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Database: PDB
Entry: 1UZJ
LinkDB: 1UZJ
Original site: 1UZJ 
HEADER    MATRIX PROTEIN                          12-MAR-04   1UZJ              
TITLE     INTEGRIN BINDING CBEGF22-TB4-CBEGF33 FRAGMENT OF HUMAN                
TITLE    2 FIBRILLIN-1, HOLO FORM.                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBRILLIN-1;                                               
COMPND   3 CHAIN: A, B, C;                                                      
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             
KEYWDS   2 DOMAIN, TB DOMAIN MATRIX PROTEIN                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.S.J.LEE,V.KNOTT,K.HARLOS,P.A.HANDFORD,D.I.STUART                    
REVDAT   2   24-FEB-09 1UZJ    1       VERSN                                    
REVDAT   1   08-APR-04 1UZJ    0                                                
JRNL        AUTH   S.S.J.LEE,V.KNOTT,J.JOVANOVI,K.HARLOS,J.GRIMES,              
JRNL        AUTH 2 L.CHOULIER,H.MARDON,D.I.STUART,P.A.HANDFORD                  
JRNL        TITL   STRUCTURE OF THE INTEGRIN BINDING FRAGMENT FROM              
JRNL        TITL 2 FIBRILLIN-1 GIVES NEW INSIGHTS INTO MICROFIBRIL              
JRNL        TITL 3 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.    2.25 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) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.0                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000                          
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 25736                          
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) : 0.247                           
REMARK   3   FREE R VALUE                     : 0.318                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.6                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1240                            
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           : 24                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.28                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 969                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.288                        
REMARK   3   BIN FREE R VALUE                    : 0.329                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 40                           
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            : 3585                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 215                                     
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) : 1.1                                                  
REMARK   3    B22 (A**2) : 7.7                                                  
REMARK   3    B33 (A**2) : -8.8                                                 
REMARK   3    B12 (A**2) : 0.0                                                  
REMARK   3    B13 (A**2) : -2.9                                                 
REMARK   3    B23 (A**2) : 0.0                                                  
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) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.54                            
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) : 3.5   ; 4.0                  
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.8   ; 5.0                  
REMARK   3   SIDE-CHAIN BOND              (A**2) : 5.1   ; 5.0                  
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.2   ; 8.0                  
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 69                                                   
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  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1UZJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAR-04.                  
REMARK 100 THE PDBE ID CODE IS EBI-14777.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-00                          
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                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87                               
