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Database: PDB
Entry: 2JJS
LinkDB: 2JJS
Original site: 2JJS 
HEADER    CELL ADHESION                           22-APR-08   2JJS              
TITLE     STRUCTURE OF HUMAN CD47 IN COMPLEX WITH HUMAN SIGNAL REGULATORY       
TITLE    2 PROTEIN (SIRP) ALPHA                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE SUBSTRATE 1;
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: N-TERMINAL ECTODOMAIN, RESIDUES 31-148;                    
COMPND   5 SYNONYM: SIRP ALPHA, SHP SUBSTRATE 1, SHPS-1, INHIBITORY RECEPTOR    
COMPND   6 SHPS-1, SIGNAL REGULATORY PROTEIN ALPHA-1, SIRP-ALPHA-1, SIRP-ALPHA- 
COMPND   7 2, SIRP-ALPHA- 3, MYD-1 ANTIGEN, BRAIN IG-LIKE MOLECULE WITH         
COMPND   8 TYROSINE- BASED ACTIVATION MOTIFS, BIT, MACROPHAGE FUSION RECEPTOR,  
COMPND   9 P84, CD172A ANTIGEN;                                                 
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: LEUKOCYTE SURFACE ANTIGEN CD47;                            
COMPND  13 CHAIN: C, D;                                                         
COMPND  14 FRAGMENT: IMMUNOGLOBULIN-SUPERFAMILY ECTODOMAIN, RESIDUES 19-136;    
COMPND  15 SYNONYM: CD47, INTEGRIN-ASSOCIATED PROTEIN, IAP, ANTIGENIC SURFACE   
COMPND  16 DETERMINANT PROTEIN OA3, PROTEIN MER6;                               
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 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;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  17 EXPRESSION_SYSTEM_VARIANT: LEC3.2.8.1;                               
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: CHO;                                    
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PEE14                                     
KEYWDS    SIGNAL REGULATORY PROTEIN ALPHA, IMMUNOGLOBULIN SUPERFAMILY,          
KEYWDS   2 TRANSMEMBRANE, PHOSPHOPROTEIN, PAIRED RECEPTOR, POLYMORPHISM,        
KEYWDS   3 GLYCOPROTEIN, CELL ADHESION, PYRROLIDONE CARBOXYLIC ACID,            
KEYWDS   4 ALTERNATIVE SPLICING, IMMUNOGLOBULIN DOMAIN, SIRP, CD47, SIRPA,      
KEYWDS   5 MEMBRANE, SH3-BINDING                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.HATHERLEY,S.C.GRAHAM,J.TURNER,K.HARLOS,D.I.STUART,A.N.BARCLAY       
REVDAT   5   11-MAR-20 2JJS    1       SEQRES                                   
REVDAT   4   03-APR-19 2JJS    1       SOURCE                                   
REVDAT   3   13-MAR-19 2JJS    1       TITLE  JRNL   REMARK LINK                
REVDAT   2   24-FEB-09 2JJS    1       VERSN                                    
REVDAT   1   05-AUG-08 2JJS    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 1097-4164                               
JRNL        PMID   18657508                                                     
JRNL        DOI    10.1016/J.MOLCEL.2008.05.026                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 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) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 89.44                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 43948                          
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) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2345                            
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) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3208                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 168                          
REMARK   3   BIN FREE R VALUE                    : 0.3000                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3626                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 102                                     
REMARK   3   SOLVENT ATOMS            : 540                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.50000                                              
REMARK   3    B22 (A**2) : 0.34000                                              
REMARK   3    B33 (A**2) : -0.86000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.09000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.127         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.125         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.085         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.986         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3797 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2563 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5158 ; 1.269 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6243 ; 0.842 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   467 ; 6.715 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   156 ;33.176 ;24.615       