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Database: PDB
Entry: 1PGR
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Original site: 1PGR 
HEADER    CYTOKINE                                08-MAR-99   1PGR              
TITLE     2:2 COMPLEX OF G-CSF WITH ITS RECEPTOR                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (GRANULOCYTE COLONY-STIMULATING FACTOR);           
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 SYNONYM: G-CSF;                                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PROTEIN (G-CSF RECEPTOR);                                  
COMPND   8 CHAIN: B, D, F, H;                                                   
COMPND   9 FRAGMENT: CRH REGION (BN DOMAIN:H1-108, BC DOMAIN:H109-              
COMPND  10 215);                                                                
COMPND  11 SYNONYM: G-CSF-R;                                                    
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELLULAR_LOCATION: EXTRACELLULAR;                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  12 ORGANISM_TAXID: 10090;                                               
SOURCE  13 CELLULAR_LOCATION: CELLULAR MEMBRANE;                                
SOURCE  14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: SF-9;                                   
SOURCE  18 EXPRESSION_SYSTEM_CELLULAR_LOCATION: NUCLEUS;                        
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS;                                
SOURCE  20 EXPRESSION_SYSTEM_VECTOR: AUTOGRAPHA CALIFORNICA NUCLEAR             
SOURCE  21 POLYHEDROSIS VIRUS                                                   
KEYWDS    CLASS1 CYTOKINE, HEMATOPOIETIC RECEPTOR, SIGNAL TRANSDUCTION          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.ARITOMI,N.KUNISHIMA,T.OKAMOTO,R.KUROKI,Y.OTA,K.MORIKAWA             
REVDAT   2   24-FEB-09 1PGR    1       VERSN                                    
REVDAT   1   08-MAR-00 1PGR    0                                                
JRNL        AUTH   M.ARITOMI,N.KUNISHIMA,T.OKAMOTO,R.KUROKI,Y.OTA,              
JRNL        AUTH 2 K.MORIKAWA                                                   
JRNL        TITL   ATOMIC STRUCTURE OF THE GCSF-RECEPTOR COMPLEX                
JRNL        TITL 2 SHOWING A NEW CYTOKINE-RECEPTOR RECOGNITION SCHEME.          
JRNL        REF    NATURE                        V. 401   713 1999              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   10537111                                                     
JRNL        DOI    10.1038/44394                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 69.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 24595                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.317                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.64                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3020                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3350                       
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11424                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 61.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.00                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RIGID-BODY REFINEMENT  THE 107TH          
REMARK   3  VALINES IN CHAINS B,D,F,H WERE REMOVED FOR THE RIGID-BODY           
REMARK   3  REFINEMENT. INITIAL MODEL WAS OBTAINED BY A MOLECULAR               
REMARK   3  REPLACEMENT OF 1IGR. A RIGID-BODY REFINEMENT WAS APPLIED TO         
REMARK   3  THE MODEL AS INDEPENDENT 12 GROUPS. FURTHER POSITIONAL OR B-        
REMARK   3  FACTOR REFINEMENTS FOR INDIVIDUAL ATOMS WERE NOT APPLIED.           
REMARK   4                                                                      
REMARK   4 1PGR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB000596.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : DEC-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6B                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : BENT MIRROR                        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26681                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 69.1                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.19800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1IGR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
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      186.65250            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       62.86250            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       62.86250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      279.97875            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       62.86250            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       62.86250            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       93.32625            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       62.86250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       62.86250            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      279.97875            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       62.86250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       62.86250            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       93.32625            