REMARK 200  MONOCHROMATOR                  : SI111                              
REMARK 200  OPTICS                         : MIRRORS/MONOCHROMATOR              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
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) : 2.250                              
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     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 2.780                              
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PBD FIBRILLIN I222 FORM                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): NULL                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5MG/ML PROTEIN IN 10MM                   
REMARK 280  MES 10MM CACL2 PH6.                                                 
REMARK 280  DEHYDRATED AGAINST: 15% PEG 8000, 10MM MES PH 6                     
REMARK 280  10MM CACL2                                                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       52.80000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 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 350 BIOMOLECULE:  2                                                      
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: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  3                                                      
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: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    CYS A1497       84.88     66.99                                   
REMARK 500    SER A1508     -130.42   -138.26                                   
REMARK 500    ASP A1516       -5.58     83.37                                   
REMARK 500    ILE A1538      -82.39   -142.58                                   
REMARK 500    ARG A1539      149.87     56.67                                   
REMARK 500    ASP A1543     -139.56     83.38                                   
REMARK 500    THR A1547      166.07     86.49                                   
REMARK 500    ALA A1548      -52.50   -165.12                                   
REMARK 500    ASN A1551       60.24     62.56                                   
REMARK 500    SER A1565     -135.77   -113.59                                   
REMARK 500    VAL A1580       -9.03    -57.77                                   
REMARK 500    CYS A1589       68.72   -115.46                                   
REMARK 500    VAL A1602       -2.83     70.75                                   
REMARK 500    SER A1628     -148.24   -166.89                                   
REMARK 500    CYS A1646       91.30    -56.96                                   
REMARK 500    SER B2508     -119.31   -103.78                                   
REMARK 500    ASP B2516       -6.27     85.89                                   
REMARK 500    ILE B2538      -20.94   -155.27                                   
REMARK 500    PRO B2540       -9.80    -58.40                                   
REMARK 500    ASN B2551       81.98     38.88                                   
REMARK 500    SER B2565     -133.09   -112.34                                   
REMARK 500    CYS B2617       54.57   -153.58                                   
REMARK 500    SER B2628     -134.20   -154.60                                   
REMARK 500    PHE B2629      168.42    175.37                                   
REMARK 500    CYS B2646       93.14    -68.15                                   
REMARK 500    CYS C3497       76.48     62.67                                   
REMARK 500    SER C3508     -141.75   -168.67                                   
REMARK 500    ASP C3516      -20.05     86.52                                   
REMARK 500    ILE C3538       16.96   -161.31                                   
REMARK 500    ASP C3543      150.85     55.24                                   
REMARK 500    ASP C3546       73.56   -157.65                                   
REMARK 500    ALA C3548       39.42    178.32                                   
REMARK 500    ASN C3551       80.32     63.90                                   
REMARK 500    SER C3565     -135.69   -125.75                                   
