GenomeNet

Database: PDB
Entry: 2D9Q
LinkDB: 2D9Q
Original site: 2D9Q 
HEADER    SIGNALING PROTEIN/CYTOKINE              12-DEC-05   2D9Q              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN GCSF-RECEPTOR SIGNALING COMPLEX        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CSF3;                                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-174;                                            
COMPND   5 SYNONYM: GRANULOCYTE COLONY STIMULATING FACTOR, GCSF;                
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: GRANULOCYTE COLONY-STIMULATING FACTOR RECEPTOR;            
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: IG-CRH DOMAIN;                                             
COMPND  11 SYNONYM: G-CSF-R, CD114 ANTIGEN, GCSF-R;                             
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  13 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  15 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: BACUROVIRUS                           
KEYWDS    CYTOKINE, LIGAND-RECEPTOR COMPLEX, SIGNALING PROTEIN-CYTOKINE COMPLEX 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.TAMADA,R.KUROKI                                                     
REVDAT   6   10-NOV-21 2D9Q    1       SEQADV HETSYN                            
REVDAT   5   29-JUL-20 2D9Q    1       COMPND REMARK SEQADV HETNAM              
REVDAT   5 2                   1       LINK   SITE   ATOM                       
REVDAT   4   13-JUL-11 2D9Q    1       VERSN                                    
REVDAT   3   24-FEB-09 2D9Q    1       VERSN                                    
REVDAT   2   20-JUN-06 2D9Q    1       JRNL                                     
REVDAT   1   07-FEB-06 2D9Q    0                                                
JRNL        AUTH   T.TAMADA,E.HONJO,Y.MAEDA,T.OKAMOTO,M.ISHIBASHI,M.TOKUNAGA,   
JRNL        AUTH 2 R.KUROKI                                                     
JRNL        TITL   HOMODIMERIC CROSS-OVER STRUCTURE OF THE HUMAN GRANULOCYTE    
JRNL        TITL 2 COLONY-STIMULATING FACTOR (GCSF) RECEPTOR SIGNALING COMPLEX  
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 103  3135 2006              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   16492764                                                     
JRNL        DOI    10.1073/PNAS.0511264103                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.HONJO,T.TAMADA,Y.MEADA,T.KOSHIBA,Y.MATSUKURA,T.OKAMOTO,    
REMARK   1  AUTH 2 M.ISHIBASHI,M.TOKUNAGA,R.KUROKI                              
REMARK   1  TITL   CRYSTALLIZATION OF A 2:2 COMPLEX OF GRANULOCYTE-COLONY       
REMARK   1  TITL 2 STIMULATING FACTOR (GCSF) WITH THE LIGAND-BINDING REGION OF  
REMARK   1  TITL 3 THE GCSF RECEPTOR                                            
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  61   788 2005              
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  DOI    10.1107/S1744309105023080                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   S.MINE,T.KOSHIBA,E.HONJO,T.OKAMOTO,T.TAMADA,Y.MAEDA,         
REMARK   1  AUTH 2 Y.MATSUKURA,A.HORIE,M.ISHIBASHI,M.SATO,M.AZUMA,M.TOKUNAGA,   
REMARK   1  AUTH 3 K.NITTA,R.KUROKI                                             
REMARK   1  TITL   THERMODYNAMIC ANALYSIS OF THE ACTIVATION MECHANISM OF THE    
REMARK   1  TITL 2 GCSF RECEPTOR INDUCED BY LIGAND BINDING                      
REMARK   1  REF    BIOCHEMISTRY                  V.  43  2458 2004              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   14992583                                                     
REMARK   1  DOI    10.1021/BI0356855                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.19                                        
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 23837                          
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) : 0.253                           
REMARK   3   R VALUE            (WORKING SET) : 0.251                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1264                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1494                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4390                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 60                           
REMARK   3   BIN FREE R VALUE                    : 0.4390                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3605                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 14                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 68.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.32000                                              
