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Database: PDB
Entry: 2M74
LinkDB: 2M74
Original site: 2M74 
HEADER    STRUCTURAL PROTEIN                      17-APR-13   2M74              
TITLE     1H, 13C AND 15N ASSIGNMENTS OF THE FOUR N-TERMINAL DOMAINS OF HUMAN   
TITLE    2 FIBRILLIN-1                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBRILLIN-1;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: FUN-EGF3 REGION OF FIBRILLIN-1, UNP RESIDUES 45-178;       
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 GENE: FBN, FBN1;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PQE-30;                                    
SOURCE  10 OTHER_DETAILS: CELLS WERE ALSO TRANSFORMED WITH THE PREP4 PLASMID,   
SOURCE  11 ENABLING INDUCIBLE EXPRESSION                                        
KEYWDS    STRUCTURAL PROTEIN                                                    
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    D.A.YADIN,I.B.ROBERTSON,S.A.JENSEN,P.A.HANDFORD,C.REDFIELD            
REVDAT   2   20-NOV-13 2M74    1       JRNL                                     
REVDAT   1   25-SEP-13 2M74    0                                                
JRNL        AUTH   D.A.YADIN,I.B.ROBERTSON,J.MCNAUGHT-DAVIS,P.EVANS,D.STODDART, 
JRNL        AUTH 2 P.A.HANDFORD,S.A.JENSEN,C.REDFIELD                           
JRNL        TITL   STRUCTURE OF THE FIBRILLIN-1 N-TERMINAL DOMAINS SUGGESTS     
JRNL        TITL 2 THAT HEPARAN SULFATE REGULATES THE EARLY STAGES OF           
JRNL        TITL 3 MICROFIBRIL ASSEMBLY.                                        
JRNL        REF    STRUCTURE                     V.  21  1743 2013              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   24035709                                                     
JRNL        DOI    10.1016/J.STR.2013.08.004                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR_NIH 2.29, X-PLOR                              
REMARK   3   AUTHORS     : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE (X-PLOR_    
REMARK   3                 NIH), (X-PLOR)                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: AN ENSEMBLE OF 100 STRUCTURES WAS         
REMARK   3  GENERATED. FLOATING CHIRALITY OF PROCHIRAL GROUPS WAS USED FOR      
REMARK   3  STEREOSPECIFIC ASSIGNMENT., AN INITIAL ENSEMBLE OF 200 STRUCTURES   
REMARK   3  WAS USING SIMULATED ANNEALING FROM AN EXTENDED TEMPLATE USING NOE   
REMARK   3  -DERIVED DISTANCE RESTRAINTS WITH STEREOSPECIFIC ASSIGNMENTS.       
REMARK   3  COORDINATES OF THE 10 LOWEST-ENERGY STRUCTURES WERE THEN USED AS    
REMARK   3  TEMPLATES FOR REFINEMENT CALCULATIONS, INCLUDING THE 'RAMA' AND '   
REMARK   3  HBDB' DATABASE POTENTIALS. THE RESULTING 10 LOWEST-ENERGY           
REMARK   3  STRUCTURES WERE THEN REFINED FURTHER USING RDCS. SEPARATE           
REMARK   3  ALIGNMENT TENSORS WERE USED FOR THE TWO HALVES OF THE MOLECULE ('   
REMARK   3  NE1' AND 'E2E3'). ALIGNMENT TENSOR PARAMETERS WERE ESTIMATED        
REMARK   3  USING PARTIALLY REFINED STRUCTURES. THE 20 LOWEST-STRUCTURES FROM   
REMARK   3  THE FINAL ENSEMBLE OF 200 STRUCTURES WERE SELECTED AS THE           
REMARK   3  REPRESENTATIVE STRUCTURE ENSEMBLE.                                  
