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Database: PDB
Entry: 2VSC
LinkDB: 2VSC
Original site: 2VSC 
HEADER    CELL ADHESION                           22-APR-08   2VSC              
TITLE     STRUCTURE OF THE IMMUNOGLOBULIN-SUPERFAMILY ECTODOMAIN OF HUMAN CD47  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LEUKOCYTE SURFACE ANTIGEN CD47;                            
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: IMMUNOGLOBULIN-SUPERFAMILY ECTODOMAIN, RESIDUES 19-136;    
COMPND   5 SYNONYM: INTEGRIN-ASSOCIATED PROTEIN, IAP, ANTIGENIC SURFACE         
COMPND   6 DETERMINANT PROTEIN OA3, PROTEIN MER6, CD47;                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: LEC3.2.8.1;                               
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: CHO;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PEE14                                     
KEYWDS    IMMUNOGLOBULIN DOMAIN, SIGNAL REGULATORY PROTEIN, CD47, MEMBRANE,     
KEYWDS   2 GLYCOPROTEIN, CELL ADHESION, IMMUNOGLOBULIN SUPERFAMILY, PYRROLIDONE 
KEYWDS   3 CARBOXYLIC ACID, TRANSMEMBRANE, PAIRED RECEPTOR, ALTERNATIVE         
KEYWDS   4 SPLICING                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.HATHERLEY,S.C.GRAHAM,J.TURNER,K.HARLOS,D.I.STUART,A.N.BARCLAY       
REVDAT   4   11-MAR-20 2VSC    1       SEQRES                                   
REVDAT   3   03-APR-19 2VSC    1       SOURCE LINK                              
REVDAT   2   24-FEB-09 2VSC    1       VERSN                                    
REVDAT   1   12-AUG-08 2VSC    0                                                
JRNL        AUTH   D.HATHERLEY,S.C.GRAHAM,J.TURNER,K.HARLOS,D.I.STUART,         
JRNL        AUTH 2 A.N.BARCLAY                                                  
JRNL        TITL   PAIRED RECEPTOR SPECIFICITY EXPLAINED BY STRUCTURES OF       
JRNL        TITL 2 SIGNAL REGULATORY PROTEINS ALONE AND COMPLEXED WITH CD47.    
JRNL        REF    MOL.CELL                      V.  31   266 2008              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   18657508                                                     
JRNL        DOI    10.1016/J.MOLCEL.2008.05.026                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 39392                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2100                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2484                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2490                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 139                          
REMARK   3   BIN FREE R VALUE                    : 0.3530                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3647                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 170                                     
REMARK   3   SOLVENT ATOMS            : 353                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.59                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.07000                                              
REMARK   3    B22 (A**2) : -0.76000                                             
REMARK   3    B33 (A**2) : 0.74000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.15000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.180         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.166         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.135         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.331         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3916 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2605 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5333 ; 1.367 ; 2.017       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6313 ; 0.847 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   459 ; 6.621 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   161 ;33.938 ;25.155       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   676 ;13.381 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.853 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   651 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4355 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   734 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   615 ; 0.181 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2624 ; 0.196 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1845 ; 0.176 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2087 ; 0.108 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   303 ; 0.150 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    19 ; 0.136 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    41 ; 0.200 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.176 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2978 ; 0.621 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3747 ; 0.769 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1903 ; 1.411 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1579 ; 2.133 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   100                          
REMARK   3    RESIDUE RANGE :   A  1001        A  1100                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3517 -36.9360  20.4823              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1980 T22:  -0.1319                                     
REMARK   3      T33:  -0.0712 T12:  -0.0630                                     
REMARK   3      T13:   0.0384 T23:  -0.0633                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3743 L22:   3.6883                                     
REMARK   3      L33:   2.6814 L12:   1.8284                                     
REMARK   3      L13:   0.4405 L23:   0.9978                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0172 S12:   0.1094 S13:  -0.5437                       
REMARK   3      S21:   0.0634 S22:  -0.0433 S23:   0.0915                       
REMARK   3      S31:   0.1989 S32:  -0.2981 S33:   0.0605                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   101        A   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.3216  -7.5475  41.2028              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1369 T22:  -0.1832                                     
REMARK   3      T33:  -0.1737 T12:  -0.1732                                     
