607     1555   1555  1.78  
LINK         CE2 TYR A 303                 SG  CYS A 305     1555   1555  1.68  
LINK         CE2 TYR B 303                 SG  CYS B 305     1555   1555  1.68  
SITE     1 AC1 24 HIS A 113  ALA A 114  ASP A 125  HIS A 126                    
SITE     2 AC1 24 VAL A 129  ARG A 131  CYS A 184  CYS A 187                    
SITE     3 AC1 24 LYS A 188  ARG A 242  CYS A 299  HIS A 300                    
SITE     4 AC1 24 TYR A 303  CYS A 305  HIS A 361  ASN A 486                    
SITE     5 AC1 24 HEC A 603  NO2 A 609  HOH A 714  HOH A 800                    
SITE     6 AC1 24 HOH A 801  HOH A 806  HOH A 918  HOH A1175                    
SITE     1 AC2 16 CYS A  66  HIS A  70  GLN A  73  LEU A 225                    
SITE     2 AC2 16 CYS A 227  CYS A 230  HIS A 231  ALA A 290                    
SITE     3 AC2 16 MET A 384  TYR A 395  THR A 396  HIS A 398                    
SITE     4 AC2 16 HEC A 607  HOH A 779  HOH A 863  HOH A 879                    
SITE     1 AC3 21 SER A  84  PRO A 116  ARG A 117  HIS A 119                    
SITE     2 AC3 21 PHE A 121  MET A 122  ASP A 125  CYS A 187                    
SITE     3 AC3 21 LYS A 188  MET A 229  CYS A 296  CYS A 299                    
SITE     4 AC3 21 HIS A 300  HIS A 383  MET A 384  HEC A 601                    
SITE     5 AC3 21 HEC A 604   CA A 611  HOH A 704  HOH A 719                    
SITE     6 AC3 21 HOH A 797                                                     
SITE     1 AC4 24 HIS A 300  PHE A 367  HIS A 372  VAL A 377                    
SITE     2 AC4 24 ALA A 378  CYS A 379  CYS A 382  HIS A 383                    
SITE     3 AC4 24 THR A 402  ARG A 404  LYS A 431  ASN A 486                    
SITE     4 AC4 24 PHE A 490  HIS A 491  HEC A 603  HEC A 605                    
SITE     5 AC4 24  CA A 611  GOL A 613  HOH A 797  HOH A 807                    
SITE     6 AC4 24 HOH A 908  HOH A 915  HOH A 987  HOH A1029                    
SITE     1 AC5 13 ASN A 141  TRP A 142  GLN A 143  HIS A 372                    
SITE     2 AC5 13 PRO A 403  ALA A 410  CYS A 411  CYS A 414                    
SITE     3 AC5 13 HIS A 415  TRP A 418  ILE A 427  HEC A 604                    
SITE     4 AC5 13 HOH A 940                                                     
SITE     1 AC6 23 CYS A  14  PHE A  15  HIS A  18  HIS A  25                    
SITE     2 AC6 23 VAL A  33  ASN A  34  CYS A  35  CYS A  38                    
SITE     3 AC6 23 HIS A  39  THR A  59  LEU A 194  PHE A 228                    
SITE     4 AC6 23 PRO A 233  HIS A 234  ARG A 239  PHE A 274                    
SITE     5 AC6 23 ARG A 276  ARG A 282  HEC A 607  HEC A 608                    
SITE     6 AC6 23 HOH A 758  HOH A1178  HOH A1215                               
SITE     1 AC7 18 LYS A  29  HIS A  30  HIS A  37  ALA A  65                    
SITE     2 AC7 18 CYS A  66  THR A  68  CYS A  69  HIS A  70                    
SITE     3 AC7 18 CYS A 227  HIS A 231  ALA A 236  HEC A 602                    
SITE     4 AC7 18 HEC A 606  HOH A1163  HOH A1167  HOH A1223                    
SITE     5 AC7 18 HOH A1282  THR B  68                                          
SITE     1 AC8 23 GLN A  13  CYS A  14  CYS A  17  HIS A  18                    
SITE     2 AC8 23 HIS A  39  HIS A  44  ALA A  48  SER A  49                    
SITE     3 AC8 23 SER A  50  ARG A  52  MET A  53  ARG A  56                    
SITE     4 AC8 23 PRO A  57  THR A  59  LEU A 194  ARG A 276                    
SITE     5 AC8 23 GLY A 277  HEC A 606  HOH A 760  HOH A 777                    
SITE     6 AC8 23 HOH A1000  HOH A1212  HOH A1217                               
SITE     1 AC9  5 TYR A 303  HIS A 361  HEC A 601  HOH A 916                    
SITE     2 AC9  5 HOH A1175                                                     
SITE     1 BC1  6 GLU A 302  TYR A 303  LYS A 358  GLN A 360                    
SITE     2 BC1  6 HOH A 866  HOH A 962                                          
SITE     1 BC2  7 PRO A 116  HEC A 603  HEC A 604  GOL A 613                    
SITE     2 BC2  7 HOH A 908  HOH A 925  HOH A1029                               
SITE     1 BC3  8 ARG A  87  VAL A 128  GLN A 138  PHE A 139                    
SITE     2 BC3  8 TRP A 142  TYR A 433  ARG A 497  HOH A1098                    
SITE     1 BC4  9 ARG A  96  GLU A 115  PRO A 116  ASN A 486                    
SITE     2 BC4  9 HEC A 604   CA A 611  HOH A 807  HOH A1029                    
SITE     3 BC4  9 HOH A1033                                                     
SITE     1 BC5  9 ASP A 101  ALA A 110  PHE A 111  GLN A 175                    
SITE     2 BC5  9 TRP A 444  ILE A 504  LYS A 508  HOH A 716                    
SITE     3 BC5  9 HOH A 935                                                     
SITE     1 BC6  4 ASP A 251  LYS A 271  ARG A 322  HOH A 842                    
SITE     1 BC7  7 THR A 351  LYS A 447  ASN A 515  HOH A 743                    
SITE     2 BC7  7 HOH A 896  HOH A1061  HOH A1165                               
SITE     1 BC8  8 SER A 212  GLU A 213  VAL A 214  NO2 A 618                    
SITE     2 BC8  8 HOH A 819  HOH A 959  HOH A1047  HOH A1106                    
SITE     1 BC9  5 VAL A 214  NO2 A 617  HOH A 903  HOH A1047                    
SITE     2 BC9  5 HOH A1106                                                     
SITE     1 CC1 24 HIS B 113  ALA B 114  ASP B 125  HIS B 126                    
SITE     2 CC1 24 VAL B 129  ARG B 131  CYS B 184  CYS B 187                    
SITE     3 CC1 24 LYS B 188  ARG B 242  CYS B 299  HIS B 300                    
SITE     4 CC1 24 TYR B 303  CYS B 305  HIS B 361  ASN B 486                    
SITE     5 CC1 24 HEC B 603  NO2 B 609  HOH B 739  HOH B 827                    
SITE     6 CC1 24 HOH B 828  HOH B 833  HOH B 946  HOH B1205                    
SITE     1 CC2 17 CYS B  66  HIS B  70  GLN B  73  LEU B 225                    
SITE     2 CC2 17 CYS B 227  CYS B 230  HIS B 231  MET B 384                    
SITE     3 CC2 17 TYR B 395  THR B 396  HIS B 398  HEC B 607                    
