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Database: PDB
Entry: 1UZK
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Original site: 1UZK 
HEADER    GLYCOPROTEIN                            13-MAR-04   1UZK              
TITLE     INTEGRIN BINDING CBEGF22-TB4-CBEGF33 FRAGMENT OF HUMAN FIBRILLIN-1, CA
TITLE    2 BOUND TO 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-CELLULAR MATRIX;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: NM554                                      
KEYWDS    GLYCOPROTEIN, EXTRA-CELLULAR MATRIX, CALCIUM, TB DOMAIN, FIBRILLIN-1, 
KEYWDS   2 DISEASE MUTATION, EXTRACELLULAR MATRIX, POLYMORPHISM, CBEGF DOMAIN,  
KEYWDS   3 EGF-LIKE DOMAIN                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.S.J.LEE,V.KNOTT,K.HARLOS,P.A.HANDFORD,D.I.STUART                    
REVDAT   4   08-MAY-19 1UZK    1       REMARK LINK                              
REVDAT   3   24-FEB-09 1UZK    1       VERSN                                    
REVDAT   2   05-JUL-06 1UZK    1       JRNL                                     
REVDAT   1   24-MAY-06 1UZK    0                                                
JRNL        AUTH   S.S.J.LEE,V.KNOTT,J.JOVANOVI,K.HARLOS,J.M.GRIMES,L.CHOULIER, 
JRNL        AUTH 2 H.J.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.    1.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELX                                                
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.202                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.261                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 1612                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 32331                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.177                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.234                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 1254                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 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    : 1                                             
REMARK   3   SOLVENT ATOMS      : 151                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL                    
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL                    
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 11831                   
REMARK   3   NUMBER OF RESTRAINTS                     : 14105                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.011                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.031                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : NULL                    
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : NULL                    
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : NULL                    
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL                    
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL                    
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL                    
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL                    
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS & KRETSINGER                                    
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1UZK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-MAR-04.                  
REMARK 100 THE DEPOSITION ID IS D_1290014799.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-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) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9787                             
REMARK 200  MONOCHROMATOR                  : SI111                              
REMARK 200  OPTICS                         : MIRRORS/MONOCHROMATOR              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25753                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
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), PH       
REMARK 280  8.50, 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       21.25000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       35.40000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       51.30000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       21.25000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       35.40000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       51.30000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       21.25000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       35.40000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       51.30000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       21.25000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       35.40000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       51.30000            
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2001  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A2002  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 FIBRILLIN-1-CONTAINING MICROFIBRILS PROVIDE LONG-TERM FORCE          
REMARK 400  BEARING STRUCTURAL SUPPORT                                          
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: 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   OD1  ASP A  1516     O    HOH A  2044              1.32            
REMARK 500   CB   TYR A  1509     O    HOH A  2036              1.41            
REMARK 500   O    ASP A  1537     O    ILE A  1538              1.60            
REMARK 500   CA   TYR A  1509     O    HOH A  2036              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ARG A1523   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    CYS A1549   CA  -  CB  -  SG  ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ARG A1644   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A1644   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ASP A1647   CA  -  CB  -  CG  ANGL. DEV. = -20.5 DEGREES          
REMARK 500    ASP A1647   OD1 -  CG  -  OD2 ANGL. DEV. =  13.2 DEGREES          
REMARK 500    ASP A1647   CB  -  CG  -  OD2 ANGL. DEV. =  -9.9 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       79.54     66.41                                   
REMARK 500    SER A1508     -142.76   -159.19                                   
REMARK 500    ASP A1516      -10.83     81.57                                   
REMARK 500    ASN A1551       64.01     62.11                                   
REMARK 500    SER A1565     -134.43   -105.17                                   
REMARK 500    CYS A1617       57.62   -149.81                                   
REMARK 500    SER A1628     -151.39   -153.33                                   
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 CYS A 1646     ASP A 1647                 -148.48                    
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 A2512  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A1606   OD2                                                    
REMARK 620 2 SER A1628   O   143.0                                              
REMARK 620 3 ILE A1607   O    68.4 144.3                                        
REMARK 620 4 GLU A1609   OE2 136.8  72.9  71.6                                  
REMARK 620 5 HOH A2114   O   115.7  90.0  84.8  75.3                            
REMARK 620 6 ASP A1606   OD1  48.2 129.6  81.9 139.2  71.7                      
REMARK 620 7 THR A1625   O    73.5  71.7 141.8 143.1 114.2  74.2                
REMARK 620 8 ASN A1624   OD1  80.8  82.8  89.2  83.1 158.4 128.0  82.8          
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 A2512                  
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: 1UZJ   RELATED DB: PDB                                   
REMARK 900 INTEGRIN BINDING CBEGF22-TB4-CBEGF33 FRAGMENT OF HUMAN FIBRILLIN-1,  
REMARK 900 HOLO FORM.                                                           
REMARK 900 RELATED ID: 1UZP   RELATED DB: PDB                                   
REMARK 900 INTEGRIN BINDING CBEGF22-TB4-CBEGF33 FRAGMENT OF HUMAN FIBRILLIN-1,  
REMARK 900 SM BOUND FORM CBEGF23 DOMAIN ONLY.                                   