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      186.65250            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
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     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     PRO A   129                                                      
REMARK 465     ALA A   130                                                      
REMARK 465     LEU A   131                                                      
REMARK 465     GLN A   132                                                      
REMARK 465     PRO A   133                                                      
REMARK 465     THR A   134                                                      
REMARK 465     GLN A   135                                                      
REMARK 465     GLY A   136                                                      
REMARK 465     VAL B   107                                                      
REMARK 465     VAL B   123                                                      
REMARK 465     VAL B   124                                                      
REMARK 465     SER B   125                                                      
REMARK 465     HIS B   126                                                      
REMARK 465     LYS B   214                                                      
REMARK 465     ALA B   215                                                      
REMARK 465     MET C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     PRO C     3                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     PRO C     6                                                      
REMARK 465     ALA C     7                                                      
REMARK 465     GLN C    68                                                      
REMARK 465     ALA C    69                                                      
REMARK 465     LEU C    70                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     HIS D    33                                                      
REMARK 465     LEU D    34                                                      
REMARK 465     PRO D    35                                                      
REMARK 465     VAL D   107                                                      
REMARK 465     GLY D   120                                                      
REMARK 465     PRO D   121                                                      
REMARK 465     ASP D   122                                                      
REMARK 465     VAL D   123                                                      
REMARK 465     VAL D   124                                                      
REMARK 465     SER D   125                                                      
REMARK 465     HIS D   126                                                      
REMARK 465     LYS D   214                                                      
REMARK 465     ALA D   215                                                      
REMARK 465     MET E     1                                                      
REMARK 465     THR E     2                                                      
REMARK 465     PRO E     3                                                      
REMARK 465     LEU E     4                                                      
REMARK 465     PRO E   129                                                      
REMARK 465     ALA E   130                                                      
REMARK 465     LEU E   131                                                      
REMARK 465     GLN E   132                                                      
REMARK 465     PRO E   133                                                      
REMARK 465     THR E   134                                                      
REMARK 465     GLN E   135                                                      
REMARK 465     GLY E   136                                                      
REMARK 465     VAL F   107                                                      
REMARK 465     VAL F   123                                                      
REMARK 465     VAL F   124                                                      
REMARK 465     SER F   125                                                      
REMARK 465     LYS F   214                                                      
REMARK 465     ALA F   215                                                      
REMARK 465     MET G     1                                                      
REMARK 465     THR G     2                                                      
REMARK 465     PRO G     3                                                      
REMARK 465     LEU G     4                                                      
REMARK 465     GLY G     5                                                      
REMARK 465     PRO G     6                                                      
REMARK 465     ALA G     7                                                      
REMARK 465     GLN G    68                                                      
REMARK 465     ALA G    69                                                      
