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Database: PDB
Entry: 4D90
LinkDB: 4D90
Original site: 4D90 
HEADER    CELL ADHESION                           11-JAN-12   4D90              
TITLE     CRYSTAL STRUCTURE OF DEL-1 EGF DOMAINS                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EGF-LIKE REPEAT AND DISCOIDIN I-LIKE DOMAIN-CONTAINING     
COMPND   3 PROTEIN 3;                                                           
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: EGF DOMAINS;                                               
COMPND   6 SYNONYM: DEVELOPMENTALLY-REGULATED ENDOTHELIAL CELL LOCUS 1 PROTEIN, 
COMPND   7 INTEGRIN-BINDING PROTEIN DEL1;                                       
COMPND   8 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: DEL-1, DEL1, EDIL3;                                            
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: 293 GNTI(-);                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PLEXM                                     
KEYWDS    RGD FINGER, CELL ADHESION, INNATE IMMUNITY, EXTRACELLULAR MATRIX      
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.CHEN,T.SCHURPF,T.SPRINGER,J.WANG                                    
REVDAT   3   15-NOV-17 4D90    1       REMARK                                   
REVDAT   2   02-JAN-13 4D90    1       JRNL                                     
REVDAT   1   30-MAY-12 4D90    0                                                
JRNL        AUTH   T.SCHURPF,Q.CHEN,J.H.LIU,R.WANG,T.A.SPRINGER,J.H.WANG        
JRNL        TITL   THE RGD FINGER OF DEL-1 IS A UNIQUE STRUCTURAL FEATURE       
JRNL        TITL 2 CRITICAL FOR INTEGRIN BINDING.                               
JRNL        REF    FASEB J.                      V.  26  3412 2012              
JRNL        REFN                   ISSN 0892-6638                               
JRNL        PMID   22601780                                                     
JRNL        DOI    10.1096/FJ.11-202036                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.7.3_928                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.32                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.970                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 13233                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.920                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 651                             
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 44.3232 -  4.4471    1.00     2524   129  0.2036 0.2488        
REMARK   3     2  4.4471 -  3.5303    1.00     2515   120  0.1840 0.2591        
REMARK   3     3  3.5303 -  3.0842    1.00     2517   140  0.2086 0.2530        
REMARK   3     4  3.0842 -  2.8022    1.00     2485   147  0.2198 0.2748        
REMARK   3     5  2.8022 -  2.6014    1.00     2541   115  0.2532 0.2994        
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              : 0.34                                          
REMARK   3   B_SOL              : 45.78                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.790           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.86460                                              
REMARK   3    B22 (A**2) : 8.86460                                              
REMARK   3    B33 (A**2) : -17.72920                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  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      :  0.010           2012                                  
REMARK   3   ANGLE     :  1.460           2710                                  
REMARK   3   CHIRALITY :  0.100            289                                  
REMARK   3   PLANARITY :  0.008            373                                  
REMARK   3   DIHEDRAL  : 16.633            746                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4D90 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000070033.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAR-10; 08-JUL-09               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : APS; APS                           
REMARK 200  BEAMLINE                       : 24-ID-C; 19-ID                     
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794; 0.9794                     
REMARK 200  MONOCHROMATOR                  : CRYO-COOLED SI(III) DOUBLE         
REMARK 200                                   CRYSTAL; ROSENBAUM-ROCK HIGH-      
