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Database: PDB
Entry: 5E6V
LinkDB: 5E6V
Original site: 5E6V 
HEADER    CELL ADHESION                           10-OCT-15   5E6V              
TITLE     RE-REFINEMENT OF THE CRYSTAL STRUCTURE OF THE PLEXIN-SEMAPHORIN-      
TITLE    2 INTEGRIN DOMAIN/HYBRID DOMAIN/I-EGF1 SEGMENT FROM THE HUMAN INTEGRIN 
TITLE    3 B2 SUBUNIT                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN BETA-2;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 23-125, 365-482;                              
COMPND   5 SYNONYM: CELL SURFACE ADHESION GLYCOPROTEINS LFA-1/CR3/P150,95       
COMPND   6 SUBUNIT BETA,COMPLEMENT RECEPTOR C3 SUBUNIT BETA;                    
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ITGB2, CD18, MFI7;                                             
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK;                                    
SOURCE   9 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3022                              
KEYWDS    LYMPHOCYTE FUNCTION-ASSOCIATED ANTIGEN-1, LFA-1, CELL ADHESION        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.SEN,T.A.SPRINGER                                                    
REVDAT   7   29-JUL-20 5E6V    1       COMPND REMARK HETNAM LINK                
REVDAT   7 2                   1       SITE   ATOM                              
REVDAT   6   04-DEC-19 5E6V    1       SEQRES                                   
REVDAT   5   27-SEP-17 5E6V    1       REMARK                                   
REVDAT   4   15-MAR-17 5E6V    1       JRNL   REMARK                            
REVDAT   3   11-MAY-16 5E6V    1       JRNL                                     
REVDAT   2   16-MAR-16 5E6V    1       JRNL                                     
REVDAT   1   02-MAR-16 5E6V    0                                                
JRNL        AUTH   M.SEN,T.A.SPRINGER                                           
JRNL        TITL   LEUKOCYTE INTEGRIN ALPHA L BETA 2 HEADPIECE STRUCTURES: THE  
JRNL        TITL 2 ALPHA I DOMAIN, THE POCKET FOR THE INTERNAL LIGAND, AND      
JRNL        TITL 3 CONCERTED MOVEMENTS OF ITS LOOPS.                            
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 113  2940 2016              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   26936951                                                     
JRNL        DOI    10.1073/PNAS.1601379113                                      
REMARK   0                                                                      
REMARK   0 THIS ENTRY 5E6V REFLECTS AN ALTERNATIVE MODELING OF THE              
REMARK   0 STRUCTURAL DATA IN R1YUKSF ORIGINAL DATA DETERMINED BY AUTHORS:      
REMARK   0 SHI, M., SUNDRAMURTHY, K., LIU, B., TAN, S.M., LAW, S.K., LESCAR,    
REMARK   0 J.                                                                   
REMARK   0 ORIGINAL DATA REFERENCE 1                                            
REMARK   0  PDB ID: 1YUK                                                        
REMARK   0  AUTH   M.SHI,K.SUNDRAMURTHY,B.LIU,S.M.TAN,S.K.LAW,J.LESCAR          
REMARK   0  TITL   THE CRYSTAL STRUCTURE OF THE PLEXIN-SEMAPHORIN-INTEGRIN      
REMARK   0  TITL 2 DOMAIN/HYBRID DOMAIN/I-EGF1 SEGMENT FROM THE HUMAN INTEGRIN  
REMARK   0  TITL 3 BETA2 SUBUNIT AT 1.8-A RESOLUTION.                           