REMARK   3      T13:   0.0352 T23:   0.0199                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.8474 L22:  23.2528                                     
REMARK   3      L33:   9.1519 L12:  17.4682                                     
REMARK   3      L13:  10.2800 L23:  14.4387                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6887 S12:  -0.6872 S13:   0.5712                       
REMARK   3      S21:   1.5321 S22:  -0.9897 S23:   0.6256                       
REMARK   3      S31:   0.5558 S32:  -0.5237 S33:   0.3010                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   100                          
REMARK   3    RESIDUE RANGE :   B  1000        B  1100                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.4424  -8.3877  34.3321              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1206 T22:  -0.2026                                     
REMARK   3      T33:  -0.1667 T12:  -0.0652                                     
REMARK   3      T13:  -0.0179 T23:   0.0042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3665 L22:   6.1029                                     
REMARK   3      L33:   2.4037 L12:   2.1208                                     
REMARK   3      L13:   0.8551 L23:   0.8227                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1638 S12:  -0.1475 S13:  -0.0388                       
REMARK   3      S21:   0.4664 S22:  -0.2482 S23:  -0.1528                       
REMARK   3      S31:  -0.1123 S32:  -0.1177 S33:   0.0844                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   101        B   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.2322 -36.8520  12.5952              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2332 T22:  -0.0132                                     
REMARK   3      T33:  -0.0672 T12:  -0.0801                                     
REMARK   3      T13:   0.0906 T23:  -0.1600                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.4008 L22:  21.4441                                     
REMARK   3      L33:  10.5476 L12:  15.2660                                     
REMARK   3      L13:  10.8060 L23:  12.8670                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1032 S12:   0.7086 S13:  -0.6953                       
REMARK   3      S21:  -0.4737 S22:   0.2510 S23:  -0.1347                       
REMARK   3      S31:   0.0499 S32:  -0.0077 S33:  -0.1478                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   100                          
REMARK   3    RESIDUE RANGE :   C  1000        C  1100                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.1736   0.6398  14.0996              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1704 T22:  -0.2042                                     
REMARK   3      T33:  -0.1882 T12:   0.0344                                     
REMARK   3      T13:   0.0214 T23:   0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3001 L22:   4.2933                                     
REMARK   3      L33:   1.7118 L12:  -1.6607                                     
REMARK   3      L13:   0.2255 L23:  -0.6805                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1450 S12:   0.1344 S13:   0.0503                       
REMARK   3      S21:  -0.0431 S22:  -0.0968 S23:  -0.0690                       
REMARK   3      S31:   0.0108 S32:   0.0567 S33:  -0.0482                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   101        C   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.7436  31.1458   3.9436              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1111 T22:   0.0344                                     
REMARK   3      T33:  -0.1419 T12:   0.2551                                     
REMARK   3      T13:   0.0094 T23:   0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  16.7554 L22:  23.0595                                     
REMARK   3      L33:   5.9056 L12: -18.2883                                     
REMARK   3      L13:   7.9958 L23: -11.1822                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5244 S12:  -0.4559 S13:   0.0653                       
REMARK   3      S21:   0.7686 S22:   0.7445 S23:   0.5412                       
REMARK   3      S31:  -0.7255 S32:  -0.7020 S33:  -0.2201                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   100                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.4941  28.6316  -2.6344              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0732 T22:   0.2197                                     
REMARK   3      T33:  -0.1474 T12:   0.2405                                     
REMARK   3      T13:   0.0152 T23:   0.0667                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.9259 L22:  10.5664                                     
REMARK   3      L33:   3.6604 L12:  -8.2921                                     
REMARK   3      L13:   3.4921 L23:  -5.2178                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5960 S12:   1.3724 S13:   0.0928                       
REMARK   3      S21:  -0.6637 S22:  -0.5994 S23:   0.1420                       
REMARK   3      S31:  -0.0342 S32:  -0.0314 S33:   0.0034                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   101        D   120                          
REMARK   3    RESIDUE RANGE :   D  1000        D  1100                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.0700   3.7364   5.5193              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1141 T22:  -0.1402                                     
REMARK   3      T33:  -0.1127 T12:   0.0595                                     
REMARK   3      T13:   0.0636 T23:   0.0594                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.8131 L22:  21.1371                                     
REMARK   3      L33:   4.1742 L12: -18.0176                                     
REMARK   3      L13:   5.8780 L23:  -7.1184                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3104 S12:   0.7379 S13:   0.8698                       
REMARK   3      S21:  -0.4489 S22:  -0.6610 S23:  -1.0930                       
REMARK   3      S31:  -0.0789 S32:   0.1259 S33:   0.3506                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. B VALUES INCLUDE TLS CONTRIBUTIONS.                      
