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***  SIGNALING PROTEIN 26-NOV-02 1N9U  ***

elNémo ID: 201027191958118520

Job options:

ID        	=	 201027191958118520
JOBID     	=	 SIGNALING PROTEIN 26-NOV-02 1N9U
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    SIGNALING PROTEIN                       26-NOV-02   1N9U              
TITLE     DIFFERENCES AND SIMILARITIES IN SOLUTION STRUCTURES OF ANGIOTENSIN I &
TITLE    2 II: IMPLICATION FOR STRUCTURE-FUNCTION RELATIONSHIP                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN I;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ANG I;                                                      
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 OTHER_DETAILS: THE PEPTIDE WAS MADE THROUGH SOLID PHASE SYNTHESIS    
SOURCE   4 USING FMOC CHEMISTRY. THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND 
SOURCE   5 IN HOMO SAPIENS.                                                     
KEYWDS    ANGIOTENSIN, RENIN-ANGIOTENSIN SYSTEM, SOLID PHASE PEPTIDE SYNTHESIS, 
KEYWDS   2 NMR SOLUTION STRUCTURE, PEPTIDES, SIGNALING PROTEIN                  
EXPDTA    SOLUTION NMR                                                          
NUMMDL    21                                                                    
AUTHOR    G.A.SPYROULIAS,P.NIKOLAKOPOULOU,A.TZAKOS,I.P.GEROTHANASSIS,V.MAGAFA,  
AUTHOR   2 E.MANESSI-ZOUPA,P.CORDOPATIS                                         
REVDAT   3   21-DEC-16 1N9U    1       TITLE  VERSN                             
REVDAT   2   24-FEB-09 1N9U    1       VERSN                                    
REVDAT   1   29-JUL-03 1N9U    0                                                
JRNL        AUTH   G.A.SPYROULIAS,P.NIKOLAKOPOULOU,A.TZAKOS,I.P.GEROTHANASSIS,  
JRNL        AUTH 2 V.MAGAFA,E.MANESSI-ZOUPA,P.CORDOPATIS                        
JRNL        TITL   COMPARISON OF THE SOLUTION STRUCTURES OF ANGIOTENSIN I & II. 
JRNL        TITL 2 IMPLICATION FOR STRUCTURE-FUNCTION RELATIONSHIP.             
JRNL        REF    EUR.J.BIOCHEM.                V. 270  2163 2003              
JRNL        REFN                   ISSN 0014-2956                               
JRNL        PMID   12752436                                                     
JRNL        DOI    10.1046/J.1432-1033.2003.03573.X                             
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.M.MATSOUKAS,J.HONDRELIS,M.KERAMIDA,T.MAVROMOUSTAKOS,       
REMARK   1  AUTH 2 A.MAKRIYANNIS,R.YAMDAGNI,Q.WU,G.J.MOORE                      
REMARK   1  TITL   ROLE OF THE NH2-TERMINAL DOMAIN OF ANGIOTENSIN II (ANG II)   
REMARK   1  TITL 2 AND [SAR1]ANGIOTENSIN II ON CONFORMATION AND ACTIVITY. NMR   
REMARK   1  TITL 3 EVIDENCE FOR AROMATIC RING CLUSTERING AND PEPTIDE BACKBONE   
REMARK   1  TITL 4 FOLDING COMPARED WITH [DES-1,2,3]ANGIOTENSIN II              
REMARK   1  REF    J.BIOL.CHEM.                  V. 269  5303 1994              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : AMBER 5.0                                            
REMARK   3   AUTHORS     : KOLLMAN, CASE, MERZ, CHEATHAM, SIMMERLING, DARDEN,   
REMARK   3                 PEARLMAN                                             
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THIS STRUCTURE IS BASED ON A 225 NOE-     
REMARK   3  DERIVED DISTANCE CONSTRAINTS, 7 DIHEDRAL ANGLE RESTRAINTS, 1        
REMARK   3  DISTANCE RESTRAINT FROM HYDROGEN BOND                               
REMARK   4                                                                      
REMARK   4 1N9U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB017698.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : NULL                               
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 2.5 MM; DMSO-D6                    
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : DQF-COSY; 2D TOCSY; 2D NOESY       