REMARK 500    PRO C3573      166.57    -47.76                                   
REMARK 500    GLU C3575      102.73   -174.66                                   
REMARK 500    ASN C3581      -48.28    172.14                                   
REMARK 500    CYS C3589       59.60   -113.34                                   
REMARK 500    SER C3628     -145.15   -163.64                                   
REMARK 500    CYS C3646       92.90    -62.85                                   
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 A1648  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A1490   OE1                                                    
REMARK 620 2 SER A1508   O    75.2                                              
REMARK 620 3 ASP A1487   OD1 137.2 136.6                                        
REMARK 620 4 ASP A1487   OD2 138.1 137.0  44.2                                  
REMARK 620 5 VAL A1488   O    78.5 151.0  62.1  71.8                            
REMARK 620 6 ASN A1504   OD1  84.3  84.0  74.6 118.8  81.7                      
REMARK 620 7 THR A1505   O   140.0  66.9  72.4  81.1 134.0  79.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1649  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A1624   OD1                                                    
REMARK 620 2 THR A1625   O    86.2                                              
REMARK 620 3 SER A1628   O    78.3  63.3                                        
REMARK 620 4 GLU A1609   OE2  75.2 141.7  80.2                                  
REMARK 620 5 ASP A1606   OD1 120.9  62.5 120.0 155.0                            
REMARK 620 6 ASP A1606   OD2  83.4  84.9 143.9 124.6  47.6                      
REMARK 620 7 HOH A2068   O   165.5 100.8  93.4  91.8  73.6 109.8                
REMARK 620 8 ILE A1607   O    95.7 146.9 149.5  69.4  88.9  62.6  85.5          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2648  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B2504   OD1                                                    
REMARK 620 2 VAL B2488   O    71.2                                              
REMARK 620 3 ASP B2487   OD1  78.9  63.4                                        
REMARK 620 4 ASP B2487   OD2 124.4  91.3  47.2                                  
REMARK 620 5 THR B2505   O    90.3 140.0  78.7  69.9                            
REMARK 620 6 SER B2508   O    94.7 145.1 147.0 122.0  68.9                      
REMARK 620 7 GLU B2490   OE1  80.2  70.3 133.1 143.5 142.7  76.0                
REMARK 620 8 GLY B2507   O   168.6 114.6 112.5  66.4  90.5  74.9  92.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2649  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B2609   OE2                                                    
REMARK 620 2 SER B2628   O    71.0                                              
REMARK 620 3 HOH B2067   O    85.0 104.1                                        
REMARK 620 4 ASP B2606   OD1 147.7 127.4  65.7                                  
REMARK 620 5 THR B2625   O   137.9  70.1 119.5  72.3                            
REMARK 620 6 ILE B2607   O    78.0 148.4  78.7  82.9 136.5                      
REMARK 620 7 ASP B2606   OD2 133.7 146.7 100.5  47.1  78.5  58.7                
REMARK 620 8 ASN B2624   OD1  87.5  79.1 170.4 119.8  70.1  93.8  80.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C3648  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C3505   O                                                      
REMARK 620 2 ASP C3487   OD1  83.5                                              
REMARK 620 3 ASP C3487   OD2  72.0  42.1                                        
REMARK 620 4 VAL C3488   O   147.1  65.3  90.1                                  
REMARK 620 5 ASN C3504   OD1  82.8  90.0 126.7  86.6                            
REMARK 620 6 SER C3508   O    63.9 145.8 126.9 142.5  76.1                      
REMARK 620 7 GLU C3490   OE1 136.8 128.3 151.1  66.1  70.5  76.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C3649  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER C3628   N                                                      
REMARK 620 2 ILE C3607   O   141.7                                              