REMARK   4                                                                      
REMARK   4 2VSC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-APR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290035998.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-APR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978                              
REMARK 200  MONOCHROMATOR                  : SI(111) MONOCHROMATOR              
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41496                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2JJS, CHAIN C                              
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 NL 17 MG/ML CD47 PLUS 100 NL         
REMARK 280  RESERVOIR (0.2 M MGCL2, 0.1 M BIS-TRIS PH 5.5, 25% W/V PEG 3350)    
REMARK 280  EQUILIBRATED AGAINST 95 UL OF RESERVOIR AT 20.5 C.                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      100.56850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.75100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      100.56850            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.75100            
REMARK 290   SMTRY3   4  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 5900 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 6270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2037  LIES ON A SPECIAL POSITION.                          
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     VAL A   116                                                      
REMARK 465     SER A   117                                                      
REMARK 465     TRP A   118                                                      
REMARK 465     SER A   119                                                      
REMARK 465     THR A   120                                                      
REMARK 465     ARG A   121                                                      
REMARK 465     HIS A   122                                                      
REMARK 465     HIS A   123                                                      
REMARK 465     HIS A   124                                                      
REMARK 465     HIS A   125                                                      
REMARK 465     HIS A   126                                                      
REMARK 465     HIS A   127                                                      
REMARK 465     VAL B   116                                                      
REMARK 465     SER B   117                                                      
REMARK 465     TRP B   118                                                      
REMARK 465     SER B   119                                                      
REMARK 465     THR B   120                                                      
REMARK 465     ARG B   121                                                      
REMARK 465     HIS B   122                                                      
REMARK 465     HIS B   123                                                      
REMARK 465     HIS B   124                                                      
REMARK 465     HIS B   125                                                      
REMARK 465     HIS B   126                                                      
REMARK 465     HIS B   127                                                      
REMARK 465     VAL C   116                                                      
REMARK 465     SER C   117                                                      
REMARK 465     TRP C   118                                                      
REMARK 465     SER C   119                                                      
REMARK 465     THR C   120                                                      
REMARK 465     ARG C   121                                                      
REMARK 465     HIS C   122                                                      
REMARK 465     HIS C   123                                                      
REMARK 465     HIS C   124                                                      
REMARK 465     HIS C   125                                                      
REMARK 465     HIS C   126                                                      
