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Database: PDB
Entry: 2W86
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Original site: 2W86 
HEADER    GLYCOPROTEIN                            09-JAN-09   2W86              
TITLE     CRYSTAL STRUCTURE OF FIBRILLIN-1 DOMAINS CBEGF9HYB2CBEGF10,           
TITLE    2 CALCIUM SATURATED FORM                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBRILLIN-1;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CBEGF9HYB2CBEGF10, RESIDUES 807-951;                       
COMPND   5 SYNONYM: FIBRILLIN1;                                                 
COMPND   6 ENGINEERED: 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: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PQE30                                     
KEYWDS    FIBRILLIN, PHOSPHOPROTEIN, EGF-LIKE DOMAIN, DISEASE                   
KEYWDS   2 MUTATION, CRANIOSYNOSTOSIS, EXTRACELLULAR MATRIX,                    
KEYWDS   3 FIBRILLIN CALCIUM CBEGF HYBRID, CALCIUM, SECRETED,                   
KEYWDS   4 POLYMORPHISM, GLYCOPROTEIN                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.A.JENSEN,S.IQBAL,E.D.LOWE,C.REDFIELD,P.A.HANDFORD                   
REVDAT   1   26-MAY-09 2W86    0                                                
JRNL        AUTH   S.A.JENSEN,S.IQBAL,E.D.LOWE,C.REDFIELD,P.A.HANDFORD          
JRNL        TITL   STRUCTURE AND INTERDOMAIN INTERACTIONS OF A HYBRID           
JRNL        TITL 2 DOMAIN: A DISULPHIDE-RICH MODULE OF THE                      
JRNL        TITL 3 FIBRILLIN/LTBP SUPERFAMILY OF MATRIX PROTEINS.               
JRNL        REF    STRUCTURE                     V.  17   759 2009              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   19446531                                                     
JRNL        DOI    10.1016/J.STR.2009.03.014                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.800                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.750                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.09                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.91                          
REMARK   3   NUMBER OF REFLECTIONS             : 12682                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1872                          
REMARK   3   R VALUE            (WORKING SET) : 0.1851                          
REMARK   3   FREE R VALUE                     : 0.2212                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.3                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 673                             
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 41.7608 -  3.0776    1.00     2540   164  0.2027 0.2178        
REMARK   3     2  3.0776 -  2.4429    1.00     2422   135  0.1837 0.2274        
REMARK   3     3  2.4429 -  2.1341    0.99     2378   124  0.1705 0.2139        
REMARK   3     4  2.1341 -  1.9390    0.99     2349   119  0.1614 0.2140        
REMARK   3     5  1.9390 -  1.8000    0.97     2320   131  0.1663 0.2406        
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              : 0.366                                         
REMARK   3   B_SOL              : 55.373                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.23             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.88            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1118                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 148                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.46                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.19                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.5055                                              
REMARK   3    B22 (A**2) : -6.6722                                              
REMARK   3    B33 (A**2) : -6.4337                                              
REMARK   3    B12 (A**2) : -0.0000                                              
REMARK   3    B13 (A**2) : -0.0000                                              
REMARK   3    B23 (A**2) : -0.0000                                              
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      :  0.006           1089                                  
REMARK   3   ANGLE     :  1.027           1459                                  
REMARK   3   CHIRALITY :  0.068            170                                  
REMARK   3   PLANARITY :  0.005            191                                  
REMARK   3   DIHEDRAL  : 16.375            397                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 6:43                                
REMARK   3    ORIGIN FOR THE GROUP (A):  21.9716  25.5377  42.1944              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2128 T22:   0.1949                                     
REMARK   3      T33:   0.1569 T12:   0.0163                                     
REMARK   3      T13:  -0.0341 T23:   0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9758 L22:   0.6855                                     
REMARK   3      L33:  -0.0843 L12:  -0.1248                                     
REMARK   3      L13:   0.1056 L23:   0.0890                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1022 S12:   0.1967 S13:  -0.0129                       
REMARK   3      S21:   0.1692 S22:  -0.1682 S23:  -0.0931                       
REMARK   3      S31:  -0.1419 S32:   0.1461 S33:   0.0481                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 44:109                              
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8243  29.2869  59.6935              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1378 T22:   0.1400                                     
REMARK   3      T33:   0.1350 T12:  -0.0113                                     
REMARK   3      T13:   0.0139 T23:  -0.0027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2547 L22:  -0.0373                                     