REMARK 210  SPECTROMETER FIELD STRENGTH    : 400 MHZ                            
REMARK 210  SPECTROMETER MODEL             : DPX                                
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : XWINNMR 2.6, XEASY 1.3, DYANA 1.5  
REMARK 210   METHOD USED                   : SIMULATED ANNEALING, TORSION       
REMARK 210                                   ANGLE DYNAMICS                     
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 300                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 21                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : TARGET FUNCTION FOR MODELS 1-20,   
REMARK 210                                   MEAN ENERGY MINIMIZED FOR MODEL 21 
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 21                  
REMARK 210                                                                      
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D              
REMARK 210  HOMONUCLEAR TECHNIQUES. MODELS 1-20 ARE THE FAMILY ENSEMBLE,        
REMARK 210  WHILE MODEL 21 IS THE MINIMIZED AVERAGE STRUCTURE DERIVED FROM      
REMARK 210  THAT ENSEMBLE.                                                      
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 PHE A   8      117.36   -171.75                                   
REMARK 500  1 HIS A   9       58.75   -149.53                                   
REMARK 500  2 PHE A   8      118.30   -171.58                                   
REMARK 500  2 HIS A   9       56.59   -146.96                                   
REMARK 500  3 PHE A   8      118.30   -171.58                                   
REMARK 500  3 HIS A   9       56.59   -146.96                                   
REMARK 500  4 PHE A   8      119.30   -171.72                                   
REMARK 500  4 HIS A   9       64.97   -151.55                                   
REMARK 500  5 PHE A   8      117.86   -171.89                                   
REMARK 500  6 PHE A   8      118.93   -171.07                                   
REMARK 500  6 HIS A   9       58.33   -148.27                                   
REMARK 500  7 PHE A   8      119.21   -172.11                                   
REMARK 500  7 HIS A   9       59.63   -148.35                                   
REMARK 500  8 PHE A   8      117.84   -170.91                                   
REMARK 500  8 HIS A   9       65.66   -151.10                                   
REMARK 500  9 PHE A   8      118.31   -171.91                                   
REMARK 500 10 PHE A   8      119.85   -170.43                                   
REMARK 500 11 PHE A   8      118.80   -171.77                                   
REMARK 500 12 PHE A   8      120.14   -171.48                                   
REMARK 500 13 PHE A   8      118.31   -172.61                                   
REMARK 500 14 PHE A   8      119.07   -171.25                                   
REMARK 500 14 HIS A   9       58.30   -151.60                                   
REMARK 500 15 PHE A   8      117.20   -171.72                                   
REMARK 500 16 PHE A   8      117.45   -171.92                                   
REMARK 500 16 HIS A   9       63.70   -151.34                                   
REMARK 500 17 PHE A   8      119.55   -171.81                                   
REMARK 500 17 HIS A   9       61.79   -153.46                                   
REMARK 500 18 PHE A   8      119.22   -172.14                                   
REMARK 500 18 HIS A   9       57.10   -149.75                                   
REMARK 500 19 PHE A   8      118.47   -171.24                                   
REMARK 500 19 HIS A   9       63.29   -150.37                                   
REMARK 500 20 PHE A   8      115.71   -170.95                                   