REMARK 465     HIS C   127                                                      
REMARK 465     SER D   117                                                      
REMARK 465     TRP D   118                                                      
REMARK 465     SER D   119                                                      
REMARK 465     THR D   120                                                      
REMARK 465     ARG D   121                                                      
REMARK 465     HIS D   122                                                      
REMARK 465     HIS D   123                                                      
REMARK 465     HIS D   124                                                      
REMARK 465     HIS D   125                                                      
REMARK 465     HIS D   126                                                      
REMARK 465     HIS D   127                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER D  85   CB    SER D  85   OG      0.175                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG C 103   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER B  71       -9.69    -59.86                                   
REMARK 500    ASN D  55       49.09     38.62                                   
REMARK 500    PHE D  63       67.27   -110.52                                   
REMARK 500    HIS D  90       49.55   -141.73                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2008        DISTANCE =  6.39 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1120  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2080   O                                                      
REMARK 620 2 HOH A2082   O    87.5                                              
REMARK 620 3 HOH A2078   O    90.5  87.6                                        
REMARK 620 4 HOH A2079   O    88.4 175.9  93.1                                  
REMARK 620 5 HOH A2081   O   176.2  92.0  85.7  92.1                            
REMARK 620 6 HOH A2077   O    93.5  92.1 175.9  87.5  90.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C1120  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C2122   O                                                      
REMARK 620 2 HOH C2124   O    89.9                                              
REMARK 620 3 HOH C2123   O   177.4  91.9                                        
REMARK 620 4 HOH C2120   O    87.2  91.6  90.8                                  
REMARK 620 5 HOH C2121   O    90.5 175.0  87.9  93.4                            
REMARK 620 6 HOH C2119   O    91.3  87.5  90.7 178.3  87.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1116                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1117                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1118                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1119                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1116                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1117                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1116                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1117                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1118                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1119                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1117                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1118                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1120                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C1120                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2JJS   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN CD47 IN COMPLEX WITH HUMAN SIGNAL REGULATORY      
REMARK 900 PROTEIN (SIRP) ALPHA                                                 
REMARK 900 RELATED ID: 2JJT   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN CD47 IN COMPLEX WITH HUMAN SIGNAL REGULATORY      
REMARK 900 PROTEIN (SIRP) ALPHA                                                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUE NUMBERING IS FOR MATURE PROTEIN (LACKING N-                  
REMARK 999 TERMINAL 18 AMINO ACID SIGNAL SEQUENCE).  RESIDUE 1 (GLN)            