SITE     4 CC2 17 HOH B 805  HOH B 890  HOH B 906  HOH B1180                    
SITE     5 CC2 17 HOH B1264                                                     
SITE     1 CC3 22 SER B  84  PRO B 116  ARG B 117  HIS B 119                    
SITE     2 CC3 22 PHE B 121  MET B 122  ASP B 125  CYS B 187                    
SITE     3 CC3 22 LYS B 188  MET B 229  CYS B 296  CYS B 299                    
SITE     4 CC3 22 HIS B 300  HIS B 383  MET B 384  HEC B 601                    
SITE     5 CC3 22 HEC B 604   CA B 611  HOH B 729  HOH B 745                    
SITE     6 CC3 22 HOH B 824  HOH B1059                                          
SITE     1 CC4 23 PHE B 367  HIS B 372  VAL B 377  ALA B 378                    
SITE     2 CC4 23 CYS B 379  CYS B 382  HIS B 383  THR B 402                    
SITE     3 CC4 23 ARG B 404  LYS B 431  ASN B 486  PHE B 490                    
SITE     4 CC4 23 HIS B 491  HEC B 603  HEC B 605   CA B 611                    
SITE     5 CC4 23 GOL B 613  HOH B 824  HOH B 834  HOH B 936                    
SITE     6 CC4 23 HOH B 943  HOH B1016  HOH B1059                               
SITE     1 CC5 14 ASN B 141  TRP B 142  GLN B 143  VAL B 371                    
SITE     2 CC5 14 HIS B 372  ASN B 375  PRO B 403  ALA B 410                    
SITE     3 CC5 14 CYS B 411  CYS B 414  HIS B 415  TRP B 418                    
SITE     4 CC5 14 ILE B 427  HEC B 604                                          
SITE     1 CC6 21 CYS B  14  PHE B  15  HIS B  18  HIS B  25                    
SITE     2 CC6 21 VAL B  33  ASN B  34  CYS B  35  CYS B  38                    
SITE     3 CC6 21 HIS B  39  LEU B 194  PHE B 228  PRO B 233                    
SITE     4 CC6 21 HIS B 234  ARG B 239  PHE B 274  ARG B 276                    
SITE     5 CC6 21 ARG B 282  HEC B 607  HEC B 608  HOH B 784                    
SITE     6 CC6 21 HOH B1202                                                     
SITE     1 CC7 19 THR A  68  LYS B  29  HIS B  30  HIS B  37                    
SITE     2 CC7 19 ALA B  65  CYS B  66  THR B  68  CYS B  69                    
SITE     3 CC7 19 HIS B  70  CYS B 227  HIS B 231  ALA B 236                    
SITE     4 CC7 19 HEC B 602  HEC B 606  HOH B 708  HOH B1193                    
SITE     5 CC7 19 HOH B1197  HOH B1257  HOH B1272                               
SITE     1 CC8 25 GLN B  13  CYS B  14  CYS B  17  HIS B  18                    
SITE     2 CC8 25 HIS B  39  HIS B  44  VAL B  45  ALA B  48                    
SITE     3 CC8 25 SER B  49  ARG B  51  ARG B  52  MET B  53                    
SITE     4 CC8 25 ARG B  56  PRO B  57  THR B  59  LEU B 194                    
SITE     5 CC8 25 GLN B 275  ARG B 276  HEC B 606  HOH B 786                    
SITE     6 CC8 25 HOH B 803  HOH B1029  HOH B1202  HOH B1255                    
SITE     7 CC8 25 HOH B1283                                                     
SITE     1 CC9  5 TYR B 303  HIS B 361  HEC B 601  HOH B 944                    
SITE     2 CC9  5 HOH B1205                                                     
SITE     1 DC1  6 GLU B 302  TYR B 303  LYS B 358  GLN B 360                    
SITE     2 DC1  6 HOH B 893  HOH B 990                                          
SITE     1 DC2  7 PRO B 116  HEC B 603  HEC B 604  GOL B 613                    
SITE     2 DC2  7 HOH B 936  HOH B 953  HOH B1059                               
SITE     1 DC3  7 ARG B  87  VAL B 128  GLN B 138  PHE B 139                    
SITE     2 DC3  7 TRP B 142  ARG B 497  HOH B1128                               
SITE     1 DC4 10 ARG B  96  GLU B 115  PRO B 116  ASN B 486                    
SITE     2 DC4 10 HEC B 604   CA B 611  HOH B 830  HOH B 834                    
SITE     3 DC4 10 HOH B1059  HOH B1063                                          
SITE     1 DC5  8 ASP B 101  ALA B 110  GLN B 175  TRP B 444                    
SITE     2 DC5  8 ILE B 504  LYS B 508  HOH B 742  HOH B 963                    
SITE     1 DC6  6 THR B 351  LYS B 447  ASN B 515  HOH B 769                    
SITE     2 DC6  6 HOH B1091  HOH B1236                                          
SITE     1 DC7  7 GLN B 169  GLU B 213  VAL B 214  NO2 B 617                    
SITE     2 DC7  7 HOH B 931  HOH B1077  HOH B1136                               
SITE     1 DC8  8 SER B 212  GLU B 213  VAL B 214  NO2 B 616                    
SITE     2 DC8  8 HOH B 846  HOH B 987  HOH B1077  HOH B1136                    
CRYST1  194.980  194.980  194.980  90.00  90.00  90.00 P 21 3       24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005129  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005129  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005129        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
HEADER    SUGAR BINDING PROTEIN                   01-APR-14   4P8X              
TITLE     THE CRYSTAL STRUCTURES OF YKL-39 IN THE PRESENCE OF                   
TITLE    2 CHITOOLIGOSACCHARIDES (GLCNAC6) WERE SOLVED TO RESOLUTIONS OF 2.48   
TITLE    3 ANGSTROM                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHITINASE-3-LIKE PROTEIN 2;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CHONDROCYTE PROTEIN 39,YKL-39;                              
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CHI3L2;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET32A(+)                                 
KEYWDS    CHITINASE 3-LIKE PROTEIN 2, HUMAN YKL-39, FAMILY-18 CHITINASE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.SUGINTA,A.RANOK,R.C.ROBINSON,J.WONGSANTICHON                        
REVDAT   3   11-FEB-15 4P8X    1       JRNL                                     
REVDAT   2   17-DEC-14 4P8X    1       JRNL                                     
REVDAT   1   03-DEC-14 4P8X    0                                                
JRNL        AUTH   A.RANOK,J.WONGSANTICHON,R.C.ROBINSON,W.SUGINTA               
JRNL        TITL   STRUCTURAL AND THERMODYNAMIC INSIGHTS INTO                   
JRNL        TITL 2 CHITOOLIGOSACCHARIDE BINDING TO HUMAN CARTILAGE CHITINASE    
JRNL        TITL 3 3-LIKE PROTEIN 2 (CHI3L2 OR YKL-39).                         