REMARK   0  REF    J. BIOL. CHEM.                V. 280 30586 2005              
REMARK   0  REFN                   ISSN 0021-9258                               
REMARK   0  PMID   15965234                                                     
REMARK   0  DOI    10.1074/JBC.M502525200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_1839                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.48                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 24802                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1322                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 27.4820 -  3.7413    0.99     2830   165  0.1693 0.2233        
REMARK   3     2  3.7413 -  2.9707    1.00     2780   151  0.1618 0.2261        
REMARK   3     3  2.9707 -  2.5956    1.00     2727   165  0.1776 0.2187        
REMARK   3     4  2.5956 -  2.3584    1.00     2760   133  0.1857 0.2336        
REMARK   3     5  2.3584 -  2.1894    1.00     2750   146  0.1718 0.2137        
REMARK   3     6  2.1894 -  2.0604    1.00     2713   164  0.1852 0.2418        
REMARK   3     7  2.0604 -  1.9572    1.00     2717   144  0.1933 0.2526        
REMARK   3     8  1.9572 -  1.8720    1.00     2727   130  0.2127 0.2725        
REMARK   3     9  1.8720 -  1.8000    0.96     2634   124  0.2513 0.2794        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.860           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           1840                                  
REMARK   3   ANGLE     :  1.213           2506                                  
REMARK   3   CHIRALITY :  0.049            288                                  
REMARK   3   PLANARITY :  0.005            327                                  
REMARK   3   DIHEDRAL  : 12.294            701                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 55 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5345   6.9731  -1.3187              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1624 T22:   0.1633                                     
REMARK   3      T33:   0.2573 T12:   0.0133                                     
REMARK   3      T13:  -0.0235 T23:  -0.0351                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9497 L22:   1.1120                                     
REMARK   3      L33:   1.2769 L12:  -0.3717                                     
REMARK   3      L13:  -0.1630 L23:  -0.0671                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0157 S12:   0.0542 S13:  -0.2031                       
REMARK   3      S21:  -0.0810 S22:   0.1570 S23:  -0.1182                       
REMARK   3      S31:   0.2661 S32:   0.2669 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 56 THROUGH 79 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.1616  16.4135  16.1344              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3184 T22:   0.1865                                     
REMARK   3      T33:   0.3706 T12:   0.0914                                     
REMARK   3      T13:   0.0853 T23:  -0.0950                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5702 L22:   0.2368                                     
REMARK   3      L33:   1.3872 L12:  -0.1857                                     
REMARK   3      L13:  -0.2923 L23:  -0.1062                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7273 S12:   0.0316 S13:   1.2161                       
REMARK   3      S21:   0.1461 S22:  -0.2289 S23:  -0.0665                       
REMARK   3      S31:  -1.0050 S32:  -0.4175 S33:  -0.0035                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 80 THROUGH 343 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.6550   9.7724  20.3146              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2891 T22:   0.2459                                     
REMARK   3      T33:   0.1921 T12:   0.0168                                     
REMARK   3      T13:  -0.0126 T23:  -0.0427                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5807 L22:   1.2380                                     
REMARK   3      L33:   0.3292 L12:  -0.0799                                     
REMARK   3      L13:   0.4773 L23:  -0.1599                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1321 S12:  -0.2667 S13:   0.2815                       
REMARK   3      S21:   0.4025 S22:  -0.0079 S23:  -0.1082                       
REMARK   3      S31:   0.0444 S32:  -0.1693 S33:  -0.0118                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 344 THROUGH 395 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.6810   2.5109  25.3735              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2878 T22:   0.3510                                     
REMARK   3      T33:   0.1199 T12:   0.0373                                     
REMARK   3      T13:  -0.0752 T23:   0.0434                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9691 L22:   0.6985                                     
REMARK   3      L33:   0.5914 L12:  -0.2237                                     
REMARK   3      L13:  -0.3261 L23:   0.0950                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1605 S12:  -0.4699 S13:  -0.2924                       
REMARK   3      S21:   0.2230 S22:   0.0799 S23:  -0.2766                       