REMARK 465     LEU G    70                                                      
REMARK 465     ALA H     1                                                      
REMARK 465     GLY H     2                                                      
REMARK 465     HIS H    33                                                      
REMARK 465     LEU H    34                                                      
REMARK 465     PRO H    35                                                      
REMARK 465     VAL H   107                                                      
REMARK 465     GLY H   120                                                      
REMARK 465     PRO H   121                                                      
REMARK 465     ASP H   122                                                      
REMARK 465     VAL H   123                                                      
REMARK 465     VAL H   124                                                      
REMARK 465     SER H   125                                                      
REMARK 465     HIS H   126                                                      
REMARK 465     LYS H   214                                                      
REMARK 465     ALA H   215                                                      
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     GLN A  71    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  63    CG   CD   CE   NZ                                   
REMARK 470     ARG B  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C  71    CG   CD   OE1  NE2                                  
REMARK 470     LYS D  62    CG   CD   CE   NZ                                   
REMARK 470     ARG D  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE D 119    CG1  CG2  CD1                                       
REMARK 470     GLN D 127    CG   CD   OE1  NE2                                  
REMARK 470     MET D 213    CG   SD   CE                                        
REMARK 470     GLN E  71    CG   CD   OE1  NE2                                  
REMARK 470     LYS F  63    CG   CD   CE   NZ                                   
REMARK 470     ARG F  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS F 126    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN G  71    CG   CD   OE1  NE2                                  
REMARK 470     LYS H  62    CG   CD   CE   NZ                                   
REMARK 470     ARG H  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE H 119    CG1  CG2  CD1                                       
REMARK 470     GLN H 127    CG   CD   OE1  NE2                                  
REMARK 470     MET H 213    CG   SD   CE                                        
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   CE   MET B   213     O    LEU D    91     6555     1.99            
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    LYS A  41       35.56     38.15                                   
REMARK 500    LEU A  62       31.70   -147.28                                   
REMARK 500    SER A  67     -165.89   -170.39                                   
REMARK 500    GLN A  68     -178.97     71.93                                   
REMARK 500    ALA A  69      -86.34    173.50                                   
REMARK 500    LEU A  72       41.16   -151.86                                   
REMARK 500    GLU A  94       50.45     39.60                                   
REMARK 500    ILE A  96      -65.49     62.96                                   
REMARK 500    MET A 127       -7.38    -58.09                                   
REMARK 500    PRO A 139      174.22    -59.45                                   
REMARK 500    PHE A 141       73.27     43.57                                   
REMARK 500    HIS B  33        3.82     82.09                                   
REMARK 500    SER B  45     -150.30   -150.75                                   
REMARK 500    CYS B  49       41.37     31.78                                   
REMARK 500    ASN B  66       44.64    -97.22                                   
REMARK 500    GLU B  88      137.88   -170.20                                   
REMARK 500    PRO B 111      153.70    -49.54                                   
REMARK 500    ASP B 118       77.48   -100.90                                   
REMARK 500    SER B 195       -1.74     67.26                                   
REMARK 500    SER C  63       86.90    -17.03                                   
REMARK 500    SER C  64       64.46     21.55                                   
REMARK 500    LEU C  93        1.27    -59.11                                   
REMARK 500    GLU C  94       40.77     32.81                                   
REMARK 500    ILE C  96      -53.96     72.56                                   
REMARK 500    SER C  97      156.80    174.08                                   
REMARK 500    PHE C 141       71.22   -104.06                                   
REMARK 500    ALA C 173       95.94    -64.76                                   
REMARK 500    LYS D  63      -86.48    -37.46                                   
REMARK 500    ASN D  66       48.17    -85.94                                   
REMARK 500    CYS D  68     -141.78   -126.27                                   
REMARK 500    SER D  69      106.46    168.81                                   
