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Database: PDB
Entry: 5MN2
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Original site: 5MN2 
HEADER    IMMUNE SYSTEM                           12-DEC-16   5MN2              
TITLE     COCRYSTAL STRUCTURE OF FC GAMMA RECEPTOR IIIA INTERACTING WITH AFFIMER
TITLE    2 G3, A SPECIFIC BINDING PROTEIN WHICH BLOCKS IGG BINDING TO THE       
TITLE    3 RECEPTOR.                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LOW AFFINITY IMMUNOGLOBULIN GAMMA FC REGION RECEPTOR III-A;
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CD16A ANTIGEN,FC-GAMMA RIII-ALPHA,FCRIIIA,FCR-10,IGG FC     
COMPND   5 RECEPTOR III-2;                                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: AFFIMER G3;                                                
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 VARIANT: 158F;                                                       
SOURCE   6 TISSUE: WHOLE BLOOD;                                                 
SOURCE   7 GENE: FCGR3A, CD16A, FCG3, FCGR3, IGFR3;                             
SOURCE   8 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  10 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;                                
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: POPING;                                   
SOURCE  13 MOL_ID: 2;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  15 ORGANISM_TAXID: 32630;                                               
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    FC GAMMA RECEPTOR IIIA AFFIMER ALLOSTERIC INHIBITOR FCGR3A, IMMUNE    
KEYWDS   2 SYSTEM                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.I.ROBINSON,R.L.OWEN,D.C.TOMLINSON,E.W.BAXTER,J.E.NETTLESHIP,        
AUTHOR   2 M.P.WATERHOUSE,S.A.HARRIS,R.J.OWENS,M.J.MCPHERSON,A.W.MORGAN,        
AUTHOR   3 C.TIEDE,A.GOLDMAN,M.THOMSEN                                          
REVDAT   4   31-JAN-18 5MN2    1       REMARK                                   
REVDAT   3   10-JAN-18 5MN2    1       JRNL                                     
REVDAT   2   27-DEC-17 5MN2    1       JRNL                                     
REVDAT   1   13-DEC-17 5MN2    0                                                
JRNL        AUTH   J.I.ROBINSON,E.W.BAXTER,R.L.OWEN,M.THOMSEN,D.C.TOMLINSON,    
JRNL        AUTH 2 M.P.WATERHOUSE,S.J.WIN,J.E.NETTLESHIP,C.TIEDE,R.J.FOSTER,    
JRNL        AUTH 3 R.J.OWENS,C.W.G.FISHWICK,S.A.HARRIS,A.GOLDMAN,M.J.MCPHERSON, 
JRNL        AUTH 4 A.W.MORGAN                                                   
JRNL        TITL   AFFIMER PROTEINS INHIBIT IMMUNE COMPLEX BINDING TO FC GAMMA  
JRNL        TITL 2 RIIIA WITH HIGH SPECIFICITY THROUGH COMPETITIVE AND          
JRNL        TITL 3 ALLOSTERIC MODES OF ACTION.                                  