REMARK 500 20 HIS A   9       35.98   -153.52                                   
REMARK 500 21 PHE A   8      122.61   -170.23                                   
REMARK 500 21 HIS A   9       59.70   -153.61                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500 14 ARG A   2         0.10    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1N9U A    1    10  UNP    P01019   ANGT_HUMAN      34     43             
SEQRES   1 A   10  ASP ARG VAL TYR ILE HIS PRO PHE HIS LEU                      
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   ASP A   1      -5.069  -8.815  -3.529  1.00  1.16           N  
ATOM      2  CA  ASP A   1      -4.131  -8.607  -4.648  1.00  0.28           C  
ATOM      3  C   ASP A   1      -3.643  -7.171  -4.625  1.00  0.23           C  
ATOM      4  O   ASP A   1      -4.399  -6.267  -4.965  1.00  0.36           O  
ATOM      5  CB  ASP A   1      -4.790  -8.937  -5.991  1.00  1.60           C  
ATOM      6  CG  ASP A   1      -5.010 -10.439  -6.087  1.00  2.12           C  
ATOM      7  OD1 ASP A   1      -5.434 -10.982  -5.043  1.00  2.36           O  
ATOM      8  OD2 ASP A   1      -4.707 -11.009  -7.153  1.00  3.05           O  
ATOM      9  H1  ASP A   1      -5.859  -8.199  -3.651  1.00  1.85           H  
ATOM     10  H2  ASP A   1      -5.390  -9.775  -3.530  1.00  1.09           H  
ATOM     11  H3  ASP A   1      -4.609  -8.615  -2.655  1.00  1.80           H  
ATOM     12  HA  ASP A   1      -3.281  -9.279  -4.530  1.00  1.09           H  
ATOM     13  HB2 ASP A   1      -5.749  -8.422  -6.071  1.00  2.40           H  
ATOM     14  HB3 ASP A   1      -4.142  -8.611  -6.806  1.00  2.24           H  
ATOM     15  N   ARG A   2      -2.405  -6.936  -4.184  1.00  0.20           N  
ATOM     16  CA  ARG A   2      -1.796  -5.617  -4.186  1.00  0.17           C  
ATOM     17  C   ARG A   2      -0.319  -5.820  -4.494  1.00  0.17           C  
ATOM     18  O   ARG A   2       0.368  -6.491  -3.733  1.00  0.27           O  
ATOM     19  CB  ARG A   2      -2.001  -4.961  -2.808  1.00  0.26           C  
ATOM     20  CG  ARG A   2      -3.141  -3.932  -2.824  1.00  0.77           C  
ATOM     21  CD  ARG A   2      -2.540  -2.557  -3.113  1.00  1.45           C  
ATOM     22  NE  ARG A   2      -3.544  -1.541  -3.442  1.00  1.67           N  
ATOM     23  CZ  ARG A   2      -3.230  -0.273  -3.738  1.00  2.67           C  
ATOM     24  NH1 ARG A   2      -1.958   0.129  -3.683  1.00  3.83           N  
ATOM     25  NH2 ARG A   2      -4.185   0.587  -4.093  1.00  3.07           N  
ATOM     26  H   ARG A   2      -1.803  -7.669  -3.834  1.00  0.29           H  
ATOM     27  HA  ARG A   2      -2.251  -5.002  -4.964  1.00  0.22           H  
ATOM     28  HB2 ARG A   2      -2.219  -5.730  -2.065  1.00  0.86           H  
ATOM     29  HB3 ARG A   2      -1.082  -4.460  -2.500  1.00  0.80           H  
ATOM     30  HG2 ARG A   2      -3.880  -4.192  -3.582  1.00  2.13           H  
ATOM     31  HG3 ARG A   2      -3.627  -3.907  -1.848  1.00  2.07           H  
ATOM     32  HD2 ARG A   2      -2.000  -2.237  -2.223  1.00  2.49           H  
ATOM     33  HD3 ARG A   2      -1.844  -2.643  -3.949  1.00  2.62           H  
ATOM     34  HE  ARG A   2      -4.506  -1.848  -3.459  1.00  1.89           H  
ATOM     35 HH11 ARG A   2      -1.234  -0.515  -3.377  1.00  3.97           H  
ATOM     36 HH12 ARG A   2      -1.680   1.074  -3.892  1.00  4.80           H  
ATOM     37 HH21 ARG A   2      -5.152   0.301  -4.140  1.00  3.02           H  
ATOM     38 HH22 ARG A   2      -3.973   1.548  -4.318  1.00  3.85           H  
ATOM     39  N   VAL A   3       0.162  -5.253  -5.601  1.00  0.14           N  
ATOM     40  CA  VAL A   3       1.579  -5.274  -5.958  1.00  0.12           C  
ATOM     41  C   VAL A   3       2.376  -4.401  -4.995  1.00  0.11           C  
