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Database: PDB
Entry: 5MS9
LinkDB: 5MS9
Original site: 5MS9 
HEADER    STRUCTURAL PROTEIN                      01-JAN-17   5MS9              
TITLE     SOLUTION STRUCTURE OF HUMAN FIBRILLIN-1 EGF2-EGF3-HYBRID1-CBEGF1 FOUR 
TITLE    2 DOMAIN FRAGMENT                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBRILLIN-1;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: FBN1, FBN;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    FIBRILLIN EGF HYBRID EXTRACELLULAR, STRUCTURAL PROTEIN                
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    I.B.ROBERTSON,C.REDFIELD,P.A.HANDFORD                                 
REVDAT   2   08-MAY-19 5MS9    1       REMARK                                   
REVDAT   1   09-AUG-17 5MS9    0                                                
JRNL        AUTH   I.B.ROBERTSON,H.F.DIAS,I.H.OSUCH,E.D.LOWE,S.A.JENSEN,        
JRNL        AUTH 2 C.REDFIELD,P.A.HANDFORD                                      
JRNL        TITL   THE N-TERMINAL REGION OF FIBRILLIN-1 MEDIATES A BIPARTITE    
JRNL        TITL 2 INTERACTION WITH LTBP1.                                      
JRNL        REF    STRUCTURE                     V.  25  1208 2017              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   28669633                                                     
JRNL        DOI    10.1016/J.STR.2017.06.003                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   I.B.ROBERTSON,I.OSUCH,D.A.YADIN,P.A.HANDFORD,S.A.JENSEN,     
REMARK   1  AUTH 2 C.REDFIELD                                                   
REMARK   1  TITL   1H, 13C AND 15N RESONANCE ASSIGNMENTS FOR THE FIBRILLIN-1    
REMARK   1  TITL 2 EGF2-EGF3-HYBRID1-CBEGF1 FOUR-DOMAIN FRAGMENT.               
REMARK   1  REF    BIOMOL NMR ASSIGN             V.   8   189 2014              
REMARK   1  REFN                   ESSN 1874-270X                               
REMARK   1  PMID   23649688                                                     
REMARK   1  DOI    10.1007/S12104-013-9481-7                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : XPLOR-NIH, ARIA                                      
REMARK   3   AUTHORS     : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE (XPLOR      
REMARK   3                 -NIH), LINGE, O'DONOGHUE AND NILGES (ARIA)           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5MS9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200002729.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 268                                
REMARK 210  PH                             : 5.4                                
REMARK 210  IONIC STRENGTH                 : 15                                 
REMARK 210  PRESSURE                       : 1 ATM                              
REMARK 210  SAMPLE CONTENTS                : 1 MM FIBRILLIN-1 E2CB1, 5 MM       
REMARK 210                                   CALCIUM ION, 100% D2O; 1 MM [U-    
REMARK 210                                   15N] FIBRILLIN-1 E2CB1, 5 MM       
REMARK 210                                   CALCIUM ION, 95% H2O/5% D2O; 1     
REMARK 210                                   MM [U-13C; U-15N] FIBRILLIN-1      
REMARK 210                                   E2CB1, 5 MM CALCIUM ION, 95% H2O/  
REMARK 210                                   5% D2O; 1 MM [U-15N] FIBRILLIN-1   
REMARK 210                                   E2CB1, 5 MM CALCIUM ION, 4 %       
REMARK 210                                   BICELLES, 90% H2O/10% D2O; 1 MM    
REMARK 210                                   [U-15N] FIBRILLIN-1 E2CB1, 5 MM    
REMARK 210                                   CALCIUM ION, 2.2 % PEG-HEXANOL     
REMARK 210                                   SOLUTION, 90% H2O/10% D2O          
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D NOESY; 3D 1H-15N NOESY; 3D 1H   
REMARK 210                                   -13C NOESY; 3D 1H-13C NOESY        
REMARK 210                                   AROMATIC; IPAP                     
REMARK 210  SPECTROMETER FIELD STRENGTH    : 950 MHZ; 750 MHZ; 600 MHZ; 500     
REMARK 210                                   MHZ                                
REMARK 210  SPECTROMETER MODEL             : OMEGA; AVANCE                      
REMARK 210  SPECTROMETER MANUFACTURER      : HOME-BUILT; BRUKER                 
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : CCPNMR ANALYSIS                    
REMARK 210   METHOD USED                   : SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 40                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST         