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 115   E72 2018              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   29247053                                                     
JRNL        DOI    10.1073/PNAS.1707856115                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.12_2829: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.39                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 30208                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1510                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 43.3973 -  5.2237    0.91     2575   141  0.1988 0.2248        
REMARK   3     2  5.2237 -  4.1473    0.93     2567   131  0.1628 0.1721        
REMARK   3     3  4.1473 -  3.6233    0.94     2550   152  0.1829 0.2326        
REMARK   3     4  3.6233 -  3.2922    0.95     2597   140  0.2083 0.2700        
REMARK   3     5  3.2922 -  3.0563    0.96     2640   109  0.2338 0.2808        
REMARK   3     6  3.0563 -  2.8761    0.96     2625   137  0.2386 0.2819        
REMARK   3     7  2.8761 -  2.7321    0.97     2626   123  0.2371 0.2799        
REMARK   3     8  2.7321 -  2.6132    0.97     2622   134  0.2619 0.2997        
REMARK   3     9  2.6132 -  2.5126    0.97     2605   146  0.2784 0.3660        
REMARK   3    10  2.5126 -  2.4259    0.97     2671   132  0.2827 0.3370        
REMARK   3    11  2.4259 -  2.3501    0.97     2620   165  0.2857 0.3706        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.640           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 55.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           4311                                  
REMARK   3   ANGLE     :  0.459           5883                                  
REMARK   3   CHIRALITY :  0.041            669                                  
REMARK   3   PLANARITY :  0.003            739                                  
REMARK   3   DIHEDRAL  : 12.807           2505                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5MN2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-OCT-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200002367.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-AUG-12                          
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30227                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 51.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : 0.04900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.200                              
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: A SUBSECTION OF A COMPLEX OF AN ADHIRON BOUND TO A   
REMARK 200  SOLUBLE PROTEIN (MANUSCRIPT IN PREPARATION) WAS USED AS A SEARCH    
REMARK 200  MODEL.                                                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20.0% V/V GLYCEROL 16.0% W/V             
REMARK 280  POLYETHYLENE GLYCOL 8000 0.04 M POTASSIUM DI-HYDROGEN PHOSPHATE,    
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       29.96250            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     ARG A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     ARG B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     LEU B   118                                                      
REMARK 465     HIS B   119                                                      
REMARK 465     HIS B   135                                                      
REMARK 465     GLY B   175                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     VAL C     4                                                      
REMARK 465     ARG C     5                                                      
REMARK 465     ALA C     6                                                      
REMARK 465     VAL C     7                                                      
REMARK 465     PRO C     8                                                      
REMARK 465     GLY C     9                                                      
REMARK 465     ASN C    10                                                      
REMARK 465     GLU C    11                                                      
REMARK 465     ASN C    12                                                      
REMARK 465     GLY C   101                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     VAL D     4                                                      
REMARK 465     ARG D     5                                                      
REMARK 465     ALA D     6                                                      