REMARK   4                                                                      
REMARK   4 2M74 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB103292.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298; 308                           
REMARK 210  PH                             : 5.40; 5.40                         
REMARK 210  IONIC STRENGTH                 : 0; 0                               
REMARK 210  PRESSURE                       : 1 ATM; 1 ATM                       
REMARK 210  SAMPLE CONTENTS                : 1.5 MM [U-99% 15N] FUN-EGF3, 95%   
REMARK 210                                   H2O/5% D2O; 0.5 MM [U-99% 15N]     
REMARK 210                                   FUN-EGF3, 100% D2O; 1.5 MM [U-99%  
REMARK 210                                   13C; U-99% 15N] FUN-EGF3, 95%      
REMARK 210                                   H2O/5% D2O; 1.5 MM [U-99% 13C; U-  
REMARK 210                                   99% 15N] FUN-EGF3, 100% D2O; 0.5   
REMARK 210                                   MM [U-99% 13C; U-99% 15N] FUN-     
REMARK 210                                   EGF3, 90% H2O/10% D2O              
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D 1H-15N HSQC; 3D 1H-15N NOESY;   
REMARK 210                                   3D 1H-15N TOCSY; 2D 1H-1H TOCSY;   
REMARK 210                                   2D DQF-COSY; 2D 1H-1H NOESY; 3D    
REMARK 210                                   HNCA; 3D (H)CC(CO)NH; 3D HNCO; 3D  
REMARK 210                                   HN(CA)CO; 2D 1H-13C HSQC           
REMARK 210                                   ALIPHATIC; 3D HCCH-TOCSY; 3D 1H-   
REMARK 210                                   13C NOESY ALIPHATIC; 2D 1H-13C     
REMARK 210                                   HSQC AROMATIC; 3D 1H-15N HSQC-     
REMARK 210                                   NOESY-HSQC; 2D 1H-15N HMQC-J; 2D   
REMARK 210                                   1H-15N IPAP-HSQC                   
REMARK 210  SPECTROMETER FIELD STRENGTH    : 750 MHZ; 600 MHZ; 500 MHZ          
REMARK 210  SPECTROMETER MODEL             : HOME-BUILT USING GE OMEGA          
REMARK 210                                   SOFTWARE; AVANCE                   
REMARK 210  SPECTROMETER MANUFACTURER      : HOME-BUILT; BRUKER                 
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NMRPIPE JUNE 2006 SUN SOLARIS,     
REMARK 210                                   CCPN_ANALYSIS 2.1.5, X-PLOR 3.8,   
REMARK 210                                   X-PLOR_NIH 2.29, TALOS+ 3.3,       
REMARK 210                                   FELIX 2.3                          
REMARK 210   METHOD USED                   : SIMULATED ANNEALING, TORSION       
REMARK 210                                   ANGLE DYNAMICS                     
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 200                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST 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 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 ASN A  57       65.79   -119.88                                   
REMARK 500  1 CYS A  68      169.00    -47.10                                   
REMARK 500  1 LYS A  72     -164.52   -121.98                                   
REMARK 500  1 PRO A  75      107.76    -40.44                                   
REMARK 500  1 CYS A  80       55.26    -95.66                                   
REMARK 500  1 GLN A 117      118.47   -171.80                                   
REMARK 500  1 HIS A 118     -106.01     49.39                                   
REMARK 500  1 ASN A 156     -147.62   -170.66                                   
REMARK 500  1 CYS A 177     -104.93   -111.61                                   
REMARK 500  2 PRO A  75      105.47    -39.04                                   
REMARK 500  2 HIS A  87     -118.08   -123.33                                   
REMARK 500  2 CYS A 111       20.31    -76.25                                   
REMARK 500  2 ASP A 131     -118.32     39.88                                   
REMARK 500  2 CYS A 145      140.65     71.14                                   
REMARK 500  2 CYS A 177      119.62     58.75                                   
REMARK 500  3 ALA A  44       56.63   -103.05                                   
REMARK 500  3 ARG A  45       85.31     41.54                                   
REMARK 500  3 ALA A  52     -167.78    179.20                                   
REMARK 500  3 ASN A  57       74.42   -112.54                                   
REMARK 500  3 ASN A  78       16.77   -146.90                                   
REMARK 500  3 CYS A  80       39.23    -88.43                                   
REMARK 500  3 GLN A 117       41.71   -142.18                                   
REMARK 500  3 ASN A 164       23.02     47.90                                   
REMARK 500  3 CYS A 177       11.55     50.19                                   
REMARK 500  4 ALA A  52      155.94     56.70                                   
REMARK 500  4 SER A 115       93.17     38.31                                   
REMARK 500  4 ASN A 156      -58.92    161.67                                   
REMARK 500  4 CYS A 177      124.50     59.56                                   
