HEADER    DE NOVO PROTEIN                         25-FEB-02   1L2Y              
TITLE     NMR STRUCTURE OF TRP-CAGE MINIPROTEIN CONSTRUCT TC5B                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TC5B;                                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 OTHER_DETAILS: THE PROTEIN WAS SYNTHESIZED USING STANDARD            
SOURCE   4 FMOC SOLID-PHASE SYNTHESIS METHODS ON AN APPLIED                     
SOURCE   5 BIOSYSTEMS 433A PEPTIDE SYNTHESIZER.                                 
KEYWDS    MINIPROTEIN, TWO-STATE FOLDING, TRP-CAGE, DE NOVO PROTEIN             
EXPDTA    SOLUTION NMR                                                          
NUMMDL    38                                                                    
AUTHOR    J.W.NEIDIGH,R.M.FESINMEYER,N.H.ANDERSEN                               
REVDAT   2   24-FEB-09 1L2Y    1       VERSN                                    
REVDAT   1   29-MAY-02 1L2Y    0                                                
JRNL        AUTH   J.W.NEIDIGH,R.M.FESINMEYER,N.H.ANDERSEN                      
JRNL        TITL   DESIGNING A 20-RESIDUE PROTEIN.                              
JRNL        REF    NAT.STRUCT.BIOL.              V.   9   425 2002              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   11979279                                                     
JRNL        DOI    10.1038/NSB798                                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : AMBER 6.0                                            
REMARK   3   AUTHORS     : KOLLMAN                                              
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 169 NOE DISTANCE CONSTRAINTS WERE         
REMARK   3  EMPLOYED. CNS WAS EMPLOYED FOR S.A., FOLLOWED BY MINIMIZATION       
REMARK   3  USING THE SANDER MODULE OF AMBER.                                   
REMARK   4                                                                      
REMARK   4 1L2Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB015598.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 282                                
REMARK 210  PH                             : 7                                  
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 1.0-1.8 MM TC5B                    
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D NOESY                           
REMARK 210  SPECTROMETER FIELD STRENGTH    : 500 MHZ                            
REMARK 210  SPECTROMETER MODEL             : DRX                                
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : XWINNMR 2.6, FELIX 95, CNS         
REMARK 210                                   1.0, AMBER 6.0                     
REMARK 210   METHOD USED                   : SIMULATED ANNEALING FROM           
REMARK 210                                   RANDOM STRUCTURES FOLLOWED BY      
REMARK 210                                   STEEPEST DESCENT MINIMIZATION      
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 50                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 38                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH ACCEPTABLE         
REMARK 210                                   COVALENT GEOMETRY, STRUCTURES      
REMARK 210                                   WITH THE LEAST RESTRAINT           
REMARK 210                                   VIOLATIONS                         
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL                
REMARK 210                                                                      
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D              
REMARK 210  HOMONUCLEAR TECHNIQUES.                                             
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500  2 ARG A  16   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500 13 ARG A  16   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500  5 LEU A   2      -34.83     72.95                                   
REMARK 500  6 LEU A   2      -33.93     63.45                                   
REMARK 500  9 LEU A   2      -18.34     57.13                                   
REMARK 500 13 LEU A   2      -33.72     66.32                                   
REMARK 500 18 LEU A   2       -3.11     60.50                                   
REMARK 500 19 LEU A   2       -1.16     58.98                                   
REMARK 500 20 LEU A   2      -32.96     68.39                                   
REMARK 500 23 LEU A   2      -47.12     63.92                                   
REMARK 500 28 LEU A   2       -2.46     61.26                                   
REMARK 500 29 LEU A   2      -42.02     66.43                                   
REMARK 500 34 PRO A  12       11.15    -66.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5292   RELATED DB: BMRB                                  
REMARK 900 BMRB 5292 IS CHEMICAL SHIFTS FOR TC5B IN BUFFER AND BUFFER           
REMARK 900 CONTAINING 30 VOL-% TFE.                                             
REMARK 900 RELATED ID: 1JRJ   RELATED DB: PDB                                   
REMARK 900 1JRJ IS AN ANALAGOUS C-TERMINAL STRUCTURE.                           