ATOM     42  O   VAL A   3       3.568  -4.608  -4.797  1.00  0.14           O  
ATOM     43  CB  VAL A   3       1.746  -4.850  -7.429  1.00  0.15           C  
ATOM     44  CG1 VAL A   3       3.212  -4.821  -7.875  1.00  0.21           C  
ATOM     45  CG2 VAL A   3       0.994  -5.835  -8.335  1.00  0.25           C  
ATOM     46  H   VAL A   3      -0.457  -4.746  -6.213  1.00  0.20           H  
ATOM     47  HA  VAL A   3       1.970  -6.277  -5.837  1.00  0.13           H  
ATOM     48  HB  VAL A   3       1.319  -3.855  -7.565  1.00  0.17           H  
ATOM     49 HG11 VAL A   3       3.683  -5.783  -7.671  1.00  1.53           H  
ATOM     50 HG12 VAL A   3       3.272  -4.611  -8.943  1.00  1.56           H  
ATOM     51 HG13 VAL A   3       3.753  -4.038  -7.343  1.00  1.68           H  
ATOM     52 HG21 VAL A   3       1.383  -6.843  -8.187  1.00  1.67           H  
ATOM     53 HG22 VAL A   3      -0.073  -5.829  -8.118  1.00  1.44           H  
ATOM     54 HG23 VAL A   3       1.131  -5.554  -9.380  1.00  1.56           H  
ATOM     55  N   TYR A   4       1.715  -3.421  -4.385  1.00  0.10           N  
ATOM     56  CA  TYR A   4       2.343  -2.483  -3.490  1.00  0.10           C  
ATOM     57  C   TYR A   4       1.316  -2.141  -2.422  1.00  0.14           C  
ATOM     58  O   TYR A   4       0.217  -1.686  -2.747  1.00  0.32           O  
ATOM     59  CB  TYR A   4       2.769  -1.271  -4.317  1.00  0.14           C  
ATOM     60  CG  TYR A   4       2.956   0.002  -3.513  1.00  0.12           C  
ATOM     61  CD1 TYR A   4       3.840   0.028  -2.418  1.00  1.69           C  
ATOM     62  CD2 TYR A   4       2.198   1.146  -3.829  1.00  1.65           C  
ATOM     63  CE1 TYR A   4       3.958   1.189  -1.635  1.00  1.68           C  
ATOM     64  CE2 TYR A   4       2.318   2.313  -3.057  1.00  1.68           C  
ATOM     65  CZ  TYR A   4       3.199   2.336  -1.952  1.00  0.16           C  
ATOM     66  OH  TYR A   4       3.313   3.460  -1.194  1.00  0.22           O  
ATOM     67  H   TYR A   4       0.733  -3.279  -4.552  1.00  0.14           H  
ATOM     68  HA  TYR A   4       3.223  -2.932  -3.025  1.00  0.08           H  
ATOM     69  HB2 TYR A   4       3.694  -1.530  -4.835  1.00  0.18           H  
ATOM     70  HB3 TYR A   4       2.010  -1.104  -5.082  1.00  0.20           H  
ATOM     71  HD1 TYR A   4       4.422  -0.845  -2.159  1.00  2.98           H  
ATOM     72  HD2 TYR A   4       1.521   1.132  -4.670  1.00  2.93           H  
ATOM     73  HE1 TYR A   4       4.620   1.202  -0.781  1.00  2.96           H  
ATOM     74  HE2 TYR A   4       1.736   3.187  -3.312  1.00  2.96           H  
ATOM     75  HH  TYR A   4       2.842   4.203  -1.578  1.00  1.41           H  
ATOM     76  N   ILE A   5       1.672  -2.393  -1.165  1.00  0.10           N  
ATOM     77  CA  ILE A   5       0.888  -2.059   0.009  1.00  0.10           C  
ATOM     78  C   ILE A   5       1.567  -0.872   0.660  1.00  0.09           C  
ATOM     79  O   ILE A   5       2.785  -0.724   0.577  1.00  0.12           O  
ATOM     80  CB  ILE A   5       0.822  -3.277   0.964  1.00  0.12           C  
ATOM     81  CG1 ILE A   5      -0.465  -4.090   0.752  1.00  0.16           C  
ATOM     82  CG2 ILE A   5       0.992  -2.967   2.464  1.00  0.15           C  
ATOM     83  CD1 ILE A   5      -1.746  -3.275   0.961  1.00  0.20           C  
ATOM     84  H   ILE A   5       2.621  -2.679  -0.975  1.00  0.20           H  
ATOM     85  HA  ILE A   5      -0.108  -1.751  -0.297  1.00  0.11           H  
ATOM     86  HB  ILE A   5       1.656  -3.928   0.715  1.00  0.12           H  
ATOM     87 HG12 ILE A   5      -0.467  -4.504  -0.255  1.00  0.17           H  
ATOM     88 HG13 ILE A   5      -0.469  -4.926   1.453  1.00  0.19           H  
ATOM     89 HG21 ILE A   5       1.988  -2.564   2.653  1.00  1.32           H  