REMARK 500    LEU D  77      -60.66    -95.92                                   
REMARK 500    TYR D  78       56.81    -92.29                                   
REMARK 500    PRO D 111      153.25    -49.72                                   
REMARK 500    GLN D 181        3.11   -178.21                                   
REMARK 500    ALA D 182      158.21    177.22                                   
REMARK 500    SER D 194      -70.09    -48.37                                   
REMARK 500    THR D 212      100.71    -37.01                                   
REMARK 500    LYS E  41       35.64     38.11                                   
REMARK 500    LEU E  62       31.70   -147.19                                   
REMARK 500    SER E  67     -165.96   -170.38                                   
REMARK 500    GLN E  68     -179.04     72.02                                   
REMARK 500    ALA E  69      -86.35    173.60                                   
REMARK 500    LEU E  72       41.22   -151.70                                   
REMARK 500    GLU E  94       50.59     39.50                                   
REMARK 500    ILE E  96      -65.47     62.91                                   
REMARK 500    MET E 127       -7.49    -57.86                                   
REMARK 500    PRO E 139      174.34    -59.45                                   
REMARK 500    PHE E 141       73.29     43.65                                   
REMARK 500    HIS F  33        3.78     82.28                                   
REMARK 500    SER F  45     -150.30   -150.72                                   
REMARK 500    CYS F  49       41.39     31.83                                   
REMARK 500    ASN F  66       44.67    -97.13                                   
REMARK 500    GLU F  88      138.00   -170.13                                   
REMARK 500    PRO F 111      153.81    -49.55                                   
REMARK 500    ASP F 118       77.39   -100.68                                   
REMARK 500    SER F 195       -1.62     67.14                                   
REMARK 500    SER G  63       86.73    -16.82                                   
REMARK 500    SER G  64       64.41     21.60                                   
REMARK 500    LEU G  93        1.26    -59.09                                   
REMARK 500    GLU G  94       40.83     32.64                                   
REMARK 500    ILE G  96      -54.08     72.67                                   
REMARK 500    SER G  97      156.80    174.04                                   
REMARK 500    PHE G 141       71.14   -104.12                                   
REMARK 500    ALA G 173       95.87    -64.74                                   
REMARK 500    LYS H  63      -86.32    -37.61                                   
REMARK 500    ASN H  66       48.19    -85.97                                   
REMARK 500    CYS H  68     -141.76   -126.12                                   
REMARK 500    SER H  69      106.50    168.77                                   
REMARK 500    LEU H  77      -60.75    -95.94                                   
REMARK 500    TYR H  78       56.75    -92.20                                   
REMARK 500    PRO H 111      153.21    -49.79                                   
REMARK 500    ASP H 118      -71.09    -87.73                                   
REMARK 500    GLN H 181        3.25   -178.31                                   
REMARK 500    ALA H 182      158.23    177.10                                   
REMARK 500    SER H 194      -70.23    -48.27                                   
REMARK 500    THR H 212      100.63    -36.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1PGR A    2   175  UNP    P09919   CSF3_HUMAN      13    186             
DBREF  1PGR B    1   215  UNP    P40223   CSF3R_MOUSE    120    334             
DBREF  1PGR C    2   175  UNP    P09919   CSF3_HUMAN      13    186             
DBREF  1PGR D    1   215  UNP    P40223   CSF3R_MOUSE    120    334             
DBREF  1PGR E    2   175  UNP    P09919   CSF3_HUMAN      13    186             
DBREF  1PGR F    1   215  UNP    P40223   CSF3R_MOUSE    120    334             
DBREF  1PGR G    2   175  UNP    P09919   CSF3_HUMAN      13    186             
DBREF  1PGR H    1   215  UNP    P40223   CSF3R_MOUSE    120    334             
SEQRES   1 A  175  MET THR PRO LEU GLY PRO ALA SER SER LEU PRO GLN SER          
SEQRES   2 A  175  PHE LEU LEU LYS CYS LEU GLU GLN VAL ARG LYS ILE GLN          
SEQRES   3 A  175  GLY ASP GLY ALA ALA LEU GLN GLU LYS LEU CYS ALA THR          
SEQRES   4 A  175  TYR LYS LEU CYS HIS PRO GLU GLU LEU VAL LEU LEU GLY          
SEQRES   5 A  175  HIS SER LEU GLY ILE PRO TRP ALA PRO LEU SER SER CYS          
SEQRES   6 A  175  PRO SER GLN ALA LEU GLN LEU ALA GLY CYS LEU SER GLN          
SEQRES   7 A  175  LEU HIS SER GLY LEU PHE LEU TYR GLN GLY LEU LEU GLN          
SEQRES   8 A  175  ALA LEU GLU GLY ILE SER PRO GLU LEU GLY PRO THR LEU          
SEQRES   9 A  175  ASP THR LEU GLN LEU ASP VAL ALA ASP PHE ALA THR THR          
SEQRES  10 A  175  ILE TRP GLN GLN MET GLU GLU LEU GLY MET ALA PRO ALA          
SEQRES  11 A  175  LEU GLN PRO THR GLN GLY ALA MET PRO ALA PHE ALA SER          
SEQRES  12 A  175  ALA PHE GLN ARG ARG ALA GLY GLY VAL LEU VAL ALA SER          
