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***  PLANT PROTEIN 30-APR-81 1CRN  ***

elNémo ID: 221109122551125182

Job options:

ID        	=	 221109122551125182
JOBID     	=	 PLANT PROTEIN 30-APR-81 1CRN
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    PLANT PROTEIN                           30-APR-81   1CRN              
TITLE     WATER STRUCTURE OF A HYDROPHOBIC PROTEIN AT ATOMIC RESOLUTION.        
TITLE    2 PENTAGON RINGS OF WATER MOLECULES IN CRYSTALS OF CRAMBIN             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CRAMBIN;                                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CRAMBE HISPANICA SUBSP. ABYSSINICA;             
SOURCE   3 ORGANISM_TAXID: 3721;                                                
SOURCE   4 STRAIN: SUBSP. ABYSSINICA                                            
KEYWDS    PLANT SEED PROTEIN, PLANT PROTEIN                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.A.HENDRICKSON,M.M.TEETER                                            
REVDAT   8   29-NOV-17 1CRN    1       HELIX                                    
REVDAT   7   11-JUL-12 1CRN    1       SCALE1 VERSN  HEADER                     
REVDAT   6   24-FEB-09 1CRN    1       VERSN                                    
REVDAT   5   16-APR-87 1CRN    1       HEADER                                   
REVDAT   4   04-MAR-85 1CRN    1       REMARK                                   
REVDAT   3   30-SEP-83 1CRN    1       REVDAT                                   
REVDAT   2   03-DEC-81 1CRN    1       SHEET                                    
REVDAT   1   28-JUL-81 1CRN    0                                                
JRNL        AUTH   M.M.TEETER                                                   
JRNL        TITL   WATER STRUCTURE OF A HYDROPHOBIC PROTEIN AT ATOMIC           
JRNL        TITL 2 RESOLUTION: PENTAGON RINGS OF WATER MOLECULES IN CRYSTALS OF 
JRNL        TITL 3 CRAMBIN.                                                     
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  81  6014 1984              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   16593516                                                     
JRNL        DOI    10.1073/PNAS.81.19.6014                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.A.HENDRICKSON,M.M.TEETER                                   
REMARK   1  TITL   STRUCTURE OF THE HYDROPHOBIC PROTEIN CRAMBIN DETERMINED      
REMARK   1  TITL 2 DIRECTLY FROM THE ANOMALOUS SCATTERING OF SULPHUR            
REMARK   1  REF    NATURE                        V. 290   107 1981              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.M.TEETER,W.A.HENDRICKSON                                   
REMARK   1  TITL   HIGHLY ORDERED CRYSTALS OF THE PLANT SEED PROTEIN CRAMBIN    
REMARK   1  REF    J.MOL.BIOL.                   V. 127   219 1979              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 327                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1CRN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000172485.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 32.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        9.32500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THE SECONDARY STRUCTURE SPECIFICATIONS ARE THOSE DEFINED             
REMARK 400 IN REFERENCE 1 ABOVE AND DEPEND ON PARTICULAR DEFINITIONS            
REMARK 400 THAT MAY AFFECT THE DETERMINATION OF END POINTS.  PLEASE             
REMARK 400 CONSULT THE PRIMARY REFERENCE AND EXAMINE STRUCTURAL                 
REMARK 400 DETAILS SUCH AS HYDROGEN BONDING AND CONFORMATION ANGLES             
REMARK 400 WHEN MAKING USE OF THE SPECIFICATIONS.                               