REMARK 210                                   ENERGY                             
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
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: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 11700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: 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  1 GLN A 117       47.51    -88.14                                   
REMARK 500  1 HIS A 118     -153.78   -166.47                                   
REMARK 500  1 ILE A 121     -169.89    -69.97                                   
REMARK 500  1 ASP A 131      -44.23     77.66                                   
REMARK 500  1 ASP A 132      -39.63    156.53                                   
REMARK 500  1 ASN A 156       31.25     35.43                                   
REMARK 500  1 PRO A 163      107.14    -51.16                                   
REMARK 500  1 ASN A 164      -11.35     75.28                                   
REMARK 500  1 TYR A 170      125.89    177.75                                   
REMARK 500  1 CYS A 177       59.54     24.31                                   
REMARK 500  1 ASP A 180       49.60    -80.50                                   
REMARK 500  1 SER A 191     -166.50   -117.08                                   
REMARK 500  1 GLN A 193      -73.79    -83.76                                   
REMARK 500  1 GLN A 196      -58.70   -161.27                                   
REMARK 500  1 LEU A 199      175.48     62.75                                   
REMARK 500  1 SER A 200      130.30    176.14                                   
REMARK 500  1 VAL A 213      -40.50     66.12                                   
REMARK 500  1 ARG A 215      -90.12   -128.64                                   
REMARK 500  1 CYS A 221       94.57     33.23                                   
REMARK 500  1 ALA A 226     -122.98    -63.75                                   
REMARK 500  1 GLN A 227      108.97    -52.68                                   
REMARK 500  1 CYS A 231     -103.85   -119.48                                   
REMARK 500  1 PRO A 254      114.23    -39.41                                   
REMARK 500  1 GLN A 284       44.87     29.46                                   
REMARK 500  2 SER A 115       86.26     56.64                                   
REMARK 500  2 ASP A 131       -9.57     63.10                                   
REMARK 500  2 ASP A 132       38.65    108.52                                   
REMARK 500  2 ASN A 164      -14.35     77.11                                   
REMARK 500  2 TYR A 170      -86.51   -158.19                                   
REMARK 500  2 CYS A 177       56.37     28.68                                   
REMARK 500  2 ASP A 180       48.63    -85.63                                   
REMARK 500  2 SER A 191     -166.84   -115.56                                   
REMARK 500  2 GLN A 193      -74.01    -73.30                                   
REMARK 500  2 GLN A 196      -85.90    166.06                                   
REMARK 500  2 ILE A 202       99.39    -60.09                                   
REMARK 500  2 VAL A 213      -45.05     67.55                                   
REMARK 500  2 ARG A 215      -75.98   -125.64                                   
REMARK 500  2 CYS A 221       88.85     45.17                                   
REMARK 500  2 ALA A 226     -142.24    -65.35                                   
REMARK 500  2 GLN A 227      106.37    -52.37                                   
REMARK 500  2 PRO A 230       83.27    -64.31                                   
REMARK 500  2 ARG A 240      -62.46   -100.90                                   
REMARK 500  2 PRO A 274      152.71    -48.94                                   
REMARK 500  2 SER A 283       25.75   -142.47                                   
REMARK 500  2 GLN A 284       41.93     28.57                                   
REMARK 500  3 SER A 113       46.90   -103.14                                   
REMARK 500  3 ASP A 131     -113.32     49.75                                   
REMARK 500  3 ASN A 156       27.02     48.87                                   
REMARK 500  3 ASN A 164       -1.82     69.91                                   
REMARK 500  3 TYR A 170      117.89   -175.70                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     419 RAMACHANDRAN OUTLIERS.                        