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   644 ;10.867 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;19.291 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   610 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4232 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   726 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   452 ; 0.187 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2455 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1731 ; 0.168 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1940 ; 0.098 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   366 ; 0.127 ; 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):     6 ; 0.184 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    35 ; 0.222 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    21 ; 0.132 ; 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):  2345 ; 1.708 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3795 ; 2.470 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1566 ; 3.961 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1361 ; 6.381 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   116                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.6300  -7.4900  40.6310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0958 T22:  -0.0566                                     
REMARK   3      T33:  -0.1639 T12:  -0.0330                                     
REMARK   3      T13:   0.0142 T23:  -0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1340 L22:   1.0986                                     
REMARK   3      L33:   1.2427 L12:  -0.1592                                     
REMARK   3      L13:  -0.1886 L23:  -0.0676                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0389 S12:   0.0122 S13:   0.0020                       
REMARK   3      S21:   0.0253 S22:   0.0127 S23:   0.0214                       
REMARK   3      S31:   0.0138 S32:  -0.1384 S33:   0.0262                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   119                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.4240   0.2380   3.7440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1249 T22:  -0.0875                                     
REMARK   3      T33:  -0.1665 T12:  -0.0023                                     
REMARK   3      T13:  -0.0043 T23:   0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7877 L22:   1.2321                                     
REMARK   3      L33:   0.8614 L12:   0.1547                                     
REMARK   3      L13:   0.0180 L23:  -0.0631                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0148 S12:   0.0540 S13:  -0.0208                       
REMARK   3      S21:  -0.0405 S22:   0.0004 S23:   0.0205                       
REMARK   3      S31:   0.0236 S32:  -0.0196 S33:   0.0144                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   116                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.3700 -21.1630  21.7400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1007 T22:  -0.0968                                     
REMARK   3      T33:  -0.1472 T12:  -0.0284                                     
REMARK   3      T13:  -0.0062 T23:   0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4095 L22:   0.6167                                     
REMARK   3      L33:   2.4153 L12:   0.1615                                     
REMARK   3      L13:  -0.0170 L23:   0.2880                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0373 S12:   0.0010 S13:  -0.0316                       
REMARK   3      S21:   0.0563 S22:  -0.0486 S23:  -0.0115                       
REMARK   3      S31:   0.1277 S32:   0.0425 S33:   0.0113                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   116                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.0470  14.7340  25.1970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1161 T22:  -0.0866                                     
REMARK   3      T33:  -0.1450 T12:   0.0002                                     
REMARK   3      T13:   0.0028 T23:   0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6687 L22:   0.8509                                     
REMARK   3      L33:   2.0707 L12:  -0.3992                                     
REMARK   3      L13:  -0.1681 L23:   0.4135                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0510 S12:  -0.0947 S13:   0.0581                       
REMARK   3      S21:   0.0374 S22:   0.0883 S23:  -0.0225                       
REMARK   3      S31:  -0.1219 S32:   0.0458 S33:  -0.0373                       
