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Database: PDB
Entry: 5GW9
LinkDB: 5GW9
Original site: 5GW9 
HEADER    CYTOKINE                                09-SEP-16   5GW9              
TITLE     CRYSTAL STRUCTURE OF C163, A BACKBONE CIRCULARIZED G-CSF              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GRANULOCYTE COLONY-STIMULATING FACTOR;                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 40-202;                                       
COMPND   5 SYNONYM: G-CSF,PLURIPOIETIN;                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: 1ST SER AND 173RD GLY ARE CONNECTED WITH A PEPTIDE    
COMPND   9 BOND.                                                                
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CSF3, C17ORF33, GCSF;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    CYTOKINE, FOUR-HELIX BUNDLE, BACKBONE CIRCULATIZATION                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.MIYAFUSA,S.HONDA                                                    
REVDAT   3   16-MAY-18 5GW9    1       JRNL                                     
REVDAT   2   25-APR-18 5GW9    1       JRNL                                     
REVDAT   1   13-SEP-17 5GW9    0                                                
JRNL        AUTH   T.MIYAFUSA,R.SHIBUYA,S.HONDA                                 
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE BACKBONE-CIRCULARIZED           
JRNL        TITL 2 GRANULOCYTE COLONY-STIMULATING FACTOR CONTAINING A SHORT     
JRNL        TITL 3 CONNECTOR.                                                   
JRNL        REF    BIOCHEM. BIOPHYS. RES.        V. 500   224 2018              
JRNL        REF  2 COMMUN.                                                      
JRNL        REFN                   ESSN 1090-2104                               
JRNL        PMID   29634929                                                     
JRNL        DOI    10.1016/J.BBRC.2018.04.045                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.08                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 84608                          
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) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4463                            
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) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6255                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2470                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 345                          
REMARK   3   BIN FREE R VALUE                    : 0.2770                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4940                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 478                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.45                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.09000                                             
REMARK   3    B22 (A**2) : -0.09000                                             
REMARK   3    B33 (A**2) : 0.28000                                              
REMARK   3    B12 (A**2) : -0.04000                                             
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.092         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.096         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.043         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5490 ; 0.034 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5285 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7516 ; 2.719 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 12221 ; 1.589 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   747 ; 5.847 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   218 ;36.865 ;24.587       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   934 ;16.362 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;16.459 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   845 ; 0.217 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6518 ; 0.015 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1256 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2847 ; 2.389 ; 2.177       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2846 ; 2.388 ; 2.177       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3641 ; 3.149 ; 3.253       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3642 ; 3.149 ; 3.253       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2643 ; 3.901 ; 2.557       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2644 ; 3.900 ; 2.557       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3876 ; 5.657 ; 3.700       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6900 ; 7.328 ;19.087       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  6723 ; 7.295 ;18.578       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    11        A   173                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6350 127.3980  -9.9480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0824 T22:   0.0484                                     
REMARK   3      T33:   0.0459 T12:   0.0370                                     
REMARK   3      T13:  -0.0347 T23:  -0.0194                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2837 L22:   1.0332                                     
REMARK   3      L33:   1.1441 L12:   0.2814                                     
REMARK   3      L13:   0.2007 L23:   0.7863                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0459 S12:   0.0362 S13:  -0.0115                       
REMARK   3      S21:   0.0811 S22:  -0.0127 S23:   0.0024                       
REMARK   3      S31:   0.1275 S32:   0.1309 S33:  -0.0333                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    11        B   173                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6470 118.9010  14.7190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0844 T22:   0.0520                                     
REMARK   3      T33:   0.0441 T12:  -0.0387                                     
REMARK   3      T13:   0.0357 T23:  -0.0189                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3384 L22:   1.0827                                     
REMARK   3      L33:   1.1637 L12:  -0.3344                                     
REMARK   3      L13:  -0.2070 L23:   0.8255                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0434 S12:  -0.0290 S13:   0.0145                       
REMARK   3      S21:  -0.0762 S22:  -0.0132 S23:   0.0076                       
REMARK   3      S31:  -0.1330 S32:   0.1376 S33:  -0.0302                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    11        C   173                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.8750 146.8680 -15.0290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0869 T22:   0.0406                                     
REMARK   3      T33:   0.0455 T12:   0.0340                                     
REMARK   3      T13:   0.0307 T23:   0.0197                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0946 L22:   0.2396                                     
REMARK   3      L33:   1.1843 L12:  -0.1580                                     
REMARK   3      L13:  -0.7559 L23:   0.1652                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0428 S12:   0.0814 S13:   0.0097                       
REMARK   3      S21:   0.0377 S22:  -0.0159 S23:   0.0142                       
REMARK   3      S31:  -0.1865 S32:  -0.0486 S33:  -0.0269                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    11        D   173                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.5950 152.2150  19.8050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0919 T22:   0.0415                                     
REMARK   3      T33:   0.0425 T12:  -0.0328                                     
REMARK   3      T13:  -0.0326 T23:   0.0210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1232 L22:   0.2694                                     
REMARK   3      L33:   1.1316 L12:   0.1702                                     
REMARK   3      L13:   0.7863 L23:   0.2377                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0457 S12:  -0.0780 S13:  -0.0067                       
REMARK   3      S21:  -0.0362 S22:  -0.0129 S23:   0.0131                       