REMARK   3    B22 (A**2) : 3.32000                                              
REMARK   3    B33 (A**2) : -4.98000                                             
REMARK   3    B12 (A**2) : 1.66000                                              
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): 0.464         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.327         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.302         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.388        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.914                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.895                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3738 ; 0.037 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  3371 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5105 ; 2.975 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7893 ; 1.182 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   464 ; 8.748 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   576 ; 0.143 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4085 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   660 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1037 ; 0.314 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4287 ; 0.296 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2406 ; 0.126 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   169 ; 0.241 ; 0.500       
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):    17 ; 0.350 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    54 ; 0.308 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.347 ; 0.500       
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):  2340 ; 2.089 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3773 ; 3.667 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1398 ; 1.878 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1332 ; 3.209 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 2D9Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-DEC-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000025161.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-FEB-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL38B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25214                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR AND MOLECULAR            
REMARK 200  REPLACEMENT                                                         
REMARK 200 SOFTWARE USED: MLPHARE, SHARP, PHASER                                
REMARK 200 STARTING MODEL: PDB ENTRY 1CD9                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 76.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM PHOSPHATE, PH 4.8, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.31200            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       35.15600            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       35.15600            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       70.31200            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       35.15600            
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     THR A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     SER B   215                                                      
REMARK 465     PRO B   216                                                      
REMARK 465     GLU B   217                                                      
REMARK 465     ALA B   218                                                      
REMARK 465     ALA B   219                                                      
REMARK 465     PRO B   220                                                      
REMARK 465     PRO B   221                                                      
REMARK 465     ARG B   309                                                      
REMARK 465     ALA B   310                                                      
REMARK 465     ALA B   311                                                      
REMARK 465     ALA B   312                                                      
REMARK 465     PRO B   313                                                      
REMARK 465     ARG B   314                                                      
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    PRO B   276     CG2  THR B   278              1.99            
REMARK 500   O    ASP B    33     N    GLU B    35              2.12            
REMARK 500   O    SER A   159     N    LEU A   161              2.19            
REMARK 500   NE2  GLN A    20     O    HOH A   176              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    TYR A  39   CE1   TYR A  39   CZ     -0.082                       
REMARK 500    PHE A 113   CE2   PHE A 113   CD2    -0.123                       