REMARK   3      L33:   0.3310 L12:  -0.0096                                     
REMARK   3      L13:  -0.2379 L23:  -0.1697                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0303 S12:   0.0325 S13:  -0.0126                       
REMARK   3      S21:  -0.0533 S22:   0.0036 S23:   0.0020                       
REMARK   3      S31:   0.0185 S32:  -0.0885 S33:   0.0136                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 110:147                             
REMARK   3    ORIGIN FOR THE GROUP (A):   8.8133  28.6507  74.9865              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1501 T22:   0.1503                                     
REMARK   3      T33:   0.1266 T12:  -0.0069                                     
REMARK   3      T13:   0.0158 T23:   0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6942 L22:   1.4211                                     
REMARK   3      L33:   0.7181 L12:   0.1521                                     
REMARK   3      L13:  -0.3251 L23:   0.7470                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0597 S12:  -0.0239 S13:  -0.0183                       
REMARK   3      S21:   0.1389 S22:   0.0133 S23:  -0.0177                       
REMARK   3      S31:   0.1059 S32:   0.2263 S33:  -0.0447                       
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 2W86 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JAN-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-38384.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.040                              
REMARK 200  MONOCHROMATOR                  : SINGLE SILICON (111)               
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15382                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.70                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.79                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.3                               
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.30                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.7                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.60                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXD, SHARP                                         
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.2                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 7.5, 200 MM NAI,          
REMARK 280  16% PEG 3350                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       15.61600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.55250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.62900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.55250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       15.61600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       23.62900            
REMARK 290   SMTRY3   4  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 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
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 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   OG   SER A    73  -  O    HOH A  2079              1.87            
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 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    ILE A  60       84.53     71.87                                   
REMARK 500    SER A  74      -97.47   -136.57                                   
REMARK 500    SER A 128     -152.10   -153.77                                   
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 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 A1149  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 125   O                                                      
REMARK 620 2 ASP A 106   OD1  74.1                                              
REMARK 620 3 ILE A 107   O   143.0  81.1                                        
REMARK 620 4 ASN A 124   OD1  81.2 122.0  89.4                                  
REMARK 620 5 GLU A 109   OE1 139.3 144.4  73.6  82.9                            
REMARK 620 6 SER A 128   O    68.9 130.4 145.8  83.7  72.3                      
REMARK 620 7 HOH A2110   O   112.9  74.0  85.2 162.2  79.2  91.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1148  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2069   O                                                      
REMARK 620 2 GLU A   6   OE2  81.0                                              
REMARK 620 3 ILE A   4   O    90.1  70.5                                        
REMARK 620 4 SER A  20   O   105.5 140.6 146.2                                  
REMARK 620 5 SER A  23   O    98.2  79.2 146.9  61.4                            
REMARK 620 6 ASP A   3   OD1 108.5 143.6  74.3  72.3 131.3                      
REMARK 620 7 ASP A   3   OD2  63.6 138.5  87.6  73.6 124.7  46.8                
REMARK 620 8 ASN A  19   OD1 165.6  84.7  83.2  86.8  81.0  82.0 128.5          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1148                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1149                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1150                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1151                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1152                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1UZK   RELATED DB: PDB                                   
REMARK 900  INTEGRIN BINDING CBEGF22-TB4-CBEGF33 FRAGMENT                       
REMARK 900   OF HUMAN FIBRILLIN-1, CA BOUND TO                                  
REMARK 900  CBEGF23 DOMAIN ONLY.                                                
REMARK 900 RELATED ID: 1UZJ   RELATED DB: PDB                                   
REMARK 900  INTEGRIN BINDING CBEGF22-TB4-CBEGF33 FRAGMENT                       
REMARK 900   OF HUMAN FIBRILLIN-1, HOLO FORM.                                   