DBREF  1L2Y A    1    20  PDB    1L2Y     1L2Y             1     20             
SEQRES   1 A   20  ASN LEU TYR ILE GLN TRP LEU LYS ASP GLY GLY PRO SER          
SEQRES   2 A   20  SER GLY ARG PRO PRO PRO SER                                  
HELIX    1   1 ASN A    1  ASP A    9  1                                   9    
HELIX    2   2 GLY A   10  GLY A   15  5                                   6    
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      1  N   ASN     1      -8.901   4.127  -0.555  1.00  0.00           N 1 
ATOM      2  CA  ASN A   1      -8.608   3.135  -1.618  1.00  0.00           C  
ATOM      3  C   ASN A   1      -7.117   2.964  -1.897  1.00  0.00           C  
ATOM      4  O   ASN A   1      -6.634   1.849  -1.758  1.00  0.00           O  
ATOM      5  CB  ASN A   1      -9.437   3.396  -2.889  1.00  0.00           C  
ATOM      6  CG  ASN A   1     -10.915   3.130  -2.611  1.00  0.00           C  
ATOM      7  OD1 ASN A   1     -11.269   2.700  -1.524  1.00  0.00           O  
ATOM      8  ND2 ASN A   1     -11.806   3.406  -3.543  1.00  0.00           N  
ATOM      9  H1  ASN A   1      -8.330   3.957   0.261  1.00  0.00           H  
ATOM     10  H2  ASN A   1      -8.740   5.068  -0.889  1.00  0.00           H  
ATOM     11  H3  ASN A   1      -9.877   4.041  -0.293  1.00  0.00           H  
ATOM     12  HA  ASN A   1      -8.930   2.162  -1.239  1.00  0.00           H  
ATOM     13  HB2 ASN A   1      -9.310   4.417  -3.193  1.00  0.00           H  
ATOM     14  HB3 ASN A   1      -9.108   2.719  -3.679  1.00  0.00           H  
ATOM     15 HD21 ASN A   1     -11.572   3.791  -4.444  1.00  0.00           H  
ATOM     16 HD22 ASN A   1     -12.757   3.183  -3.294  1.00  0.00           H  
ATOM     17  N   LEU A   2      -6.379   4.031  -2.228  1.00  0.00           N  
ATOM     18  CA  LEU A   2      -4.923   4.002  -2.452  1.00  0.00           C  
ATOM     19  C   LEU A   2      -4.136   3.187  -1.404  1.00  0.00           C  
ATOM     20  O   LEU A   2      -3.391   2.274  -1.760  1.00  0.00           O  
ATOM     21  CB  LEU A   2      -4.411   5.450  -2.619  1.00  0.00           C  
ATOM     22  CG  LEU A   2      -4.795   6.450  -1.495  1.00  0.00           C  
ATOM     23  CD1 LEU A   2      -3.612   6.803  -0.599  1.00  0.00           C  
ATOM     24  CD2 LEU A   2      -5.351   7.748  -2.084  1.00  0.00           C  
ATOM     25  H   LEU A   2      -6.821   4.923  -2.394  1.00  0.00           H  
ATOM     26  HA  LEU A   2      -4.750   3.494  -3.403  1.00  0.00           H  
ATOM     27  HB2 LEU A   2      -3.340   5.414  -2.672  1.00  0.00           H  
ATOM     28  HB3 LEU A   2      -4.813   5.817  -3.564  1.00  0.00           H  
ATOM     29  HG  LEU A   2      -5.568   6.022  -0.858  1.00  0.00           H  
ATOM     30 HD11 LEU A   2      -3.207   5.905  -0.146  1.00  0.00           H  
ATOM     31 HD12 LEU A   2      -2.841   7.304  -1.183  1.00  0.00           H  
ATOM     32 HD13 LEU A   2      -3.929   7.477   0.197  1.00  0.00           H  
ATOM     33 HD21 LEU A   2      -4.607   8.209  -2.736  1.00  0.00           H  
ATOM     34 HD22 LEU A   2      -6.255   7.544  -2.657  1.00  0.00           H  
ATOM     35 HD23 LEU A   2      -5.592   8.445  -1.281  1.00  0.00           H  