REMARK   3      S31:   0.1800 S32:  -0.0470 S33:  -0.0328                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5GW9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1300001584.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 89146                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 35.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2D9Q                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4M AMMONIUM SULFATE, EVAPORATION,      
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
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                                                                      
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      119.00600            
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       59.50300            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -30.47050            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -52.77645            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
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   OE1  GLN B    91     O    HOH B   201              1.68            
REMARK 500   NE2  GLN C    91     O    HOH C   201              1.87            
REMARK 500   OE1  GLN D    91     O    HOH D   201              1.89            
REMARK 500   OE1  GLN A    91     O    HOH A   201              2.04            
REMARK 500   NH2  ARG D    23     O    HOH D   202              2.05            
REMARK 500   NE2  GLN B   121     O    HOH B   202              2.08            
REMARK 500   NE2  GLN B    87     O    HOH B   203              2.13            
REMARK 500   NE2  GLN C   121     O    HOH C   202              2.14            
REMARK 500   OD1  ASP C    28     O    HOH C   203              2.15            
REMARK 500   N    SER C    11     O    GLY C   173              2.15            
REMARK 500   N    SER A    11     O    GLY A   173              2.16            
REMARK 500   NH1  ARG B    23     O    HOH B   204              2.16            
REMARK 500   N    SER D    11     O    GLY D   173              2.19            
REMARK 500   N    SER B    11     O    GLY B   173              2.19            
REMARK 500   OD2  ASP C    28     OD2  ASP C   110              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    ARG A  23   CZ    ARG A  23   NH1     0.107                       
REMARK 500    GLU A  46   CG    GLU A  46   CD      0.108                       
REMARK 500    TYR A 166   N     TYR A 166   CA      0.135                       
REMARK 500    TYR A 166   CB    TYR A 166   CG      0.180                       
REMARK 500    TYR A 166   CZ    TYR A 166   OH      0.152                       
REMARK 500    ARG B  23   CZ    ARG B  23   NH1     0.120                       
REMARK 500    GLU B  46   CD    GLU B  46   OE2     0.111                       
REMARK 500    TYR B 166   N     TYR B 166   CA      0.136                       
REMARK 500    TYR B 166   CB    TYR B 166   CG      0.159                       
REMARK 500    TYR B 166   CZ    TYR B 166   OH      0.129                       
REMARK 500    LEU B 172   N     LEU B 172   CA     -0.126                       
REMARK 500    ARG C  23   CZ    ARG C  23   NH1     0.134                       
REMARK 500    ASP C  28   CG    ASP C  28   OD2     0.144                       
REMARK 500    TRP C  59   CG    TRP C  59   CD1     0.086                       
REMARK 500    TYR C 166   N     TYR C 166   CA      0.142                       
REMARK 500    TYR C 166   CB    TYR C 166   CG      0.156                       
REMARK 500    ARG D  23   CZ    ARG D  23   NH1     0.109                       
REMARK 500    ASP D  28   CG    ASP D  28   OD2     0.140                       
REMARK 500    SER D 156   CA    SER D 156   CB      0.133                       
REMARK 500    TYR D 166   N     TYR D 166   CA      0.123                       
REMARK 500    TYR D 166   CB    TYR D 166   CG      0.166                       
REMARK 500    TYR D 166   CZ    TYR D 166   OH      0.149                       
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  19   CB  -  CG  -  CD2 ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ARG A  23   NH1 -  CZ  -  NH2 ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ARG A  23   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG A  23   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    LEU A  50   CB  -  CG  -  CD1 ANGL. DEV. =  14.2 DEGREES          