REMARK 900 RELATED ID: 1UZP   RELATED DB: PDB                                   
REMARK 900  INTEGRIN BINDING CBEGF22-TB4-CBEGF33 FRAGMENT                       
REMARK 900   OF HUMAN FIBRILLIN-1, SM BOUND FORM                                
REMARK 900  CBEGF23 DOMAIN ONLY.                                                
REMARK 900 RELATED ID: 1APJ   RELATED DB: PDB                                   
REMARK 900  NMR STUDY OF THE TRANSFORMING GROWTH FACTOR                         
REMARK 900   BETA BINDINGPROTEIN-LIKE DOMAIN (TB MODULE/                        
REMARK 900  8-CYS DOMAIN), NMR,21 STRUCTURES                                    
REMARK 900 RELATED ID: 1UZQ   RELATED DB: PDB                                   
REMARK 900  INTEGRIN BINDING CBEGF22-TB4-CBEGF33 FRAGMENT                       
REMARK 900   OF HUMAN FIBRILLIN-1, APO FORM CBEGF23                             
REMARK 900  DOMAIN ONLY.                                                        
REMARK 900 RELATED ID: 1LMJ   RELATED DB: PDB                                   
REMARK 900  NMR STUDY OF THE FIBRILLIN-1 CBEGF12-13                             
REMARK 900  PAIR OF CA2+BINDING EPIDERMAL GROWTH FACTOR                         
REMARK 900  -LIKE DOMAINS                                                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE DEPOSITED STRUCTURE CONTAINS ONLY THE                            
REMARK 999 CBEGF9HYB2CBEGF10 DOMAINS                                            
DBREF  2W86 A    1     2  PDB    2W86     2W86             1      2             
DBREF  2W86 A    3   147  UNP    P35555   FBN1_HUMAN     807    951             
SEQRES   1 A  147  SER ALA ASP ILE ASP GLU CYS GLU SER SER PRO CYS ILE          
SEQRES   2 A  147  ASN GLY VAL CYS LYS ASN SER PRO GLY SER PHE ILE CYS          
SEQRES   3 A  147  GLU CYS SER SER GLU SER THR LEU ASP PRO THR LYS THR          
SEQRES   4 A  147  ILE CYS ILE GLU THR ILE LYS GLY THR CYS TRP GLN THR          
SEQRES   5 A  147  VAL ILE ASP GLY ARG CYS GLU ILE ASN ILE ASN GLY ALA          
SEQRES   6 A  147  THR LEU LYS SER GLN CYS CYS SER SER LEU GLY ALA ALA          
SEQRES   7 A  147  TRP GLY SER PRO CYS THR LEU CYS GLN VAL ASP PRO ILE          
SEQRES   8 A  147  CYS GLY LYS GLY TYR SER ARG ILE LYS GLY THR GLN CYS          
SEQRES   9 A  147  GLU ASP ILE ASP GLU CYS GLU VAL PHE PRO GLY VAL CYS          
SEQRES  10 A  147  LYS ASN GLY LEU CYS VAL ASN THR ARG GLY SER PHE LYS          
SEQRES  11 A  147  CYS GLN CYS PRO SER GLY MET THR LEU ASP ALA THR GLY          
SEQRES  12 A  147  ARG ILE CYS LEU                                              
HET     CA  A1148       1                                                       
HET     CA  A1149       1                                                       
HET    IOD  A1150       1                                                       
HET    IOD  A1151       1                                                       
HET    IOD  A1152       1                                                       
HETNAM     IOD IODIDE ION                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   4  HOH   *148(H2 O1)                                                   
HELIX    1   1 ASP A    5  SER A   10  5                                   6    
HELIX    2   2 LEU A   67  SER A   73  1                                   7    
HELIX    3   3 ASP A  108  PHE A  113  1                                   6    
SHEET    1  AA 2 VAL A  16  SER A  20  0                                        
SHEET    2  AA 2 SER A  23  GLU A  27 -1  O  SER A  23   N  SER A  20           
SHEET    1  AB 2 SER A  32  LEU A  34  0                                        