SEQRES  13 A  175  HIS LEU GLN SER PHE LEU GLU VAL SER TYR ARG VAL LEU          
SEQRES  14 A  175  ARG HIS LEU ALA GLN PRO                                      
SEQRES   1 B  215  ALA GLY TYR PRO PRO ALA SER PRO SER ASN LEU SER CYS          
SEQRES   2 B  215  LEU MET HIS LEU THR THR ASN SER LEU VAL CYS GLN TRP          
SEQRES   3 B  215  GLU PRO GLY PRO GLU THR HIS LEU PRO THR SER PHE ILE          
SEQRES   4 B  215  LEU LYS SER PHE ARG SER ARG ALA ASP CYS GLN TYR GLN          
SEQRES   5 B  215  GLY ASP THR ILE PRO ASP CYS VAL ALA LYS LYS ARG GLN          
SEQRES   6 B  215  ASN ASN CYS SER ILE PRO ARG LYS ASN LEU LEU LEU TYR          
SEQRES   7 B  215  GLN TYR MET ALA ILE TRP VAL GLN ALA GLU ASN MET LEU          
SEQRES   8 B  215  GLY SER SER GLU SER PRO LYS LEU CYS LEU ASP PRO MET          
SEQRES   9 B  215  ASP VAL VAL LYS LEU GLU PRO PRO MET LEU GLN ALA LEU          
SEQRES  10 B  215  ASP ILE GLY PRO ASP VAL VAL SER HIS GLN PRO GLY CYS          
SEQRES  11 B  215  LEU TRP LEU SER TRP LYS PRO TRP LYS PRO SER GLU TYR          
SEQRES  12 B  215  MET GLU GLN GLU CYS GLU LEU ARG TYR GLN PRO GLN LEU          
SEQRES  13 B  215  LYS GLY ALA ASN TRP THR LEU VAL PHE HIS LEU PRO SER          
SEQRES  14 B  215  SER LYS ASP GLN PHE GLU LEU CYS GLY LEU HIS GLN ALA          
SEQRES  15 B  215  PRO VAL TYR THR LEU GLN MET ARG CYS ILE ARG SER SER          
SEQRES  16 B  215  LEU PRO GLY PHE TRP SER PRO TRP SER PRO GLY LEU GLN          
SEQRES  17 B  215  LEU ARG PRO THR MET LYS ALA                                  
SEQRES   1 C  175  MET THR PRO LEU GLY PRO ALA SER SER LEU PRO GLN SER          
SEQRES   2 C  175  PHE LEU LEU LYS CYS LEU GLU GLN VAL ARG LYS ILE GLN          
SEQRES   3 C  175  GLY ASP GLY ALA ALA LEU GLN GLU LYS LEU CYS ALA THR          
SEQRES   4 C  175  TYR LYS LEU CYS HIS PRO GLU GLU LEU VAL LEU LEU GLY          
SEQRES   5 C  175  HIS SER LEU GLY ILE PRO TRP ALA PRO LEU SER SER CYS          
SEQRES   6 C  175  PRO SER GLN ALA LEU GLN LEU ALA GLY CYS LEU SER GLN          
SEQRES   7 C  175  LEU HIS SER GLY LEU PHE LEU TYR GLN GLY LEU LEU GLN          
SEQRES   8 C  175  ALA LEU GLU GLY ILE SER PRO GLU LEU GLY PRO THR LEU          
SEQRES   9 C  175  ASP THR LEU GLN LEU ASP VAL ALA ASP PHE ALA THR THR          
SEQRES  10 C  175  ILE TRP GLN GLN MET GLU GLU LEU GLY MET ALA PRO ALA          
SEQRES  11 C  175  LEU GLN PRO THR GLN GLY ALA MET PRO ALA PHE ALA SER          
SEQRES  12 C  175  ALA PHE GLN ARG ARG ALA GLY GLY VAL LEU VAL ALA SER          
SEQRES  13 C  175  HIS LEU GLN SER PHE LEU GLU VAL SER TYR ARG VAL LEU          
SEQRES  14 C  175  ARG HIS LEU ALA GLN PRO                                      
SEQRES   1 D  215  ALA GLY TYR PRO PRO ALA SER PRO SER ASN LEU SER CYS          
SEQRES   2 D  215  LEU MET HIS LEU THR THR ASN SER LEU VAL CYS GLN TRP          
SEQRES   3 D  215  GLU PRO GLY PRO GLU THR HIS LEU PRO THR SER PHE ILE          
SEQRES   4 D  215  LEU LYS SER PHE ARG SER ARG ALA ASP CYS GLN TYR GLN          
SEQRES   5 D  215  GLY ASP THR ILE PRO ASP CYS VAL ALA LYS LYS ARG GLN          
SEQRES   6 D  215  ASN ASN CYS SER ILE PRO ARG LYS ASN LEU LEU LEU TYR          
SEQRES   7 D  215  GLN TYR MET ALA ILE TRP VAL GLN ALA GLU ASN MET LEU          
SEQRES   8 D  215  GLY SER SER GLU SER PRO LYS LEU CYS LEU ASP PRO MET          
SEQRES   9 D  215  ASP VAL VAL LYS LEU GLU PRO PRO MET LEU GLN ALA LEU          
SEQRES  10 D  215  ASP ILE GLY PRO ASP VAL VAL SER HIS GLN PRO GLY CYS          
SEQRES  11 D  215  LEU TRP LEU SER TRP LYS PRO TRP LYS PRO SER GLU TYR          
SEQRES  12 D  215  MET GLU GLN GLU CYS GLU LEU ARG TYR GLN PRO GLN LEU          
SEQRES  13 D  215  LYS GLY ALA ASN TRP THR LEU VAL PHE HIS LEU PRO SER          
SEQRES  14 D  215  SER LYS ASP GLN PHE GLU LEU CYS GLY LEU HIS GLN ALA          
SEQRES  15 D  215  PRO VAL TYR THR LEU GLN MET ARG CYS ILE ARG SER SER          
SEQRES  16 D  215  LEU PRO GLY PHE TRP SER PRO TRP SER PRO GLY LEU GLN          
SEQRES  17 D  215  LEU ARG PRO THR MET LYS ALA                                  
SEQRES   1 E  175  MET THR PRO LEU GLY PRO ALA SER SER LEU PRO GLN SER          
SEQRES   2 E  175  PHE LEU LEU LYS CYS LEU GLU GLN VAL ARG LYS ILE GLN          
SEQRES   3 E  175  GLY ASP GLY ALA ALA LEU GLN GLU LYS LEU CYS ALA THR          
SEQRES   4 E  175  TYR LYS LEU CYS HIS PRO GLU GLU LEU VAL LEU LEU GLY          
SEQRES   5 E  175  HIS SER LEU GLY ILE PRO TRP ALA PRO LEU SER SER CYS          
SEQRES   6 E  175  PRO SER GLN ALA LEU GLN LEU ALA GLY CYS LEU SER GLN          
SEQRES   7 E  175  LEU HIS SER GLY LEU PHE LEU TYR GLN GLY LEU LEU GLN          
SEQRES   8 E  175  ALA LEU GLU GLY ILE SER PRO GLU LEU GLY PRO THR LEU          
SEQRES   9 E  175  ASP THR LEU GLN LEU ASP VAL ALA ASP PHE ALA THR THR          
SEQRES  10 E  175  ILE TRP GLN GLN MET GLU GLU LEU GLY MET ALA PRO ALA          
SEQRES  11 E  175  LEU GLN PRO THR GLN GLY ALA MET PRO ALA PHE ALA SER          
SEQRES  12 E  175  ALA PHE GLN ARG ARG ALA GLY GLY VAL LEU VAL ALA SER          
SEQRES  13 E  175  HIS LEU GLN SER PHE LEU GLU VAL SER TYR ARG VAL LEU          
SEQRES  14 E  175  ARG HIS LEU ALA GLN PRO                                      
SEQRES   1 F  215  ALA GLY TYR PRO PRO ALA SER PRO SER ASN LEU SER CYS          
SEQRES   2 F  215  LEU MET HIS LEU THR THR ASN SER LEU VAL CYS GLN TRP          