REMARK 900 RELATED ID: 1UZQ   RELATED DB: PDB                                   
REMARK 900 INTEGRIN BINDING CBEGF22-TB4-CBEGF33 FRAGMENT OF HUMAN FIBRILLIN-1,  
REMARK 900 APO FORM CBEGF23 DOMAIN ONLY.                                        
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 FRAGMENT                                                             
DBREF  1UZK 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 MSE          
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                                      
MODRES 1UZK MSE A 1576  MET  SELENOMETHIONINE                                   
HET    MSE  A1576       8                                                       
HET     CA  A2512       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CA CALCIUM ION                                                      
FORMUL   1  MSE    C5 H11 N O2 SE                                               
FORMUL   2   CA    CA 2+                                                        
FORMUL   3  HOH   *151(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  O  SER A1508   N  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  MSE 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  ASN A1624  0                                        
SHEET    2  AE 2 PHE A1629  ARG A1632 -1  O  GLN A1630   N  ILE A1623           
SSBOND   1 CYS A 1491    CYS A 1502                          1555   1555  2.07  
SSBOND   2 CYS A 1497    CYS A 1511                          1555   1555  2.01  
SSBOND   3 CYS A 1513    CYS A 1526                          1555   1555  2.01  
SSBOND   4 CYS A 1534    CYS A 1562                          1555   1555  2.05  
SSBOND   5 CYS A 1549    CYS A 1574                          1555   1555  2.03  
SSBOND   6 CYS A 1563    CYS A 1577                          1555   1555  2.02  
SSBOND   7 CYS A 1564    CYS A 1589                          1555   1555  2.03  
SSBOND   8 CYS A 1610    CYS A 1622                          1555   1555  2.04  
SSBOND   9 CYS A 1617    CYS A 1631                          1555   1555  2.03  
SSBOND  10 CYS A 1633    CYS A 1646                          1555   1555  2.05  
LINK         C   GLU A1575                 N   MSE A1576     1555   1555  1.34  
LINK         C   MSE A1576                 N   CYS A1577     1555   1555  1.32  
LINK        CA    CA A2512                 OD2 ASP A1606     1555   1555  2.75  
LINK        CA    CA A2512                 O   SER A1628     1555   1555  2.46  
LINK        CA    CA A2512                 O   ILE A1607     1555   1555  2.36  
LINK        CA    CA A2512                 OE2 GLU A1609     1555   1555  2.47  
LINK        CA    CA A2512                 O   HOH A2114     1555   1555  2.44  
LINK        CA    CA A2512                 OD1 ASP A1606     1555   1555  2.48  
LINK        CA    CA A2512                 O   THR A1625     1555   1555  2.49  
LINK        CA    CA A2512                 OD1 ASN A1624     1555   1555  2.39  
CISPEP   1 THR A 1572    PRO A 1573          0       -10.20                     
SITE     1 AC1  7 ASP A1606  ILE A1607  GLU A1609  ASN A1624                    
SITE     2 AC1  7 THR A1625  SER A1628  HOH A2114                               
CRYST1   42.500   70.800  102.600  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      0.023529  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014124  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009746        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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