JRNL        REF    J.BIOL.CHEM.                  V. 290  2617 2015              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   25477513                                                     
JRNL        DOI    10.1074/JBC.M114.588905                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.48 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.48                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 12630                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 687                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.48                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 795                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.36                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 39                           
REMARK   3   BIN FREE R VALUE                    : 0.3130                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2894                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 100                                     
REMARK   3   SOLVENT ATOMS            : 263                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.42000                                              
REMARK   3    B22 (A**2) : 2.42000                                              
REMARK   3    B33 (A**2) : -4.85000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.302         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.231         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.575        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3076 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2850 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4180 ; 1.513 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6561 ; 0.802 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   364 ; 6.551 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   131 ;38.128 ;24.809       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   505 ;19.987 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;21.175 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   465 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3388 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   701 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1459 ; 3.104 ; 4.814       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1458 ; 3.104 ; 4.812       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1822 ; 4.633 ; 7.209       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1823 ; 4.631 ; 7.211       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1617 ; 3.240 ; 5.174       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1605 ; 3.214 ; 5.168       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2341 ; 5.102 ; 7.609       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3730 ; 7.119 ;39.435       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3643 ; 7.103 ;39.236       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4P8X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000200946.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-JUN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 105                                
REMARK 200  PH                             : 5.3-5.9                            
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSRRC                              
REMARK 200  BEAMLINE                       : BL13B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : LN2-COOLED, FIXED-EXIT DOUBLE      
REMARK 200                                   CRYSTAL MONOCHROMATOR              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12681                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.480                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.15000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.48                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, LITHIUM SULFATE, BIS TRIS,     
REMARK 280  PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.51150            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       35.60350            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       35.60350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       35.25575            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       35.60350            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       35.60350            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      105.76725            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       35.60350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       35.60350            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       35.25575            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       35.60350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       35.60350            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      105.76725            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       70.51150            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A    20                                                      
REMARK 465     MET A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     ASP A    23                                                      
REMARK 465     ILE A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A 182    CG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   573     O    HOH A   576              1.90            
REMARK 500   O    HOH A   538     O    HOH A   555              1.94            
REMARK 500   O    HOH A   566     O    HOH A   699              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   505     O    HOH A   521     3555     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  48      -30.55    -38.81                                   
REMARK 500    SER A 143       75.06   -114.51                                   
REMARK 500    ASP A 148     -159.96     61.34                                   
REMARK 500    LYS A 172       41.91   -106.49                                   
REMARK 500    PHE A 212     -163.60   -160.32                                   
REMARK 500    SER A 277     -146.73   -113.20                                   
REMARK 500    GLU A 297       48.06     34.68                                   
REMARK 500    GLN A 374       16.27   -146.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 695        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH A 706        DISTANCE =  6.23 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  401 through NAG A 406                                               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4P8X   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P8W   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P8V   RELATED DB: PDB                                   
DBREF  4P8X A   27   390  UNP    Q15782   CH3L2_HUMAN     27    390             
SEQADV 4P8X ALA A   20  UNP  Q15782              EXPRESSION TAG                 
SEQADV 4P8X MET A   21  UNP  Q15782              EXPRESSION TAG                 
SEQADV 4P8X ALA A   22  UNP  Q15782              EXPRESSION TAG                 
SEQADV 4P8X ASP A   23  UNP  Q15782              EXPRESSION TAG                 
SEQADV 4P8X ILE A   24  UNP  Q15782              EXPRESSION TAG                 
SEQADV 4P8X GLY A   25  UNP  Q15782              EXPRESSION TAG                 
SEQADV 4P8X SER A   26  UNP  Q15782              EXPRESSION TAG                 
SEQADV 4P8X VAL A  182  UNP  Q15782    ALA   182 ENGINEERED MUTATION            
SEQADV 4P8X TRP A  318  UNP  Q15782    ARG   318 ENGINEERED MUTATION            
SEQRES   1 A  371  ALA MET ALA ASP ILE GLY SER TYR LYS LEU VAL CYS TYR          
SEQRES   2 A  371  PHE THR ASN TRP SER GLN ASP ARG GLN GLU PRO GLY LYS          
SEQRES   3 A  371  PHE THR PRO GLU ASN ILE ASP PRO PHE LEU CYS SER HIS          
SEQRES   4 A  371  LEU ILE TYR SER PHE ALA SER ILE GLU ASN ASN LYS VAL          
SEQRES   5 A  371  ILE ILE LYS ASP LYS SER GLU VAL MET LEU TYR GLN THR          
