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Database: PDB
Entry: 1UZQ
LinkDB: 1UZQ
Original site: 1UZQ 
HEADER    MATRIX PROTEIN                          15-MAR-04   1UZQ              
TITLE     INTEGRIN BINDING CBEGF22-TB4-CBEGF33 FRAGMENT OF HUMAN FIBRILLIN-1,   
TITLE    2 APO FORM CBEGF23 DOMAIN ONLY.                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBRILLIN-1;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: BEGF22-TB4-CBEGF23, RESIDUES 1486-1647;                    
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: EXTRA-ELLULAR MATRIX;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: NM554                                      
KEYWDS    MATRIX PROTEIN, EXTRA-CELLULAR MATRIX, FIBRILLIN-1, CBEGF DOMAIN, TB  
KEYWDS   2 DOMAIN MATRIX PROTEIN                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.S.J.LEE,V.KNOTT,K.HARLOS,P.A.HANDFORD,D.I.STUART                    
REVDAT   3   08-MAY-19 1UZQ    1       REMARK                                   
REVDAT   2   24-FEB-09 1UZQ    1       VERSN                                    
REVDAT   1   08-APR-04 1UZQ    0                                                
JRNL        AUTH   S.S.J.LEE,V.KNOTT,J.JOVANOVI,K.HARLOS,J.GRIMES,L.CHOULIER,   
JRNL        AUTH 2 H.MARDON,D.I.STUART,P.A.HANDFORD                             
JRNL        TITL   STRUCTURE OF THE INTEGRIN BINDING FRAGMENT FROM FIBRILLIN-1  
JRNL        TITL 2 GIVES NEW INSIGHTS INTO MICROFIBRIL ORGANIZATION             
JRNL        REF    STRUCTURE                     V.  12   717 2004              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   15062093                                                     
JRNL        DOI    10.1016/J.STR.2004.02.023                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000.000                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 6275                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.254                           
REMARK   3   FREE R VALUE                     : 0.330                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.800                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 685                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 13                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 424                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3910                       
REMARK   3   BIN FREE R VALUE                    : 0.4510                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 48                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1123                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 2                                       
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) : 15.10000                                             
REMARK   3    B22 (A**2) : -28.50000                                            
REMARK   3    B33 (A**2) : 13.40000                                             
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.750                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.900 ; 3.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.300 ; 4.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.100 ; 4.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.500 ; 5.000                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 80.00                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1UZQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAR-04.                  
REMARK 100 THE DEPOSITION ID IS D_1290014804.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.542                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC BLUE CONFOCAL                
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH 300MM                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6275                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PBD FIBRILLIN SM BOUND FORM                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP VAPOUR DIFFUSION, 3         
REMARK 280  MICROLITRE OF 25MG/ML PROTEIN, 10MM TRIS PH7.5 + 0.5 MICROLITRES    
REMARK 280  OF 40% V/V POLYPROPYLENE GLYCOL P400 + 2.5 MICROLITRES RESERVOIR    
REMARK 280  SOLUTION (0.2M LISULFATE, 0.1M TRIS PH 8.5, 30% PEG 4000) BOTH      
