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Database: PDB
Entry: 1XQG
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Original site: 1XQG 
HEADER    ANTITUMOR PROTEIN                       12-OCT-04   1XQG              
TITLE     3.10 A CRYSTAL STRUCTURE OF MASPIN, SPACE GROUP P 4 21 2              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MASPIN;                                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SERPINB5, PI5;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PQE30                                     
KEYWDS    SERPIN, MASPIN, TUMOR SUPPRESSION, ANTITUMOR PROTEIN                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.AL-AYYOUBI,P.G.GETTINS,K.VOLZ                                       
REVDAT   3   24-FEB-09 1XQG    1       VERSN                                    
REVDAT   2   11-JAN-05 1XQG    1       JRNL                                     
REVDAT   1   26-OCT-04 1XQG    0                                                
JRNL        AUTH   M.AL-AYYOUBI,P.G.GETTINS,K.VOLZ                              
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN MASPIN, A SERPIN WITH             
JRNL        TITL 2 ANTITUMOR PROPERTIES: REACTIVE CENTER LOOP OF                
JRNL        TITL 3 MAPSIN IS EXPOSED BUT CONSTRAINED                            
JRNL        REF    J.BIOL.CHEM.                  V. 279 55540 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15501821                                                     
JRNL        DOI    10.1074/JBC.M409957200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 200322.890                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 23042                          
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 SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 241                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.016                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.29                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3415                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690                       
REMARK   3   BIN FREE R VALUE                    : 0.2890                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 1.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 35                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.049                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5922                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 152                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.16000                                              
REMARK   3    B22 (A**2) : 5.16000                                              
REMARK   3    B33 (A**2) : -10.32000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.30                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.44                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.40                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.43                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.81                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 20.42                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : CARBOHYDRATE.PARAM                             
REMARK   3  TOPOLOGY FILE  3   : WATER.PARAM                                    
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1XQG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-OCT-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030646.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23502                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
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     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB IDS 1HLE, 1BY7, 1OVA                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 45% PEG400, SODIUM CITRATE 0.2M,         
REMARK 280  TRIS 0.1M, PH 8.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z                                          
REMARK 290       4555   Y+1/2,-X+1/2,Z                                          
REMARK 290       5555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       6555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       73.73100            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       73.73100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       73.73100            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       73.73100            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       73.73100            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       73.73100            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       73.73100            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       73.73100            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        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: 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 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     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     GLU A    -7                                                      
REMARK 465     ASN A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     TYR A    -4                                                      
REMARK 465     PHE A    -3                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     GLU B    -7                                                      