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 2JJS 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_1290036000.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-07; NULL                    
REMARK 200  TEMPERATURE           (KELVIN) : 100; NULL                          
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : ESRF; ESRF                         
REMARK 200  BEAMLINE                       : ID23-2; BM14                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.873; 1.5498                      
REMARK 200  MONOCHROMATOR                  : SI(111) MONOCHROMATOR; NULL        
REMARK 200  OPTICS                         : MIRRORS; NULL                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; NULL                          
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH; NULL                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46373                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 10.30                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.79000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL                        
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2UV3 FOR CHAINS A AND B, PDB ENTRY 2ICC    
REMARK 200  FOR CHAINS C AND D                                                  
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 NL SIRP ALPHA / CD47 COMPLEX (1:1    
REMARK 280  RATIO, EACH PROTEIN AT APPROX. 0.375 UM) PLUS 100 NL RESERVOIR      
REMARK 280  (0.2 M POTASSIUM IODIDE, 20% W/V PEG 3350) EQUILIBRATED AGAINST     
REMARK 280  95 UL OF RESERVOIR AT 5 C., PH 7.4, TEMPERATURE 278K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       36.20500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 2300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.9 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 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: 2260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.1 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, CYS 33 TO GLY                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, CYS 33 TO GLY                         
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     PRO A   117                                                      
REMARK 465     SER A   118                                                      
REMARK 465     THR A   119                                                      
REMARK 465     ARG A   120                                                      
REMARK 465     HIS 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     ARG B   120                                                      
REMARK 465     HIS 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     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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 116    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG1  THR B    88     OE1  GLU B   110              2.18            
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    LEU C 101     -109.21     52.76                                   
REMARK 500    LEU D 101     -108.28     56.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1117                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1118                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1120                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1117                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1118                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1117                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B1121                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1118                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B1122                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C1122                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B1124                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D1119                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D1120                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1119                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B1125                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1121                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C1119                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1122                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C1120                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C1121                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D1121                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D1122                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VSC   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE IMMUNOGLOBULIN-SUPERFAMILY ECTODOMAIN OF HUMAN CD47 