REMARK 200                                   RESOLUTION DOUBLE CRYSTAL          
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315; ADSC QUANTUM     
REMARK 200                                   315                                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13233                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.77700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2VJ3                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE, 30% PEG 4000,     
REMARK 280  200 MM AMMONIUM ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.61467            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       18.80733            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 7.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ASP A    24                                                      
REMARK 465     ILE A    25                                                      
REMARK 465     GLY A    40                                                      
REMARK 465     LEU A    41                                                      
REMARK 465     ALA A    42                                                      
REMARK 465     ASP A    43                                                      
REMARK 465     GLY A    44                                                      
REMARK 465     GLY A   158                                                      
REMARK 465     GLY A   159                                                      
REMARK 465     GLY A   160                                                      
REMARK 465     HIS A   161                                                      
REMARK 465     HIS A   162                                                      
REMARK 465     HIS A   163                                                      
REMARK 465     HIS A   164                                                      
REMARK 465     HIS A   165                                                      
REMARK 465     HIS A   166                                                      
REMARK 465     ASP B    24                                                      
REMARK 465     ILE B    25                                                      
REMARK 465     GLY B    40                                                      
REMARK 465     LEU B    41                                                      
REMARK 465     ALA B    42                                                      
REMARK 465     ASP B    43                                                      
REMARK 465     GLY B    44                                                      
REMARK 465     SER B    45                                                      
REMARK 465     GLY B   158                                                      
REMARK 465     GLY B   159                                                      
REMARK 465     GLY B   160                                                      
REMARK 465     HIS B   161                                                      
REMARK 465     HIS B   162                                                      
REMARK 465     HIS B   163                                                      
REMARK 465     HIS B   164                                                      
REMARK 465     HIS B   165                                                      
REMARK 465     HIS B   166                                                      
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   SG   CYS B    31     CB   CYS B    48              1.92            
REMARK 500   OG1  THR B    73     C2   NGA B   601              2.03            
REMARK 500   OG1  THR A    73     C2   NGA A   601              2.11            
REMARK 500   ND2  ASN A   140     C2   NAG A   602              2.19            
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    ASN A  33       -4.40     64.22                                   
REMARK 500    GLU A  70      -11.17     84.34                                   
REMARK 500    GLU A 148      -13.64     82.20                                   
REMARK 500    PRO B  28     -152.44    -35.04                                   
REMARK 500    GLU B  70       -7.42     69.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP A   27     PRO A   28                 -130.95                    