REMARK 465     VAL D     7                                                      
REMARK 465     PRO D     8                                                      
REMARK 465     GLY D     9                                                      
REMARK 465     ASN D    10                                                      
REMARK 465     GLY D   101                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  22    CE   NZ                                             
REMARK 470     GLU A  36    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 103    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 114    CD   CE   NZ                                        
REMARK 470     LYS A 128    CE   NZ                                             
REMARK 470     LYS A 143    CG   CD   CE   NZ                                   
REMARK 470     LYS A 147    CG   CD   CE   NZ                                   
REMARK 470     LYS A 161    CG   CD   CE   NZ                                   
REMARK 470     LYS B   7    CE   NZ                                             
REMARK 470     GLU B  13    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  22    CG   CD   CE   NZ                                   
REMARK 470     LYS B  28    CG   CD   CE   NZ                                   
REMARK 470     GLU B  36    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  59    CG   OD1  OD2                                       
REMARK 470     ASP B  64    CG   OD1  OD2                                       
REMARK 470     GLU B  68    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 103    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 114    CG   CD   CE   NZ                                   
REMARK 470     LYS B 120    CG   CD   CE   NZ                                   
REMARK 470     VAL B 121    CG1  CG2                                            
REMARK 470     LEU B 124    CG   CD1  CD2                                       
REMARK 470     LYS B 128    CG   CD   CE   NZ                                   
REMARK 470     LYS B 131    CG   CD   CE   NZ                                   
REMARK 470     TYR B 132    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     HIS B 134    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN B 136    CG   OD1  ND2                                       
REMARK 470     PHE B 139    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 143    CG   CD   CE   NZ                                   
REMARK 470     LYS B 147    CG   CD   CE   NZ                                   
REMARK 470     ARG B 155    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 157    CG   CD1  CD2                                       
REMARK 470     PHE B 158    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 161    CG   CD   CE   NZ                                   
REMARK 470     VAL B 163    CG1  CG2                                            
REMARK 470     GLN B 174    CG   CD   OE1  NE2                                  
REMARK 470     LEU C  14    CG   CD1  CD2                                       
REMARK 470     GLU C  15    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  36    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  44    CG   CD   CE   NZ                                   
REMARK 470     LYS C  69    CG   CD   CE   NZ                                   
REMARK 470     GLU D  11    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  29    CG   CD   CE   NZ                                   
REMARK 470     LYS D  42    CG   CD   CE   NZ                                   
REMARK 470     LYS D  44    CG   CD   CE   NZ                                   
REMARK 470     GLU D  63    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  65    CD   CE   NZ                                        
REMARK 470     LYS D  69    CG   CD   CE   NZ                                   
REMARK 470     LYS D  70    CE   NZ                                             
REMARK 470     LYS D  71    CD   CE   NZ                                        
REMARK 470     GLU D  74    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  96    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  98    CG   CD   CE   NZ                                   
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    ASP B   148     HH   TYR B   152              1.59            
REMARK 500   O    ASP A   148     HH   TYR A   152              1.60            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  22      -10.92     84.17                                   
REMARK 500    GLU A 103      -11.33     81.02                                   