REMARK 620 3 GLU C3609   OE2 111.2  59.2                                        
REMARK 620 4 ASP C3606   OD1  82.5  90.7 146.5                                  
REMARK 620 5 ASP C3606   OD2 119.5  79.3 129.3  47.0                            
REMARK 620 6 THR C3625   O    61.7 151.5 138.9  74.7  72.8                      
REMARK 620 7 ASN C3624   OD1 129.3  86.5  75.5 120.4  74.2  80.4                
REMARK 620 8 SER C3628   O    62.0 131.9  73.4 137.2 132.3  68.0  73.5          
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 A1648                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1649                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2648                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2649                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C3648                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C3649                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
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: 1EMN   RELATED DB: PDB                                   
REMARK 900  NMR STUDY OF A PAIR OF FIBRILLIN CA==2                              
REMARK 900  +== BINDING EPIDERMAL GROWTH FACTOR-LIKE                            
REMARK 900  DOMAINS, MINIMIZED AVERAGE STRUCTURE                                
REMARK 900 RELATED ID: 1EMO   RELATED DB: PDB                                   
REMARK 900  NMR STUDY OF A PAIR OF FIBRILLIN CA==2                              
REMARK 900  +== BINDING EPIDERMAL GROWTH FACTOR-LIKE                            
REMARK 900  DOMAINS, 22 STRUCTURES                                              
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 900 RELATED ID: 1UZK   RELATED DB: PDB                                   
REMARK 900  X_RAY STRUCTURE OF THE INTEGRIN BINDING                             
REMARK 900  CBEGF22-TB4-CBEGF33 FRAGMENT OF HUMAN                               
REMARK 900  FIBRILLIN-1, HOLO FORM                                              
REMARK 900 RELATED ID: 1UZP   RELATED DB: PDB                                   
REMARK 900  X_RAY STRUCTURE OF THE INTEGRIN BINDING                             
REMARK 900  CBEGF22-TB4-CBEGF33 FRAGMENT OF HUMAN                               
REMARK 900  FIBRILLIN-1, SM BOUND FORM CBEGF23                                  
REMARK 900 RELATED ID: 1UZQ   RELATED DB: PDB                                   
REMARK 900  X_RAY STRUCTURE OF THE INTEGRIN BINDING                             
REMARK 900  CBEGF22-TB4-CBEGF33 FRAGMENT OF HUMAN                               
REMARK 900  FIBRILLIN-1, APO FORM CBEGF23                                       
DBREF  1UZJ A 1486  1647  UNP    P35555   FBN1_HUMAN    1486   1647             
DBREF  1UZJ B 2486  2647  UNP    P35555   FBN1_HUMAN    1486   1647             
DBREF  1UZJ C 3486  3647  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                                      
SEQRES   1 B  162  THR ASP VAL ASN GLU CYS LEU ASP PRO THR THR CYS ILE          
SEQRES   2 B  162  SER GLY ASN CYS VAL ASN THR PRO GLY SER TYR ILE CYS          
SEQRES   3 B  162  ASP CYS PRO PRO ASP PHE GLU LEU ASN PRO THR ARG VAL          
SEQRES   4 B  162  GLY CYS VAL ASP THR ARG SER GLY ASN CYS TYR LEU ASP          
SEQRES   5 B  162  ILE ARG PRO ARG GLY ASP ASN GLY ASP THR ALA CYS SER          
SEQRES   6 B  162  ASN GLU ILE GLY VAL GLY VAL SER LYS ALA SER CYS CYS          
SEQRES   7 B  162  CYS SER LEU GLY LYS ALA TRP GLY THR PRO CYS GLU MET          
SEQRES   8 B  162  CYS PRO ALA VAL ASN THR SER GLU TYR LYS ILE LEU CYS          
SEQRES   9 B  162  PRO GLY GLY GLU GLY PHE ARG PRO ASN PRO ILE THR VAL          
SEQRES  10 B  162  ILE LEU GLU ASP ILE ASP GLU CYS GLN GLU LEU PRO GLY          
SEQRES  11 B  162  LEU CYS GLN GLY GLY LYS CYS ILE ASN THR PHE GLY SER          
SEQRES  12 B  162  PHE GLN CYS ARG CYS PRO THR GLY TYR TYR LEU ASN GLU          
SEQRES  13 B  162  ASP THR ARG VAL CYS ASP                                      
SEQRES   1 C  162  THR ASP VAL ASN GLU CYS LEU ASP PRO THR THR CYS ILE          
SEQRES   2 C  162  SER GLY ASN CYS VAL ASN THR PRO GLY SER TYR ILE CYS          