REMARK 500    ARG A 147   CG    ARG A 147   CD      0.183                       
REMARK 500    ARG A 166   CB    ARG A 166   CG      0.178                       
REMARK 500    THR B 146   CA    THR B 146   CB      0.160                       
REMARK 500    MET B 208   CB    MET B 208   CG      0.227                       
REMARK 500    MET B 208   CG    MET B 208   SD      0.374                       
REMARK 500    TRP B 230   CE3   TRP B 230   CZ3    -0.102                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
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   ATM2   ATM3                                     
REMARK 500    LEU A  15   CB  -  CG  -  CD1 ANGL. DEV. = -10.3 DEGREES          
REMARK 500    LEU A  69   CB  -  CA  -  C   ANGL. DEV. =  11.9 DEGREES          
REMARK 500    VAL A 151   CB  -  CA  -  C   ANGL. DEV. = -11.6 DEGREES          
REMARK 500    CYS B   3   CA  -  CB  -  SG  ANGL. DEV. = -11.5 DEGREES          
REMARK 500    ASP B  17   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ILE B 118   CG1 -  CB  -  CG2 ANGL. DEV. = -17.9 DEGREES          
REMARK 500    PRO B 123   N   -  CD  -  CG  ANGL. DEV. = -12.1 DEGREES          
REMARK 500    ASP B 153   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    GLU B 183   OE1 -  CD  -  OE2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    ASP B 200   CB  -  CG  -  OD1 ANGL. DEV. =   9.6 DEGREES          
REMARK 500    MET B 208   CB  -  CG  -  SD  ANGL. DEV. =  19.6 DEGREES          
REMARK 500    ARG B 251   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    LEU B 258   CA  -  CB  -  CG  ANGL. DEV. =  17.3 DEGREES          
REMARK 500    LEU B 264   CB  -  CG  -  CD1 ANGL. DEV. = -13.4 DEGREES          
REMARK 500    PRO B 290   N   -  CD  -  CG  ANGL. DEV. = -13.2 DEGREES          
REMARK 500    ARG B 305   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
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    TYR A  39        0.13   -160.10                                   
REMARK 500    LEU A  41       76.64   -100.62                                   
REMARK 500    GLU A  46       -5.83    -50.20                                   
REMARK 500    SER A  53      -18.62    -44.79                                   
REMARK 500    LEU A  61       64.16   -161.07                                   
REMARK 500    PRO A  65      -46.41    -24.68                                   
REMARK 500    SER A  66       27.90   -174.36                                   
REMARK 500    ALA A  68     -144.30    169.75                                   
REMARK 500    LEU A  71     -107.16    -62.17                                   
REMARK 500    ALA A  72      159.89    -18.37                                   
REMARK 500    LEU A  78      -98.70    -28.43                                   
REMARK 500    HIS A  79      -60.10    -11.17                                   
REMARK 500    ILE A  95      -82.04     64.21                                   
REMARK 500    LEU A  99      -68.31    -98.34                                   
REMARK 500    ILE A 117      -60.41    -92.68                                   
REMARK 500    GLN A 120      -36.90    -32.28                                   
REMARK 500    PRO A 128      147.02    -28.68                                   
REMARK 500    PRO A 132      152.00    -44.51                                   
REMARK 500    PRO A 138      170.98    -59.06                                   
REMARK 500    ALA A 139      -84.55    -58.35                                   
REMARK 500    LEU A 157      -38.79    -37.49                                   
REMARK 500    PHE A 160      -22.88    -35.31                                   
REMARK 500    VAL A 167       -3.80    -51.94                                   
REMARK 500    LEU A 171      -15.40    -47.66                                   
REMARK 500    SER B   9      -70.60    -66.76                                   
REMARK 500    LEU B  15      -82.22     17.66                                   
REMARK 500    SER B  30      118.45    164.36                                   
REMARK 500    HIS B  31      -81.04    -59.01                                   
REMARK 500    PRO B  34      -26.46     -2.71                                   
REMARK 500    GLU B  35      -64.94    -20.49                                   
REMARK 500    LEU B  42       46.78   -109.32                                   
REMARK 500    PRO B  48     -167.81    -49.00                                   
REMARK 500    GLN B  53     -141.40    -82.42                                   
REMARK 500    SER B  56      -83.76    103.98                                   
REMARK 500    THR B  59      138.60    -30.52                                   