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    ARG A  10   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    TYR A  29   CB  -  CG  -  CD1 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1CRN A    1    46  UNP    P01542   CRAM_CRAAB       1     46             
SEQRES   1 A   46  THR THR CYS CYS PRO SER ILE VAL ALA ARG SER ASN PHE          
SEQRES   2 A   46  ASN VAL CYS ARG LEU PRO GLY THR PRO GLU ALA ILE CYS          
SEQRES   3 A   46  ALA THR TYR THR GLY CYS ILE ILE ILE PRO GLY ALA THR          
SEQRES   4 A   46  CYS PRO GLY ASP TYR ALA ASN                                  
HELIX    1  H1 ILE A    7  PRO A   19  13/10 CONFORMATION RES 17,19       13    
HELIX    2  H2 GLU A   23  THR A   30  1DISTORTED 3/10 AT RES 30           8    
SHEET    1  S1 2 THR A   1  CYS A   4  0                                        
SHEET    2  S1 2 CYS A  32  ILE A  35 -1                                        
SSBOND   1 CYS A    3    CYS A   40                          1555   1555  2.00  
SSBOND   2 CYS A    4    CYS A   32                          1555   1555  2.04  
SSBOND   3 CYS A   16    CYS A   26                          1555   1555  2.05  
CRYST1   40.960   18.650   22.520  90.00  90.77  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024414  0.000000  0.000328        0.00000                         
SCALE2      0.000000  0.053619  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.044409        0.00000                         
ATOM      1  N   THR A   1      17.047  14.099   3.625  1.00 13.79           N  
ATOM      2  CA  THR A   1      16.967  12.784   4.338  1.00 10.80           C  
ATOM      3  C   THR A   1      15.685  12.755   5.133  1.00  9.19           C  
ATOM      4  O   THR A   1      15.268  13.825   5.594  1.00  9.85           O  
ATOM      5  CB  THR A   1      18.170  12.703   5.337  1.00 13.02           C  
ATOM      6  OG1 THR A   1      19.334  12.829   4.463  1.00 15.06           O  
ATOM      7  CG2 THR A   1      18.150  11.546   6.304  1.00 14.23           C  
ATOM      8  N   THR A   2      15.115  11.555   5.265  1.00  7.81           N  
ATOM      9  CA  THR A   2      13.856  11.469   6.066  1.00  8.31           C  
ATOM     10  C   THR A   2      14.164  10.785   7.379  1.00  5.80           C  
ATOM     11  O   THR A   2      14.993   9.862   7.443  1.00  6.94           O  
ATOM     12  CB  THR A   2      12.732  10.711   5.261  1.00 10.32           C  
ATOM     13  OG1 THR A   2      13.308   9.439   4.926  1.00 12.81           O  
ATOM     14  CG2 THR A   2      12.484  11.442   3.895  1.00 11.90           C  
ATOM     15  N   CYS A   3      13.488  11.241   8.417  1.00  5.24           N  
ATOM     16  CA  CYS A   3      13.660  10.707   9.787  1.00  5.39           C  
ATOM     17  C   CYS A   3      12.269  10.431  10.323  1.00  4.45           C  
ATOM     18  O   CYS A   3      11.393  11.308  10.185  1.00  6.54           O  
ATOM     19  CB  CYS A   3      14.368  11.748  10.691  1.00  5.99           C  
ATOM     20  SG  CYS A   3      15.885  12.426  10.016  1.00  7.01           S  
ATOM     21  N   CYS A   4      12.019   9.272  10.928  1.00  3.90           N  
ATOM     22  CA  CYS A   4      10.646   8.991  11.408  1.00  4.24           C  
ATOM     23  C   CYS A   4      10.654   8.793  12.919  1.00  3.72           C  
ATOM     24  O   CYS A   4      11.659   8.296  13.491  1.00  5.30           O  
ATOM     25  CB  CYS A   4      10.057   7.752  10.682  1.00  4.41           C  
ATOM     26  SG  CYS A   4       9.837   8.018   8.904  1.00  4.72           S  
ATOM     27  N   PRO A   5       9.561   9.108  13.563  1.00  3.96           N  
ATOM     28  CA  PRO A   5       9.448   9.034  15.012  1.00  4.25           C  
ATOM     29  C   PRO A   5       9.288   7.670  15.606  1.00  4.96           C  
ATOM     30  O   PRO A   5       9.490   7.519  16.819  1.00  7.44           O  
ATOM     31  CB  PRO A   5       8.230   9.957  15.345  1.00  5.11           C  
ATOM     32  CG  PRO A   5       7.338   9.786  14.114  1.00  5.24           C  
ATOM     33  CD  PRO A   5       8.366   9.804  12.958  1.00  5.20           C  
ATOM     34  N   SER A   6       8.875   6.686  14.796  1.00  4.83           N  
ATOM     35  CA  SER A   6       8.673   5.314  15.279  1.00  4.45           C  
ATOM     36  C   SER A   6       8.753   4.376  14.083  1.00  4.99           C  
ATOM     37  O   SER A   6       8.726   4.858  12.923  1.00  4.61           O  
ATOM     38  CB  SER A   6       7.340   5.121  15.996  1.00  5.05           C  
ATOM     39  OG  SER A   6       6.274   5.220  15.031  1.00  6.39           O  