SEQRES   3 C  162  ASP CYS PRO PRO ASP PHE GLU LEU ASN PRO THR ARG VAL          
SEQRES   4 C  162  GLY CYS VAL ASP THR ARG SER GLY ASN CYS TYR LEU ASP          
SEQRES   5 C  162  ILE ARG PRO ARG GLY ASP ASN GLY ASP THR ALA CYS SER          
SEQRES   6 C  162  ASN GLU ILE GLY VAL GLY VAL SER LYS ALA SER CYS CYS          
SEQRES   7 C  162  CYS SER LEU GLY LYS ALA TRP GLY THR PRO CYS GLU MET          
SEQRES   8 C  162  CYS PRO ALA VAL ASN THR SER GLU TYR LYS ILE LEU CYS          
SEQRES   9 C  162  PRO GLY GLY GLU GLY PHE ARG PRO ASN PRO ILE THR VAL          
SEQRES  10 C  162  ILE LEU GLU ASP ILE ASP GLU CYS GLN GLU LEU PRO GLY          
SEQRES  11 C  162  LEU CYS GLN GLY GLY LYS CYS ILE ASN THR PHE GLY SER          
SEQRES  12 C  162  PHE GLN CYS ARG CYS PRO THR GLY TYR TYR LEU ASN GLU          
SEQRES  13 C  162  ASP THR ARG VAL CYS ASP                                      
HET     CA  A1648       1                                                       
HET     CA  A1649       1                                                       
HET     CA  B2648       1                                                       
HET     CA  B2649       1                                                       
HET     CA  C3648       1                                                       
HET     CA  C3649       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   4   CA    6(CA 2+)                                                     
FORMUL  10  HOH   *215(H2 O1)                                                   
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    
HELIX    6   6 ASN B 2489  ASP B 2493  5                                   5    
HELIX    7   7 SER B 2558  CYS B 2564  1                                   7    
HELIX    8   8 THR B 2582  CYS B 2589  1                                   8    
HELIX    9   9 ASP B 2608  LEU B 2613  1                                   6    
HELIX   10  10 PRO B 2614  CYS B 2617  5                                   4    
HELIX   11  11 ASN C 3489  ASP C 3493  5                                   5    
HELIX   12  12 SER C 3558  CYS C 3564  1                                   7    
HELIX   13  13 THR C 3582  CYS C 3589  1                                   8    
HELIX   14  14 ASP C 3608  LEU C 3613  1                                   6    
HELIX   15  15 PRO C 3614  CYS C 3617  5                                   4    
SHEET    1  AA 2 ASN A1501  ASN A1504  0                                        
SHEET    2  AA 2 TYR A1509  ASP A1512 -1  O  ILE A1510   N  VAL A1503           
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           
SHEET    1  BA 2 ASN B2501  ASN B2504  0                                        
SHEET    2  BA 2 TYR B2509  ASP B2512 -1  O  ILE B2510   N  VAL B2503           
SHEET    1  BB 2 GLU B2518  LEU B2519  0                                        
SHEET    2  BB 2 CYS B2526  VAL B2527 -1  O  VAL B2527   N  GLU B2518           
SHEET    1  BC 4 SER B2550  VAL B2557  0                                        
SHEET    2  BC 4 GLY B2532  ASP B2537 -1  O  GLY B2532   N  VAL B2557           
SHEET    3  BC 4 ALA B2569  TRP B2570 -1  O  ALA B2569   N  TYR B2535           
SHEET    4  BC 4 GLU B2575  MET B2576 -1  O  GLU B2575   N  TRP B2570           
SHEET    1  BD 2 PHE B2595  PRO B2597  0                                        
SHEET    2  BD 2 LEU B2604  ASP B2606 -1  O  GLU B2605   N  ARG B2596           
SHEET    1  BE 2 LYS B2621  THR B2625  0                                        
SHEET    2  BE 2 SER B2628  ARG B2632 -1  O  SER B2628   N  THR B2625           
SHEET    1  BF 2 LEU B2639  ASN B2640  0                                        
SHEET    2  BF 2 VAL B2645  CYS B2646 -1  O  VAL B2645   N  ASN B2640           
SHEET    1  CA 2 ASN C3501  THR C3505  0                                        
SHEET    2  CA 2 SER C3508  ASP C3512 -1  O  SER C3508   N  THR C3505           
SHEET    1  CB 2 GLU C3518  LEU C3519  0                                        
SHEET    2  CB 2 CYS C3526  VAL C3527 -1  O  VAL C3527   N  GLU C3518           
SHEET    1  CC 3 SER C3550  VAL C3557  0                                        