REMARK   3      S31:   0.2702 S32:   0.0972 S33:  -0.2793                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 396 THROUGH 435 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   0.8717  11.3470   4.9565              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2001 T22:   0.1688                                     
REMARK   3      T33:   0.2256 T12:   0.0174                                     
REMARK   3      T13:   0.0346 T23:   0.0187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1938 L22:   0.0236                                     
REMARK   3      L33:   0.8357 L12:   0.5057                                     
REMARK   3      L13:  -0.3019 L23:  -0.1796                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0131 S12:   0.1715 S13:   0.1688                       
REMARK   3      S21:   0.0263 S22:   0.1290 S23:  -0.0567                       
REMARK   3      S31:  -0.0427 S32:  -0.2190 S33:   0.0011                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 436 THROUGH 463 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  22.0662  14.2841 -19.5924              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2412 T22:   0.3458                                     
REMARK   3      T33:   0.2474 T12:   0.0148                                     
REMARK   3      T13:   0.0628 T23:  -0.0796                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3203 L22:   0.6579                                     
REMARK   3      L33:   0.9789 L12:  -0.0718                                     
REMARK   3      L13:   0.2348 L23:   0.1425                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0411 S12:   0.2844 S13:  -0.3788                       
REMARK   3      S21:  -0.1931 S22:  -0.0162 S23:  -0.3145                       
REMARK   3      S31:   0.3710 S32:   0.4245 S33:   0.0780                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5E6V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214452.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: AUTHOR USED THE SF DATA FROM ENTRY 1YUK                      
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       15.90900            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A  73    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  74    CG   CD   CE   NZ                                   
REMARK 470     TYR A 103    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   659     O    HOH A   817              2.03            
REMARK 500   O    HOH A   608     O    HOH A   689              2.17            
REMARK 500   O    HOH A   705     O    HOH A   822              2.17            
REMARK 500   O    HOH A   640     O    HOH A   817              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   654     O    HOH A   808     2655     2.15            
REMARK 500   O    HOH A   674     O    HOH A   785     2645     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    ASP A  58       73.85   -156.38                                   
REMARK 500    ASP A  68     -179.73    -67.03                                   
REMARK 500    LYS A  74      -94.88   -102.03                                   
REMARK 500    SER A 343      -65.80    -92.67                                   
REMARK 500    GLN A 382     -175.03    -67.47                                   
REMARK 500    HIS A 438       18.55     59.41                                   
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 A 830        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH A 831        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH A 832        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH A 833        DISTANCE =  6.83 ANGSTROMS                       
REMARK 525    HOH A 834        DISTANCE =  8.12 ANGSTROMS                       
REMARK 525    HOH A 835        DISTANCE =  9.14 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1YUK   RELATED DB: PDB                                   
REMARK 900 THIS ENTRY 5E6V REFLECTS AN ALTERNATIVE MODELING OF X-RAY DATA       
REMARK 900 R1YUKSF                                                              
DBREF  5E6V A    1   103  UNP    P05107   ITB2_HUMAN      23    125             
DBREF  5E6V A  343   460  UNP    P05107   ITB2_HUMAN     365    482             
SEQADV 5E6V HIS A  461  UNP  P05107              EXPRESSION TAG                 
SEQADV 5E6V HIS A  462  UNP  P05107              EXPRESSION TAG                 
SEQADV 5E6V HIS A  463  UNP  P05107              EXPRESSION TAG                 
SEQRES   1 A  224  PCA GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU          
SEQRES   2 A  224  CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS          
SEQRES   3 A  224  LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG          
SEQRES   4 A  224  CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA          
SEQRES   5 A  224  ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR          
SEQRES   6 A  224  GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO          
SEQRES   7 A  224  GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA          
SEQRES   8 A  224  ALA PHE ASN VAL THR PHE ARG ARG ALA LYS GLY TYR SER          
SEQRES   9 A  224  ARG VAL PHE LEU ASP HIS ASN ALA LEU PRO ASP THR LEU          
SEQRES  10 A  224  LYS VAL THR TYR ASP SER PHE CYS SER ASN GLY VAL THR          
SEQRES  11 A  224  HIS ARG ASN GLN PRO ARG GLY ASP CYS ASP GLY VAL GLN          
SEQRES  12 A  224  ILE ASN VAL PRO ILE THR PHE GLN VAL LYS VAL THR ALA          
SEQRES  13 A  224  THR GLU CYS ILE GLN GLU GLN SER PHE VAL ILE ARG ALA          