SEQRES   3 F  215  GLU PRO GLY PRO GLU THR HIS LEU PRO THR SER PHE ILE          
SEQRES   4 F  215  LEU LYS SER PHE ARG SER ARG ALA ASP CYS GLN TYR GLN          
SEQRES   5 F  215  GLY ASP THR ILE PRO ASP CYS VAL ALA LYS LYS ARG GLN          
SEQRES   6 F  215  ASN ASN CYS SER ILE PRO ARG LYS ASN LEU LEU LEU TYR          
SEQRES   7 F  215  GLN TYR MET ALA ILE TRP VAL GLN ALA GLU ASN MET LEU          
SEQRES   8 F  215  GLY SER SER GLU SER PRO LYS LEU CYS LEU ASP PRO MET          
SEQRES   9 F  215  ASP VAL VAL LYS LEU GLU PRO PRO MET LEU GLN ALA LEU          
SEQRES  10 F  215  ASP ILE GLY PRO ASP VAL VAL SER HIS GLN PRO GLY CYS          
SEQRES  11 F  215  LEU TRP LEU SER TRP LYS PRO TRP LYS PRO SER GLU TYR          
SEQRES  12 F  215  MET GLU GLN GLU CYS GLU LEU ARG TYR GLN PRO GLN LEU          
SEQRES  13 F  215  LYS GLY ALA ASN TRP THR LEU VAL PHE HIS LEU PRO SER          
SEQRES  14 F  215  SER LYS ASP GLN PHE GLU LEU CYS GLY LEU HIS GLN ALA          
SEQRES  15 F  215  PRO VAL TYR THR LEU GLN MET ARG CYS ILE ARG SER SER          
SEQRES  16 F  215  LEU PRO GLY PHE TRP SER PRO TRP SER PRO GLY LEU GLN          
SEQRES  17 F  215  LEU ARG PRO THR MET LYS ALA                                  
SEQRES   1 G  175  MET THR PRO LEU GLY PRO ALA SER SER LEU PRO GLN SER          
SEQRES   2 G  175  PHE LEU LEU LYS CYS LEU GLU GLN VAL ARG LYS ILE GLN          
SEQRES   3 G  175  GLY ASP GLY ALA ALA LEU GLN GLU LYS LEU CYS ALA THR          
SEQRES   4 G  175  TYR LYS LEU CYS HIS PRO GLU GLU LEU VAL LEU LEU GLY          
SEQRES   5 G  175  HIS SER LEU GLY ILE PRO TRP ALA PRO LEU SER SER CYS          
SEQRES   6 G  175  PRO SER GLN ALA LEU GLN LEU ALA GLY CYS LEU SER GLN          
SEQRES   7 G  175  LEU HIS SER GLY LEU PHE LEU TYR GLN GLY LEU LEU GLN          
SEQRES   8 G  175  ALA LEU GLU GLY ILE SER PRO GLU LEU GLY PRO THR LEU          
SEQRES   9 G  175  ASP THR LEU GLN LEU ASP VAL ALA ASP PHE ALA THR THR          
SEQRES  10 G  175  ILE TRP GLN GLN MET GLU GLU LEU GLY MET ALA PRO ALA          
SEQRES  11 G  175  LEU GLN PRO THR GLN GLY ALA MET PRO ALA PHE ALA SER          
SEQRES  12 G  175  ALA PHE GLN ARG ARG ALA GLY GLY VAL LEU VAL ALA SER          
SEQRES  13 G  175  HIS LEU GLN SER PHE LEU GLU VAL SER TYR ARG VAL LEU          
SEQRES  14 G  175  ARG HIS LEU ALA GLN PRO                                      
SEQRES   1 H  215  ALA GLY TYR PRO PRO ALA SER PRO SER ASN LEU SER CYS          
SEQRES   2 H  215  LEU MET HIS LEU THR THR ASN SER LEU VAL CYS GLN TRP          
SEQRES   3 H  215  GLU PRO GLY PRO GLU THR HIS LEU PRO THR SER PHE ILE          
SEQRES   4 H  215  LEU LYS SER PHE ARG SER ARG ALA ASP CYS GLN TYR GLN          
SEQRES   5 H  215  GLY ASP THR ILE PRO ASP CYS VAL ALA LYS LYS ARG GLN          
SEQRES   6 H  215  ASN ASN CYS SER ILE PRO ARG LYS ASN LEU LEU LEU TYR          
SEQRES   7 H  215  GLN TYR MET ALA ILE TRP VAL GLN ALA GLU ASN MET LEU          
SEQRES   8 H  215  GLY SER SER GLU SER PRO LYS LEU CYS LEU ASP PRO MET          
SEQRES   9 H  215  ASP VAL VAL LYS LEU GLU PRO PRO MET LEU GLN ALA LEU          
SEQRES  10 H  215  ASP ILE GLY PRO ASP VAL VAL SER HIS GLN PRO GLY CYS          
SEQRES  11 H  215  LEU TRP LEU SER TRP LYS PRO TRP LYS PRO SER GLU TYR          
SEQRES  12 H  215  MET GLU GLN GLU CYS GLU LEU ARG TYR GLN PRO GLN LEU          
SEQRES  13 H  215  LYS GLY ALA ASN TRP THR LEU VAL PHE HIS LEU PRO SER          
SEQRES  14 H  215  SER LYS ASP GLN PHE GLU LEU CYS GLY LEU HIS GLN ALA          
SEQRES  15 H  215  PRO VAL TYR THR LEU GLN MET ARG CYS ILE ARG SER SER          
SEQRES  16 H  215  LEU PRO GLY PHE TRP SER PRO TRP SER PRO GLY LEU GLN          
SEQRES  17 H  215  LEU ARG PRO THR MET LYS ALA                                  
HELIX    1   1 PRO A   11  TYR A   40  1                                  30    
HELIX    2   2 HIS A   44  VAL A   49  5                                   6    
HELIX    3   3 LEU A   50  GLY A   56  1                                   7    
HELIX    4   4 LEU A   72  LEU A   93  1                                  22    
HELIX    5   5 LEU A  100  LEU A  125  1                                  26    
HELIX    6   6 SER A  143  GLN A  174  1                                  32    
HELIX    7   7 ARG B   46  GLN B   50  5                                   5    
HELIX    8   8 LYS B   73  LEU B   75  5                                   3    
HELIX    9   9 ASP B  102  VAL B  106  5                                   5    
HELIX   10  10 TRP B  138  GLU B  142  5                                   5    
HELIX   11  11 PRO C   11  LYS C   41  1                                  31    
HELIX   12  12 HIS C   44  GLY C   56  1                                  13    
HELIX   13  13 GLN C   71  LEU C   93  1                                  23    
HELIX   14  14 LEU C  100  LEU C  125  1                                  26    
HELIX   15  15 SER C  143  ALA C  173  1                                  31    
HELIX   16  16 ARG D   46  GLN D   50  5                                   5    
HELIX   17  17 LYS D   73  LEU D   75  5                                   3    
HELIX   18  18 ASP D  102  VAL D  106  5                                   5    
HELIX   19  19 TRP D  138  GLU D  142  5                                   5    
HELIX   20  20 PRO E   11  TYR E   40  1                                  30    