SHEET    2  CC 3 GLY C3532  ASP C3537 -1  O  GLY C3532   N  VAL C3557           
SHEET    3  CC 3 ALA C3569  TRP C3570 -1  O  ALA C3569   N  TYR C3535           
SHEET    1  CD 2 PHE C3595  PRO C3597  0                                        
SHEET    2  CD 2 LEU C3604  ASP C3606 -1  O  GLU C3605   N  ARG C3596           
SHEET    1  CE 2 LYS C3621  THR C3625  0                                        
SHEET    2  CE 2 SER C3628  ARG C3632 -1  O  SER C3628   N  THR C3625           
SHEET    1  CF 2 LEU C3639  ASN C3640  0                                        
SHEET    2  CF 2 VAL C3645  CYS C3646 -1  O  VAL C3645   N  ASN C3640           
SSBOND   1 CYS A 1491    CYS A 1502                          1555   1555  2.05  
SSBOND   2 CYS A 1497    CYS A 1511                          1555   1555  2.03  
SSBOND   3 CYS A 1513    CYS A 1526                          1555   1555  2.04  
SSBOND   4 CYS A 1534    CYS A 1562                          1555   1555  2.04  
SSBOND   5 CYS A 1549    CYS A 1574                          1555   1555  2.04  
SSBOND   6 CYS A 1563    CYS A 1577                          1555   1555  2.04  
SSBOND   7 CYS A 1564    CYS A 1589                          1555   1555  2.03  
SSBOND   8 CYS A 1610    CYS A 1622                          1555   1555  2.02  
SSBOND   9 CYS A 1617    CYS A 1631                          1555   1555  2.03  
SSBOND  10 CYS A 1633    CYS A 1646                          1555   1555  2.04  
SSBOND  11 CYS B 2491    CYS B 2502                          1555   1555  2.04  
SSBOND  12 CYS B 2497    CYS B 2511                          1555   1555  2.04  
SSBOND  13 CYS B 2513    CYS B 2526                          1555   1555  2.04  
SSBOND  14 CYS B 2534    CYS B 2562                          1555   1555  2.05  
SSBOND  15 CYS B 2549    CYS B 2574                          1555   1555  2.03  
SSBOND  16 CYS B 2563    CYS B 2577                          1555   1555  2.05  
SSBOND  17 CYS B 2564    CYS B 2589                          1555   1555  2.04  
SSBOND  18 CYS B 2610    CYS B 2622                          1555   1555  2.04  
SSBOND  19 CYS B 2617    CYS B 2631                          1555   1555  2.04  
SSBOND  20 CYS B 2633    CYS B 2646                          1555   1555  2.04  
SSBOND  21 CYS C 3491    CYS C 3502                          1555   1555  2.03  
SSBOND  22 CYS C 3497    CYS C 3511                          1555   1555  2.04  
SSBOND  23 CYS C 3513    CYS C 3526                          1555   1555  2.04  
SSBOND  24 CYS C 3534    CYS C 3562                          1555   1555  2.04  
SSBOND  25 CYS C 3549    CYS C 3574                          1555   1555  2.03  
SSBOND  26 CYS C 3563    CYS C 3577                          1555   1555  2.03  
SSBOND  27 CYS C 3564    CYS C 3589                          1555   1555  2.03  
SSBOND  28 CYS C 3610    CYS C 3622                          1555   1555  2.03  
SSBOND  29 CYS C 3617    CYS C 3631                          1555   1555  2.03  
SSBOND  30 CYS C 3633    CYS C 3646                          1555   1555  2.04  
LINK        CA    CA A1648                 OE1 GLU A1490     1555   1555  2.55  
LINK        CA    CA A1648                 O   SER A1508     1555   1555  2.51  
LINK        CA    CA A1648                 OD1 ASP A1487     1555   1555  3.13  
LINK        CA    CA A1648                 OD2 ASP A1487     1555   1555  2.54  
LINK        CA    CA A1648                 O   VAL A1488     1555   1555  2.47  
LINK        CA    CA A1648                 OD1 ASN A1504     1555   1555  2.20  
LINK        CA    CA A1648                 O   THR A1505     1555   1555  2.63  
LINK        CA    CA A1649                 OD1 ASN A1624     1555   1555  2.34  
LINK        CA    CA A1649                 O   THR A1625     1555   1555  2.57  
LINK        CA    CA A1649                 O   SER A1628     1555   1555  2.33  
LINK        CA    CA A1649                 OE2 GLU A1609     1555   1555  2.42  
LINK        CA    CA A1649                 OD1 ASP A1606     1555   1555  2.54  
LINK        CA    CA A1649                 OD2 ASP A1606     1555   1555  2.88  
LINK        CA    CA A1649                 O   HOH A2068     1555   1555  2.40  