REMARK 999 CYCLISES TO FORM A PYROGLUTAMIC ACID.  RESIDUE 15 WAS                
REMARK 999 MUTATED FROM CYS TO GLY.                                             
DBREF  2VSC A    1   118  UNP    Q08722   CD47_HUMAN      19    136             
DBREF  2VSC A  119   127  PDB    2VSC     2VSC           119    127             
DBREF  2VSC B    1   118  UNP    Q08722   CD47_HUMAN      19    136             
DBREF  2VSC B  119   127  PDB    2VSC     2VSC           119    127             
DBREF  2VSC C    1   118  UNP    Q08722   CD47_HUMAN      19    136             
DBREF  2VSC C  119   127  PDB    2VSC     2VSC           119    127             
DBREF  2VSC D    1   118  UNP    Q08722   CD47_HUMAN      19    136             
DBREF  2VSC D  119   127  PDB    2VSC     2VSC           119    127             
SEQADV 2VSC GLY A   15  UNP  Q08722    CYS    33 ENGINEERED MUTATION            
SEQADV 2VSC GLY B   15  UNP  Q08722    CYS    33 ENGINEERED MUTATION            
SEQADV 2VSC GLY C   15  UNP  Q08722    CYS    33 ENGINEERED MUTATION            
SEQADV 2VSC GLY D   15  UNP  Q08722    CYS    33 ENGINEERED MUTATION            
SEQRES   1 A  127  PCA LEU LEU PHE ASN LYS THR LYS SER VAL GLU PHE THR          
SEQRES   2 A  127  PHE GLY ASN ASP THR VAL VAL ILE PRO CYS PHE VAL THR          
SEQRES   3 A  127  ASN MET GLU ALA GLN ASN THR THR GLU VAL TYR VAL LYS          
SEQRES   4 A  127  TRP LYS PHE LYS GLY ARG ASP ILE TYR THR PHE ASP GLY          
SEQRES   5 A  127  ALA LEU ASN LYS SER THR VAL PRO THR ASP PHE SER SER          
SEQRES   6 A  127  ALA LYS ILE GLU VAL SER GLN LEU LEU LYS GLY ASP ALA          
SEQRES   7 A  127  SER LEU LYS MET ASP LYS SER ASP ALA VAL SER HIS THR          
SEQRES   8 A  127  GLY ASN TYR THR CYS GLU VAL THR GLU LEU THR ARG GLU          
SEQRES   9 A  127  GLY GLU THR ILE ILE GLU LEU LYS TYR ARG VAL VAL SER          
SEQRES  10 A  127  TRP SER THR ARG HIS HIS HIS HIS HIS HIS                      
SEQRES   1 B  127  PCA LEU LEU PHE ASN LYS THR LYS SER VAL GLU PHE THR          
SEQRES   2 B  127  PHE GLY ASN ASP THR VAL VAL ILE PRO CYS PHE VAL THR          
SEQRES   3 B  127  ASN MET GLU ALA GLN ASN THR THR GLU VAL TYR VAL LYS          
SEQRES   4 B  127  TRP LYS PHE LYS GLY ARG ASP ILE TYR THR PHE ASP GLY          
SEQRES   5 B  127  ALA LEU ASN LYS SER THR VAL PRO THR ASP PHE SER SER          
SEQRES   6 B  127  ALA LYS ILE GLU VAL SER GLN LEU LEU LYS GLY ASP ALA          
SEQRES   7 B  127  SER LEU LYS MET ASP LYS SER ASP ALA VAL SER HIS THR          
SEQRES   8 B  127  GLY ASN TYR THR CYS GLU VAL THR GLU LEU THR ARG GLU          
SEQRES   9 B  127  GLY GLU THR ILE ILE GLU LEU LYS TYR ARG VAL VAL SER          
SEQRES  10 B  127  TRP SER THR ARG HIS HIS HIS HIS HIS HIS                      
SEQRES   1 C  127  PCA LEU LEU PHE ASN LYS THR LYS SER VAL GLU PHE THR          
SEQRES   2 C  127  PHE GLY ASN ASP THR VAL VAL ILE PRO CYS PHE VAL THR          
SEQRES   3 C  127  ASN MET GLU ALA GLN ASN THR THR GLU VAL TYR VAL LYS          
SEQRES   4 C  127  TRP LYS PHE LYS GLY ARG ASP ILE TYR THR PHE ASP GLY          
SEQRES   5 C  127  ALA LEU ASN LYS SER THR VAL PRO THR ASP PHE SER SER          
SEQRES   6 C  127  ALA LYS ILE GLU VAL SER GLN LEU LEU LYS GLY ASP ALA          
SEQRES   7 C  127  SER LEU LYS MET ASP LYS SER ASP ALA VAL SER HIS THR          
SEQRES   8 C  127  GLY ASN TYR THR CYS GLU VAL THR GLU LEU THR ARG GLU          
SEQRES   9 C  127  GLY GLU THR ILE ILE GLU LEU LYS TYR ARG VAL VAL SER          
SEQRES  10 C  127  TRP SER THR ARG HIS HIS HIS HIS HIS HIS                      
SEQRES   1 D  127  PCA LEU LEU PHE ASN LYS THR LYS SER VAL GLU PHE THR          
SEQRES   2 D  127  PHE GLY ASN ASP THR VAL VAL ILE PRO CYS PHE VAL THR          
SEQRES   3 D  127  ASN MET GLU ALA GLN ASN THR THR GLU VAL TYR VAL LYS          
SEQRES   4 D  127  TRP LYS PHE LYS GLY ARG ASP ILE TYR THR PHE ASP GLY          
SEQRES   5 D  127  ALA LEU ASN LYS SER THR VAL PRO THR ASP PHE SER SER          
SEQRES   6 D  127  ALA LYS ILE GLU VAL SER GLN LEU LEU LYS GLY ASP ALA          
SEQRES   7 D  127  SER LEU LYS MET ASP LYS SER ASP ALA VAL SER HIS THR          
SEQRES   8 D  127  GLY ASN TYR THR CYS GLU VAL THR GLU LEU THR ARG GLU          
SEQRES   9 D  127  GLY GLU THR ILE ILE GLU LEU LYS TYR ARG VAL VAL SER          