REMARK 900 RELATED ID: 2JJT   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN CD47 IN COMPLEX WITH HUMAN SIGNAL RECEPTOR        
REMARK 900 PEPTIDE (SIRP) ALPHA                                                 
REMARK 900 RELATED ID: 2UV3   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE SIGNAL-REGULATORY PROTEIN ( SIRP) ALPHA DOMAIN      
REMARK 900 THAT BINDS CD47.                                                     
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SIRP ALPHA (CHAINS A AND B) RESIDUE NUMBERING IS FOR THE             
REMARK 999 MATURE PROTEIN (LACKING N-TERMINAL 30 AMINO ACID SIGNAL              
REMARK 999 SEQUENCE).  C-TERMINAL PURIFICATION TAG (TRHHHHHH) IS                
REMARK 999 ADDED.                                                               
REMARK 999 CD47 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.  C-TERMINAL PURIFICATION TAG (              
REMARK 999 STRHHHHHH) IS ADDED.                                                 
DBREF  2JJS A    1   118  UNP    P78324   SHPS1_HUMAN     31    148             
DBREF  2JJS A  119   126  PDB    2JJS     2JJS           119    126             
DBREF  2JJS B    1   118  UNP    P78324   SHPS1_HUMAN     31    148             
DBREF  2JJS B  119   126  PDB    2JJS     2JJS           119    126             
DBREF  2JJS C    1   118  UNP    Q08722   CD47_HUMAN      19    136             
DBREF  2JJS C  119   127  PDB    2JJS     2JJS           119    127             
DBREF  2JJS D    1   118  UNP    Q08722   CD47_HUMAN      19    136             
DBREF  2JJS D  119   127  PDB    2JJS     2JJS           119    127             
SEQADV 2JJS GLY C   15  UNP  Q08722    CYS    33 ENGINEERED MUTATION            
SEQADV 2JJS GLY D   15  UNP  Q08722    CYS    33 ENGINEERED MUTATION            
SEQRES   1 A  126  GLU GLU GLU LEU GLN VAL ILE GLN PRO ASP LYS SER VAL          
SEQRES   2 A  126  SER VAL ALA ALA GLY GLU SER ALA ILE LEU HIS CYS THR          
SEQRES   3 A  126  VAL THR SER LEU ILE PRO VAL GLY PRO ILE GLN TRP PHE          
SEQRES   4 A  126  ARG GLY ALA GLY PRO ALA ARG GLU LEU ILE TYR ASN GLN          
SEQRES   5 A  126  LYS GLU GLY HIS PHE PRO ARG VAL THR THR VAL SER GLU          
SEQRES   6 A  126  SER THR LYS ARG GLU ASN MET ASP PHE SER ILE SER ILE          
SEQRES   7 A  126  SER ASN ILE THR PRO ALA ASP ALA GLY THR TYR TYR CYS          
SEQRES   8 A  126  VAL LYS PHE ARG LYS GLY SER PRO ASP THR GLU PHE LYS          
SEQRES   9 A  126  SER GLY ALA GLY THR GLU LEU SER VAL ARG ALA LYS PRO          
SEQRES  10 A  126  SER THR ARG HIS HIS HIS HIS HIS HIS                          
SEQRES   1 B  126  GLU GLU GLU LEU GLN VAL ILE GLN PRO ASP LYS SER VAL          
SEQRES   2 B  126  SER VAL ALA ALA GLY GLU SER ALA ILE LEU HIS CYS THR          
SEQRES   3 B  126  VAL THR SER LEU ILE PRO VAL GLY PRO ILE GLN TRP PHE          
SEQRES   4 B  126  ARG GLY ALA GLY PRO ALA ARG GLU LEU ILE TYR ASN GLN          
SEQRES   5 B  126  LYS GLU GLY HIS PHE PRO ARG VAL THR THR VAL SER GLU          
SEQRES   6 B  126  SER THR LYS ARG GLU ASN MET ASP PHE SER ILE SER ILE          
SEQRES   7 B  126  SER ASN ILE THR PRO ALA ASP ALA GLY THR TYR TYR CYS          
SEQRES   8 B  126  VAL LYS PHE ARG LYS GLY SER PRO ASP THR GLU PHE LYS          
SEQRES   9 B  126  SER GLY ALA GLY THR GLU LEU SER VAL ARG ALA LYS PRO          
SEQRES  10 B  126  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 2JJS ASN C   16  ASN  GLYCOSYLATION SITE                                 
MODRES 2JJS ASN C   32  ASN  GLYCOSYLATION SITE                                 
MODRES 2JJS ASN C   93  ASN  GLYCOSYLATION SITE                                 
MODRES 2JJS ASN D   16  ASN  GLYCOSYLATION SITE                                 
MODRES 2JJS ASN D   32  ASN  GLYCOSYLATION SITE                                 
MODRES 2JJS ASN D   93  ASN  GLYCOSYLATION SITE                                 
MODRES 2JJS PCA C    1  GLU  PYROGLUTAMIC ACID                                  
MODRES 2JJS PCA D    1  GLU  PYROGLUTAMIC ACID                                  
HET    PCA  C   1       8                                                       
HET    PCA  D   1       8                                                       
HET    NAG  A1117      14                                                       
HET    IOD  A1118       1                                                       
HET    IOD  A1119       1                                                       
HET    IOD  A1120       1                                                       
HET    IOD  A1121       1                                                       