LINK        CA    CA A1649                 O   ILE A1607     1555   1555  2.26  
LINK        CA    CA B2648                 OD1 ASN B2504     1555   1555  2.62  
LINK        CA    CA B2648                 O   VAL B2488     1555   1555  2.23  
LINK        CA    CA B2648                 OD1 ASP B2487     1555   1555  2.57  
LINK        CA    CA B2648                 OD2 ASP B2487     1555   1555  2.85  
LINK        CA    CA B2648                 O   THR B2505     1555   1555  2.52  
LINK        CA    CA B2648                 O   SER B2508     1555   1555  2.50  
LINK        CA    CA B2648                 OE1 GLU B2490     1555   1555  2.46  
LINK        CA    CA B2648                 O   GLY B2507     1555   1555  3.24  
LINK        CA    CA B2649                 O   SER B2628     1555   1555  2.26  
LINK        CA    CA B2649                 O   HOH B2067     1555   1555  2.51  
LINK        CA    CA B2649                 OD1 ASP B2606     1555   1555  2.68  
LINK        CA    CA B2649                 O   THR B2625     1555   1555  2.47  
LINK        CA    CA B2649                 O   ILE B2607     1555   1555  2.37  
LINK        CA    CA B2649                 OD2 ASP B2606     1555   1555  2.85  
LINK        CA    CA B2649                 OD1 ASN B2624     1555   1555  2.30  
LINK        CA    CA B2649                 OE2 GLU B2609     1555   1555  2.40  
LINK        CA    CA C3648                 OD1 ASP C3487     1555   1555  3.07  
LINK        CA    CA C3648                 OD2 ASP C3487     1555   1555  2.97  
LINK        CA    CA C3648                 O   VAL C3488     1555   1555  2.36  
LINK        CA    CA C3648                 OD1 ASN C3504     1555   1555  2.26  
LINK        CA    CA C3648                 O   SER C3508     1555   1555  2.63  
LINK        CA    CA C3648                 OE1 GLU C3490     1555   1555  2.87  
LINK        CA    CA C3648                 O   THR C3505     1555   1555  2.52  
LINK        CA    CA C3649                 O   ILE C3607     1555   1555  2.61  
LINK        CA    CA C3649                 OE2 GLU C3609     1555   1555  2.58  
LINK        CA    CA C3649                 OD1 ASP C3606     1555   1555  2.46  
LINK        CA    CA C3649                 OD2 ASP C3606     1555   1555  2.97  
LINK        CA    CA C3649                 O   THR C3625     1555   1555  2.40  
LINK        CA    CA C3649                 OD1 ASN C3624     1555   1555  2.68  
LINK        CA    CA C3649                 O   SER C3628     1555   1555  2.14  
LINK        CA    CA C3649                 N   SER C3628     1555   1555  3.09  
CISPEP   1 THR A 1572    PRO A 1573          0        -0.06                     
CISPEP   2 THR B 2572    PRO B 2573          0         0.07                     
CISPEP   3 THR C 3572    PRO C 3573          0        -0.27                     
SITE     1 AC1  6 ASP A1487  VAL A1488  GLU A1490  ASN A1504                    
SITE     2 AC1  6 THR A1505  SER A1508                                          
SITE     1 AC2  7 ASP A1606  ILE A1607  GLU A1609  ASN A1624                    
SITE     2 AC2  7 THR A1625  SER A1628  HOH A2068                               
SITE     1 AC3  7 ASP B2487  VAL B2488  GLU B2490  ASN B2504                    
SITE     2 AC3  7 THR B2505  GLY B2507  SER B2508                               
SITE     1 AC4  7 HOH B2067  ASP B2606  ILE B2607  GLU B2609                    
SITE     2 AC4  7 ASN B2624  THR B2625  SER B2628                               
SITE     1 AC5  6 ASP C3487  VAL C3488  GLU C3490  ASN C3504                    
SITE     2 AC5  6 THR C3505  SER C3508                                          
SITE     1 AC6  6 ASP C3606  ILE C3607  GLU C3609  ASN C3624                    
SITE     2 AC6  6 THR C3625  SER C3628                                          
CRYST1   43.100  105.600   65.000  90.00 104.20  90.00 P 1 21 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.023202  0.000000  0.005871        0.00000                         
SCALE2      0.000000  0.009470  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015869        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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