REMARK 280  PROTEIN AND RESERVOIR SOLUTIONS CONTAINED 5MM EDTA, PH 8.50,        
REMARK 280  VAPOR DIFFUSION, SITTING DROP                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       21.20000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       35.40000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       51.35000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       21.20000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       35.40000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       51.35000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       21.20000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       35.40000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       51.35000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       21.20000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       35.40000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       51.35000            
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: 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 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     ARG A  1539                                                      
REMARK 465     PRO A  1540                                                      
REMARK 465     ARG A  1541                                                      
REMARK 465     GLY A  1542                                                      
REMARK 465     ASP A  1543                                                      
REMARK 465     ASN A  1544                                                      
REMARK 465     GLY A  1545                                                      
REMARK 465     ASP A  1546                                                      
REMARK 465     THR A  1547                                                      
REMARK 465     ALA A  1548                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A1494   C   -  N   -  CA  ANGL. DEV. =  10.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS A1497       80.81     58.15                                   
REMARK 500    SER A1508     -122.04   -154.03                                   
REMARK 500    TYR A1509      172.57    178.04                                   
REMARK 500    ASP A1516       -1.95     82.99                                   
REMARK 500    ASN A1551       61.56     66.78                                   
REMARK 500    SER A1565     -151.54   -120.33                                   
REMARK 500    CYS A1574      116.33    -27.70                                   
REMARK 500    LEU A1613       61.03   -119.17                                   
REMARK 500    LEU A1616        4.76    -57.00                                   
REMARK 500    CYS A1617       55.98   -162.87                                   
REMARK 500    SER A1628     -155.43   -159.36                                   
REMARK 500    THR A1635      130.36    -36.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1APJ   RELATED DB: PDB                                   
REMARK 900 NMR STUDY OF THE TRANSFORMING GROWTH FACTOR BETA BINDINGPROTEIN-     
REMARK 900 LIKE DOMAIN (TB MODULE/ 8-CYS DOMAIN), NMR,21 STRUCTURES             
REMARK 900 RELATED ID: 1EMN   RELATED DB: PDB                                   
REMARK 900 NMR STUDY OF A PAIR OF FIBRILLIN CA==2 +== BINDING EPIDERMAL GROWTH  
REMARK 900 FACTOR-LIKE DOMAINS, MINIMIZED AVERAGE STRUCTURE                     
REMARK 900 RELATED ID: 1EMO   RELATED DB: PDB                                   
REMARK 900 NMR STUDY OF A PAIR OF FIBRILLIN CA==2 +== BINDING EPIDERMAL GROWTH  
REMARK 900 FACTOR-LIKE DOMAINS, 22 STRUCTURES                                   
REMARK 900 RELATED ID: 1LMJ   RELATED DB: PDB                                   
REMARK 900 NMR STUDY OF THE FIBRILLIN-1 CBEGF12-13 PAIR OF CA2+BINDING          
REMARK 900 EPIDERMAL GROWTH FACTOR -LIKE DOMAINS                                
REMARK 900 RELATED ID: 1UZK   RELATED DB: PDB                                   
REMARK 900 X_RAY STRUCTURE OF THE INTEGRIN BINDING CBEGF22-TB4-CBEGF33          
REMARK 900 FRAGMENT OF HUMAN FIBRILLIN-1, CA BOUND FORM                         
REMARK 900 RELATED ID: 1UZJ   RELATED DB: PDB                                   
REMARK 900 X_RAY STRUCTURE OF THE INTEGRIN BINDING CBEGF22-TB4-CBEGF33          