REMARK 500  5 ARG A  45       81.12     50.87                                   
REMARK 500  5 PRO A  56     -167.46    -68.52                                   
REMARK 500  5 CYS A  80       43.49    -99.21                                   
REMARK 500  5 SER A 113      132.91     58.09                                   
REMARK 500  5 ASP A 131      -97.15     36.11                                   
REMARK 500  5 GLN A 137     -174.77    -68.19                                   
REMARK 500  5 ASN A 156      -60.79    178.23                                   
REMARK 500  5 GLN A 176       47.90    -92.15                                   
REMARK 500  5 CYS A 177      -89.27     57.88                                   
REMARK 500  6 PRO A  56     -169.36    -73.47                                   
REMARK 500  6 CYS A  68      162.52    -45.62                                   
REMARK 500  6 LYS A  72     -157.99   -125.70                                   
REMARK 500  6 PRO A  75      105.98    -40.66                                   
REMARK 500  6 CYS A  80       47.66    -90.96                                   
REMARK 500  6 GLN A 117       90.32   -171.80                                   
REMARK 500  6 HIS A 118     -162.80     42.31                                   
REMARK 500  6 ASN A 120       29.59   -161.75                                   
REMARK 500  6 ASP A 132      -40.68     78.29                                   
REMARK 500  6 GLN A 137      176.13    -59.95                                   
REMARK 500  6 CYS A 145      139.13     60.68                                   
REMARK 500  6 CYS A 177      159.80     57.17                                   
REMARK 500  7 ALA A  52      138.58   -178.29                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     169 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 18843   RELATED DB: BMRB                                 
REMARK 900 CHEMICAL SHIFT ASSIGNMENTS FOR THE FUN-EGF3 RECOMBINANT              
REMARK 900 FRAGMENT OF HUMAN FIBRILLIN-1                                        
DBREF  2M74 A   45   178  UNP    P35555   FBN1_HUMAN      45    178             
SEQADV 2M74 SER A   43  UNP  P35555              EXPRESSION TAG                 
SEQADV 2M74 ALA A   44  UNP  P35555              EXPRESSION TAG                 
SEQRES   1 A  136  SER ALA ARG GLY GLY GLY GLY HIS ASP ALA LEU LYS GLY          
SEQRES   2 A  136  PRO ASN VAL CYS GLY SER ARG TYR ASN ALA TYR CYS CYS          
SEQRES   3 A  136  PRO GLY TRP LYS THR LEU PRO GLY GLY ASN GLN CYS ILE          
SEQRES   4 A  136  VAL PRO ILE CYS ARG HIS SER CYS GLY ASP GLY PHE CYS          
SEQRES   5 A  136  SER ARG PRO ASN MET CYS THR CYS PRO SER GLY GLN ILE          
SEQRES   6 A  136  ALA PRO SER CYS GLY SER ARG SER ILE GLN HIS CYS ASN          
SEQRES   7 A  136  ILE ARG CYS MET ASN GLY GLY SER CYS SER ASP ASP HIS          
SEQRES   8 A  136  CYS LEU CYS GLN LYS GLY TYR ILE GLY THR HIS CYS GLY          
SEQRES   9 A  136  GLN PRO VAL CYS GLU SER GLY CYS LEU ASN GLY GLY ARG          
SEQRES  10 A  136  CYS VAL ALA PRO ASN ARG CYS ALA CYS THR TYR GLY PHE          
SEQRES  11 A  136  THR GLY PRO GLN CYS GLU                                      
SHEET    1   A 2 VAL A  58  CYS A  59  0                                        
SHEET    2   A 2 TYR A  66  CYS A  67 -1  O  TYR A  66   N  CYS A  59           
SHEET    1   B 2 TRP A  71  LYS A  72  0                                        
SHEET    2   B 2 VAL A  82  PRO A  83 -1  O  VAL A  82   N  LYS A  72           
SHEET    1   C 3 PHE A  93  ARG A  96  0                                        
SHEET    2   C 3 MET A  99  THR A 101 -1  O  THR A 101   N  PHE A  93           
SHEET    3   C 3 ILE A 107  ALA A 108 -1  O  ALA A 108   N  CYS A 100           
SHEET    1   D 2 SER A 128  CYS A 129  0                                        
SHEET    2   D 2 CYS A 134  LEU A 135 -1  O  LEU A 135   N  SER A 128           
SHEET    1   E 2 TYR A 140  ILE A 141  0                                        
SHEET    2   E 2 GLN A 147  PRO A 148 -1  O  GLN A 147   N  ILE A 141           
SHEET    1   F 2 ARG A 159  ALA A 162  0                                        
SHEET    2   F 2 ARG A 165  ALA A 167 -1  O  ALA A 167   N  ARG A 159           
SSBOND   1 CYS A   59    CYS A   68                          1555   1555  2.02  
SSBOND   2 CYS A   67    CYS A   80                          1555   1555  2.02  
SSBOND   3 CYS A   85    CYS A   94                          1555   1555  2.02  
SSBOND   4 CYS A   89    CYS A  100                          1555   1555  2.02  
SSBOND   5 CYS A  102    CYS A  111                          1555   1555  2.01  
SSBOND   6 CYS A  119    CYS A  129                          1555   1555  2.02  
SSBOND   7 CYS A  123    CYS A  134                          1555   1555  2.02  
SSBOND   8 CYS A  136    CYS A  145                          1555   1555  2.02  
SSBOND   9 CYS A  150    CYS A  160                          1555   1555  2.02  
SSBOND  10 CYS A  154    CYS A  166                          1555   1555  2.02  
SSBOND  11 CYS A  168    CYS A  177                          1555   1555  2.03  
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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