ATOM     36  N   TYR A   3      -4.354   3.455  -0.111  1.00  0.00           N  
TER      36      SER A  20                                                      
ENDMDL                                                                          
MODEL        2                                                                  
ATOM      1  Hg  ASN A   1      -6.919   6.901   0.917  1.00  0.00           N  
ATOM      2  CA  ASN A   1      -7.682   6.025  -0.010  1.00  0.00           Hg 
ATOM      3  C   ASN A   1      -6.840   4.889  -0.589  1.00  0.00           C  
ATOM      4  O   ASN A   1      -7.106   3.741  -0.253  1.00  0.00           O  
ATOM      5  CB  ASN A   1      -8.428   6.847  -1.072  1.00  0.00           C  
ATOM      6  CG  ASN A   1      -9.504   7.659  -0.362  1.00  0.00           C  
ATOM      7  OD1 ASN A   1      -9.180   8.568   0.382  1.00  0.00           O  
ATOM      8  ND2 ASN A   1     -10.768   7.290  -0.468  1.00  0.00           N  
ATOM      9  H1  ASN A   1      -6.513   6.358   1.667  1.00  0.00           H  
ATOM     10  H2  ASN A   1      -6.191   7.398   0.422  1.00  0.00           H  
ATOM     11  H3  ASN A   1      -7.553   7.592   1.308  1.00  0.00           H  
ATOM     12  HA  ASN A   1      -8.451   5.523   0.581  1.00  0.00           H  
ATOM     13  HB2 ASN A   1      -7.743   7.506  -1.571  1.00  0.00           H  
ATOM     14  HB3 ASN A   1      -8.886   6.189  -1.811  1.00  0.00           H  
ATOM     15 HD21 ASN A   1     -11.078   6.519  -1.037  1.00  0.00           H  
ATOM     16 HD22 ASN A   1     -11.417   7.848   0.064  1.00  0.00           H  
ATOM     17  N   LEU A   2      -5.819   5.175  -1.412  1.00  0.00           N  
ATOM     18  CA  LEU A   2      -5.020   4.162  -2.130  1.00  0.00           C  
ATOM     19  C   LEU A   2      -4.244   3.179  -1.224  1.00  0.00           C  
ATOM     20  O   LEU A   2      -3.761   2.148  -1.693  1.00  0.00           O  
ATOM     21  CB  LEU A   2      -4.073   4.863  -3.128  1.00  0.00           C  
ATOM     22  CG  LEU A   2      -4.831   5.608  -4.250  1.00  0.00           C  
ATOM     23  CD1 LEU A   2      -5.010   7.109  -3.963  1.00  0.00           C  
ATOM     24  CD2 LEU A   2      -4.110   5.465  -5.592  1.00  0.00           C  
ATOM     25  H   LEU A   2      -5.631   6.133  -1.665  1.00  0.00           H  
ATOM     26  HA  LEU A   2      -5.709   3.545  -2.710  1.00  0.00           H  
ATOM     27  HB2 LEU A   2      -3.472   5.572  -2.591  1.00  0.00           H  
ATOM     28  HB3 LEU A   2      -3.451   4.089  -3.583  1.00  0.00           H  
ATOM     29  HG  LEU A   2      -5.820   5.160  -4.359  1.00  0.00           H  
ATOM     30 HD11 LEU A   2      -5.173   7.303  -2.907  1.00  0.00           H  
ATOM     31 HD12 LEU A   2      -4.124   7.663  -4.273  1.00  0.00           H  
ATOM     32 HD13 LEU A   2      -5.867   7.480  -4.526  1.00  0.00           H  
ATOM     33 HD21 LEU A   2      -3.114   5.904  -5.535  1.00  0.00           H  
ATOM     34 HD22 LEU A   2      -4.023   4.410  -5.855  1.00  0.00           H  
ATOM     35 HD23 LEU A   2      -4.683   5.969  -6.371  1.00  0.00           H  
ATOM     36  N   TYR A   3      -4.181   3.456   0.082  1.00  0.00           N  
TER      36      SER A  20                                                      
ENDMDL