REMARK 900 FRAGMENT OF HUMAN FIBRILLIN-1, HOLO FORM                             
REMARK 900 RELATED ID: 1UZP   RELATED DB: PDB                                   
REMARK 900 X_RAY STRUCTURE OF THE INTEGRIN BINDING CBEGF22-TB4-CBEGF33          
REMARK 900 FRAGMENT OF HUMAN FIBRILLIN-1, SM BOUND FORM CBEGF23                 
DBREF  1UZQ A 1486  1647  UNP    P35555   FBN1_HUMAN    1486   1647             
SEQRES   1 A  162  THR ASP VAL ASN GLU CYS LEU ASP PRO THR THR CYS ILE          
SEQRES   2 A  162  SER GLY ASN CYS VAL ASN THR PRO GLY SER TYR ILE CYS          
SEQRES   3 A  162  ASP CYS PRO PRO ASP PHE GLU LEU ASN PRO THR ARG VAL          
SEQRES   4 A  162  GLY CYS VAL ASP THR ARG SER GLY ASN CYS TYR LEU ASP          
SEQRES   5 A  162  ILE ARG PRO ARG GLY ASP ASN GLY ASP THR ALA CYS SER          
SEQRES   6 A  162  ASN GLU ILE GLY VAL GLY VAL SER LYS ALA SER CYS CYS          
SEQRES   7 A  162  CYS SER LEU GLY LYS ALA TRP GLY THR PRO CYS GLU MET          
SEQRES   8 A  162  CYS PRO ALA VAL ASN THR SER GLU TYR LYS ILE LEU CYS          
SEQRES   9 A  162  PRO GLY GLY GLU GLY PHE ARG PRO ASN PRO ILE THR VAL          
SEQRES  10 A  162  ILE LEU GLU ASP ILE ASP GLU CYS GLN GLU LEU PRO GLY          
SEQRES  11 A  162  LEU CYS GLN GLY GLY LYS CYS ILE ASN THR PHE GLY SER          
SEQRES  12 A  162  PHE GLN CYS ARG CYS PRO THR GLY TYR TYR LEU ASN GLU          
SEQRES  13 A  162  ASP THR ARG VAL CYS ASP                                      
FORMUL   2  HOH   *2(H2 O)                                                      
HELIX    1   1 ASN A 1489  ASP A 1493  5                                   5    
HELIX    2   2 SER A 1558  CYS A 1564  1                                   7    
HELIX    3   3 THR A 1582  CYS A 1589  1                                   8    
HELIX    4   4 ASP A 1608  LEU A 1613  1                                   6    
HELIX    5   5 PRO A 1614  CYS A 1617  5                                   4    
SHEET    1  AA 2 ASN A1501  THR A1505  0                                        
SHEET    2  AA 2 SER A1508  ASP A1512 -1  N  SER A1508   O  THR A1505           
SHEET    1  AB 2 GLU A1518  LEU A1519  0                                        
SHEET    2  AB 2 CYS A1526  VAL A1527 -1  O  VAL A1527   N  GLU A1518           
SHEET    1  AC 4 SER A1550  VAL A1557  0                                        
SHEET    2  AC 4 GLY A1532  ASP A1537 -1  O  GLY A1532   N  VAL A1557           
SHEET    3  AC 4 ALA A1569  TRP A1570 -1  O  ALA A1569   N  TYR A1535           
SHEET    4  AC 4 GLU A1575  MET A1576 -1  O  GLU A1575   N  TRP A1570           
SHEET    1  AD 2 PHE A1595  PRO A1597  0                                        
SHEET    2  AD 2 LEU A1604  ASP A1606 -1  O  GLU A1605   N  ARG A1596           
SHEET    1  AE 2 LYS A1621  THR A1625  0                                        
SHEET    2  AE 2 SER A1628  ARG A1632 -1  O  SER A1628   N  THR A1625           
SHEET    1  AF 2 LEU A1639  ASN A1640  0                                        
SHEET    2  AF 2 VAL A1645  CYS A1646 -1  O  VAL A1645   N  ASN A1640           
SSBOND   1 CYS A 1491    CYS A 1502                          1555   1555  2.03  
SSBOND   2 CYS A 1497    CYS A 1511                          1555   1555  2.02  
SSBOND   3 CYS A 1513    CYS A 1526                          1555   1555  2.02  
SSBOND   4 CYS A 1534    CYS A 1562                          1555   1555  2.04  
SSBOND   5 CYS A 1549    CYS A 1574                          1555   1555  2.03  
SSBOND   6 CYS A 1563    CYS A 1577                          1555   1555  2.03  
SSBOND   7 CYS A 1564    CYS A 1589                          1555   1555  2.02  
SSBOND   8 CYS A 1610    CYS A 1622                          1555   1555  2.04  
SSBOND   9 CYS A 1617    CYS A 1631                          1555   1555  2.04  
SSBOND  10 CYS A 1633    CYS A 1646                          1555   1555  2.02  
CISPEP   1 THR A 1572    PRO A 1573          0         1.13                     
CRYST1   42.400   70.800  102.700  90.00  90.00  90.00 I 2 2 2       8          
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      0.023585  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014124  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009737        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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