REMARK 465     ASN B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     TYR B    -4                                                      
REMARK 465     PHE B    -3                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A  -2    CG   CD   OE1  NE2                                  
REMARK 470     SER A   0    OG                                                  
REMARK 470     ARG A 340    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B  -2    CG   CD   OE1  NE2                                  
REMARK 470     SER B   0    OG                                                  
REMARK 470     ARG B 340    CG   CD   NE   CZ   NH1  NH2                        
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    GLU A  61      -42.46    -27.53                                   
REMARK 500    SER A  97       -4.05    -51.68                                   
REMARK 500    ASN A  99      101.63    -58.86                                   
REMARK 500    TYR A 112       54.80   -119.29                                   
REMARK 500    ALA A 113     -109.88    -21.46                                   
REMARK 500    LYS A 122      -86.97    -59.01                                   
REMARK 500    ASP A 141       25.48     42.61                                   
REMARK 500    ASN A 151       46.02   -109.21                                   
REMARK 500    PHE A 167      124.51   -172.00                                   
REMARK 500    LYS A 189      -53.75    -29.19                                   
REMARK 500    ASN A 213       59.68     36.67                                   
REMARK 500    GLN A 222      126.87    -36.17                                   
REMARK 500    LYS A 224       23.73     30.46                                   
REMARK 500    GLU A 237       58.14   -111.56                                   
REMARK 500    SER A 240     -117.77   -129.83                                   
REMARK 500    ASN A 266      151.02    -45.80                                   
REMARK 500    PRO A 284        0.66    -58.41                                   
REMARK 500    PHE A 304       57.03   -106.99                                   
REMARK 500    MET A 307      -48.72   -130.22                                   
REMARK 500    THR A 327     -159.18   -133.15                                   
REMARK 500    PRO A 337      -69.47    -25.33                                   
REMARK 500    ALA A 339       30.63    -70.21                                   
REMARK 500    LYS A 345       63.62   -105.07                                   
REMARK 500    PRO A 353      138.58    -31.43                                   
REMARK 500    SER A 374      173.18    170.57                                   
REMARK 500    PRO B  24       25.74    -71.40                                   
REMARK 500    LEU B  25       -3.78   -149.39                                   
REMARK 500    LEU B  29      130.05   -171.06                                   
REMARK 500    GLU B  61       -6.86    -48.48                                   
REMARK 500    SER B  85       48.09    -85.37                                   
REMARK 500    LYS B  87      123.81   -171.97                                   
REMARK 500    ALA B 113     -110.74    -27.74                                   
REMARK 500    LYS B 114       30.15    -92.47                                   
REMARK 500    ALA B 149     -112.21    -63.20                                   
REMARK 500    ASP B 150      -60.65   -126.39                                   
REMARK 500    GLN B 156       40.68   -101.13                                   
REMARK 500    LYS B 158      -71.65    -86.58                                   
REMARK 500    PHE B 167      115.31   -168.71                                   
REMARK 500    MET B 200      148.69    177.24                                   
REMARK 500    SER B 211      -37.28    -35.96                                   
REMARK 500    LYS B 224       22.07     49.92                                   
REMARK 500    GLU B 237       42.33   -106.03                                   
REMARK 500    SER B 240      -99.78   -123.15                                   
REMARK 500    PRO B 284        0.32    -62.03                                   
REMARK 500    LYS B 294      -66.44   -102.61                                   
REMARK 500    PHE B 304       36.18    -93.13                                   
REMARK 500    LYS B 311      157.35    -43.18                                   
REMARK 500    THR B 327     -168.42   -129.59                                   
REMARK 500    GLN B 343      139.25   -174.32                                   
REMARK 500    LYS B 345       71.50   -103.13                                   
REMARK 500    PRO B 353      134.65    -36.73                                   
REMARK 500    ARG B 364       -0.65     77.65                                   
REMARK 500    SER B 374     -179.83    176.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 HOH 1-76 ARE ASSOCIATED WITH CHAIN A.                                
REMARK 600 HOH 101-177 ARE ASSOCIATED WITH CHAIN B.                             
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1XQJ   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE AUTHORS STATE THAT RESIDUES 66, 176, AND                         
REMARK 999 187 WERE VAL, SER, AND VAL IN THE CONSTRUCT,                         
REMARK 999 WHICH CONFLICTS WITH SWS ENTRY P36952.                               