SEQRES  10 D  127  TRP SER THR ARG HIS HIS HIS HIS HIS HIS                      
MODRES 2VSC ASN A   16  ASN  GLYCOSYLATION SITE                                 
MODRES 2VSC ASN A   32  ASN  GLYCOSYLATION SITE                                 
MODRES 2VSC ASN A   55  ASN  GLYCOSYLATION SITE                                 
MODRES 2VSC ASN A   93  ASN  GLYCOSYLATION SITE                                 
MODRES 2VSC ASN B   16  ASN  GLYCOSYLATION SITE                                 
MODRES 2VSC ASN B   93  ASN  GLYCOSYLATION SITE                                 
MODRES 2VSC ASN C   16  ASN  GLYCOSYLATION SITE                                 
MODRES 2VSC ASN C   32  ASN  GLYCOSYLATION SITE                                 
MODRES 2VSC ASN C   55  ASN  GLYCOSYLATION SITE                                 
MODRES 2VSC ASN C   93  ASN  GLYCOSYLATION SITE                                 
MODRES 2VSC ASN D   16  ASN  GLYCOSYLATION SITE                                 
MODRES 2VSC ASN D   32  ASN  GLYCOSYLATION SITE                                 
MODRES 2VSC PCA A    1  GLU  PYROGLUTAMIC ACID                                  
MODRES 2VSC PCA B    1  GLU  PYROGLUTAMIC ACID                                  
MODRES 2VSC PCA C    1  GLU  PYROGLUTAMIC ACID                                  
MODRES 2VSC PCA D    1  GLU  PYROGLUTAMIC ACID                                  
HET    PCA  A   1       8                                                       
HET    PCA  B   1       8                                                       
HET    PCA  C   1       8                                                       
HET    PCA  D   1       8                                                       
HET    NAG  A1116      14                                                       
HET    NAG  A1117      14                                                       
HET    NAG  A1118      14                                                       
HET    NAG  A1119      14                                                       
HET     MG  A1120       1                                                       
HET    NAG  B1116      14                                                       
HET    NAG  B1117      14                                                       
HET    NAG  C1116      14                                                       
HET    NAG  C1117      14                                                       
HET    NAG  C1118      14                                                       
HET    NAG  C1119      14                                                       
HET     MG  C1120       1                                                       
HET    NAG  D1117      14                                                       
HET    NAG  D1118      14                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   1  PCA    4(C5 H7 N O3)                                                
FORMUL   5  NAG    12(C8 H15 N O6)                                              
FORMUL   9   MG    2(MG 2+)                                                     
FORMUL  19  HOH   *353(H2 O)                                                    
HELIX    1   1 VAL A   70  LYS A   75  5                                   6    
HELIX    2   2 LYS A   84  VAL A   88  1                                   5    
HELIX    3   3 VAL B   70  LYS B   75  5                                   6    
HELIX    4   4 LYS B   84  VAL B   88  1                                   5    
HELIX    5   5 VAL C   70  LYS C   75  5                                   6    
HELIX    6   6 LYS C   84  VAL C   88  1                                   5    
HELIX    7   7 VAL D   70  LYS D   75  5                                   6    
HELIX    8   8 LYS D   84  VAL D   88  1                                   5    
SHEET    1  AA 6 SER A   9  PHE A  12  0                                        
SHEET    2  AA 6 ARG B 103  TYR B 113  1  O  GLU B 110   N  VAL A  10           
SHEET    3  AA 6 GLY A  92  GLU A 100 -1  O  GLY A  92   N  LEU B 111           
SHEET    4  AA 6 VAL A  36  PHE A  42 -1  O  TYR A  37   N  THR A  99           
SHEET    5  AA 6 ARG A  45  ASP A  51 -1  O  ARG A  45   N  PHE A  42           