HELIX   21  21 HIS E   44  VAL E   49  5                                   6    
HELIX   22  22 LEU E   50  GLY E   56  1                                   7    
HELIX   23  23 LEU E   72  LEU E   93  1                                  22    
HELIX   24  24 LEU E  100  LEU E  125  1                                  26    
HELIX   25  25 SER E  143  GLN E  174  1                                  32    
HELIX   26  26 ARG F   46  GLN F   50  5                                   5    
HELIX   27  27 LYS F   73  LEU F   75  5                                   3    
HELIX   28  28 ASP F  102  VAL F  106  5                                   5    
HELIX   29  29 TRP F  138  GLU F  142  5                                   5    
HELIX   30  30 PRO G   11  LYS G   41  1                                  31    
HELIX   31  31 HIS G   44  GLY G   56  1                                  13    
HELIX   32  32 GLN G   71  LEU G   93  1                                  23    
HELIX   33  33 LEU G  100  LEU G  125  1                                  26    
HELIX   34  34 SER G  143  ALA G  173  1                                  31    
HELIX   35  35 ARG H   46  GLN H   50  5                                   5    
HELIX   36  36 LYS H   73  LEU H   75  5                                   3    
HELIX   37  37 ASP H  102  VAL H  106  5                                   5    
HELIX   38  38 TRP H  138  GLU H  142  5                                   5    
SHEET    1   A 3 SER B   9  HIS B  16  0                                        
SHEET    2   A 3 SER B  21  GLU B  27 -1  O  SER B  21   N  HIS B  16           
SHEET    3   A 3 ASN B  67  PRO B  71 -1  O  CYS B  68   N  CYS B  24           
SHEET    1   B 4 THR B  55  VAL B  60  0                                        
SHEET    2   B 4 SER B  37  ARG B  44 -1  N  LEU B  40   O  CYS B  59           
SHEET    3   B 4 MET B  81  ASN B  89 -1  N  ALA B  82   O  PHE B  43           
SHEET    4   B 4 GLY B  92  GLU B  95 -1  N  GLY B  92   O  ASN B  89           
SHEET    1   C 4 THR B  55  VAL B  60  0                                        
SHEET    2   C 4 SER B  37  ARG B  44 -1  N  LEU B  40   O  CYS B  59           
SHEET    3   C 4 MET B  81  ASN B  89 -1  N  ALA B  82   O  PHE B  43           
SHEET    4   C 4 LEU B  99  LEU B 101 -1  N  LEU B  99   O  ILE B  83           
SHEET    1   D 3 MET B 113  LEU B 117  0                                        
SHEET    2   D 3 LEU B 131  LYS B 136 -1  O  TRP B 132   N  LEU B 117           
SHEET    3   D 3 LYS B 171  LEU B 176 -1  N  LYS B 171   O  TRP B 135           
SHEET    1   E 4 THR B 162  PRO B 168  0                                        
SHEET    2   E 4 GLN B 146  PRO B 154 -1  O  CYS B 148   N  LEU B 167           
SHEET    3   E 4 TYR B 185  ARG B 193 -1  N  THR B 186   O  GLN B 153           
SHEET    4   E 4 LEU B 207  LEU B 209 -1  N  LEU B 207   O  LEU B 187           
SHEET    1   F 3 SER D   9  HIS D  16  0                                        
SHEET    2   F 3 SER D  21  GLU D  27 -1  O  SER D  21   N  HIS D  16           
SHEET    3   F 3 ILE D  70  PRO D  71 -1  N  ILE D  70   O  LEU D  22           
SHEET    1   G 4 THR D  55  VAL D  60  0                                        
SHEET    2   G 4 PHE D  38  ARG D  44 -1  N  LEU D  40   O  CYS D  59           
SHEET    3   G 4 MET D  81  ASN D  89 -1  N  ALA D  82   O  PHE D  43           
SHEET    4   G 4 GLY D  92  GLU D  95 -1  O  GLY D  92   N  ASN D  89           
SHEET    1   H 4 THR D  55  VAL D  60  0                                        
SHEET    2   H 4 PHE D  38  ARG D  44 -1  N  LEU D  40   O  CYS D  59           
SHEET    3   H 4 MET D  81  ASN D  89 -1  N  ALA D  82   O  PHE D  43           
SHEET    4   H 4 LEU D  99  LEU D 101 -1  N  LEU D  99   O  ILE D  83           
SHEET    1   I 3 MET D 113  ALA D 116  0                                        
SHEET    2   I 3 CYS D 130  LYS D 136 -1  O  SER D 134   N  GLN D 115           
SHEET    3   I 3 LYS D 171  CYS D 177 -1  N  LYS D 171   O  TRP D 135           
SHEET    1   J 3 THR D 162  PRO D 168  0                                        
SHEET    2   J 3 GLN D 146  PRO D 154 -1  N  CYS D 148   O  LEU D 167           
SHEET    3   J 3 TYR D 185  ARG D 193 -1  N  THR D 186   O  GLN D 153           
SHEET    1   K 3 SER F   9  HIS F  16  0                                        
SHEET    2   K 3 SER F  21  GLU F  27 -1  O  SER F  21   N  HIS F  16           
SHEET    3   K 3 ASN F  67  PRO F  71 -1  O  CYS F  68   N  CYS F  24           
SHEET    1   L 4 THR F  55  VAL F  60  0                                        
SHEET    2   L 4 SER F  37  ARG F  44 -1  N  LEU F  40   O  CYS F  59           
SHEET    3   L 4 MET F  81  ASN F  89 -1  N  ALA F  82   O  PHE F  43           
SHEET    4   L 4 GLY F  92  GLU F  95 -1  N  GLY F  92   O  ASN F  89           
SHEET    1   M 4 THR F  55  VAL F  60  0                                        
SHEET    2   M 4 SER F  37  ARG F  44 -1  N  LEU F  40   O  CYS F  59           
SHEET    3   M 4 MET F  81  ASN F  89 -1  N  ALA F  82   O  PHE F  43           
SHEET    4   M 4 LEU F  99  LEU F 101 -1  N  LEU F  99   O  ILE F  83           
SHEET    1   N 3 MET F 113  LEU F 117  0                                        
SHEET    2   N 3 LEU F 131  LYS F 136 -1  O  TRP F 132   N  LEU F 117           
SHEET    3   N 3 LYS F 171  LEU F 176 -1  N  LYS F 171   O  TRP F 135           