REMARK 500 ASP B   27     PRO B   28                 -132.95                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    PRO B  28         10.47                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 604  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 119   OD1                                                    
REMARK 620 2 ILE B 120   O    81.2                                              
REMARK 620 3 LEU B 137   O   119.5 153.8                                        
REMARK 620 4 GLU B 122   OE1 123.4  71.2  83.5                                  
REMARK 620 5 ASP B 136   OD1 135.5  80.2  92.7  87.6                            
REMARK 620 6 HOH B 701   O    69.1  80.1  92.3  58.3 144.6                      
REMARK 620 7 ASP B 136   OD2  93.9  91.8 101.7 134.1  47.0 162.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 604  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A 120   O                                                      
REMARK 620 2 LEU A 137   O   156.0                                              
REMARK 620 3 ASN A 119   OD1  86.9 112.0                                        
REMARK 620 4 HOH A 701   O    85.6  89.4  64.7                                  
REMARK 620 5 ASP A 136   OD2  86.7 103.4 100.3 163.4                            
REMARK 620 6 ASP A 136   OD1  82.3  88.7 145.9 145.5  47.0                      
REMARK 620 7 GLU A 122   OE1  87.3  69.0 134.3  69.7 124.6  77.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGA A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGA B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 604                  
DBREF  4D90 A   24   157  UNP    O43854   EDIL3_HUMAN     24    157             
DBREF  4D90 B   24   157  UNP    O43854   EDIL3_HUMAN     24    157             
SEQADV 4D90 GLY A  158  UNP  O43854              EXPRESSION TAG                 
SEQADV 4D90 GLY A  159  UNP  O43854              EXPRESSION TAG                 
SEQADV 4D90 GLY A  160  UNP  O43854              EXPRESSION TAG                 
SEQADV 4D90 HIS A  161  UNP  O43854              EXPRESSION TAG                 
SEQADV 4D90 HIS A  162  UNP  O43854              EXPRESSION TAG                 
SEQADV 4D90 HIS A  163  UNP  O43854              EXPRESSION TAG                 
SEQADV 4D90 HIS A  164  UNP  O43854              EXPRESSION TAG                 
SEQADV 4D90 HIS A  165  UNP  O43854              EXPRESSION TAG                 
SEQADV 4D90 HIS A  166  UNP  O43854              EXPRESSION TAG                 
SEQADV 4D90 GLY B  158  UNP  O43854              EXPRESSION TAG                 
SEQADV 4D90 GLY B  159  UNP  O43854              EXPRESSION TAG                 
SEQADV 4D90 GLY B  160  UNP  O43854              EXPRESSION TAG                 
SEQADV 4D90 HIS B  161  UNP  O43854              EXPRESSION TAG                 
SEQADV 4D90 HIS B  162  UNP  O43854              EXPRESSION TAG                 
SEQADV 4D90 HIS B  163  UNP  O43854              EXPRESSION TAG                 
SEQADV 4D90 HIS B  164  UNP  O43854              EXPRESSION TAG                 
SEQADV 4D90 HIS B  165  UNP  O43854              EXPRESSION TAG                 
SEQADV 4D90 HIS B  166  UNP  O43854              EXPRESSION TAG                 
SEQRES   1 A  143  ASP ILE CYS ASP PRO ASN PRO CYS GLU ASN GLY GLY ILE          
SEQRES   2 A  143  CYS LEU PRO GLY LEU ALA ASP GLY SER PHE SER CYS GLU          
SEQRES   3 A  143  CYS PRO ASP GLY PHE THR ASP PRO ASN CYS SER SER VAL          
SEQRES   4 A  143  VAL GLU VAL ALA SER ASP GLU GLU GLU PRO THR SER ALA          
SEQRES   5 A  143  GLY PRO CYS THR PRO ASN PRO CYS HIS ASN GLY GLY THR          
SEQRES   6 A  143  CYS GLU ILE SER GLU ALA TYR ARG GLY ASP THR PHE ILE          
SEQRES   7 A  143  GLY TYR VAL CYS LYS CYS PRO ARG GLY PHE ASN GLY ILE          
SEQRES   8 A  143  HIS CYS GLN HIS ASN ILE ASN GLU CYS GLU VAL GLU PRO          
SEQRES   9 A  143  CYS LYS ASN GLY GLY ILE CYS THR ASP LEU VAL ALA ASN          
SEQRES  10 A  143  TYR SER CYS GLU CYS PRO GLY GLU PHE MET GLY ARG ASN          
SEQRES  11 A  143  CYS GLN TYR LYS GLY GLY GLY HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  143  ASP ILE CYS ASP PRO ASN PRO CYS GLU ASN GLY GLY ILE          
SEQRES   2 B  143  CYS LEU PRO GLY LEU ALA ASP GLY SER PHE SER CYS GLU          
SEQRES   3 B  143  CYS PRO ASP GLY PHE THR ASP PRO ASN CYS SER SER VAL          
SEQRES   4 B  143  VAL GLU VAL ALA SER ASP GLU GLU GLU PRO THR SER ALA          
SEQRES   5 B  143  GLY PRO CYS THR PRO ASN PRO CYS HIS ASN GLY GLY THR          