REMARK 500    LYS A 114       19.14     55.94                                   
REMARK 500    LYS B  22      -10.48     83.77                                   
REMARK 500    GLU B 103       -9.11     79.90                                   
REMARK 500    VAL C  38      -59.70   -122.38                                   
REMARK 500    MET C  48       55.12   -143.94                                   
REMARK 500    HIS C  85      -98.40     57.07                                   
REMARK 500    VAL D  38      -61.98   -121.98                                   
REMARK 500    MET D  48       56.73   -142.84                                   
REMARK 500    HIS D  85     -100.67     57.91                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PEG B  403                                                       
REMARK 610     PG4 D  501                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 403 bound   
REMARK 800  to ASN A 38                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 401 bound   
REMARK 800  to ASN A 45                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 404 bound   
REMARK 800  to ASN A 74                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 402 bound   
REMARK 800  to ASN A 162                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 405 bound   
REMARK 800  to ASN A 169                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 401 bound   
REMARK 800  to ASN B 45                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 402 bound   
REMARK 800  to ASN B 74                                                         
DBREF  5MN2 A    1   175  UNP    P08637   FCG3A_HUMAN     19    193             
DBREF  5MN2 B    1   175  UNP    P08637   FCG3A_HUMAN     19    193             
DBREF  5MN2 C    1   101  PDB    5MN2     5MN2             1    101             
DBREF  5MN2 D    1   101  PDB    5MN2     5MN2             1    101             
SEQRES   1 A  175  ARG THR GLU ASP LEU PRO LYS ALA VAL VAL PHE LEU GLU          
SEQRES   2 A  175  PRO GLN TRP TYR ARG VAL LEU GLU LYS ASP SER VAL THR          
SEQRES   3 A  175  LEU LYS CYS GLN GLY ALA TYR SER PRO GLU ASP ASN SER          
SEQRES   4 A  175  THR GLN TRP PHE HIS ASN GLU SER LEU ILE SER SER GLN          
SEQRES   5 A  175  ALA SER SER TYR PHE ILE ASP ALA ALA THR VAL ASP ASP          
SEQRES   6 A  175  SER GLY GLU TYR ARG CYS GLN THR ASN LEU SER THR LEU          
SEQRES   7 A  175  SER ASP PRO VAL GLN LEU GLU VAL HIS ILE GLY TRP LEU          
SEQRES   8 A  175  LEU LEU GLN ALA PRO ARG TRP VAL PHE LYS GLU GLU ASP          
SEQRES   9 A  175  PRO ILE HIS LEU ARG CYS HIS SER TRP LYS ASN THR ALA          
SEQRES  10 A  175  LEU HIS LYS VAL THR TYR LEU GLN ASN GLY LYS GLY ARG          
SEQRES  11 A  175  LYS TYR PHE HIS HIS ASN SER ASP PHE TYR ILE PRO LYS          
SEQRES  12 A  175  ALA THR LEU LYS ASP SER GLY SER TYR PHE CYS ARG GLY          
SEQRES  13 A  175  LEU PHE GLY SER LYS ASN VAL SER SER GLU THR VAL ASN          
SEQRES  14 A  175  ILE THR ILE THR GLN GLY                                      
SEQRES   1 B  175  ARG THR GLU ASP LEU PRO LYS ALA VAL VAL PHE LEU GLU          
SEQRES   2 B  175  PRO GLN TRP TYR ARG VAL LEU GLU LYS ASP SER VAL THR          
SEQRES   3 B  175  LEU LYS CYS GLN GLY ALA TYR SER PRO GLU ASP ASN SER          
SEQRES   4 B  175  THR GLN TRP PHE HIS ASN GLU SER LEU ILE SER SER GLN          
SEQRES   5 B  175  ALA SER SER TYR PHE ILE ASP ALA ALA THR VAL ASP ASP          
SEQRES   6 B  175  SER GLY GLU TYR ARG CYS GLN THR ASN LEU SER THR LEU          
SEQRES   7 B  175  SER ASP PRO VAL GLN LEU GLU VAL HIS ILE GLY TRP LEU          
SEQRES   8 B  175  LEU LEU GLN ALA PRO ARG TRP VAL PHE LYS GLU GLU ASP          
SEQRES   9 B  175  PRO ILE HIS LEU ARG CYS HIS SER TRP LYS ASN THR ALA          
SEQRES  10 B  175  LEU HIS LYS VAL THR TYR LEU GLN ASN GLY LYS GLY ARG          
SEQRES  11 B  175  LYS TYR PHE HIS HIS ASN SER ASP PHE TYR ILE PRO LYS          
SEQRES  12 B  175  ALA THR LEU LYS ASP SER GLY SER TYR PHE CYS ARG GLY          
SEQRES  13 B  175  LEU PHE GLY SER LYS ASN VAL SER SER GLU THR VAL ASN          
SEQRES  14 B  175  ILE THR ILE THR GLN GLY                                      
SEQRES   1 C  101  ALA THR GLY VAL ARG ALA VAL PRO GLY ASN GLU ASN SER          
SEQRES   2 C  101  LEU GLU ILE GLU GLU LEU ALA ARG PHE ALA VAL ASP GLU          
SEQRES   3 C  101  HIS ASN LYS LYS GLU ASN ALA LEU LEU GLU PHE VAL ARG          
SEQRES   4 C  101  VAL VAL LYS ALA LYS GLU GLN ALA MET ASN THR GLY PHE          
SEQRES   5 C  101  THR LEU ALA THR MET TYR TYR LEU THR LEU GLU ALA LYS          