SHEET    6  AA 6 LYS A  56  THR A  58 -1  O  LYS A  56   N  ASP A  51           
SHEET    1  AB 2 THR A  18  ILE A  21  0                                        
SHEET    2  AB 2 LEU A  80  ASP A  83 -1  O  LEU A  80   N  ILE A  21           
SHEET    1  BA12 SER B   9  PHE B  12  0                                        
SHEET    2  BA12 ARG A 103  TYR A 113  1  O  GLU A 110   N  VAL B  10           
SHEET    3  BA12 GLY B  92  GLU B 100 -1  O  GLY B  92   N  LEU A 111           
SHEET    4  BA12 VAL B  36  PHE B  42 -1  O  TYR B  37   N  THR B  99           
SHEET    5  BA12 ARG B  45  ASP B  51 -1  O  ARG B  45   N  PHE B  42           
SHEET    6  BA12 LYS B  56  PRO B  60 -1  O  LYS B  56   N  ASP B  51           
SHEET    7  BA12 LYS C  56  PRO C  60 -1  O  SER C  57   N  VAL B  59           
SHEET    8  BA12 ARG C  45  ASP C  51 -1  O  THR C  49   N  THR C  58           
SHEET    9  BA12 VAL C  36  PHE C  42 -1  O  VAL C  38   N  PHE C  50           
SHEET   10  BA12 GLY C  92  GLU C 100 -1  O  THR C  95   N  LYS C  41           
SHEET   11  BA12 ARG D 103  TYR D 113 -1  O  ARG D 103   N  GLU C 100           
SHEET   12  BA12 SER C   9  PHE C  12  1  O  VAL C  10   N  LYS D 112           
SHEET    1  BB 2 PHE B   4  ASN B   5  0                                        
SHEET    2  BB 2 PHE B  24  VAL B  25 -1  O  PHE B  24   N  ASN B   5           
SHEET    1  BC 2 THR B  18  ILE B  21  0                                        
SHEET    2  BC 2 LEU B  80  ASP B  83 -1  O  LEU B  80   N  ILE B  21           
SHEET    1  CA 2 THR C  18  ILE C  21  0                                        
SHEET    2  CA 2 LEU C  80  ASP C  83 -1  O  LEU C  80   N  ILE C  21           
SHEET    1  DA 6 SER D   9  PHE D  12  0                                        
SHEET    2  DA 6 ARG C 103  TYR C 113  1  O  GLU C 110   N  VAL D  10           
SHEET    3  DA 6 GLY D  92  GLU D 100 -1  O  GLY D  92   N  LEU C 111           
SHEET    4  DA 6 VAL D  36  PHE D  42 -1  O  TYR D  37   N  THR D  99           
SHEET    5  DA 6 ARG D  45  ASP D  51 -1  O  ARG D  45   N  PHE D  42           
SHEET    6  DA 6 LYS D  56  THR D  58 -1  O  LYS D  56   N  ASP D  51           
SHEET    1  DB 2 THR D  18  ILE D  21  0                                        
SHEET    2  DB 2 LEU D  80  ASP D  83 -1  O  LEU D  80   N  ILE D  21           
SSBOND   1 CYS A   23    CYS A   96                          1555   1555  2.04  
SSBOND   2 CYS B   23    CYS B   96                          1555   1555  2.05  
SSBOND   3 CYS C   23    CYS C   96                          1555   1555  2.04  
SSBOND   4 CYS D   23    CYS D   96                          1555   1555  2.04  
LINK         C   PCA A   1                 N   LEU A   2     1555   1555  1.34  
LINK         ND2 ASN A  16                 C1  NAG A1116     1555   1555  1.45  
LINK         ND2 ASN A  32                 C1  NAG A1117     1555   1555  1.45  
LINK         ND2 ASN A  55                 C1  NAG A1118     1555   1555  1.44  
LINK         ND2 ASN A  93                 C1  NAG A1119     1555   1555  1.46  
LINK        MG    MG A1120                 O   HOH A2080     1555   1555  2.19  
LINK        MG    MG A1120                 O   HOH A2082     1555   1555  2.17  
LINK        MG    MG A1120                 O   HOH A2078     1555   1555  2.15  
LINK        MG    MG A1120                 O   HOH A2079     1555   1555  2.17  
LINK        MG    MG A1120                 O   HOH A2081     1555   1555  2.18  
LINK        MG    MG A1120                 O   HOH A2077     1555   1555  2.16  
LINK         C   PCA B   1                 N   LEU B   2     1555   1555  1.33  
LINK         ND2 ASN B  16                 C1  NAG B1116     1555   1555  1.46  
LINK         ND2 ASN B  93                 C1  NAG B1117     1555   1555  1.44  
LINK         C   PCA C   1                 N   LEU C   2     1555   1555  1.33  
LINK         ND2 ASN C  16                 C1  NAG C1116     1555   1555  1.44  
LINK         ND2 ASN C  32                 C1  NAG C1117     1555   1555  1.43  
LINK         ND2 ASN C  55                 C1  NAG C1118     1555   1555  1.43  
LINK         ND2 ASN C  93                 C1  NAG C1119     1555   1555  1.45  
LINK        MG    MG C1120                 O   HOH C2122     1555   1555  2.18  