SEQRES   6 B  143  CYS GLU ILE SER GLU ALA TYR ARG GLY ASP THR PHE ILE          
SEQRES   7 B  143  GLY TYR VAL CYS LYS CYS PRO ARG GLY PHE ASN GLY ILE          
SEQRES   8 B  143  HIS CYS GLN HIS ASN ILE ASN GLU CYS GLU VAL GLU PRO          
SEQRES   9 B  143  CYS LYS ASN GLY GLY ILE CYS THR ASP LEU VAL ALA ASN          
SEQRES  10 B  143  TYR SER CYS GLU CYS PRO GLY GLU PHE MET GLY ARG ASN          
SEQRES  11 B  143  CYS GLN TYR LYS GLY GLY GLY HIS HIS HIS HIS HIS HIS          
MODRES 4D90 THR B   88  THR  GLYCOSYLATION SITE                                 
MODRES 4D90 THR A   88  THR  GLYCOSYLATION SITE                                 
MODRES 4D90 THR B   73  THR  GLYCOSYLATION SITE                                 
MODRES 4D90 THR A   73  THR  GLYCOSYLATION SITE                                 
MODRES 4D90 ASN B  140  ASN  GLYCOSYLATION SITE                                 
MODRES 4D90 ASN A  140  ASN  GLYCOSYLATION SITE                                 
HET    NGA  A 601      14                                                       
HET    NAG  A 602      14                                                       
HET    FUC  A 603      10                                                       
HET     CA  A 604       1                                                       
HET    NGA  B 601      14                                                       
HET    NAG  B 602      14                                                       
HET    FUC  B 603      10                                                       
HET     CA  B 604       1                                                       
HETNAM     NGA N-ACETYL-D-GALACTOSAMINE                                         
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  NGA    2(C8 H15 N O6)                                               
FORMUL   4  NAG    2(C8 H15 N O6)                                               
FORMUL   5  FUC    2(C6 H12 O5)                                                 
FORMUL   6   CA    2(CA 2+)                                                     
FORMUL  11  HOH   *50(H2 O)                                                     
HELIX    1   1 CYS A   31  GLY A   35  5                                   5    
HELIX    2   2 CYS B   31  GLY B   35  5                                   5    
HELIX    3   3 VAL B   65  GLU B   69  5                                   5    
SHEET    1   A 2 ILE A  36  LEU A  38  0                                        
SHEET    2   A 2 SER A  47  GLU A  49 -1  O  GLU A  49   N  ILE A  36           
SHEET    1   B 2 THR A  88  ILE A  91  0                                        
SHEET    2   B 2 TYR A 103  LYS A 106 -1  O  LYS A 106   N  THR A  88           
SHEET    1   C 2 TYR A  95  ARG A  96  0                                        
SHEET    2   C 2 THR A  99  PHE A 100 -1  O  THR A  99   N  ARG A  96           
SHEET    1   D 2 PHE A 111  ASN A 112  0                                        
SHEET    2   D 2 HIS A 118  ASN A 119 -1  O  HIS A 118   N  ASN A 112           
SHEET    1   E 2 ILE A 133  LEU A 137  0                                        
SHEET    2   E 2 ASN A 140  GLU A 144 -1  O  ASN A 140   N  LEU A 137           
SHEET    1   F 2 ILE B  36  LEU B  38  0                                        
SHEET    2   F 2 SER B  47  GLU B  49 -1  O  GLU B  49   N  ILE B  36           
SHEET    1   G 2 PHE B  54  THR B  55  0                                        
SHEET    2   G 2 SER B  61  VAL B  62 -1  O  SER B  61   N  THR B  55           
SHEET    1   H 2 THR B  88  ILE B  91  0                                        
SHEET    2   H 2 TYR B 103  LYS B 106 -1  O  LYS B 106   N  THR B  88           
SHEET    1   I 2 TYR B  95  ARG B  96  0                                        
SHEET    2   I 2 THR B  99  PHE B 100 -1  O  THR B  99   N  ARG B  96           
SHEET    1   J 2 PHE B 111  ASN B 112  0                                        
SHEET    2   J 2 HIS B 118  ASN B 119 -1  O  HIS B 118   N  ASN B 112           
SHEET    1   K 2 ILE B 133  LEU B 137  0                                        
SHEET    2   K 2 ASN B 140  GLU B 144 -1  O  GLU B 144   N  ILE B 133           
SSBOND   1 CYS A   26    CYS A   37                          1555   1555  2.03  
SSBOND   2 CYS A   31    CYS A   48                          1555   1555  2.03  
SSBOND   3 CYS A   50    CYS A   59                          1555   1555  2.04  
SSBOND   4 CYS A   78    CYS A   89                          1555   1555  2.07  