HET    IOD  A1122       1                                                       
HET    NAG  B1120      14                                                       
HET    IOD  B1121       1                                                       
HET    IOD  B1122       1                                                       
HET    IOD  B1123       1                                                       
HET    IOD  B1124       1                                                       
HET    IOD  B1125       1                                                       
HET    NAG  C1117      14                                                       
HET    NAG  C1118      14                                                       
HET    IOD  C1119       1                                                       
HET    IOD  C1120       1                                                       
HET    IOD  C1121       1                                                       
HET    IOD  C1122       1                                                       
HET    NAG  D1117      14                                                       
HET    NAG  D1118      14                                                       
HET    IOD  D1119       1                                                       
HET    IOD  D1120       1                                                       
HET    IOD  D1121       1                                                       
HET    IOD  D1122       1                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     IOD IODIDE ION                                                       
FORMUL   3  PCA    2(C5 H7 N O3)                                                
FORMUL   5  NAG    6(C8 H15 N O6)                                               
FORMUL   6  IOD    18(I 1-)                                                     
FORMUL  29  HOH   *540(H2 O)                                                    
HELIX    1   1 PRO A   83  ASP A   85  5                                   3    
HELIX    2   2 PRO B   83  ASP B   85  5                                   3    
HELIX    3   6 VAL C   70  LYS C   75  5                                   6    
HELIX    4   7 LYS C   84  VAL C   88  1                                   5    
HELIX    5  10 VAL D   70  LYS D   75  5                                   6    
HELIX    6  11 LYS D   84  VAL D   88  1                                   5    
SHEET    1  AA 2 VAL A   6  ILE A   7  0                                        
SHEET    2  AA 2 THR A  26  VAL A  27 -1  O  THR A  26   N  ILE A   7           
SHEET    1  AB 5 SER A  12  ALA A  16  0                                        
SHEET    2  AB 5 THR A 109  ARG A 114  1  O  GLU A 110   N  VAL A  13           
SHEET    3  AB 5 GLY A  87  ARG A  95 -1  O  GLY A  87   N  LEU A 111           
SHEET    4  AB 5 ILE A  36  ARG A  40 -1  O  GLN A  37   N  VAL A  92           
SHEET    5  AB 5 GLU A  47  TYR A  50 -1  O  GLU A  47   N  ARG A  40           
SHEET    1  AC 4 SER A  12  ALA A  16  0                                        
SHEET    2  AC 4 THR A 109  ARG A 114  1  O  GLU A 110   N  VAL A  13           
SHEET    3  AC 4 GLY A  87  ARG A  95 -1  O  GLY A  87   N  LEU A 111           
SHEET    4  AC 4 THR A 101  SER A 105 -1  O  THR A 101   N  ARG A  95           
SHEET    1  AD 3 ALA A  21  LEU A  23  0                                        
SHEET    2  AD 3 ILE A  76  ILE A  78 -1  O  ILE A  76   N  LEU A  23           
SHEET    3  AD 3 VAL A  60  THR A  62 -1  O  THR A  61   N  SER A  77           
SHEET    1  BA 2 VAL B   6  ILE B   7  0                                        
SHEET    2  BA 2 THR B  26  VAL B  27 -1  O  THR B  26   N  ILE B   7           
SHEET    1  BB 5 SER B  12  ALA B  16  0                                        
SHEET    2  BB 5 THR B 109  ARG B 114  1  O  GLU B 110   N  VAL B  13           
SHEET    3  BB 5 GLY B  87  ARG B  95 -1  O  GLY B  87   N  LEU B 111           
SHEET    4  BB 5 ILE B  36  ARG B  40 -1  O  GLN B  37   N  VAL B  92           
SHEET    5  BB 5 GLU B  47  TYR B  50 -1  O  GLU B  47   N  ARG B  40           
SHEET    1  BC 4 SER B  12  ALA B  16  0                                        
SHEET    2  BC 4 THR B 109  ARG B 114  1  O  GLU B 110   N  VAL B  13           
SHEET    3  BC 4 GLY B  87  ARG B  95 -1  O  GLY B  87   N  LEU B 111           
SHEET    4  BC 4 THR B 101  SER B 105 -1  O  THR B 101   N  ARG B  95           
SHEET    1  BD 3 ALA B  21  LEU B  23  0                                        
SHEET    2  BD 3 ILE B  76  ILE B  78 -1  O  ILE B  76   N  LEU B  23           
SHEET    3  BD 3 VAL B  60  THR B  62 -1  O  THR B  61   N  SER B  77           
SHEET    1  CA 6 SER C   9  PHE C  12  0                                        