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 ILE A  190     SER A  191          4       145.87                    
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 A 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 246   OD1                                                    
REMARK 620 2 ASP A 246   OD2  63.2                                              
REMARK 620 3 VAL A 247   O   113.0  78.3                                        
REMARK 620 4 GLU A 249   OE1  87.1 133.2  81.9                                  
REMARK 620 5 GLU A 249   OE2 143.0 153.3  83.4  61.6                            
REMARK 620 6 ASN A 264   OD1 136.2  79.1  77.7 136.5  78.2                      
REMARK 620 7 THR A 265   O    76.1  74.8 143.3 134.8 111.2  73.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 301                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 19078   RELATED DB: BMRB                                 
DBREF  5MS9 A  113   287  UNP    P35555   FBN1_HUMAN     113    287             
SEQADV 5MS9 SER A  111  UNP  P35555              EXPRESSION TAG                 
SEQADV 5MS9 ALA A  112  UNP  P35555              EXPRESSION TAG                 
SEQADV 5MS9 SER A  204  UNP  P35555    CYS   204 CONFLICT                       
SEQRES   1 A  177  SER ALA SER ARG SER ILE GLN HIS CYS ASN ILE ARG CYS          
SEQRES   2 A  177  MET ASN GLY GLY SER CYS SER ASP ASP HIS CYS LEU CYS          
SEQRES   3 A  177  GLN LYS GLY TYR ILE GLY THR HIS CYS GLY GLN PRO VAL          
SEQRES   4 A  177  CYS GLU SER GLY CYS LEU ASN GLY GLY ARG CYS VAL ALA          
SEQRES   5 A  177  PRO ASN ARG CYS ALA CYS THR TYR GLY PHE THR GLY PRO          
SEQRES   6 A  177  GLN CYS GLU ARG ASP TYR ARG THR GLY PRO CYS PHE THR          
SEQRES   7 A  177  VAL ILE SER ASN GLN MET CYS GLN GLY GLN LEU SER GLY          
SEQRES   8 A  177  ILE VAL SER THR LYS THR LEU CYS CYS ALA THR VAL GLY          
SEQRES   9 A  177  ARG ALA TRP GLY HIS PRO CYS GLU MET CYS PRO ALA GLN          
SEQRES  10 A  177  PRO HIS PRO CYS ARG ARG GLY PHE ILE PRO ASN ILE ARG          
SEQRES  11 A  177  THR GLY ALA CYS GLN ASP VAL ASP GLU CYS GLN ALA ILE          
SEQRES  12 A  177  PRO GLY LEU CYS GLN GLY GLY ASN CYS ILE ASN THR VAL          
SEQRES  13 A  177  GLY SER PHE GLU CYS LYS CYS PRO ALA GLY HIS LYS LEU          
SEQRES  14 A  177  ASN GLU VAL SER GLN LYS CYS GLU                              
HET     CA  A 301       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   2   CA    CA 2+                                                        
HELIX    1 AA1 THR A  205  THR A  212  1                                   8    
HELIX    2 AA2 ASP A  248  ILE A  253  1                                   6    
SHEET    1 AA1 2 SER A 128  SER A 130  0                                        
SHEET    2 AA1 2 HIS A 133  LEU A 135 -1  O  LEU A 135   N  SER A 128           
SHEET    1 AA2 2 TYR A 140  ILE A 141  0                                        
SHEET    2 AA2 2 GLN A 147  PRO A 148 -1  O  GLN A 147   N  ILE A 141           
SHEET    1 AA3 2 ARG A 159  ALA A 162  0                                        
SHEET    2 AA3 2 ARG A 165  ALA A 167 -1  O  ARG A 165   N  VAL A 161           
SHEET    1 AA4 4 VAL A 203  SER A 204  0                                        
SHEET    2 AA4 4 GLY A 184  PHE A 187 -1  N  GLY A 184   O  SER A 204           
SHEET    3 AA4 4 ALA A 216  TRP A 217 -1  O  ALA A 216   N  PHE A 187           
SHEET    4 AA4 4 GLU A 222  MET A 223 -1  O  GLU A 222   N  TRP A 217           
SHEET    1 AA5 2 PHE A 235  PRO A 237  0                                        
SHEET    2 AA5 2 CYS A 244  ASP A 246 -1  O  GLN A 245   N  ILE A 236           
SHEET    1 AA6 2 ASN A 261  THR A 265  0                                        