SSBOND   5 CYS A   83    CYS A  105                          1555   1555  2.03  
SSBOND   6 CYS A  107    CYS A  116                          1555   1555  2.11  
SSBOND   7 CYS A  123    CYS A  134                          1555   1555  2.07  
SSBOND   8 CYS A  128    CYS A  143                          1555   1555  2.04  
SSBOND   9 CYS A  145    CYS A  154                          1555   1555  2.08  
SSBOND  10 CYS B   26    CYS B   37                          1555   1555  2.03  
SSBOND  11 CYS B   31    CYS B   48                          1555   1555  2.03  
SSBOND  12 CYS B   50    CYS B   59                          1555   1555  2.04  
SSBOND  13 CYS B   78    CYS B   89                          1555   1555  2.07  
SSBOND  14 CYS B   83    CYS B  105                          1555   1555  2.04  
SSBOND  15 CYS B  107    CYS B  116                          1555   1555  2.10  
SSBOND  16 CYS B  123    CYS B  134                          1555   1555  2.08  
SSBOND  17 CYS B  128    CYS B  143                          1555   1555  2.03  
SSBOND  18 CYS B  145    CYS B  154                          1555   1555  2.08  
LINK         OG1 THR B  88                 C1  FUC B 603     1555   1555  1.41  
LINK         OG1 THR A  88                 C1  FUC A 603     1555   1555  1.41  
LINK         OG1 THR B  73                 C1  NGA B 601     1555   1555  1.45  
LINK         OG1 THR A  73                 C1  NGA A 601     1555   1555  1.45  
LINK         ND2 ASN B 140                 C1  NAG B 602     1555   1555  1.45  
LINK         ND2 ASN A 140                 C1  NAG A 602     1555   1555  1.45  
LINK         OD1 ASN B 119                CA    CA B 604     1555   1555  2.62  
LINK         O   ILE A 120                CA    CA A 604     1555   1555  2.63  
LINK         O   ILE B 120                CA    CA B 604     1555   1555  2.64  
LINK         O   LEU A 137                CA    CA A 604     1555   1555  2.70  
LINK         OD1 ASN A 119                CA    CA A 604     1555   1555  2.70  
LINK         O   LEU B 137                CA    CA B 604     1555   1555  2.71  
LINK         OE1 GLU B 122                CA    CA B 604     1555   1555  2.71  
LINK        CA    CA A 604                 O   HOH A 701     1555   1555  2.73  
LINK         OD1 ASP B 136                CA    CA B 604     1555   1555  2.76  
LINK         OD2 ASP A 136                CA    CA A 604     1555   1555  2.77  
LINK        CA    CA B 604                 O   HOH B 701     1555   1555  2.80  
LINK         OD1 ASP A 136                CA    CA A 604     1555   1555  2.81  
LINK         OD2 ASP B 136                CA    CA B 604     1555   1555  2.81  
LINK         OE1 GLU A 122                CA    CA A 604     1555   1555  2.83  
CISPEP   1 ASP A   56    PRO A   57          0         0.66                     
CISPEP   2 THR A   79    PRO A   80          0       -12.58                     
CISPEP   3 ASP B   56    PRO B   57          0        11.62                     
CISPEP   4 THR B   79    PRO B   80          0        -4.56                     
SITE     1 AC1  1 THR A  73                                                     
SITE     1 AC2  3 ASN A 140  TYR A 141  ARG A 152                               
SITE     1 AC3  7 GLY A  86  THR A  88  LYS A 106  CYS A 107                    
SITE     2 AC3  7 HOH A 717  HOH A 725  HOH A 729                               
SITE     1 AC4  6 ASN A 119  ILE A 120  GLU A 122  ASP A 136                    
SITE     2 AC4  6 LEU A 137  HOH A 701                                          
SITE     1 AC5  2 THR B  73  ALA B  75                                          
SITE     1 AC6  1 ASN B 140                                                     
SITE     1 AC7  5 GLY B  86  THR B  88  LYS B 106  CYS B 107                    
SITE     2 AC7  5 HOH B 709                                                     
SITE     1 AC8  6 ASN B 119  ILE B 120  GLU B 122  ASP B 136                    
SITE     2 AC8  6 LEU B 137  HOH B 701                                          
CRYST1   82.680   82.680   56.422  90.00  90.00 120.00 P 32          6          
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      0.012095  0.006983  0.000000        0.00000                         
SCALE2      0.000000  0.013966  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017724        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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