ATOM     90 HG22 ILE A   5       0.245  -2.260   2.821  1.00  1.37           H  
ATOM     91 HG23 ILE A   5       0.899  -3.888   3.041  1.00  1.38           H  
ATOM     92 HD11 ILE A   5      -1.660  -2.644   1.847  1.00  1.33           H  
ATOM     93 HD12 ILE A   5      -1.940  -2.649   0.092  1.00  1.49           H  
ATOM     94 HD13 ILE A   5      -2.585  -3.960   1.076  1.00  1.47           H  
ATOM     95  N   HIS A   6       0.778  -0.075   1.371  1.00  0.09           N  
ATOM     96  CA  HIS A   6       1.309   0.909   2.284  1.00  0.09           C  
ATOM     97  C   HIS A   6       0.465   0.873   3.549  1.00  0.10           C  
ATOM     98  O   HIS A   6      -0.758   0.785   3.464  1.00  0.11           O  
ATOM     99  CB  HIS A   6       1.300   2.302   1.643  1.00  0.09           C  
ATOM    100  CG  HIS A   6      -0.079   2.823   1.307  1.00  0.10           C  
ATOM    101  ND1 HIS A   6      -0.974   3.434   2.164  1.00  0.11           N  
ATOM    102  CD2 HIS A   6      -0.654   2.788   0.068  1.00  0.15           C  
ATOM    103  CE1 HIS A   6      -2.079   3.719   1.451  1.00  0.16           C  
ATOM    104  NE2 HIS A   6      -1.929   3.349   0.168  1.00  0.20           N  
ATOM    105  H   HIS A   6      -0.205  -0.290   1.463  1.00  0.10           H  
ATOM    106  HA  HIS A   6       2.333   0.631   2.516  1.00  0.12           H  
ATOM    107  HB2 HIS A   6       1.789   3.001   2.318  1.00  0.11           H  
ATOM    108  HB3 HIS A   6       1.891   2.264   0.728  1.00  0.12           H  
ATOM    109  HD1 HIS A   6      -0.852   3.644   3.143  1.00  0.11           H  
ATOM    110  HD2 HIS A   6      -0.186   2.413  -0.827  1.00  0.17           H  
ATOM    111  HE1 HIS A   6      -2.965   4.193   1.849  1.00  0.19           H  
ATOM    112  N   PRO A   7       1.086   0.975   4.727  1.00  0.12           N  
ATOM    113  CA  PRO A   7       0.365   1.270   5.950  1.00  0.13           C  
ATOM    114  C   PRO A   7      -0.133   2.705   5.976  1.00  0.11           C  
ATOM    115  O   PRO A   7      -1.057   3.043   6.707  1.00  0.13           O  
ATOM    116  CB  PRO A   7       1.331   0.925   7.082  1.00  0.17           C  
ATOM    117  CG  PRO A   7       2.716   1.107   6.454  1.00  0.19           C  
ATOM    118  CD  PRO A   7       2.513   0.869   4.958  1.00  0.14           C  
ATOM    119  HA  PRO A   7      -0.521   0.674   6.007  1.00  0.15           H  
ATOM    120  HB2 PRO A   7       1.193   1.566   7.954  1.00  0.17           H  
ATOM    121  HB3 PRO A   7       1.197  -0.122   7.356  1.00  0.21           H  
ATOM    122  HG2 PRO A   7       3.059   2.128   6.612  1.00  0.20           H  
ATOM    123  HG3 PRO A   7       3.426   0.388   6.861  1.00  0.26           H  
ATOM    124  HD2 PRO A   7       3.063   1.617   4.385  1.00  0.13           H  
ATOM    125  HD3 PRO A   7       2.851  -0.134   4.694  1.00  0.16           H  
ATOM    126  N   PHE A   8       0.486   3.548   5.161  1.00  0.09           N  
ATOM    127  CA  PHE A   8       0.291   4.978   5.175  1.00  0.09           C  
ATOM    128  C   PHE A   8       1.026   5.526   3.955  1.00  0.09           C  
ATOM    129  O   PHE A   8       2.230   5.336   3.815  1.00  0.12           O  
ATOM    130  CB  PHE A   8       0.840   5.511   6.505  1.00  0.12           C  
ATOM    131  CG  PHE A   8       1.140   6.998   6.563  1.00  0.13           C  
ATOM    132  CD1 PHE A   8       0.174   7.942   6.164  1.00  1.79           C  
ATOM    133  CD2 PHE A   8       2.384   7.442   7.049  1.00  1.89           C  
ATOM    134  CE1 PHE A   8       0.464   9.317   6.235  1.00  1.74           C  
ATOM    135  CE2 PHE A   8       2.669   8.816   7.126  1.00  1.94           C  
ATOM    136  CZ  PHE A   8       1.710   9.754   6.711  1.00  0.26           C  
ATOM    137  H   PHE A   8       1.259   3.171   4.640  1.00  0.09           H  