DBREF  1XQG A    1   375  UNP    P36952   MASP_HUMAN       1    375             
DBREF  1XQG B    1   375  UNP    P36952   MASP_HUMAN       1    375             
SEQADV 1XQG HIS A  -13  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG HIS A  -12  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG HIS A  -11  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG HIS A  -10  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG HIS A   -9  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG HIS A   -8  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG GLU A   -7  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG ASN A   -6  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG LEU A   -5  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG TYR A   -4  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG PHE A   -3  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG GLN A   -2  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG GLY A   -1  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG SER A    0  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG SER A   20  UNP  P36952    CYS    20 ENGINEERED                     
SEQADV 1XQG ALA A   34  UNP  P36952    CYS    34 ENGINEERED                     
SEQADV 1XQG VAL A   66  UNP  P36952    ILE    66 SEE REMARK 999                 
SEQADV 1XQG SER A  176  UNP  P36952    PRO   176 SEE REMARK 999                 
SEQADV 1XQG SER A  183  UNP  P36952    CYS   183 ENGINEERED                     
SEQADV 1XQG VAL A  187  UNP  P36952    LEU   187 SEE REMARK 999                 
SEQADV 1XQG SER A  205  UNP  P36952    CYS   205 ENGINEERED                     
SEQADV 1XQG SER A  214  UNP  P36952    CYS   214 ENGINEERED                     
SEQADV 1XQG SER A  287  UNP  P36952    CYS   287 ENGINEERED                     
SEQADV 1XQG SER A  323  UNP  P36952    CYS   323 ENGINEERED                     
SEQADV 1XQG SER A  373  UNP  P36952    CYS   373 ENGINEERED                     
SEQADV 1XQG HIS B  -13  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG HIS B  -12  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG HIS B  -11  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG HIS B  -10  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG HIS B   -9  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG HIS B   -8  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG GLU B   -7  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG ASN B   -6  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG LEU B   -5  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG TYR B   -4  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG PHE B   -3  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG GLN B   -2  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG GLY B   -1  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG SER B    0  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XQG SER B   20  UNP  P36952    CYS    20 ENGINEERED                     
SEQADV 1XQG ALA B   34  UNP  P36952    CYS    34 ENGINEERED                     
SEQADV 1XQG VAL B   66  UNP  P36952    ILE    66 SEE REMARK 999                 
SEQADV 1XQG SER B  176  UNP  P36952    PRO   176 SEE REMARK 999                 
SEQADV 1XQG SER B  183  UNP  P36952    CYS   183 ENGINEERED                     
SEQADV 1XQG VAL B  187  UNP  P36952    LEU   187 SEE REMARK 999                 
SEQADV 1XQG SER B  205  UNP  P36952    CYS   205 ENGINEERED                     
SEQADV 1XQG SER B  214  UNP  P36952    CYS   214 ENGINEERED                     
SEQADV 1XQG SER B  287  UNP  P36952    CYS   287 ENGINEERED                     