SHEET    2  AB 2 CYS A  41  GLU A  43 -1  O  ILE A  42   N  THR A  33           
SHEET    1  AC 4 ARG A  57  THR A  66  0                                        
SHEET    2  AC 4 GLY A  47  ILE A  54 -1  O  GLY A  47   N  THR A  66           
SHEET    3  AC 4 ALA A  78  TRP A  79 -1  O  ALA A  78   N  TRP A  50           
SHEET    4  AC 4 THR A  84  LEU A  85 -1  O  THR A  84   N  TRP A  79           
SHEET    1  AD 2 TYR A  96  LYS A 100  0                                        
SHEET    2  AD 2 GLN A 103  ASP A 106 -1  O  GLN A 103   N  ILE A  99           
SHEET    1  AE 2 LEU A 121  THR A 125  0                                        
SHEET    2  AE 2 SER A 128  GLN A 132 -1  O  SER A 128   N  THR A 125           
SSBOND   1 CYS A    7    CYS A   17                          1555   1555  2.05  
SSBOND   2 CYS A   12    CYS A   26                          1555   1555  2.02  
SSBOND   3 CYS A   28    CYS A   41                          1555   1555  2.03  
SSBOND   4 CYS A   49    CYS A   71                          1555   1555  2.04  
SSBOND   5 CYS A   58    CYS A   83                          1555   1555  2.09  
SSBOND   6 CYS A   72    CYS A   86                          1555   1555  2.04  
SSBOND   7 CYS A   92    CYS A  104                          1555   1555  2.03  
SSBOND   8 CYS A  110    CYS A  122                          1555   1555  2.05  
SSBOND   9 CYS A  117    CYS A  131                          1555   1555  2.02  
SSBOND  10 CYS A  133    CYS A  146                          1555   1555  2.07  
LINK        CA    CA A1148                 O   HOH A2069     1555   4466  2.47  
LINK        CA    CA A1148                 OD1 ASN A  19     1555   1555  2.41  
LINK        CA    CA A1148                 OD2 ASP A   3     1555   1555  2.87  
LINK        CA    CA A1148                 OD1 ASP A   3     1555   1555  2.61  
LINK        CA    CA A1148                 O   SER A  23     1555   1555  2.58  
LINK        CA    CA A1148                 O   SER A  20     1555   1555  2.59  
LINK        CA    CA A1148                 O   ILE A   4     1555   1555  2.39  
LINK        CA    CA A1148                 OE2 GLU A   6     1555   1555  2.54  
LINK        CA    CA A1149                 O   HOH A2110     1555   1555  2.49  
LINK        CA    CA A1149                 O   SER A 128     1555   1555  2.44  
LINK        CA    CA A1149                 OE1 GLU A 109     1555   1555  2.51  
LINK        CA    CA A1149                 OD1 ASN A 124     1555   1555  2.40  
LINK        CA    CA A1149                 O   ILE A 107     1555   1555  2.42  
LINK        CA    CA A1149                 OD1 ASP A 106     1555   1555  2.49  
LINK        CA    CA A1149                 O   THR A 125     1555   1555  2.54  
SITE     1 AC1  7 ASP A   3  ILE A   4  GLU A   6  ASN A  19                    
SITE     2 AC1  7 SER A  20  SER A  23  HOH A2069                               
SITE     1 AC2  7 ASP A 106  ILE A 107  GLU A 109  ASN A 124                    
SITE     2 AC2  7 THR A 125  SER A 128  HOH A2110                               
SITE     1 AC3  2 ARG A  98  SER A 135                                          
SITE     1 AC4  1 LEU A  67                                                     
SITE     1 AC5  3 GLY A  56  ARG A  57  ALA A  65                               
CRYST1   31.232   47.258   89.105  90.00  90.00  90.00 P 21 21 21    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      0.032018  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.021160  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011223        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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