SHEET    2  CA 6 ARG C 103  TYR C 113  1  O  GLU C 110   N  VAL C  10           
SHEET    3  CA 6 GLY C  92  GLU C 100 -1  O  GLY C  92   N  LEU C 111           
SHEET    4  CA 6 VAL C  36  PHE C  42 -1  O  TYR C  37   N  THR C  99           
SHEET    5  CA 6 ARG C  45  ASP C  51 -1  O  ARG C  45   N  PHE C  42           
SHEET    6  CA 6 LYS C  56  THR C  58 -1  O  LYS C  56   N  ASP C  51           
SHEET    1  CB 2 THR C  18  ILE C  21  0                                        
SHEET    2  CB 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 D 103  TYR D 113  1  O  GLU D 110   N  VAL D  10           
SHEET    3  DA 6 GLY D  92  GLU D 100 -1  O  GLY D  92   N  LEU D 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 3 THR D  18  ILE D  21  0                                        
SHEET    2  DB 3 LEU D  80  ASP D  83 -1  O  LEU D  80   N  ILE D  21           
SHEET    3  DB 3 LYS D  67  ILE D  68 -1  O  LYS D  67   N  LYS D  81           
SSBOND   1 CYS A   25    CYS A   91                          1555   1555  2.06  
SSBOND   2 CYS B   25    CYS B   91                          1555   1555  2.07  
SSBOND   3 CYS C   23    CYS C   96                          1555   1555  2.05  
SSBOND   4 CYS D   23    CYS D   96                          1555   1555  2.05  
LINK         C   PCA C   1                 N   LEU C   2     1555   1555  1.33  
LINK         ND2 ASN C  16                 C1  NAG C1117     1555   1555  1.45  
LINK         ND2 ASN C  32                 C1  NAG C1118     1555   1555  1.46  
LINK         ND2 ASN C  93                 C1  NAG B1120     1555   1555  1.45  
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  1.45  
LINK         ND2 ASN D  93                 C1  NAG A1117     1555   1555  1.46  
CISPEP   1 ILE A   31    PRO A   32          0         4.52                     
CISPEP   2 SER A   98    PRO A   99          0         3.54                     
CISPEP   3 ILE B   31    PRO B   32          0         5.29                     
CISPEP   4 SER B   98    PRO B   99          0         3.33                     
SITE     1 AC1  7 GLU C  11  ASN C  16  VAL C  19  VAL C  20                    
SITE     2 AC1  7 HOH C2133  HOH C2135  HOH C2136                               
SITE     1 AC2  3 ASN C  32  HOH C2137  HOH C2138                               
SITE     1 AC3 10 SER B  20  PRO B  58  ARG B  59  THR B  61                    
SITE     2 AC3 10 SER B  77  SER B  79  HOH B2136  ASN C  93                    
SITE     3 AC3 10 GLU C 110  HOH C2104                                          
SITE     1 AC4  8 ALA A 115  LYS A 116  GLU D  11  ASN D  16                    
SITE     2 AC4  8 VAL D  19  VAL D  20  HOH D2145  HOH D2146                    
SITE     1 AC5  1 ASN D  32                                                     
SITE     1 AC6  9 SER A  20  PRO A  58  ARG A  59  THR A  61                    
SITE     2 AC6  9 SER A  77  SER A  79  ASN D  93  GLU D 110                    
SITE     3 AC6  9 HOH D2117                                                     
SITE     1 AC7  1 ARG B  95                                                     
SITE     1 AC8  1 ARG A  95                                                     
SITE     1 AC9  1 LEU B  30                                                     
SITE     1 BC1  2 GLU C  11  HOH C2019                                          
SITE     1 BC2  1 THR B  88                                                     
SITE     1 BC3  3 THR D  34  GLU D  35  HOH D2061                               
SITE     1 BC4  1 ARG D  45                                                     
SITE     1 BC5  1 LEU A  30                                                     
SITE     1 BC6  1 ASN B  51                                                     
SITE     1 BC7  1 ASN A  51                                                     
SITE     1 BC8  1 ARG C  45                                                     
SITE     1 BC9  1 THR A  88                                                     
SITE     1 CC1  2 LYS C  67  LYS C  81                                          
SITE     1 CC2  2 THR C  34  HOH C2058                                          
SITE     1 CC3  1 LYS D  81                                                     
SITE     1 CC4  2 GLU D  11  HOH D2020                                          
CRYST1   42.477   72.410   89.826  90.00  95.01  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.023542  0.000000  0.002064        0.00000                         
SCALE2      0.000000  0.013810  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011175        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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