SEQADV 1XQG SER B  323  UNP  P36952    CYS   323 ENGINEERED                     
SEQADV 1XQG SER B  373  UNP  P36952    CYS   373 ENGINEERED                     
SEQRES   1 A  389  HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN GLY          
SEQRES   2 A  389  SER MET ASP ALA LEU GLN LEU ALA ASN SER ALA PHE ALA          
SEQRES   3 A  389  VAL ASP LEU PHE LYS GLN LEU SER GLU LYS GLU PRO LEU          
SEQRES   4 A  389  GLY ASN VAL LEU PHE SER PRO ILE ALA LEU SER THR SER          
SEQRES   5 A  389  LEU SER LEU ALA GLN VAL GLY ALA LYS GLY ASP THR ALA          
SEQRES   6 A  389  ASN GLU ILE GLY GLN VAL LEU HIS PHE GLU ASN VAL LYS          
SEQRES   7 A  389  ASP VAL PRO PHE GLY PHE GLN THR VAL THR SER ASP VAL          
SEQRES   8 A  389  ASN LYS LEU SER SER PHE TYR SER LEU LYS LEU ILE LYS          
SEQRES   9 A  389  ARG LEU TYR VAL ASP LYS SER LEU ASN LEU SER THR GLU          
SEQRES  10 A  389  PHE ILE SER SER THR LYS ARG PRO TYR ALA LYS GLU LEU          
SEQRES  11 A  389  GLU THR VAL ASP PHE LYS ASP LYS LEU GLU GLU THR LYS          
SEQRES  12 A  389  GLY GLN ILE ASN ASN SER ILE LYS ASP LEU THR ASP GLY          
SEQRES  13 A  389  HIS PHE GLU ASN ILE LEU ALA ASP ASN SER VAL ASN ASP          
SEQRES  14 A  389  GLN THR LYS ILE LEU VAL VAL ASN ALA ALA TYR PHE VAL          
SEQRES  15 A  389  GLY LYS TRP MET LYS LYS PHE SER GLU SER GLU THR LYS          
SEQRES  16 A  389  GLU SER PRO PHE ARG VAL ASN LYS THR ASP THR LYS PRO          
SEQRES  17 A  389  VAL GLN MET MET ASN MET GLU ALA THR PHE SER MET GLY          
SEQRES  18 A  389  ASN ILE ASP SER ILE ASN SER LYS ILE ILE GLU LEU PRO          
SEQRES  19 A  389  PHE GLN ASN LYS HIS LEU SER MET PHE ILE LEU LEU PRO          
SEQRES  20 A  389  LYS ASP VAL GLU ASP GLU SER THR GLY LEU GLU LYS ILE          
SEQRES  21 A  389  GLU LYS GLN LEU ASN SER GLU SER LEU SER GLN TRP THR          
SEQRES  22 A  389  ASN PRO SER THR MET ALA ASN ALA LYS VAL LYS LEU SER          
SEQRES  23 A  389  ILE PRO LYS PHE LYS VAL GLU LYS MET ILE ASP PRO LYS          
SEQRES  24 A  389  ALA SER LEU GLU ASN LEU GLY LEU LYS HIS ILE PHE SER          
SEQRES  25 A  389  GLU ASP THR SER ASP PHE SER GLY MET SER GLU THR LYS          
SEQRES  26 A  389  GLY VAL ALA LEU SER ASN VAL ILE HIS LYS VAL SER LEU          
SEQRES  27 A  389  GLU ILE THR GLU ASP GLY GLY ASP SER ILE GLU VAL PRO          
SEQRES  28 A  389  GLY ALA ARG ILE LEU GLN HIS LYS ASP GLU LEU ASN ALA          
SEQRES  29 A  389  ASP HIS PRO PHE ILE TYR ILE ILE ARG HIS ASN LYS THR          
SEQRES  30 A  389  ARG ASN ILE ILE PHE PHE GLY LYS PHE SER SER PRO              
SEQRES   1 B  389  HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN GLY          
SEQRES   2 B  389  SER MET ASP ALA LEU GLN LEU ALA ASN SER ALA PHE ALA          
SEQRES   3 B  389  VAL ASP LEU PHE LYS GLN LEU SER GLU LYS GLU PRO LEU          
SEQRES   4 B  389  GLY ASN VAL LEU PHE SER PRO ILE ALA LEU SER THR SER          
SEQRES   5 B  389  LEU SER LEU ALA GLN VAL GLY ALA LYS GLY ASP THR ALA          
SEQRES   6 B  389  ASN GLU ILE GLY GLN VAL LEU HIS PHE GLU ASN VAL LYS          
SEQRES   7 B  389  ASP VAL PRO PHE GLY PHE GLN THR VAL THR SER ASP VAL          
SEQRES   8 B  389  ASN LYS LEU SER SER PHE TYR SER LEU LYS LEU ILE LYS          
SEQRES   9 B  389  ARG LEU TYR VAL ASP LYS SER LEU ASN LEU SER THR GLU          
SEQRES  10 B  389  PHE ILE SER SER THR LYS ARG PRO TYR ALA LYS GLU LEU          
SEQRES  11 B  389  GLU THR VAL ASP PHE LYS ASP LYS LEU GLU GLU THR LYS          
SEQRES  12 B  389  GLY GLN ILE ASN ASN SER ILE LYS ASP LEU THR ASP GLY          
SEQRES  13 B  389  HIS PHE GLU ASN ILE LEU ALA ASP ASN SER VAL ASN ASP          