SEQRES   6 A  371  ILE ASN SER LEU LYS THR LYS ASN PRO LYS LEU LYS ILE          
SEQRES   7 A  371  LEU LEU SER ILE GLY GLY TYR LEU PHE GLY SER LYS GLY          
SEQRES   8 A  371  PHE HIS PRO MET VAL ASP SER SER THR SER ARG LEU GLU          
SEQRES   9 A  371  PHE ILE ASN SER ILE ILE LEU PHE LEU ARG ASN HIS ASN          
SEQRES  10 A  371  PHE ASP GLY LEU ASP VAL SER TRP ILE TYR PRO ASP GLN          
SEQRES  11 A  371  LYS GLU ASN THR HIS PHE THR VAL LEU ILE HIS GLU LEU          
SEQRES  12 A  371  ALA GLU ALA PHE GLN LYS ASP PHE THR LYS SER THR LYS          
SEQRES  13 A  371  GLU ARG LEU LEU LEU THR VAL GLY VAL SER ALA GLY ARG          
SEQRES  14 A  371  GLN MET ILE ASP ASN SER TYR GLN VAL GLU LYS LEU ALA          
SEQRES  15 A  371  LYS ASP LEU ASP PHE ILE ASN LEU LEU SER PHE ASP PHE          
SEQRES  16 A  371  HIS GLY SER TRP GLU LYS PRO LEU ILE THR GLY HIS ASN          
SEQRES  17 A  371  SER PRO LEU SER LYS GLY TRP GLN ASP ARG GLY PRO SER          
SEQRES  18 A  371  SER TYR TYR ASN VAL GLU TYR ALA VAL GLY TYR TRP ILE          
SEQRES  19 A  371  HIS LYS GLY MET PRO SER GLU LYS VAL VAL MET GLY ILE          
SEQRES  20 A  371  PRO THR TYR GLY HIS SER PHE THR LEU ALA SER ALA GLU          
SEQRES  21 A  371  THR THR VAL GLY ALA PRO ALA SER GLY PRO GLY ALA ALA          
SEQRES  22 A  371  GLY PRO ILE THR GLU SER SER GLY PHE LEU ALA TYR TYR          
SEQRES  23 A  371  GLU ILE CYS GLN PHE LEU LYS GLY ALA LYS ILE THR TRP          
SEQRES  24 A  371  LEU GLN ASP GLN GLN VAL PRO TYR ALA VAL LYS GLY ASN          
SEQRES  25 A  371  GLN TRP VAL GLY TYR ASP ASP VAL LYS SER MET GLU THR          
SEQRES  26 A  371  LYS VAL GLN PHE LEU LYS ASN LEU ASN LEU GLY GLY ALA          
SEQRES  27 A  371  MET ILE TRP SER ILE ASP MET ASP ASP PHE THR GLY LYS          
SEQRES  28 A  371  SER CYS ASN GLN GLY PRO TYR PRO LEU VAL GLN ALA VAL          
SEQRES  29 A  371  LYS ARG SER LEU GLY SER LEU                                  
MODRES 4P8X NAG A  401  NAG  -D                                                 
MODRES 4P8X NAG A  402  NAG  -D                                                 
MODRES 4P8X NAG A  403  NAG  -D                                                 
MODRES 4P8X NAG A  404  NAG  -D                                                 
MODRES 4P8X NAG A  405  NAG  -D                                                 
MODRES 4P8X NAG A  406  NAG  -D                                                 
HET    NAG  A 401      15                                                       
HET    NAG  A 402      14                                                       
HET    NAG  A 403      14                                                       
HET    NAG  A 404      14                                                       
HET    NAG  A 405      14                                                       
HET    NAG  A 406      14                                                       
HET    SO4  A 407       5                                                       
HET    SO4  A 408       5                                                       
HET    SO4  A 409       5                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  NAG    6(C8 H15 N O6)                                               
FORMUL   3  SO4    3(O4 S 2-)                                                   
FORMUL   6  HOH   *263(H2 O)                                                    
HELIX    1 AA1 TRP A   36  ARG A   40  5                                   5    
HELIX    2 AA2 THR A   47  ILE A   51  5                                   5    
HELIX    3 AA3 SER A   77  ASN A   92  1                                  16    
HELIX    4 AA4 SER A  108  HIS A  112  5                                   5    
HELIX    5 AA5 PRO A  113  ASP A  116  5                                   4    
HELIX    6 AA6 SER A  117  ASN A  136  1                                  20    
HELIX    7 AA7 PRO A  147  LYS A  172  1                                  26    
HELIX    8 AA8 GLY A  187  TYR A  195  1                                   9    
HELIX    9 AA9 GLN A  196  LEU A  204  1                                   9    
HELIX   10 AB1 ARG A  237  TYR A  243  5                                   7    
HELIX   11 AB2 ASN A  244  GLY A  256  1                                  13    
HELIX   12 AB3 PRO A  258  GLU A  260  5                                   3    
HELIX   13 AB4 TYR A  304  LYS A  312  1                                   9    
HELIX   14 AB5 ASP A  338  LEU A  352  1                                  15    
HELIX   15 AB6 SER A  361  ASP A  365  5                                   5    
HELIX   16 AB7 TYR A  377  SER A  389  1                                  13    
SHEET    1 AA110 LYS A  70  ILE A  72  0                                        
SHEET    2 AA110 HIS A  58  GLU A  67 -1  N  SER A  65   O  ILE A  72           
SHEET    3 AA110 LYS A  96  GLY A 103  1  O  LEU A  98   N  LEU A  59           
SHEET    4 AA110 GLY A 139  TRP A 144  1  O  ASP A 141   N  LEU A  99           
SHEET    5 AA110 LEU A 179  SER A 185  1  O  LEU A 179   N  LEU A 140           
SHEET    6 AA110 PHE A 206  LEU A 210  1  O  LEU A 210   N  VAL A 184           
SHEET    7 AA110 VAL A 262  PRO A 267  1  O  VAL A 263   N  LEU A 209           
SHEET    8 AA110 GLY A 356  TRP A 360  1  O  MET A 358   N  MET A 264           
SHEET    9 AA110 LYS A  28  THR A  34  1  N  VAL A  30   O  ALA A 357           
SHEET   10 AA110 HIS A  58  GLU A  67  1  O  ILE A  60   N  CYS A  31           
SHEET    1 AA2 3 ALA A 286  PRO A 289  0                                        
SHEET    2 AA2 3 TYR A 269  LEU A 275 -1  N  THR A 274   O  GLY A 288           
SHEET    3 AA2 3 PHE A 301  ALA A 303 -1  O  LEU A 302   N  GLY A 270           
SHEET    1 AA3 5 ALA A 286  PRO A 289  0                                        
SHEET    2 AA3 5 TYR A 269  LEU A 275 -1  N  THR A 274   O  GLY A 288           
SHEET    3 AA3 5 GLN A 332  GLY A 335 -1  O  TRP A 333   N  PHE A 273           
SHEET    4 AA3 5 PRO A 325  LYS A 329 -1  N  ALA A 327   O  VAL A 334           
SHEET    5 AA3 5 LYS A 315  TRP A 318 -1  N  THR A 317   O  TYR A 326           
SSBOND   1 CYS A   31    CYS A   56                          1555   1555  2.01  
SSBOND   2 CYS A  308    CYS A  372                          1555   1555  2.02  
LINK         O4  NAG A 401                 C1  NAG A 402     1555   1555  1.45  
LINK         O4  NAG A 402                 C1  NAG A 403     1555   1555  1.43  
LINK         O4  NAG A 403                 C1  NAG A 404     1555   1555  1.46  
LINK         O4  NAG A 404                 C1  NAG A 405     1555   1555  1.43  
LINK         O4  NAG A 405                 C1  NAG A 406     1555   1555  1.46  
CISPEP   1 GLU A   42    PRO A   43          0         7.48                     
CISPEP   2 SER A   62    PHE A   63          0       -10.73                     
CISPEP   3 HIS A  112    PRO A  113          0         9.85                     
CISPEP   4 ILE A  145    TYR A  146          0        -5.46                     
CISPEP   5 LYS A  220    PRO A  221          0         7.22                     
CISPEP   6 TRP A  360    SER A  361          0        -8.36                     
SITE     1 AC1  3 GLY A 107  SER A 108  LYS A 109                               
SITE     1 AC2  6 SER A  65  LYS A  74  PHE A 106  HOH A 639                    
SITE     2 AC2  6 HOH A 730  HOH A 731                                          
SITE     1 AC3  6 SER A  26  SER A 117  SER A 118  ARG A 121                    
SITE     2 AC3  6 HOH A 507  HOH A 527                                          
SITE     1 AC4 25 TRP A  36  TYR A 104  LEU A 105  SER A 143                    
SITE     2 AC4 25 ILE A 145  TYR A 146  GLY A 187  ASP A 213                    
SITE     3 AC4 25 TRP A 218  TYR A 243  TYR A 269  SER A 298                    
SITE     4 AC4 25 TRP A 360  MET A 364  HOH A 581  HOH A 582                    
SITE     5 AC4 25 HOH A 586  HOH A 593  HOH A 594  HOH A 602                    
SITE     6 AC4 25 HOH A 608  HOH A 628  HOH A 645  HOH A 734                    