REMARK 500    TYR A  86   CB  -  CG  -  CD1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ASP A 105   CB  -  CG  -  OD1 ANGL. DEV. =   8.6 DEGREES          
REMARK 500    ASP A 110   CB  -  CG  -  OD1 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ASP A 110   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    MET A 138   CG  -  SD  -  CE  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ARG A 147   CG  -  CD  -  NE  ANGL. DEV. = -15.7 DEGREES          
REMARK 500    ARG A 147   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ARG A 170   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG B  23   NH1 -  CZ  -  NH2 ANGL. DEV. =  10.7 DEGREES          
REMARK 500    ARG B  23   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ARG B  23   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    LEU B  50   CB  -  CG  -  CD1 ANGL. DEV. =  12.7 DEGREES          
REMARK 500    CYS B  65   CA  -  CB  -  SG  ANGL. DEV. =   7.7 DEGREES          
REMARK 500    TYR B  86   CB  -  CG  -  CD1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    TYR B  86   CZ  -  CE2 -  CD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ASP B 105   CB  -  CG  -  OD1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ASP B 110   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    MET B 122   CG  -  SD  -  CE  ANGL. DEV. = -10.1 DEGREES          
REMARK 500    LEU C  19   CB  -  CG  -  CD2 ANGL. DEV. =  14.5 DEGREES          
REMARK 500    ARG C  23   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    CYS C  65   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES          
REMARK 500    TYR C  86   CB  -  CG  -  CD1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP C 105   CB  -  CG  -  OD1 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ASP C 110   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    MET C 122   CG  -  SD  -  CE  ANGL. DEV. = -10.8 DEGREES          
REMARK 500    ARG C 147   CG  -  CD  -  NE  ANGL. DEV. = -16.0 DEGREES          
REMARK 500    ARG C 147   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG C 147   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG C 167   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    VAL C 168   CB  -  CA  -  C   ANGL. DEV. = -12.0 DEGREES          
REMARK 500    LEU C 172   CA  -  CB  -  CG  ANGL. DEV. = -19.7 DEGREES          
REMARK 500    ARG D  23   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    LEU D 104   CB  -  CG  -  CD1 ANGL. DEV. = -11.7 DEGREES          
REMARK 500    ASP D 105   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP D 110   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP D 110   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    MET D 138   CG  -  SD  -  CE  ANGL. DEV. = -15.2 DEGREES          
REMARK 500    ARG D 147   CG  -  CD  -  NE  ANGL. DEV. = -19.1 DEGREES          
REMARK 500    ARG D 147   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.1 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    ILE A  96      -52.05     61.27                                   
REMARK 500    TYR A 166      -38.79    -28.20                                   
REMARK 500    TYR A 166      -38.79    -29.22                                   
REMARK 500    ILE B  96      -55.43     66.84                                   
REMARK 500    ALA B 142       49.81    -88.89                                   
REMARK 500    TYR B 166      -38.43    -31.85                                   
REMARK 500    TYR B 166      -38.43    -31.94                                   
REMARK 500    ILE C  96      -54.15     65.89                                   
REMARK 500    ALA C 142       48.14    -89.16                                   
REMARK 500    ILE D  96      -56.82     64.07                                   
REMARK 500    ALA D 142       44.44    -85.10                                   
REMARK 500    TYR D 166      -38.22    -30.17                                   
REMARK 500    TYR D 166      -38.22    -30.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR D 166         0.06    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    LEU B 169         10.53                                           
REMARK 500    LEU C 169         11.78                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5GW9 A   11   173  UNP    P09919   CSF3_HUMAN      40    202             