SEQRES  14 B  389  GLN THR LYS ILE LEU VAL VAL ASN ALA ALA TYR PHE VAL          
SEQRES  15 B  389  GLY LYS TRP MET LYS LYS PHE SER GLU SER GLU THR LYS          
SEQRES  16 B  389  GLU SER PRO PHE ARG VAL ASN LYS THR ASP THR LYS PRO          
SEQRES  17 B  389  VAL GLN MET MET ASN MET GLU ALA THR PHE SER MET GLY          
SEQRES  18 B  389  ASN ILE ASP SER ILE ASN SER LYS ILE ILE GLU LEU PRO          
SEQRES  19 B  389  PHE GLN ASN LYS HIS LEU SER MET PHE ILE LEU LEU PRO          
SEQRES  20 B  389  LYS ASP VAL GLU ASP GLU SER THR GLY LEU GLU LYS ILE          
SEQRES  21 B  389  GLU LYS GLN LEU ASN SER GLU SER LEU SER GLN TRP THR          
SEQRES  22 B  389  ASN PRO SER THR MET ALA ASN ALA LYS VAL LYS LEU SER          
SEQRES  23 B  389  ILE PRO LYS PHE LYS VAL GLU LYS MET ILE ASP PRO LYS          
SEQRES  24 B  389  ALA SER LEU GLU ASN LEU GLY LEU LYS HIS ILE PHE SER          
SEQRES  25 B  389  GLU ASP THR SER ASP PHE SER GLY MET SER GLU THR LYS          
SEQRES  26 B  389  GLY VAL ALA LEU SER ASN VAL ILE HIS LYS VAL SER LEU          
SEQRES  27 B  389  GLU ILE THR GLU ASP GLY GLY ASP SER ILE GLU VAL PRO          
SEQRES  28 B  389  GLY ALA ARG ILE LEU GLN HIS LYS ASP GLU LEU ASN ALA          
SEQRES  29 B  389  ASP HIS PRO PHE ILE TYR ILE ILE ARG HIS ASN LYS THR          
SEQRES  30 B  389  ARG ASN ILE ILE PHE PHE GLY LYS PHE SER SER PRO              
FORMUL   3  HOH   *152(H2 O)                                                    
HELIX    1   1 MET A    1  GLU A   23  1                                  23    
HELIX    2   2 SER A   31  ALA A   46  1                                  16    
HELIX    3   3 LYS A   47  LEU A   58  1                                  12    
HELIX    4   4 HIS A   59  VAL A   63  5                                   5    
HELIX    5   5 ASP A   65  SER A   81  1                                  17    
HELIX    6   6 SER A  101  THR A  108  1                                   8    
HELIX    7   7 ASP A  120  THR A  140  1                                  21    
HELIX    8   8 SER A  176  THR A  180  5                                   5    
HELIX    9   9 ASP A  210  ILE A  212  5                                   3    
HELIX   10  10 GLN A  222  HIS A  225  5                                   4    
HELIX   11  11 LEU A  243  GLN A  249  1                                   7    
HELIX   12  12 ASN A  251  THR A  259  1                                   9    
HELIX   13  13 ASN A  260  MET A  264  5                                   5    
HELIX   14  14 PRO A  284  GLY A  292  1                                   9    
HELIX   15  15 LYS A  294  SER A  298  5                                   5    
HELIX   16  16 GLY B   -1  GLU B   23  1                                  25    
HELIX   17  17 SER B   31  GLY B   45  1                                  15    
HELIX   18  18 GLY B   48  LEU B   58  1                                  11    
HELIX   19  19 ASP B   65  SER B   81  1                                  17    
HELIX   20  20 SER B  101  SER B  107  1                                   7    
HELIX   21  21 TYR B  112  LYS B  114  5                                   3    
HELIX   22  22 ASP B  120  THR B  140  1                                  21    
HELIX   23  23 SER B  176  SER B  178  5                                   3    
HELIX   24  24 ASP B  210  ILE B  212  5                                   3    
HELIX   25  25 GLN B  222  LYS B  224  5                                   3    
HELIX   26  26 LEU B  243  LEU B  250  1                                   8    
HELIX   27  27 ASN B  251  THR B  259  1                                   9    