REMARK 500    GLN B  60       61.40   -105.29                                   
REMARK 500    PRO B  67      -74.50    -63.82                                   
REMARK 500    LEU B  69       96.00    -58.27                                   
REMARK 500    ASN B  70       31.48    -99.92                                   
REMARK 500    LEU B  80     -154.29    -96.29                                   
REMARK 500    ASN B  84       77.33   -105.25                                   
REMARK 500    SER B  85      137.32    176.25                                   
REMARK 500    ASN B 105       42.21     79.52                                   
REMARK 500    PRO B 125      130.03    -34.63                                   
REMARK 500    PRO B 130      105.37    -59.21                                   
REMARK 500    SER B 140     -162.19   -128.22                                   
REMARK 500    CYS B 144       -8.24     57.30                                   
REMARK 500    THR B 146       99.44    -56.05                                   
REMARK 500    GLN B 147      123.86    -39.29                                   
REMARK 500    ASP B 158      108.05    -16.91                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      60 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2D9Q A    1   174  UNP    P09919   CSF3_HUMAN      31    204             
DBREF  2D9Q B    2   309  UNP    Q99062   CSF3R_HUMAN     25    332             
SEQADV 2D9Q SER B   79  UNP  Q99062    CYS   102 ENGINEERED MUTATION            
SEQADV 2D9Q SER B  164  UNP  Q99062    CYS   187 ENGINEERED MUTATION            
SEQADV 2D9Q SER B  229  UNP  Q99062    CYS   252 ENGINEERED MUTATION            
SEQADV 2D9Q ALA B  310  UNP  Q99062              CLONING ARTIFACT               
SEQADV 2D9Q ALA B  311  UNP  Q99062              CLONING ARTIFACT               
SEQADV 2D9Q ALA B  312  UNP  Q99062              CLONING ARTIFACT               
SEQADV 2D9Q PRO B  313  UNP  Q99062              CLONING ARTIFACT               
SEQADV 2D9Q ARG B  314  UNP  Q99062              CLONING ARTIFACT               
SEQRES   1 A  174  THR PRO LEU GLY PRO ALA SER SER LEU PRO GLN SER PHE          
SEQRES   2 A  174  LEU LEU LYS CYS LEU GLU GLN VAL ARG LYS ILE GLN GLY          
SEQRES   3 A  174  ASP GLY ALA ALA LEU GLN GLU LYS LEU CYS ALA THR TYR          
SEQRES   4 A  174  LYS LEU CYS HIS PRO GLU GLU LEU VAL LEU LEU GLY HIS          
SEQRES   5 A  174  SER LEU GLY ILE PRO TRP ALA PRO LEU SER SER CYS PRO          
SEQRES   6 A  174  SER GLN ALA LEU GLN LEU ALA GLY CYS LEU SER GLN LEU          
SEQRES   7 A  174  HIS SER GLY LEU PHE LEU TYR GLN GLY LEU LEU GLN ALA          
SEQRES   8 A  174  LEU GLU GLY ILE SER PRO GLU LEU GLY PRO THR LEU ASP          
SEQRES   9 A  174  THR LEU GLN LEU ASP VAL ALA ASP PHE ALA THR THR ILE          
SEQRES  10 A  174  TRP GLN GLN MET GLU GLU LEU GLY MET ALA PRO ALA LEU          
SEQRES  11 A  174  GLN PRO THR GLN GLY ALA MET PRO ALA PHE ALA SER ALA          
SEQRES  12 A  174  PHE GLN ARG ARG ALA GLY GLY VAL LEU VAL ALA SER HIS          
SEQRES  13 A  174  LEU GLN SER PHE LEU GLU VAL SER TYR ARG VAL LEU ARG          
SEQRES  14 A  174  HIS LEU ALA GLN PRO                                          
SEQRES   1 B  313  GLU CYS GLY HIS ILE SER VAL SER ALA PRO ILE VAL HIS          
SEQRES   2 B  313  LEU GLY ASP PRO ILE THR ALA SER CYS ILE ILE LYS GLN          
SEQRES   3 B  313  ASN CYS SER HIS LEU ASP PRO GLU PRO GLN ILE LEU TRP          
SEQRES   4 B  313  ARG LEU GLY ALA GLU LEU GLN PRO GLY GLY ARG GLN GLN          
SEQRES   5 B  313  ARG LEU SER ASP GLY THR GLN GLU SER ILE ILE THR LEU          
SEQRES   6 B  313  PRO HIS LEU ASN HIS THR GLN ALA PHE LEU SER CYS SER          
SEQRES   7 B  313  LEU ASN TRP GLY ASN SER LEU GLN ILE LEU ASP GLN VAL          
SEQRES   8 B  313  GLU LEU ARG ALA GLY TYR PRO PRO ALA ILE PRO HIS ASN          
SEQRES   9 B  313  LEU SER CYS LEU MET ASN LEU THR THR SER SER LEU ILE          
SEQRES  10 B  313  CYS GLN TRP GLU PRO GLY PRO GLU THR HIS LEU PRO THR          
SEQRES  11 B  313  SER PHE THR LEU LYS SER PHE LYS SER ARG GLY ASN CYS          
SEQRES  12 B  313  GLN THR GLN GLY ASP SER ILE LEU ASP CYS VAL PRO LYS          
SEQRES  13 B  313  ASP GLY GLN SER HIS CYS SER ILE PRO ARG LYS HIS LEU          
SEQRES  14 B  313  LEU LEU TYR GLN ASN MET GLY ILE TRP VAL GLN ALA GLU          
SEQRES  15 B  313  ASN ALA LEU GLY THR SER MET SER PRO GLN LEU CYS LEU          
SEQRES  16 B  313  ASP PRO MET ASP VAL VAL LYS LEU GLU PRO PRO MET LEU          
SEQRES  17 B  313  ARG THR MET ASP PRO SER PRO GLU ALA ALA PRO PRO GLN          
SEQRES  18 B  313  ALA GLY CYS LEU GLN LEU SER TRP GLU PRO TRP GLN PRO          