SITE     7 AC4 25 HOH A 747                                                     
CRYST1   71.207   71.207  141.023  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014044  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014044  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007091        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
HEADER    VIRAL PROTEIN                           15-SEP-99   1D1D              
TITLE     NMR SOLUTION STRUCTURE OF THE CAPSID PROTEIN FROM ROUS                
TITLE    2 SARCOMA VIRUS                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (CAPSID PROTEIN);                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ROUS SARCOMA VIRUS;                             
SOURCE   3 ORGANISM_TAXID: 11886;                                               
SOURCE   4 STRAIN: SCHMIDT RUPPIN A-2;                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: HMS174(DE3) PLYSS;                         
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-16B (NOVAGEN);                        
SOURCE  10 OTHER_DETAILS: THE SOURCE OF THE CA_RSV GENE IS PLASMID              
SOURCE  11 PSRA-2 OF ATCC 45000, WHICH IS A PLASMID CLONE CONTAINING            
SOURCE  12 FULL LENGTH ROUS SARCOMA VIRUS, STRAIN SCHMIDT RUPPIN A-2,           
SOURCE  13 DERIVED FROM UNINTEGRATED DNA FROM AN ACUTE INFECTION OF             
SOURCE  14 QT-6 CELLS                                                           
KEYWDS    TWO INDEPENDENT DOMAINS HELICAL BUNDLES, VIRUS/VIRAL PROTEIN          
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    R.CAMPOS-OLIVAS,J.L.NEWMAN,M.F.SUMMERS                                
REVDAT   4   24-FEB-09 1D1D    1       VERSN                                    
REVDAT   3   01-APR-03 1D1D    1       JRNL                                     
REVDAT   2   10-APR-00 1D1D    1       JRNL                                     
REVDAT   1   10-DEC-99 1D1D    0                                                
JRNL        AUTH   R.CAMPOS-OLIVAS,J.L.NEWMAN,M.F.SUMMERS                       
JRNL        TITL   SOLUTION STRUCTURE AND DYNAMICS OF THE ROUS                  
JRNL        TITL 2 SARCOMA VIRUS CAPSID PROTEIN AND COMPARISON WITH             
JRNL        TITL 3 CAPSID PROTEINS OF OTHER RETROVIRUSES.                       
JRNL        REF    J.MOL.BIOL.                   V. 296   633 2000              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   10669613                                                     
JRNL        DOI    10.1006/JMBI.1999.3475                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : DYANA 1.5                                            
REMARK   3   AUTHORS     : P.GUNTHER, ETH-ZURICH                                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 20 CONFORMERS COMPATIBLE WITH THE         
REMARK   3  NMR CONSTRAINTS WERE CALCULATED USING DYANA 1.5 AND THE             
REMARK   3  STANDARD TORSION ANGLE SIMULATED ANHEALING PROTOCOL.                
REMARK   3  PRELIMINARY CALCULATIONS WERE CARRIED OUT INDEPENDENTLY FOR         
REMARK   3  EACH OF THE TWO N- AND C- TERMINAL DOMAINS OF THE PROTEIN.          
REMARK   3  INITIALLY ONLY NOE DISTANCE CONSTRAINTS WERE IMPOSED. THE           
REMARK   3  INITIAL STRUCTURES WERE THEN USED TO ASSES THE ACCURACY OF THE      
REMARK   3  TORSION ANGLE CONSTRAINTS GENERATED BY ANALYSIS OF HA, CA, CB,      
REMARK   3  CO AND N CHEMICAL SHIFTS WITH THE PROGRAM TALOS. FINALLY,           
REMARK   3  UPPER AND LOWER LIMIT DISTANCE CONSTRAINTS WERE IMPOSED FOR         
REMARK   3  UNAMBIGUOUS INTRAHELICAL H-BONDS.                                   
REMARK   4                                                                      
REMARK   4 1D1D COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-SEP-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB009702.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 303.00                             
REMARK 210  PH                             : 6.00                               
REMARK 210  IONIC STRENGTH                 : 10 MM PHOSPHATE                    
REMARK 210  PRESSURE                       : 1 ATM                              
REMARK 210  SAMPLE CONTENTS                : ~1 MM CA_RSV, 10 MM PHOSPHATE      
REMARK 210                                   (PH 6.0), 0.2 MM N3NA, 0.1 MM      
REMARK 210                                   EDTA, 0.1 MM PMSF, 1 MG/L          
REMARK 210                                   PEPSTATIN A, 5 MM BETA-            
REMARK 210                                   MERCAPTOETHANOL; ~1 MM CA_RSV,     
REMARK 210                                   10 MM PHOSPHATE (PH 6.0), 0.2      
REMARK 210                                   MM N3NA, 0.1 MM EDTA, 0.1 MM       
REMARK 210                                   PMSF, 1 MG/L PEPSTATIN A, 5 MM     
REMARK 210                                   BETA-MERCAPTOETHANOL               
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 4D_13C-SEPARATED_NOESY, 4D_        
REMARK 210                                   13C/15N-SEPARATED_ NOESY, 4D_      
REMARK 210                                   15N-SEPARATED_ NOESY, 3D_15N-      
REMARK 210                                   SEPARATED_NOESY                    
REMARK 210  SPECTROMETER FIELD STRENGTH    : 800 MHZ                            
REMARK 210  SPECTROMETER MODEL             : DRX                                
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : XWINNMR 2.5, NMRPIPE 1999,         
REMARK 210                                   NMRVIEW 3.0, TALOS                 
REMARK 210                                   1999.019.15.47                     
REMARK 210   METHOD USED                   : TORSION ANGLE DYNAMICS             
REMARK 210                                   SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 20                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : TARGET FUNCTION                    
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7                   
REMARK 210                                                                      
REMARK 210 REMARK: THE 1H, 13C, AND 15N CHEMICAL SHIFT ASSIGNMENTS HAVE         
REMARK 210  BEEN DEPOSITED ATTHE BIOMOLECULAR RESONANCE DATABANK (BMRB          
REMARK 210  ENTRY 4384).                                                        
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;                   
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                            
REMARK 465   MODELS 1-20                                                        
REMARK 465     RES C SSSEQI                                                     
REMARK 465     GLY A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     SER A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     ILE A    -7                                                      
REMARK 465     GLU A    -6                                                      
REMARK 465     GLY A    -5                                                      
REMARK 465     ARG A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     ASN A    -2                                                      
REMARK 465     MET A    -1                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     PRO A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     LEU A   231                                                      
REMARK 465     THR A   232                                                      
REMARK 465     ASP A   233                                                      
REMARK 465     GLN A   234                                                      
REMARK 465     GLY A   235                                                      
REMARK 465     ILE A   236                                                      
REMARK 465     ALA A   237                                                      
REMARK 465     ALA A   238                                                      
REMARK 465     ALA A   239                                                      