SHEET    2 AA6 2 SER A 268  LYS A 272 -1  O  GLU A 270   N  ILE A 263           
SHEET    1 AA7 2 LEU A 279  ASN A 280  0                                        
SHEET    2 AA7 2 LYS A 285  CYS A 286 -1  O  LYS A 285   N  ASN A 280           
SSBOND   1 CYS A  119    CYS A  129                          1555   1555  2.02  
SSBOND   2 CYS A  123    CYS A  134                          1555   1555  2.03  
SSBOND   3 CYS A  136    CYS A  145                          1555   1555  2.03  
SSBOND   4 CYS A  150    CYS A  160                          1555   1555  2.02  
SSBOND   5 CYS A  154    CYS A  166                          1555   1555  2.03  
SSBOND   6 CYS A  168    CYS A  177                          1555   1555  2.03  
SSBOND   7 CYS A  186    CYS A  209                          1555   1555  2.03  
SSBOND   8 CYS A  195    CYS A  221                          1555   1555  2.03  
SSBOND   9 CYS A  210    CYS A  224                          1555   1555  2.03  
SSBOND  10 CYS A  231    CYS A  244                          1555   1555  2.03  
SSBOND  11 CYS A  250    CYS A  262                          1555   1555  2.03  
SSBOND  12 CYS A  257    CYS A  271                          1555   1555  2.03  
SSBOND  13 CYS A  273    CYS A  286                          1555   1555  2.03  
LINK         OD1 ASP A 246                CA    CA A 301     1555   1555  1.95  
LINK         OD2 ASP A 246                CA    CA A 301     1555   1555  2.14  
LINK         O   VAL A 247                CA    CA A 301     1555   1555  2.15  
LINK         OE1 GLU A 249                CA    CA A 301     1555   1555  2.08  
LINK         OE2 GLU A 249                CA    CA A 301     1555   1555  2.11  
LINK         OD1 ASN A 264                CA    CA A 301     1555   1555  2.03  
LINK         O   THR A 265                CA    CA A 301     1555   1555  2.84  
CISPEP   1 HIS A  219    PRO A  220          1        -5.07                     
CISPEP   2 HIS A  219    PRO A  220          2        -4.49                     
CISPEP   3 HIS A  219    PRO A  220          3        -5.28                     
CISPEP   4 HIS A  219    PRO A  220          4        -2.03                     
CISPEP   5 HIS A  219    PRO A  220          5        -4.98                     
CISPEP   6 HIS A  219    PRO A  220          6        -0.65                     
CISPEP   7 HIS A  219    PRO A  220          7        -4.78                     
CISPEP   8 HIS A  219    PRO A  220          8        -5.07                     
CISPEP   9 HIS A  219    PRO A  220          9        -3.48                     
CISPEP  10 HIS A  219    PRO A  220         10        -3.90                     
CISPEP  11 HIS A  219    PRO A  220         11        -3.14                     
CISPEP  12 HIS A  219    PRO A  220         12        -1.13                     
CISPEP  13 HIS A  219    PRO A  220         13        -3.85                     
CISPEP  14 HIS A  219    PRO A  220         14        -9.01                     
CISPEP  15 HIS A  219    PRO A  220         15        -3.67                     
CISPEP  16 HIS A  219    PRO A  220         16        -0.35                     
CISPEP  17 HIS A  219    PRO A  220         17        -4.73                     
CISPEP  18 HIS A  219    PRO A  220         18        -2.50                     
CISPEP  19 HIS A  219    PRO A  220         19        -4.77                     
CISPEP  20 HIS A  219    PRO A  220         20        -2.61                     
SITE     1 AC1  5 ASP A 246  VAL A 247  GLU A 249  ASN A 264                    
SITE     2 AC1  5 THR A 265                                                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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