DBREF  5GW9 B   11   173  UNP    P09919   CSF3_HUMAN      40    202             
DBREF  5GW9 C   11   173  UNP    P09919   CSF3_HUMAN      40    202             
DBREF  5GW9 D   11   173  UNP    P09919   CSF3_HUMAN      40    202             
SEQADV 5GW9 SER A   11  UNP  P09919    PRO    40 ENGINEERED MUTATION            
SEQADV 5GW9 SER A   18  UNP  P09919    CYS    47 ENGINEERED MUTATION            
SEQADV 5GW9 GLY A  173  UNP  P09919    ALA   202 ENGINEERED MUTATION            
SEQADV 5GW9 SER B   11  UNP  P09919    PRO    40 ENGINEERED MUTATION            
SEQADV 5GW9 SER B   18  UNP  P09919    CYS    47 ENGINEERED MUTATION            
SEQADV 5GW9 GLY B  173  UNP  P09919    ALA   202 ENGINEERED MUTATION            
SEQADV 5GW9 SER C   11  UNP  P09919    PRO    40 ENGINEERED MUTATION            
SEQADV 5GW9 SER C   18  UNP  P09919    CYS    47 ENGINEERED MUTATION            
SEQADV 5GW9 GLY C  173  UNP  P09919    ALA   202 ENGINEERED MUTATION            
SEQADV 5GW9 SER D   11  UNP  P09919    PRO    40 ENGINEERED MUTATION            
SEQADV 5GW9 SER D   18  UNP  P09919    CYS    47 ENGINEERED MUTATION            
SEQADV 5GW9 GLY D  173  UNP  P09919    ALA   202 ENGINEERED MUTATION            
SEQRES   1 A  163  SER GLN SER PHE LEU LEU LYS SER LEU GLU GLN VAL ARG          
SEQRES   2 A  163  LYS ILE GLN GLY ASP GLY ALA ALA LEU GLN GLU LYS LEU          
SEQRES   3 A  163  CYS ALA THR TYR LYS LEU CYS HIS PRO GLU GLU LEU VAL          
SEQRES   4 A  163  LEU LEU GLY HIS SER LEU GLY ILE PRO TRP ALA PRO LEU          
SEQRES   5 A  163  SER SER CYS PRO SER GLN ALA LEU GLN LEU ALA GLY CYS          
SEQRES   6 A  163  LEU SER GLN LEU HIS SER GLY LEU PHE LEU TYR GLN GLY          
SEQRES   7 A  163  LEU LEU GLN ALA LEU GLU GLY ILE SER PRO GLU LEU GLY          
SEQRES   8 A  163  PRO THR LEU ASP THR LEU GLN LEU ASP VAL ALA ASP PHE          
SEQRES   9 A  163  ALA THR THR ILE TRP GLN GLN MET GLU GLU LEU GLY MET          
SEQRES  10 A  163  ALA PRO ALA LEU GLN PRO THR GLN GLY ALA MET PRO ALA          
SEQRES  11 A  163  PHE ALA SER ALA PHE GLN ARG ARG ALA GLY GLY VAL LEU          
SEQRES  12 A  163  VAL ALA SER HIS LEU GLN SER PHE LEU GLU VAL SER TYR          
SEQRES  13 A  163  ARG VAL LEU ARG HIS LEU GLY                                  
SEQRES   1 B  163  SER GLN SER PHE LEU LEU LYS SER LEU GLU GLN VAL ARG          
SEQRES   2 B  163  LYS ILE GLN GLY ASP GLY ALA ALA LEU GLN GLU LYS LEU          
SEQRES   3 B  163  CYS ALA THR TYR LYS LEU CYS HIS PRO GLU GLU LEU VAL          
SEQRES   4 B  163  LEU LEU GLY HIS SER LEU GLY ILE PRO TRP ALA PRO LEU          
SEQRES   5 B  163  SER SER CYS PRO SER GLN ALA LEU GLN LEU ALA GLY CYS          
SEQRES   6 B  163  LEU SER GLN LEU HIS SER GLY LEU PHE LEU TYR GLN GLY          
SEQRES   7 B  163  LEU LEU GLN ALA LEU GLU GLY ILE SER PRO GLU LEU GLY          
SEQRES   8 B  163  PRO THR LEU ASP THR LEU GLN LEU ASP VAL ALA ASP PHE          
SEQRES   9 B  163  ALA THR THR ILE TRP GLN GLN MET GLU GLU LEU GLY MET          
SEQRES  10 B  163  ALA PRO ALA LEU GLN PRO THR GLN GLY ALA MET PRO ALA          
SEQRES  11 B  163  PHE ALA SER ALA PHE GLN ARG ARG ALA GLY GLY VAL LEU          
SEQRES  12 B  163  VAL ALA SER HIS LEU GLN SER PHE LEU GLU VAL SER TYR          
SEQRES  13 B  163  ARG VAL LEU ARG HIS LEU GLY                                  
SEQRES   1 C  163  SER GLN SER PHE LEU LEU LYS SER LEU GLU GLN VAL ARG          
SEQRES   2 C  163  LYS ILE GLN GLY ASP GLY ALA ALA LEU GLN GLU LYS LEU          
SEQRES   3 C  163  CYS ALA THR TYR LYS LEU CYS HIS PRO GLU GLU LEU VAL          
SEQRES   4 C  163  LEU LEU GLY HIS SER LEU GLY ILE PRO TRP ALA PRO LEU          
SEQRES   5 C  163  SER SER CYS PRO SER GLN ALA LEU GLN LEU ALA GLY CYS          
SEQRES   6 C  163  LEU SER GLN LEU HIS SER GLY LEU PHE LEU TYR GLN GLY          
SEQRES   7 C  163  LEU LEU GLN ALA LEU GLU GLY ILE SER PRO GLU LEU GLY          
SEQRES   8 C  163  PRO THR LEU ASP THR LEU GLN LEU ASP VAL ALA ASP PHE          
SEQRES   9 C  163  ALA THR THR ILE TRP GLN GLN MET GLU GLU LEU GLY MET          
SEQRES  10 C  163  ALA PRO ALA LEU GLN PRO THR GLN GLY ALA MET PRO ALA          
SEQRES  11 C  163  PHE ALA SER ALA PHE GLN ARG ARG ALA GLY GLY VAL LEU          
SEQRES  12 C  163  VAL ALA SER HIS LEU GLN SER PHE LEU GLU VAL SER TYR          
SEQRES  13 C  163  ARG VAL LEU ARG HIS LEU GLY                                  