SEQRES  14 A  224  LEU GLY PHE THR ASP ILE VAL THR VAL GLN VAL LEU PRO          
SEQRES  15 A  224  GLN CYS GLU CYS ARG CYS ARG ASP GLN SER ARG ASP ARG          
SEQRES  16 A  224  SER LEU CYS HIS GLY LYS GLY PHE LEU GLU CYS GLY ILE          
SEQRES  17 A  224  CYS ARG CYS ASP THR GLY TYR ILE GLY LYS ASN CYS GLU          
SEQRES  18 A  224  HIS HIS HIS                                                  
MODRES 5E6V PCA A    1  GLN  MODIFIED RESIDUE                                   
HET    PCA  A   1       8                                                       
HET    NAG  B   1      14                                                       
HET    NAG  B   2      14                                                       
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    FUL  C   3      10                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     FUL BETA-L-FUCOPYRANOSE                                              
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE                                         
FORMUL   1  PCA    C5 H7 N O3                                                   
FORMUL   2  NAG    4(C8 H15 N O6)                                               
FORMUL   3  FUL    C6 H12 O5                                                    
FORMUL   4  HOH   *235(H2 O)                                                    
HELIX    1 AA1 SER A   10  GLU A   16  1                                   7    
HELIX    2 AA2 PRO A   35  ILE A   38  5                                   4    
HELIX    3 AA3 THR A   42  ARG A   49  1                                   8    
HELIX    4 AA4 ALA A   52  ASP A   54  5                                   3    
HELIX    5 AA5 SER A  435  GLY A  439  5                                   5    
SHEET    1 AA1 3 CYS A  40  ASP A  41  0                                        
SHEET    2 AA1 3 THR A  22  CYS A  24 -1  N  THR A  22   O  ASP A  41           
SHEET    3 AA1 3 ILE A  56  MET A  57 -1  O  MET A  57   N  TRP A  23           
SHEET    1 AA2 6 LEU A  62  GLN A  66  0                                        
SHEET    2 AA2 6 LYS A  80  LEU A  85 -1  O  THR A  82   N  GLU A  64           
SHEET    3 AA2 6 VAL A 415  PRO A 421  1  O  GLN A 418   N  LEU A  83           
SHEET    4 AA2 6 GLN A 402  ALA A 408 -1  N  GLN A 402   O  VAL A 419           
SHEET    5 AA2 6 TYR A 103  HIS A 349 -1  N  ASP A 348   O  ARG A 407           
SHEET    6 AA2 6 GLY A 376  VAL A 381 -1  O  GLY A 380   N  SER A 343           
SHEET    1 AA3 5 LEU A  76  SER A  77  0                                        
SHEET    2 AA3 5 ALA A  91  PHE A  97 -1  O  THR A  96   N  SER A  77           
SHEET    3 AA3 5 ILE A 387  ALA A 395 -1  O  VAL A 391   N  PHE A  93           
SHEET    4 AA3 5 LEU A 356  PHE A 363 -1  N  PHE A 363   O  THR A 388           
SHEET    5 AA3 5 THR A 369  GLN A 373 -1  O  GLN A 373   N  TYR A 360           
SHEET    1 AA4 2 GLY A 441  GLU A 444  0                                        
SHEET    2 AA4 2 ILE A 447  CYS A 450 -1  O  ARG A 449   N  PHE A 442           
SHEET    1 AA5 2 TYR A 454  ILE A 455  0                                        
SHEET    2 AA5 2 HIS A 461  HIS A 462 -1  O  HIS A 461   N  ILE A 455           
SSBOND   1 CYS A    3    CYS A   21                          1555   1555  2.08  
SSBOND   2 CYS A   11    CYS A  425                          1555   1555  2.01  
SSBOND   3 CYS A   14    CYS A   40                          1555   1555  2.08  
SSBOND   4 CYS A   24    CYS A   51                          1555   1555  2.09  
SSBOND   5 CYS A  364    CYS A  378                          1555   1555  2.04  
SSBOND   6 CYS A  398    CYS A  423                          1555   1555  2.05  
SSBOND   7 CYS A  427    CYS A  445                          1555   1555  2.05  
SSBOND   8 CYS A  437    CYS A  448                          1555   1555  2.06  
SSBOND   9 CYS A  450    CYS A  459                          1555   1555  2.05  
LINK         C   PCA A   1                 N   GLU A   2     1555   1555  1.33  
LINK         ND2 ASN A  28                 C1  NAG C   1     1555   1555  1.43  
LINK         ND2 ASN A  94                 C1  NAG B   1     1555   1555  1.43  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.44  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.44  
LINK         O6  NAG C   1                 C1  FUL C   3     1555   1555  1.44  
CISPEP   1 SER A   77    PRO A   78          0         0.32                     
CRYST1   58.600   31.818   74.950  90.00  91.20  90.00 P 1 21 1      2          
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      0.017065  0.000000  0.000357        0.00000                         
SCALE2      0.000000  0.031429  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013345        0.00000                         
HETATM    1  N   PCA A   1      21.134   3.309  12.563  1.00 60.27           N  
HETATM    2  CA  PCA A   1      20.325   2.938  11.411  1.00 54.61           C  
HETATM    3  CB  PCA A   1      20.039   4.179  10.571  1.00 54.77           C  
HETATM    4  CG  PCA A   1      21.079   5.221  10.961  1.00 48.69           C  
HETATM    5  CD  PCA A   1      21.588   4.671  12.269  1.00 64.14           C  
HETATM    6  OE  PCA A   1      22.313   5.329  13.020  1.00 68.62           O  
HETATM    7  C   PCA A   1      21.102   1.958  10.547  1.00 44.77           C  
HETATM    8  O   PCA A   1      22.335   1.962  10.572  1.00 43.26           O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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