REMARK 465     MET A   240                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500  1 SER A  45      -32.11    -37.20                                   
REMARK 500  1 ARG A  89       22.49   -153.48                                   
REMARK 500  1 GLN A  95      -43.32   -165.03                                   
REMARK 500  1 ARG A 100      132.09     64.09                                   
REMARK 500  1 ARG A 125      157.92    -43.99                                   
REMARK 500  1 ALA A 147       71.55   -176.86                                   
REMARK 500  1 SER A 183      -37.14   -179.73                                   
REMARK 500  1 ALA A 186      -57.54    175.45                                   
REMARK 500  1 LYS A 196      -84.64   -126.79                                   
REMARK 500  1 SER A 197     -150.10     34.44                                   
REMARK 500  1 THR A 213       47.55   -158.03                                   
REMARK 500  1 LYS A 227     -150.29     41.90                                   
REMARK 500  2 ILE A  35      -31.21    168.43                                   
REMARK 500  2 SER A  45      -35.30    -35.34                                   
REMARK 500  2 ARG A  89       14.35   -141.44                                   
REMARK 500  2 GLN A  95       50.99   -159.58                                   
REMARK 500  2 GLU A  99       70.06     69.53                                   
REMARK 500  2 ALA A 110      171.09    -58.39                                   
REMARK 500  2 ARG A 125      159.09    -39.19                                   
REMARK 500  2 LEU A 146      100.45    -49.19                                   
REMARK 500  2 SER A 183      -30.89    163.90                                   
REMARK 500  2 ALA A 186      -57.76    175.08                                   
REMARK 500  2 LYS A 196       71.04   -163.91                                   
REMARK 500  2 GLN A 198      154.46    -38.34                                   
REMARK 500  2 THR A 213       43.17   -159.87                                   
REMARK 500  2 ALA A 229       87.57   -168.49                                   
REMARK 500  3 SER A  45      -31.20    -37.72                                   
REMARK 500  3 GLN A  95       48.15   -173.42                                   
REMARK 500  3 GLU A  99      -73.29    -74.11                                   
REMARK 500  3 ARG A 100      147.40     60.72                                   
REMARK 500  3 ARG A 125      158.33    -39.50                                   
REMARK 500  3 LEU A 146      158.22    -45.06                                   
REMARK 500  3 ALA A 147      -84.07   -176.67                                   
REMARK 500  3 SER A 183      -38.75    179.49                                   
REMARK 500  3 ALA A 186      -56.45    172.67                                   
REMARK 500  3 LYS A 196       73.57   -171.94                                   
REMARK 500  3 GLN A 198      159.21    -39.59                                   
REMARK 500  3 THR A 213       45.16   -160.75                                   
REMARK 500  3 PRO A 215       49.45    -75.01                                   
REMARK 500  4 SER A  45      -39.02    -35.22                                   
REMARK 500  4 ARG A  89       26.23   -152.37                                   
REMARK 500  4 GLU A  99      -73.23   -136.98                                   
REMARK 500  4 ARG A 100      148.45     61.24                                   
REMARK 500  4 ARG A 125      158.01    -40.55                                   
REMARK 500  4 ASP A 179       70.77   -100.07                                   
REMARK 500  4 SER A 183      -30.06    164.73                                   
REMARK 500  4 ALA A 186      -56.47    171.76                                   
REMARK 500  4 LYS A 196      -89.09   -145.52                                   
REMARK 500  4 SER A 197     -158.46     38.77                                   
REMARK 500  4 THR A 213       51.11   -161.27                                   
REMARK 500  4 LYS A 227      149.26     62.59                                   
REMARK 500  5 ILE A  35      -27.89    163.37                                   
REMARK 500  5 SER A  45      -36.85    -34.28                                   
REMARK 500  5 ARG A  89       15.87   -143.48                                   
REMARK 500  5 GLN A  95       36.95   -157.11                                   
REMARK 500  5 GLU A  99       40.91     35.97                                   
REMARK 500  5 ASN A 116      117.61   -161.76                                   
REMARK 500  5 ARG A 125      158.89    -41.29                                   
REMARK 500  5 SER A 183      -27.73    161.19                                   
REMARK 500  5 ALA A 186      -57.05    175.10                                   
REMARK 500  5 LYS A 196       73.80   -168.54                                   
REMARK 500  5 GLN A 198      167.60    -43.87                                   
REMARK 500  5 THR A 213       45.06   -158.42                                   
REMARK 500  5 ALA A 229       86.21   -150.96                                   
REMARK 500  6 SER A  45      -35.51    -34.62                                   
REMARK 500  6 GLN A  95       36.93   -179.58                                   
REMARK 500  6 ARG A 100      123.80     65.70                                   
REMARK 500  6 ARG A 125      157.67    -38.43                                   
REMARK 500  6 LEU A 146      163.80     57.16                                   
REMARK 500  6 ALA A 147      116.14    163.83                                   
REMARK 500  6 SER A 183      -31.19    164.38                                   
REMARK 500  6 ALA A 186      -56.29    172.18                                   
REMARK 500  6 LYS A 196      -59.05   -146.56                                   
REMARK 500  6 SER A 197      153.72    -37.05                                   
REMARK 500  6 GLN A 198      170.14    -45.19                                   
REMARK 500  6 THR A 213       45.50   -160.13                                   
REMARK 500  6 LYS A 227     -179.14     50.42                                   
REMARK 500  6 ALA A 229      156.11     69.35                                   
REMARK 500  7 ILE A  35      -31.87    164.30                                   
REMARK 500  7 SER A  45      -33.28    -36.33                                   
REMARK 500  7 ARG A 100      141.10     61.33                                   
REMARK 500  7 ARG A 125      160.09    -43.35                                   
REMARK 500  7 LEU A 146       98.60    -41.12                                   
REMARK 500  7 ALA A 186      -55.18    170.47                                   
REMARK 500  7 LYS A 196      -92.46   -141.17                                   
REMARK 500  7 SER A 197     -156.46     36.78                                   
REMARK 500  7 THR A 213       50.54   -160.95                                   
REMARK 500  7 ALA A 229      158.29     59.31                                   
REMARK 500  8 SER A  45      -35.88    -34.41                                   
REMARK 500  8 GLN A  95       42.17   -175.89                                   
REMARK 500  8 GLU A  99       42.44     39.49                                   
REMARK 500  8 ARG A 125      156.98    -45.98                                   
REMARK 500  8 ALA A 147      160.25    179.06                                   
REMARK 500  8 SER A 183      -37.71   -179.18                                   
REMARK 500  8 ALA A 186      -57.10    174.59                                   
REMARK 500  8 LYS A 196       78.56   -176.55                                   
REMARK 500  8 GLN A 198      156.00     51.25                                   
REMARK 500  8 THR A 213       46.66   -161.12                                   
REMARK 500  9 SER A  45      -31.08    -37.65                                   