SEQRES   1 D  163  SER GLN SER PHE LEU LEU LYS SER LEU GLU GLN VAL ARG          
SEQRES   2 D  163  LYS ILE GLN GLY ASP GLY ALA ALA LEU GLN GLU LYS LEU          
SEQRES   3 D  163  CYS ALA THR TYR LYS LEU CYS HIS PRO GLU GLU LEU VAL          
SEQRES   4 D  163  LEU LEU GLY HIS SER LEU GLY ILE PRO TRP ALA PRO LEU          
SEQRES   5 D  163  SER SER CYS PRO SER GLN ALA LEU GLN LEU ALA GLY CYS          
SEQRES   6 D  163  LEU SER GLN LEU HIS SER GLY LEU PHE LEU TYR GLN GLY          
SEQRES   7 D  163  LEU LEU GLN ALA LEU GLU GLY ILE SER PRO GLU LEU GLY          
SEQRES   8 D  163  PRO THR LEU ASP THR LEU GLN LEU ASP VAL ALA ASP PHE          
SEQRES   9 D  163  ALA THR THR ILE TRP GLN GLN MET GLU GLU LEU GLY MET          
SEQRES  10 D  163  ALA PRO ALA LEU GLN PRO THR GLN GLY ALA MET PRO ALA          
SEQRES  11 D  163  PHE ALA SER ALA PHE GLN ARG ARG ALA GLY GLY VAL LEU          
SEQRES  12 D  163  VAL ALA SER HIS LEU GLN SER PHE LEU GLU VAL SER TYR          
SEQRES  13 D  163  ARG VAL LEU ARG HIS LEU GLY                                  
FORMUL   5  HOH   *478(H2 O)                                                    
HELIX    1 AA1 SER A   11  LYS A   41  1                                  31    
HELIX    2 AA2 HIS A   44  GLY A   56  1                                  13    
HELIX    3 AA3 GLN A   71  LEU A   93  1                                  23    
HELIX    4 AA4 LEU A  100  GLY A  126  1                                  27    
HELIX    5 AA5 SER A  143  ARG A  170  1                                  28    
HELIX    6 AA6 GLN B   12  LYS B   41  1                                  30    
HELIX    7 AA7 HIS B   44  GLU B   47  5                                   4    
HELIX    8 AA8 LEU B   48  GLY B   56  1                                   9    
HELIX    9 AA9 GLN B   71  LEU B   93  1                                  23    
HELIX   10 AB1 LEU B  100  GLY B  126  1                                  27    
HELIX   11 AB2 SER B  143  ARG B  170  1                                  28    
HELIX   12 AB3 GLN C   12  LYS C   41  1                                  30    
HELIX   13 AB4 HIS C   44  GLU C   47  5                                   4    
HELIX   14 AB5 LEU C   48  GLY C   56  1                                   9    
HELIX   15 AB6 GLN C   71  LEU C   93  1                                  23    
HELIX   16 AB7 LEU C  100  GLY C  126  1                                  27    
HELIX   17 AB8 SER C  143  ARG C  170  1                                  28    
HELIX   18 AB9 GLN D   12  LYS D   41  1                                  30    
HELIX   19 AC1 HIS D   44  GLU D   47  5                                   4    
HELIX   20 AC2 LEU D   48  GLY D   56  1                                   9    
HELIX   21 AC3 GLN D   71  LEU D   93  1                                  23    
HELIX   22 AC4 LEU D  100  GLY D  126  1                                  27    
HELIX   23 AC5 SER D  143  ARG D  170  1                                  28    
SSBOND   1 CYS A   37    CYS A   43                          1555   1555  2.14  
SSBOND   2 CYS A   65    CYS A   75                          1555   1555  2.05  
SSBOND   3 CYS B   37    CYS B   43                          1555   1555  2.17  
SSBOND   4 CYS B   65    CYS B   75                          1555   1555  2.07  
SSBOND   5 CYS C   37    CYS C   43                          1555   1555  2.15  
SSBOND   6 CYS C   65    CYS C   75                          1555   1555  2.03  
SSBOND   7 CYS D   37    CYS D   43                          1555   1555  2.15  
SSBOND   8 CYS D   65    CYS D   75                          1555   1555  2.04  
LINK         N   SER A  11                 C   GLY A 173     1555   1555  1.29  
LINK         N   SER B  11                 C   GLY B 173     1555   1555  1.30  
LINK         N   SER C  11                 C   GLY C 173     1555   1555  1.28  
LINK         N   SER D  11                 C   GLY D 173     1555   1555  1.30  
CRYST1   60.941   60.941  178.509  90.00  90.00 120.00 P 32         12          
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      0.016409  0.009474  0.000000        0.00000                         
SCALE2      0.000000  0.018948  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005602        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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