LINK        MG    MG C1120                 O   HOH C2124     1555   1555  2.19  
LINK        MG    MG C1120                 O   HOH C2123     1555   1555  2.18  
LINK        MG    MG C1120                 O   HOH C2120     1555   1555  2.18  
LINK        MG    MG C1120                 O   HOH C2121     1555   1555  2.18  
LINK        MG    MG C1120                 O   HOH C2119     1555   1555  2.16  
LINK         C   PCA D   1                 N   LEU D   2     1555   1555  1.33  
LINK         ND2 ASN D  16                 C1  NAG D1117     1555   1555  1.45  
LINK         ND2 ASN D  32                 C1  NAG D1118     1555   1555  1.46  
SITE     1 AC1  6 GLU A  11  ASN A  16  VAL A  19  VAL A  20                    
SITE     2 AC1  6 HOH A2074  HOH A2075                                          
SITE     1 AC2  5 ASN A  32  THR A  34  NAG A1118  LYS D  56                    
SITE     2 AC2  5 SER D  57                                                     
SITE     1 AC3  4 THR A  34  ASN A  55  THR A  61  NAG A1117                    
SITE     1 AC4  2 ASN A  93  GLU B 110                                          
SITE     1 AC5 10 GLU B  11  ASN B  16  VAL B  19  VAL B  20                    
SITE     2 AC5 10 HOH B2102  HOH B2103  HOH B2104  VAL C  25                    
SITE     3 AC5 10 THR C  26  HOH C2026                                          
SITE     1 AC6  2 GLU A 110  ASN B  93                                          
SITE     1 AC7  7 LYS B  75  GLU C  11  ASN C  16  VAL C  19                    
SITE     2 AC7  7 VAL C  20  HOH C2022  HOH C2108                               
SITE     1 AC8  8 ASN A  27  GLN B  31  ASN C  32  THR C  34                    
SITE     2 AC8  8 HOH C2109  HOH C2110  HOH C2111  HOH C2113                    
SITE     1 AC9  3 THR C  34  ASN C  55  HOH C2114                               
SITE     1 BC1  6 ARG A 114  GLU B  11  ASN C  93  HOH C2115                    
SITE     2 BC1  6 HOH C2116  GLU D 110                                          
SITE     1 BC2  5 GLU D  11  ASN D  16  VAL D  19  VAL D  20                    
SITE     2 BC2  5 HOH D2043                                                     
SITE     1 BC3  3 GLU C  11  ASN D  32  ARG D 114                               
SITE     1 BC4  8 LEU A 101  HOH A2077  HOH A2078  HOH A2079                    
SITE     2 BC4  8 HOH A2080  HOH A2081  HOH A2082  LEU B 101                    
SITE     1 BC5  6 HOH C2119  HOH C2120  HOH C2121  HOH C2122                    
SITE     2 BC5  6 HOH C2123  HOH C2124                                          
CRYST1  201.137   47.502   56.811  90.00  99.31  90.00 C 1 2 1      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      0.004972  0.000000  0.000815        0.00000                         
SCALE2      0.000000  0.021052  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017837        0.00000                         
HETATM    1  N   PCA A   1      17.722 -24.467  17.105  1.00 24.87           N  
ANISOU    1  N   PCA A   1     2585   2992   3871  -1043    519    -36       N  
HETATM    2  CA  PCA A   1      19.059 -25.066  17.091  1.00 24.85           C  
ANISOU    2  CA  PCA A   1     2456   3113   3872  -1109    621   -187       C  
HETATM    3  CB  PCA A   1      20.023 -24.214  17.924  1.00 25.85           C  
ANISOU    3  CB  PCA A   1     2511   3095   4217  -1166    599   -249       C  
HETATM    4  CG  PCA A   1      19.279 -22.940  18.311  1.00 26.77           C  
ANISOU    4  CG  PCA A   1     2722   2970   4480  -1160    505   -133       C  
HETATM    5  CD  PCA A   1      17.861 -23.242  17.882  1.00 25.69           C  
ANISOU    5  CD  PCA A   1     2695   2855   4211  -1055    454    -19       C  
HETATM    6  OE  PCA A   1      16.894 -22.518  18.153  1.00 25.09           O  
ANISOU    6  OE  PCA A   1     2682   2602   4247   -985    365     53       O  
HETATM    7  C   PCA A   1      19.037 -26.521  17.560  1.00 22.83           C  
ANISOU    7  C   PCA A   1     2149   2948   3578   -974    612   -381       C  
HETATM    8  O   PCA A   1      20.082 -27.178  17.550  1.00 22.25           O  
ANISOU    8  O   PCA A   1     1941   2956   3556   -989    677   -523       O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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