REMARK 500  9 ARG A  89       14.66   -142.53                                   
REMARK 500  9 GLU A  99      -72.60   -141.17                                   
REMARK 500  9 ARG A 100      151.79     59.57                                   
REMARK 500  9 PRO A 117      -77.15    -75.01                                   
REMARK 500  9 ALA A 147       87.83   -157.51                                   
REMARK 500  9 SER A 183      -31.46    157.89                                   
REMARK 500  9 GLN A 198      160.28    -39.29                                   
REMARK 500  9 THR A 213       46.76   -160.19                                   
REMARK 500  9 LYS A 227      112.89     59.38                                   
REMARK 500  9 ALA A 229      -54.55    166.54                                   
REMARK 500 10 PRO A  34       49.41    -75.00                                   
REMARK 500 10 ILE A  35      -34.88   -131.36                                   
REMARK 500 10 SER A  45      -30.59    -38.24                                   
REMARK 500 10 ARG A  89       18.24   -148.04                                   
REMARK 500 10 GLN A  95       63.40   -169.14                                   
REMARK 500 10 GLU A  99      -51.59   -125.27                                   
REMARK 500 10 ARG A 100      139.22     66.31                                   
REMARK 500 10 ARG A 125      165.14    -47.79                                   
REMARK 500 10 SER A 183      -26.49    159.18                                   
REMARK 500 10 ALA A 186      -56.95    174.30                                   
REMARK 500 10 LYS A 196       63.98   -151.35                                   
REMARK 500 10 GLN A 198      163.70    -40.95                                   
REMARK 500 10 THR A 213       49.10   -161.22                                   
REMARK 500 11 SER A  45      -34.43    -35.93                                   
REMARK 500 11 ARG A  89       24.74   -156.58                                   
REMARK 500 11 GLN A  95      -61.50   -132.14                                   
REMARK 500 11 LEU A 146      107.96    -41.12                                   
REMARK 500 11 ASP A 179       54.02   -102.70                                   
REMARK 500 11 SER A 183      -30.12    165.22                                   
REMARK 500 11 ALA A 186      -55.80    171.57                                   
REMARK 500 11 LYS A 196      -90.30   -139.12                                   
REMARK 500 11 SER A 197     -156.95     37.80                                   
REMARK 500 11 THR A 213       43.92    176.76                                   
REMARK 500 11 ALA A 229      -54.41    167.68                                   
REMARK 500 12 SER A  45      -31.11    -37.92                                   
REMARK 500 12 GLN A  95      -50.38   -171.95                                   
REMARK 500 12 ARG A 100      137.78    -32.41                                   
REMARK 500 12 PRO A 117      -71.64    -74.99                                   
REMARK 500 12 ASP A 179       56.47   -103.07                                   
REMARK 500 12 SER A 183      -27.98    159.74                                   
REMARK 500 12 ALA A 186      -56.10    171.54                                   
REMARK 500 12 SER A 197      155.61    -37.04                                   
REMARK 500 12 GLN A 198      165.06    -41.99                                   
REMARK 500 12 THR A 213       35.84   -140.78                                   
REMARK 500 12 LYS A 227      -40.70    172.61                                   
REMARK 500 12 ILE A 228      -60.81     73.36                                   
REMARK 500 12 ALA A 229      -56.20    172.29                                   
REMARK 500 13 LEU A  14       98.91    -61.91                                   
REMARK 500 13 ILE A  35      -30.31    164.39                                   
REMARK 500 13 SER A  45      -32.64    -37.16                                   
REMARK 500 13 GLN A  95       12.64   -141.19                                   
REMARK 500 13 GLU A  99      -87.42    -82.87                                   
REMARK 500 13 ARG A 100      109.96     83.64                                   
REMARK 500 13 ARG A 125      158.16     81.44                                   
REMARK 500 13 SER A 183      -33.35    164.96                                   
REMARK 500 13 ALA A 186      -56.98    175.20                                   
REMARK 500 13 LYS A 196      -89.79   -139.84                                   
REMARK 500 13 SER A 197     -158.25     38.70                                   
REMARK 500 13 THR A 213       46.95   -161.54                                   
REMARK 500 13 ALA A 229      155.35    -49.44                                   
REMARK 500 14 ILE A  35      -29.62    163.94                                   
REMARK 500 14 GLN A  95      -57.63   -147.67                                   
REMARK 500 14 ASN A 116       86.96    176.89                                   
REMARK 500 14 ALA A 147      -62.76   -135.16                                   
REMARK 500 14 ASP A 179       56.52   -103.03                                   
REMARK 500 14 SER A 183      -27.38    159.90                                   
REMARK 500 14 ALA A 186      -56.62    167.97                                   
REMARK 500 14 LYS A 196       63.76   -155.36                                   
REMARK 500 14 THR A 213       45.35   -161.19                                   
REMARK 500 14 ILE A 228      140.43   -174.08                                   
REMARK 500 15 LEU A  14       99.24    -64.63                                   
REMARK 500 15 ILE A  35      -41.30   -141.18                                   
REMARK 500 15 SER A  45      -31.78    -37.82                                   
REMARK 500 15 ARG A  89       32.49   -165.89                                   
REMARK 500 15 GLN A  95      -62.61   -145.25                                   
REMARK 500 15 GLU A  99       65.87     65.83                                   
REMARK 500 15 PRO A 117      -74.94    -75.04                                   
REMARK 500 15 LEU A 146      105.44    -39.38                                   
REMARK 500 15 ALA A 147       78.91     64.71                                   
REMARK 500 15 SER A 183       -9.03     85.16                                   
REMARK 500 15 ALA A 186      -56.92    174.76                                   
REMARK 500 15 LYS A 196       75.52   -168.87                                   
REMARK 500 15 GLN A 198      166.35    -43.14                                   
REMARK 500 15 THR A 213       38.82   -163.33                                   
REMARK 500 16 GLN A  95       37.32   -151.64                                   
REMARK 500 16 GLU A  99      -61.69   -150.04                                   
REMARK 500 16 ARG A 100      123.32     72.02                                   
REMARK 500 16 ARG A 125      159.37    -46.96                                   
REMARK 500 16 LEU A 146      154.02     59.89                                   
REMARK 500 16 SER A 183      -35.06    158.81                                   
REMARK 500 16 ALA A 186      -55.08    171.31                                   
REMARK 500 16 SER A 197      158.71    -38.80                                   
REMARK 500 16 GLN A 198      166.34    -42.89                                   
REMARK 500 16 THR A 213       43.00   -155.50                                   
REMARK 500 16 LYS A 227      167.76     58.45                                   
REMARK 500 17 SER A  45      -37.60    -35.96                                   
REMARK 500 17 ARG A  89       23.57   -144.87                                   
REMARK 500 17 GLN A  95      -69.95   -175.97                                   
REMARK 500 17 GLU A  99       66.61     65.36                                   
REMARK 500 17 LEU A 146       86.64     31.00                                   