SEQRES   6 C  101  ASP GLY GLY LYS LYS LYS LEU TYR GLU ALA LYS VAL TRP          
SEQRES   7 C  101  VAL LYS ASN THR GLN TRP HIS ASN ALA MET THR ASN PHE          
SEQRES   8 C  101  LYS GLU LEU GLN GLU PHE LYS PRO VAL GLY                      
SEQRES   1 D  101  ALA THR GLY VAL ARG ALA VAL PRO GLY ASN GLU ASN SER          
SEQRES   2 D  101  LEU GLU ILE GLU GLU LEU ALA ARG PHE ALA VAL ASP GLU          
SEQRES   3 D  101  HIS ASN LYS LYS GLU ASN ALA LEU LEU GLU PHE VAL ARG          
SEQRES   4 D  101  VAL VAL LYS ALA LYS GLU GLN ALA MET ASN THR GLY PHE          
SEQRES   5 D  101  THR LEU ALA THR MET TYR TYR LEU THR LEU GLU ALA LYS          
SEQRES   6 D  101  ASP GLY GLY LYS LYS LYS LEU TYR GLU ALA LYS VAL TRP          
SEQRES   7 D  101  VAL LYS ASN THR GLN TRP HIS ASN ALA MET THR ASN PHE          
SEQRES   8 D  101  LYS GLU LEU GLN GLU PHE LYS PRO VAL GLY                      
HET    NAG  A 401      28                                                       
HET    NAG  A 402      28                                                       
HET    NAG  A 403      28                                                       
HET    NAG  A 404      27                                                       
HET    NAG  A 405      27                                                       
HET    PEG  A 406      17                                                       
HET    GOL  A 407      14                                                       
HET    NAG  B 401      28                                                       
HET    NAG  B 402      27                                                       
HET    PEG  B 403       9                                                       
HET    PG4  D 501      29                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     GOL GLYCEROL                                                         
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  NAG    7(C8 H15 N O6)                                               
FORMUL  10  PEG    2(C4 H10 O3)                                                 
FORMUL  11  GOL    C3 H8 O3                                                     
FORMUL  15  PG4    C8 H18 O5                                                    
FORMUL  16  HOH   *146(H2 O)                                                    
HELIX    1 AA1 THR A   62  SER A   66  5                                   5    
HELIX    2 AA2 THR A  145  SER A  149  5                                   5    
HELIX    3 AA3 THR B   62  SER B   66  5                                   5    
HELIX    4 AA4 LYS B  114  THR B  116  5                                   3    
HELIX    5 AA5 THR B  145  SER B  149  5                                   5    
HELIX    6 AA6 GLU C   15  ASN C   32  1                                  18    
HELIX    7 AA7 SER D   13  ASN D   32  1                                  20    
SHEET    1 AA1 3 VAL A   9  GLU A  13  0                                        
SHEET    2 AA1 3 VAL A  25  GLN A  30 -1  O  GLN A  30   N  VAL A   9           
SHEET    3 AA1 3 SER A  55  ILE A  58 -1  O  TYR A  56   N  LEU A  27           
SHEET    1 AA2 5 ARG A  18  LEU A  20  0                                        
SHEET    2 AA2 5 VAL A  82  HIS A  87  1  O  HIS A  87   N  VAL A  19           
SHEET    3 AA2 5 GLY A  67  THR A  73 -1  N  GLY A  67   O  LEU A  84           
SHEET    4 AA2 5 THR A  40  HIS A  44 -1  N  PHE A  43   O  ARG A  70           
SHEET    5 AA2 5 SER A  47  LEU A  48 -1  O  SER A  47   N  HIS A  44           
SHEET    1 AA3 3 LEU A  91  GLN A  94  0                                        
SHEET    2 AA3 3 ILE A 106  SER A 112 -1  O  ARG A 109   N  GLN A  94           
SHEET    3 AA3 3 PHE A 139  ILE A 141 -1  O  PHE A 139   N  LEU A 108           
SHEET    1 AA4 5 VAL A  99  LYS A 101  0                                        
SHEET    2 AA4 5 VAL A 168  THR A 173  1  O  THR A 173   N  PHE A 100           
SHEET    3 AA4 5 GLY A 150  PHE A 158 -1  N  TYR A 152   O  VAL A 168           
SHEET    4 AA4 5 HIS A 119  GLN A 125 -1  N  LEU A 124   O  PHE A 153           
SHEET    5 AA4 5 LYS A 128  HIS A 135 -1  O  ARG A 130   N  TYR A 123           
SHEET    1 AA5 4 VAL A  99  LYS A 101  0                                        
SHEET    2 AA5 4 VAL A 168  THR A 173  1  O  THR A 173   N  PHE A 100           
SHEET    3 AA5 4 GLY A 150  PHE A 158 -1  N  TYR A 152   O  VAL A 168           
SHEET    4 AA5 4 LYS A 161  SER A 164 -1  O  LYS A 161   N  PHE A 158           
SHEET    1 AA6 3 VAL B   9  GLU B  13  0                                        
SHEET    2 AA6 3 VAL B  25  GLN B  30 -1  O  GLN B  30   N  VAL B   9           