SEQRES  19 B  313  GLY LEU HIS ILE ASN GLN LYS CYS GLU LEU ARG HIS LYS          
SEQRES  20 B  313  PRO GLN ARG GLY GLU ALA SER TRP ALA LEU VAL GLY PRO          
SEQRES  21 B  313  LEU PRO LEU GLU ALA LEU GLN TYR GLU LEU CYS GLY LEU          
SEQRES  22 B  313  LEU PRO ALA THR ALA TYR THR LEU GLN ILE ARG CYS ILE          
SEQRES  23 B  313  ARG TRP PRO LEU PRO GLY HIS TRP SER ASP TRP SER PRO          
SEQRES  24 B  313  SER LEU GLU LEU ARG THR THR GLU ARG ALA ALA ALA PRO          
SEQRES  25 B  313  ARG                                                          
MODRES 2D9Q ASN B  111  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   4  HOH   *14(H2 O)                                                     
HELIX    1   1 PRO A   10  ALA A   37  1                                  28    
HELIX    2   2 LEU A   47  GLY A   55  1                                   9    
HELIX    3   3 GLY A   73  ALA A   91  1                                  19    
HELIX    4   4 LEU A   99  GLU A  123  1                                  25    
HELIX    5   5 SER A  142  HIS A  170  1                                  29    
HELIX    6   6 LYS B  168  LEU B  170  5                                   3    
HELIX    7   7 ASP B  197  ASP B  200  5                                   4    
HELIX    8   8 TRP B  233  LEU B  237  5                                   5    
SHEET    1   A 4 ILE B   6  VAL B   8  0                                        
SHEET    2   A 4 ILE B  19  CYS B  23 -1  O  SER B  22   N  SER B   7           
SHEET    3   A 4 SER B  62  LEU B  66 -1  O  SER B  62   N  CYS B  23           
SHEET    4   A 4 ARG B  51  GLN B  52 -1  N  ARG B  51   O  ILE B  63           
SHEET    1   B 4 ILE B  12  VAL B  13  0                                        
SHEET    2   B 4 LEU B  86  ALA B  96  1  O  ARG B  95   N  VAL B  13           
SHEET    3   B 4 GLN B  73  ASN B  81 -1  N  ALA B  74   O  LEU B  94           
SHEET    4   B 4 LEU B  39  ARG B  41 -1  N  LEU B  39   O  SER B  79           
SHEET    1   C 4 HIS B 162  PRO B 166  0                                        
SHEET    2   C 4 SER B 116  GLU B 122 -1  N  LEU B 117   O  ILE B 165           
SHEET    3   C 4 HIS B 104  ASN B 111 -1  N  LEU B 109   O  ILE B 118           
SHEET    4   C 4 VAL B 202  LYS B 203  1  O  LYS B 203   N  MET B 110           
SHEET    1   D 4 ILE B 151  CYS B 154  0                                        
SHEET    2   D 4 SER B 132  LYS B 139 -1  N  SER B 137   O  LEU B 152           
SHEET    3   D 4 MET B 176  ASN B 184 -1  O  GLN B 181   N  THR B 134           
SHEET    4   D 4 GLY B 187  MET B 190 -1  O  SER B 189   N  ALA B 182           
SHEET    1   E 4 ILE B 151  CYS B 154  0                                        
SHEET    2   E 4 SER B 132  LYS B 139 -1  N  SER B 137   O  LEU B 152           
SHEET    3   E 4 MET B 176  ASN B 184 -1  O  GLN B 181   N  THR B 134           
SHEET    4   E 4 LEU B 194  LEU B 196 -1  O  LEU B 194   N  ILE B 178           
SHEET    1   F 3 MET B 208  THR B 211  0                                        
SHEET    2   F 3 LEU B 226  GLU B 231 -1  O  SER B 229   N  ARG B 210           
SHEET    3   F 3 ALA B 266  LEU B 271 -1  O  TYR B 269   N  LEU B 228           
SHEET    1   G 4 ALA B 257  LEU B 262  0                                        
SHEET    2   G 4 GLN B 241  PRO B 249 -1  N  CYS B 243   O  LEU B 262           
SHEET    3   G 4 TYR B 280  ARG B 288 -1  O  ILE B 287   N  LYS B 242           
SHEET    4   G 4 LEU B 302  LEU B 304 -1  O  LEU B 304   N  TYR B 280           
SSBOND   1 CYS A   36    CYS A   42                          1555   1555  2.25  
SSBOND   2 CYS A   64    CYS A   74                          1555   1555  2.09  
SSBOND   3 CYS B    3    CYS B   29                          1555   1555  2.09  
SSBOND   4 CYS B   23    CYS B   78                          1555   1555  2.07  
SSBOND   5 CYS B  108    CYS B  119                          1555   1555  2.21  
SSBOND   6 CYS B  144    CYS B  195                          1555   1555  2.11  
SSBOND   7 CYS B  154    CYS B  163                          1555   1555  2.20  
SSBOND   8 CYS B  225    CYS B  272                          1555   1555  2.12  
SSBOND   9 CYS B  243    CYS B  286                          1555   1555  2.16  
LINK         ND2 ASN B 111                 C1  NAG C   1     1555   1555  1.43  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.47  
CRYST1  134.777  134.777  105.468  90.00  90.00 120.00 P 32 2 1      6          
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      0.007420  0.004284  0.000000        0.00000                         
SCALE2      0.000000  0.008567  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009482        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system