ATOM    138  HA  PHE A   8      -0.774   5.200   5.114  1.00  0.10           H  
ATOM    139  HB2 PHE A   8       0.113   5.284   7.286  1.00  0.15           H  
ATOM    140  HB3 PHE A   8       1.740   4.941   6.743  1.00  0.16           H  
ATOM    141  HD1 PHE A   8      -0.791   7.619   5.806  1.00  3.23           H  
ATOM    142  HD2 PHE A   8       3.129   6.727   7.369  1.00  3.28           H  
ATOM    143  HE1 PHE A   8      -0.253  10.058   5.914  1.00  3.11           H  
ATOM    144  HE2 PHE A   8       3.625   9.154   7.497  1.00  3.37           H  
ATOM    145  HZ  PHE A   8       1.924  10.813   6.750  1.00  0.32           H  
ATOM    146  N   HIS A   9       0.269   6.130   3.043  1.00  0.10           N  
ATOM    147  CA  HIS A   9       0.744   6.831   1.861  1.00  0.11           C  
ATOM    148  C   HIS A   9      -0.308   7.913   1.635  1.00  0.12           C  
ATOM    149  O   HIS A   9      -1.021   7.919   0.630  1.00  0.26           O  
ATOM    150  CB  HIS A   9       0.874   5.870   0.676  1.00  0.18           C  
ATOM    151  CG  HIS A   9       1.363   6.499  -0.601  1.00  0.20           C  
ATOM    152  ND1 HIS A   9       0.562   7.104  -1.540  1.00  1.68           N  
ATOM    153  CD2 HIS A   9       2.646   6.509  -1.077  1.00  1.55           C  
ATOM    154  CE1 HIS A   9       1.342   7.443  -2.581  1.00  1.17           C  
ATOM    155  NE2 HIS A   9       2.616   7.085  -2.350  1.00  0.84           N  
ATOM    156  H   HIS A   9      -0.719   6.238   3.221  1.00  0.11           H  
ATOM    157  HA  HIS A   9       1.717   7.277   2.053  1.00  0.12           H  
ATOM    158  HB2 HIS A   9       1.560   5.068   0.946  1.00  0.21           H  
ATOM    159  HB3 HIS A   9      -0.105   5.444   0.472  1.00  0.20           H  
ATOM    160  HD1 HIS A   9      -0.416   7.329  -1.389  1.00  3.03           H  
ATOM    161  HD2 HIS A   9       3.517   6.106  -0.580  1.00  3.06           H  
ATOM    162  HE1 HIS A   9       0.998   7.948  -3.473  1.00  2.15           H  
ATOM    163  N   LEU A  10      -0.475   8.757   2.654  1.00  0.13           N  
ATOM    164  CA  LEU A  10      -1.457   9.822   2.688  1.00  0.18           C  
ATOM    165  C   LEU A  10      -0.692  11.103   2.983  1.00  0.27           C  
ATOM    166  O   LEU A  10      -1.231  12.176   2.648  1.00  1.38           O  
ATOM    167  CB  LEU A  10      -2.513   9.588   3.780  1.00  0.42           C  
ATOM    168  CG  LEU A  10      -3.473   8.429   3.495  1.00  0.63           C  
ATOM    169  CD1 LEU A  10      -4.144   7.998   4.802  1.00  0.97           C  
ATOM    170  CD2 LEU A  10      -4.548   8.854   2.494  1.00  0.84           C  
ATOM    171  OXT LEU A  10       0.402  10.967   3.575  1.00  1.41           O  
ATOM    172  H   LEU A  10       0.219   8.823   3.390  1.00  0.20           H  
ATOM    173  HA  LEU A  10      -1.935   9.890   1.715  1.00  0.20           H  
ATOM    174  HB2 LEU A  10      -2.003   9.409   4.721  1.00  0.57           H  
ATOM    175  HB3 LEU A  10      -3.091  10.506   3.898  1.00  0.42           H  
ATOM    176  HG  LEU A  10      -2.920   7.578   3.096  1.00  0.81           H  
ATOM    177 HD11 LEU A  10      -4.851   7.192   4.607  1.00  2.04           H  
ATOM    178 HD12 LEU A  10      -3.390   7.641   5.504  1.00  1.69           H  
ATOM    179 HD13 LEU A  10      -4.672   8.843   5.246  1.00  1.66           H  
ATOM    180 HD21 LEU A  10      -4.082   9.137   1.550  1.00  1.76           H  
ATOM    181 HD22 LEU A  10      -5.235   8.027   2.315  1.00  1.45           H  
ATOM    182 HD23 LEU A  10      -5.107   9.705   2.885  1.00  1.44           H  
TER     183      LEU A  10                                                      
ENDMDL                                                                          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.