REMARK 500 17 ALA A 147      136.51   -175.88                                   
REMARK 500 17 SER A 183      -31.60    167.44                                   
REMARK 500 17 ALA A 186      -57.40    175.60                                   
REMARK 500 17 LYS A 196       72.08   -164.09                                   
REMARK 500 17 GLN A 198      162.35    -39.29                                   
REMARK 500 17 SER A 210       61.59    -69.33                                   
REMARK 500 17 THR A 211      -38.98   -156.74                                   
REMARK 500 17 THR A 213       32.59   -161.30                                   
REMARK 500 18 ILE A  35      -31.10    163.64                                   
REMARK 500 18 SER A  45      -33.02    -36.80                                   
REMARK 500 18 ARG A  89       26.40   -160.78                                   
REMARK 500 18 GLN A  95      -61.90    -96.26                                   
REMARK 500 18 GLU A  99      -72.48   -125.02                                   
REMARK 500 18 ARG A 100      145.04     65.09                                   
REMARK 500 18 LEU A 124     -169.87    -73.39                                   
REMARK 500 18 LEU A 146      -75.04     66.00                                   
REMARK 500 18 SER A 183      -41.81   -167.79                                   
REMARK 500 18 ALA A 186      -59.19    179.09                                   
REMARK 500 18 LYS A 196       73.06   -165.57                                   
REMARK 500 18 GLN A 198      167.07    -43.79                                   
REMARK 500 18 THR A 213       30.44   -167.13                                   
REMARK 500 18 LYS A 227      147.12     64.68                                   
REMARK 500 19 SER A  45      -31.60    -37.42                                   
REMARK 500 19 GLN A  95       50.12   -170.16                                   
REMARK 500 19 GLU A  99      -76.19    -83.09                                   
REMARK 500 19 ARG A 100      142.89     64.34                                   
REMARK 500 19 PRO A 117      -80.00    -75.02                                   
REMARK 500 19 LEU A 146      -70.54    -40.18                                   
REMARK 500 19 ALA A 147      -47.16   -177.02                                   
REMARK 500 19 SER A 183      -33.10    171.29                                   
REMARK 500 19 ALA A 186      -57.39    175.46                                   
REMARK 500 19 LYS A 196       67.56   -156.01                                   
REMARK 500 19 GLN A 198      154.20    -36.66                                   
REMARK 500 19 THR A 213       45.12   -160.09                                   
REMARK 500 19 LYS A 227      150.35     64.11                                   
REMARK 500 20 PRO A  34     -169.99    -75.00                                   
REMARK 500 20 ILE A  35      -41.62     77.68                                   
REMARK 500 20 SER A  45      -39.59    -35.68                                   
REMARK 500 20 GLN A  95      -67.22   -166.09                                   
REMARK 500 20 LEU A 146      -89.36    -40.60                                   
REMARK 500 20 ALA A 147      100.95     53.44                                   
REMARK 500 20 SER A 183      -27.74    161.60                                   
REMARK 500 20 ALA A 186      -56.66    173.28                                   
REMARK 500 20 SER A 197      155.81    -37.39                                   
REMARK 500 20 GLN A 198      170.45    -45.19                                   
REMARK 500 20 THR A 213       34.08   -163.27                                   
REMARK 500 20 ILE A 228      162.18     64.14                                   
REMARK 500 20 ALA A 229      -53.99    167.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1D1D A    1   240  UNP    O92954   O92954_RSVSB   240    479             
SEQADV 1D1D GLY A  -22  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D HIS A  -21  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D HIS A  -20  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D HIS A  -19  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D HIS A  -18  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D HIS A  -17  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D HIS A  -16  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D HIS A  -15  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D HIS A  -14  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D HIS A  -13  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D HIS A  -12  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D SER A  -11  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D SER A  -10  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D GLY A   -9  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D HIS A   -8  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D ILE A   -7  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D GLU A   -6  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D GLY A   -5  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D ARG A   -4  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D HIS A   -3  UNP  O92954              N-TERMINAL HIS TAG             
SEQADV 1D1D ASN A   -2  UNP  O92954              N-TERMINAL HIS TAG             
SEQRES   1 A  262  GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER SER          
SEQRES   2 A  262  GLY HIS ILE GLU GLY ARG HIS ASN MET PRO VAL VAL ILE          
SEQRES   3 A  262  LYS THR GLU GLY PRO ALA TRP THR PRO LEU GLU PRO LYS          
SEQRES   4 A  262  LEU ILE THR ARG LEU ALA ASP THR VAL ARG THR LYS GLY          
SEQRES   5 A  262  LEU ARG SER PRO ILE THR MET ALA GLU VAL GLU ALA LEU          
SEQRES   6 A  262  MET SER SER PRO LEU LEU PRO HIS ASP VAL THR ASN LEU          
SEQRES   7 A  262  MET ARG VAL ILE LEU GLY PRO ALA PRO TYR ALA LEU TRP          
SEQRES   8 A  262  MET ASP ALA TRP GLY VAL GLN LEU GLN THR VAL ILE ALA          
SEQRES   9 A  262  ALA ALA THR ARG ASP PRO ARG HIS PRO ALA ASN GLY GLN          
SEQRES  10 A  262  GLY ARG GLY GLU ARG THR ASN LEU ASP ARG LEU LYS GLY          
SEQRES  11 A  262  LEU ALA ASP GLY MET VAL GLY ASN PRO GLN GLY GLN ALA          
SEQRES  12 A  262  ALA LEU LEU ARG PRO GLY GLU LEU VAL ALA ILE THR ALA          
SEQRES  13 A  262  SER ALA LEU GLN ALA PHE ARG GLU VAL ALA ARG LEU ALA          
SEQRES  14 A  262  GLU PRO ALA GLY PRO TRP ALA ASP ILE THR GLN GLY PRO          
SEQRES  15 A  262  SER GLU SER PHE VAL ASP PHE ALA ASN ARG LEU ILE LYS          
SEQRES  16 A  262  ALA VAL GLU GLY SER ASP LEU PRO PRO SER ALA ARG ALA          
SEQRES  17 A  262  PRO VAL ILE ILE ASP CYS PHE ARG GLN LYS SER GLN PRO          
SEQRES  18 A  262  ASP ILE GLN GLN LEU ILE ARG ALA ALA PRO SER THR LEU          
SEQRES  19 A  262  THR THR PRO GLY GLU ILE ILE LYS TYR VAL LEU ASP ARG          
SEQRES  20 A  262  GLN LYS ILE ALA PRO LEU THR ASP GLN GLY ILE ALA ALA          
SEQRES  21 A  262  ALA MET                                                      
HELIX    1   1 GLU A   15  GLY A   30  1                                  16    
HELIX    2   2 PRO A   34  SER A   45  1                                  12    
HELIX    3   3 LEU A   49  LEU A   61  1                                  13    
HELIX    4   4 GLY A   62  ASP A   87  1                                  26    
HELIX    5   5 ASN A  102  GLY A  108  1                                   7    
HELIX    6   6 ASN A  116  LEU A  124  1                                   9    
HELIX    7   7 GLY A  127  LEU A  146  1                                  20    
HELIX    8   8 SER A  163  GLY A  177  1                                  15    
HELIX    9   9 ALA A  186  ARG A  194  1                                   9    
HELIX   10  10 GLN A  198  ALA A  207  1                                  10    
HELIX   11  11 GLY A  216  LYS A  227  1                                  12    
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)

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