SHEET    1   O 4 THR F 162  PRO F 168  0                                        
SHEET    2   O 4 GLN F 146  PRO F 154 -1  O  CYS F 148   N  LEU F 167           
SHEET    3   O 4 TYR F 185  ARG F 193 -1  N  THR F 186   O  GLN F 153           
SHEET    4   O 4 LEU F 207  LEU F 209 -1  N  LEU F 207   O  LEU F 187           
SHEET    1   P 3 SER H   9  HIS H  16  0                                        
SHEET    2   P 3 SER H  21  GLU H  27 -1  O  SER H  21   N  HIS H  16           
SHEET    3   P 3 ILE H  70  PRO H  71 -1  N  ILE H  70   O  LEU H  22           
SHEET    1   Q 4 THR H  55  VAL H  60  0                                        
SHEET    2   Q 4 PHE H  38  ARG H  44 -1  N  LEU H  40   O  CYS H  59           
SHEET    3   Q 4 MET H  81  ASN H  89 -1  N  ALA H  82   O  PHE H  43           
SHEET    4   Q 4 GLY H  92  GLU H  95 -1  O  GLY H  92   N  ASN H  89           
SHEET    1   R 4 THR H  55  VAL H  60  0                                        
SHEET    2   R 4 PHE H  38  ARG H  44 -1  N  LEU H  40   O  CYS H  59           
SHEET    3   R 4 MET H  81  ASN H  89 -1  N  ALA H  82   O  PHE H  43           
SHEET    4   R 4 LEU H  99  LEU H 101 -1  N  LEU H  99   O  ILE H  83           
SHEET    1   S 3 MET H 113  ALA H 116  0                                        
SHEET    2   S 3 CYS H 130  LYS H 136 -1  O  SER H 134   N  GLN H 115           
SHEET    3   S 3 LYS H 171  CYS H 177 -1  N  LYS H 171   O  TRP H 135           
SHEET    1   T 3 THR H 162  PRO H 168  0                                        
SHEET    2   T 3 GLN H 146  PRO H 154 -1  N  CYS H 148   O  LEU H 167           
SHEET    3   T 3 TYR H 185  ARG H 193 -1  N  THR H 186   O  GLN H 153           
SSBOND   1 CYS A   37    CYS A   43                          1555   1555  2.05  
SSBOND   2 CYS A   65    CYS A   75                          1555   1555  2.05  
SSBOND   3 CYS B   13    CYS B   24                          1555   1555  2.05  
SSBOND   4 CYS B   49    CYS B  100                          1555   1555  2.04  
SSBOND   5 CYS B   59    CYS B   68                          1555   1555  2.06  
SSBOND   6 CYS B  130    CYS B  177                          1555   1555  2.05  
SSBOND   7 CYS B  148    CYS B  191                          1555   1555  2.06  
SSBOND   8 CYS C   37    CYS C   43                          1555   1555  2.05  
SSBOND   9 CYS C   65    CYS C   75                          1555   1555  2.05  
SSBOND  10 CYS D   13    CYS D   24                          1555   1555  2.04  
SSBOND  11 CYS D   49    CYS D  100                          1555   1555  2.04  
SSBOND  12 CYS D   59    CYS D   68                          1555   1555  2.05  
SSBOND  13 CYS D  130    CYS D  177                          1555   1555  2.04  
SSBOND  14 CYS D  148    CYS D  191                          1555   1555  2.04  
SSBOND  15 CYS E   37    CYS E   43                          1555   1555  2.05  
SSBOND  16 CYS E   65    CYS E   75                          1555   1555  2.06  
SSBOND  17 CYS F   13    CYS F   24                          1555   1555  2.05  
SSBOND  18 CYS F   49    CYS F  100                          1555   1555  2.04  
SSBOND  19 CYS F   59    CYS F   68                          1555   1555  2.06  
SSBOND  20 CYS F  130    CYS F  177                          1555   1555  2.05  
SSBOND  21 CYS F  148    CYS F  191                          1555   1555  2.06  
SSBOND  22 CYS G   37    CYS G   43                          1555   1555  2.05  
SSBOND  23 CYS G   65    CYS G   75                          1555   1555  2.05  
SSBOND  24 CYS H   13    CYS H   24                          1555   1555  2.04  
SSBOND  25 CYS H   49    CYS H  100                          1555   1555  2.04  
SSBOND  26 CYS H   59    CYS H   68                          1555   1555  2.05  
SSBOND  27 CYS H  130    CYS H  177                          1555   1555  2.04  
SSBOND  28 CYS H  148    CYS H  191                          1555   1555  2.04  
CRYST1  125.725  125.725  373.305  90.00  90.00  90.00 P 43 21 2    32          
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      0.007954  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007954  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002679        0.00000                         
MTRIX1   1  0.782470  0.615410 -0.094930       -8.59733    1                    
MTRIX2   1  0.617860 -0.786270 -0.004440       37.67540    1                    
MTRIX3   1 -0.077370 -0.055180 -0.995470       82.13613    1                    
MTRIX1   2 -0.803720  0.594980  0.006230      191.32515    1                    
MTRIX2   2  0.592860  0.799870  0.093430      -76.77528    1                    
MTRIX3   2  0.050610  0.078790 -0.995610      291.03754    1                    
MTRIX1   3  0.859160  0.487120 -0.156710       -6.19321    1                    
MTRIX2   3  0.489070 -0.871780 -0.028550       57.74374    1                    
MTRIX3   3 -0.150530 -0.052110 -0.987230       90.00829    1                    
MTRIX1   4 -0.867060  0.497540  0.025530      200.76083    1                    
MTRIX2   4  0.495920  0.857080  0.139540      -73.60762    1                    
MTRIX3   4  0.047550  0.133650 -0.989890      288.21735    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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