HELIX   28  28 ASN B  260  MET B  264  5                                   5    
HELIX   29  29 PRO B  284  GLY B  292  1                                   9    
SHEET    1   A 7 VAL A  28  PHE A  30  0                                        
SHEET    2   A 7 ILE A 366  PHE A 372 -1  O  LYS A 371   N  VAL A  28           
SHEET    3   A 7 PHE A 354  ARG A 359 -1  N  ILE A 358   O  PHE A 368           
SHEET    4   A 7 SER A 227  PRO A 233 -1  N  LEU A 231   O  ILE A 355           
SHEET    5   A 7 SER A 214  PRO A 220 -1  N  LEU A 219   O  MET A 228           
SHEET    6   A 7 THR A 192  ILE A 209 -1  N  ILE A 209   O  SER A 214           
SHEET    7   A 7 LYS A 181  ARG A 186 -1  N  PHE A 185   O  LYS A 193           
SHEET    1   B 7 VAL A  28  PHE A  30  0                                        
SHEET    2   B 7 ILE A 366  PHE A 372 -1  O  LYS A 371   N  VAL A  28           
SHEET    3   B 7 PHE A 354  ARG A 359 -1  N  ILE A 358   O  PHE A 368           
SHEET    4   B 7 SER A 227  PRO A 233 -1  N  LEU A 231   O  ILE A 355           
SHEET    5   B 7 SER A 214  PRO A 220 -1  N  LEU A 219   O  MET A 228           
SHEET    6   B 7 THR A 192  ILE A 209 -1  N  ILE A 209   O  SER A 214           
SHEET    7   B 7 ALA A 265  PRO A 274 -1  O  LEU A 271   N  MET A 200           
SHEET    1   C 5 LEU A 116  VAL A 119  0                                        
SHEET    2   C 5 LEU A  86  ASP A  95  1  N  VAL A  94   O  GLU A 117           
SHEET    3   C 5 ILE A 159  VAL A 168 -1  O  LEU A 160   N  TYR A  93           
SHEET    4   C 5 LEU A 315  ILE A 326  1  O  ILE A 319   N  VAL A 161           
SHEET    5   C 5 PHE A 276  ILE A 282 -1  N  PHE A 276   O  ILE A 326           
SHEET    1   D 7 VAL B  28  PHE B  30  0                                        
SHEET    2   D 7 ASN B 365  PHE B 372 -1  O  PHE B 369   N  PHE B  30           
SHEET    3   D 7 PHE B 354  HIS B 360 -1  N  ILE B 358   O  PHE B 368           
SHEET    4   D 7 LEU B 226  PRO B 233 -1  N  LEU B 231   O  ILE B 355           
SHEET    5   D 7 SER B 214  PRO B 220 -1  N  LEU B 219   O  MET B 228           
SHEET    6   D 7 THR B 192  ILE B 209 -1  N  ILE B 209   O  SER B 214           
SHEET    7   D 7 THR B 180  ARG B 186 -1  N  PHE B 185   O  LYS B 193           
SHEET    1   E 8 VAL B  28  PHE B  30  0                                        
SHEET    2   E 8 ASN B 365  PHE B 372 -1  O  PHE B 369   N  PHE B  30           
SHEET    3   E 8 PHE B 354  HIS B 360 -1  N  ILE B 358   O  PHE B 368           
SHEET    4   E 8 LEU B 226  PRO B 233 -1  N  LEU B 231   O  ILE B 355           
SHEET    5   E 8 SER B 214  PRO B 220 -1  N  LEU B 219   O  MET B 228           
SHEET    6   E 8 THR B 192  ILE B 209 -1  N  ILE B 209   O  SER B 214           
SHEET    7   E 8 ALA B 265  PRO B 274 -1  O  VAL B 269   N  ALA B 202           
SHEET    8   E 8 LYS B 345  ASP B 346  1  O  ASP B 346   N  LYS B 270           
SHEET    1   F 5 LEU B 116  VAL B 119  0                                        
SHEET    2   F 5 SER B  85  ASP B  95  1  N  LEU B  92   O  GLU B 117           
SHEET    3   F 5 ILE B 159  VAL B 168 -1  O  LEU B 160   N  TYR B  93           
SHEET    4   F 5 LEU B 315  GLU B 325  1  O  ILE B 319   N  ASN B 163           
SHEET    5   F 5 LYS B 277  ILE B 282 -1  N  ILE B 282   O  HIS B 320           
CRYST1  147.462  147.462  118.038  90.00  90.00  90.00 P 4 21 2     16          
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      0.006781  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006781  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008472        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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