SHEET    3 AA6 3 SER B  55  ILE B  58 -1  O  TYR B  56   N  LEU B  27           
SHEET    1 AA7 5 ARG B  18  LEU B  20  0                                        
SHEET    2 AA7 5 VAL B  82  HIS B  87  1  O  HIS B  87   N  VAL B  19           
SHEET    3 AA7 5 GLY B  67  THR B  73 -1  N  GLY B  67   O  LEU B  84           
SHEET    4 AA7 5 THR B  40  HIS B  44 -1  N  GLN B  41   O  GLN B  72           
SHEET    5 AA7 5 SER B  47  LEU B  48 -1  O  SER B  47   N  HIS B  44           
SHEET    1 AA8 3 LEU B  91  GLN B  94  0                                        
SHEET    2 AA8 3 ILE B 106  SER B 112 -1  O  ARG B 109   N  GLN B  94           
SHEET    3 AA8 3 PHE B 139  ILE B 141 -1  O  PHE B 139   N  LEU B 108           
SHEET    1 AA9 5 VAL B  99  LYS B 101  0                                        
SHEET    2 AA9 5 VAL B 168  THR B 173  1  O  THR B 173   N  PHE B 100           
SHEET    3 AA9 5 GLY B 150  PHE B 158 -1  N  TYR B 152   O  VAL B 168           
SHEET    4 AA9 5 VAL B 121  GLN B 125 -1  N  LEU B 124   O  PHE B 153           
SHEET    5 AA9 5 LYS B 128  PHE B 133 -1  O  LYS B 128   N  GLN B 125           
SHEET    1 AB1 4 VAL B  99  LYS B 101  0                                        
SHEET    2 AB1 4 VAL B 168  THR B 173  1  O  THR B 173   N  PHE B 100           
SHEET    3 AB1 4 GLY B 150  PHE B 158 -1  N  TYR B 152   O  VAL B 168           
SHEET    4 AB1 4 LYS B 161  SER B 164 -1  O  LYS B 161   N  PHE B 158           
SHEET    1 AB2 4 LEU C  35  ALA C  47  0                                        
SHEET    2 AB2 4 THR C  53  ASP C  66 -1  O  TYR C  59   N  LYS C  44           
SHEET    3 AB2 4 LYS C  69  TRP C  84 -1  O  ALA C  75   N  LEU C  60           
SHEET    4 AB2 4 ALA C  87  PRO C  99 -1  O  LYS C  98   N  GLU C  74           
SHEET    1 AB3 4 LEU D  35  ALA D  47  0                                        
SHEET    2 AB3 4 LEU D  54  ASP D  66 -1  O  GLU D  63   N  ARG D  39           
SHEET    3 AB3 4 LYS D  69  TRP D  84 -1  O  ALA D  75   N  LEU D  60           
SHEET    4 AB3 4 ALA D  87  PRO D  99 -1  O  LYS D  98   N  GLU D  74           
SSBOND   1 CYS A   29    CYS A   71                          1555   1555  2.04  
SSBOND   2 CYS A  110    CYS A  154                          1555   1555  2.05  
SSBOND   3 CYS B   29    CYS B   71                          1555   1555  2.03  
SSBOND   4 CYS B  110    CYS B  154                          1555   1555  2.03  
LINK         ND2 ASN A  38                 C1  NAG A 403     1555   1555  1.45  
LINK         ND2 ASN A  45                 C1  NAG A 401     1555   1555  1.45  
LINK         ND2 ASN A  74                 C1  NAG A 404     1555   1555  1.45  
LINK         ND2 ASN A 162                 C1  NAG A 402     1555   1555  1.45  
LINK         ND2 ASN A 169                 C1  NAG A 405     1555   1555  1.44  
LINK         ND2 ASN B  45                 C1  NAG B 401     1555   1555  1.45  
LINK         ND2 ASN B  74                 C1  NAG B 402     1555   1555  1.45  
CISPEP   1 GLU A   13    PRO A   14          0        -2.75                     
CISPEP   2 GLU B   13    PRO B   14          0        -2.41                     
SITE     1 AC1  1 TRP A  90                                                     
SITE     1 AC2  2 PHE A  43  GLU A  46                                          
SITE     1 AC3  2 LYS B  22  ASP B  23                                          
SITE     1 AC4  3 NAG A 401  HOH A 538  TRP D  84                               
SITE     1 AC5  1 ASN A  38                                                     
SITE     1 AC6  6 HIS A  44  ASN A  45  ASP A  64  SER A  66                    
SITE     2 AC6  6 HOH A 538  PG4 D 501                                          
SITE     1 AC7  3 GLU A  36  ASP A  37  ASN A  74                               
SITE     1 AC8  5 LYS A 120  ARG A 155  ASN A 162  HOH A 502                    
SITE     2 AC8  5 ASP D  66                                                     
SITE     1 AC9  4 ASN A 126  ASN A 169  ASN D  86  MET D  88                    
SITE     1 AD1  4 ASN B  45  ASP B  64  SER B  66  TRP C  84                    
SITE     1 AD2  2 ASP B  37  ASN B  74                                          
CRYST1   64.985   59.925  100.001  90.00 102.09  90.00 P 1 21 1      4          
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      0.015388  0.000000  0.003297        0.00000                         
SCALE2      0.000000  0.016688  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010227        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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