ATOM     40  N   ILE A   7       8.881   3.075  14.358  1.00  4.94           N  
ATOM     41  CA  ILE A   7       8.912   2.083  13.258  1.00  6.33           C  
ATOM     42  C   ILE A   7       7.581   2.090  12.506  1.00  5.32           C  
ATOM     43  O   ILE A   7       7.670   2.031  11.245  1.00  6.85           O  
ATOM     44  CB  ILE A   7       9.207   0.677  13.924  1.00  8.43           C  
ATOM     45  CG1 ILE A   7      10.714   0.702  14.312  1.00  9.78           C  
ATOM     46  CG2 ILE A   7       8.811  -0.477  12.969  1.00 11.70           C  
ATOM     47  CD1 ILE A   7      11.185  -0.516  15.142  1.00  9.92           C  
ATOM     48  N   VAL A   8       6.458   2.162  13.159  1.00  5.02           N  
ATOM     49  CA  VAL A   8       5.145   2.209  12.453  1.00  6.93           C  
ATOM     50  C   VAL A   8       5.115   3.379  11.461  1.00  5.39           C  
ATOM     51  O   VAL A   8       4.664   3.268  10.343  1.00  6.30           O  
ATOM     52  CB  VAL A   8       3.995   2.354  13.478  1.00  9.64           C  
ATOM     53  CG1 VAL A   8       2.716   2.891  12.869  1.00 13.85           C  
ATOM     54  CG2 VAL A   8       3.758   1.032  14.208  1.00 11.97           C  
ATOM     55  N   ALA A   9       5.606   4.546  11.941  1.00  3.73           N  
ATOM     56  CA  ALA A   9       5.598   5.767  11.082  1.00  3.56           C  
ATOM     57  C   ALA A   9       6.441   5.527   9.850  1.00  4.13           C  
ATOM     58  O   ALA A   9       6.052   5.933   8.744  1.00  4.36           O  
ATOM     59  CB  ALA A   9       6.022   6.977  11.891  1.00  4.80           C  
ATOM     60  N   ARG A  10       7.647   4.909  10.005  1.00  3.73           N  
ATOM     61  CA  ARG A  10       8.496   4.609   8.837  1.00  3.38           C  
ATOM     62  C   ARG A  10       7.798   3.609   7.876  1.00  3.47           C  
ATOM     63  O   ARG A  10       7.878   3.778   6.651  1.00  4.67           O  
ATOM     64  CB  ARG A  10       9.847   4.020   9.305  1.00  3.95           C  
ATOM     65  CG  ARG A  10      10.752   3.607   8.149  1.00  4.55           C  
ATOM     66  CD  ARG A  10      11.226   4.699   7.244  1.00  5.89           C  
ATOM     67  NE  ARG A  10      12.143   5.571   8.035  1.00  6.20           N  
ATOM     68  CZ  ARG A  10      12.758   6.609   7.443  1.00  7.52           C  
ATOM     69  NH1 ARG A  10      12.539   6.932   6.158  1.00 10.68           N  
ATOM     70  NH2 ARG A  10      13.601   7.322   8.202  1.00  9.48           N  
ATOM     71  N   SER A  11       7.186   2.582   8.445  1.00  5.19           N  
ATOM     72  CA  SER A  11       6.500   1.584   7.565  1.00  4.60           C  
ATOM     73  C   SER A  11       5.382   2.313   6.773  1.00  4.84           C  
ATOM     74  O   SER A  11       5.213   2.016   5.557  1.00  5.84           O  
ATOM     75  CB  SER A  11       5.908   0.462   8.400  1.00  5.91           C  
ATOM     76  OG  SER A  11       6.990  -0.272   9.012  1.00  8.38           O  
ATOM     77  N   ASN A  12       4.648   3.182   7.446  1.00  3.54           N  
ATOM     78  CA  ASN A  12       3.545   3.935   6.751  1.00  4.57           C  
ATOM     79  C   ASN A  12       4.107   4.851   5.691  1.00  4.14           C  
ATOM     80  O   ASN A  12       3.536   5.001   4.617  1.00  5.52           O  
ATOM     81  CB  ASN A  12       2.663   4.677   7.748  1.00  6.42           C  
ATOM     82  CG  ASN A  12       1.802   3.735   8.610  1.00  8.25           C  
ATOM     83  OD1 ASN A  12       1.567   2.613   8.165  1.00 12.72           O  
ATOM     84  ND2 ASN A  12       1.394   4.252   9.767  1.00  9.92           N  
ATOM     85  N   PHE A  13       5.259   5.498   6.005  1.00  3.43           N  
ATOM     86  CA  PHE A  13       5.929   6.358   5.055  1.00  3.49           C  
ATOM     87  C   PHE A  13       6.304   5.578   3.799  1.00  3.40           C  
ATOM     88  O   PHE A  13       6.136   6.072   2.653  1.00  4.07           O  
ATOM     89  CB  PHE A  13       7.183   6.994   5.754  1.00  5.48           C  
ATOM     90  CG  PHE A  13       7.884   8.006   4.883  1.00  5.57           C  
ATOM     91  CD1 PHE A  13       8.906   7.586   4.027  1.00  6.99           C  
ATOM     92  CD2 PHE A  13       7.532   9.373   4.983  1.00  6.52           C  
ATOM     93  CE1 PHE A  13       9.560   8.539   3.194  1.00  8.20           C  
ATOM     94  CE2 PHE A  13       8.176  10.281   4.145  1.00  6.34           C  
ATOM     95  CZ  PHE A  13       9.141   9.845   3.292  1.00  6.84           C  
ATOM     96  N   ASN A  14       6.900   4.390   3.989  1.00  3.64           N  
ATOM     97  CA  ASN A  14       7.331   3.607   2.791  1.00  4.31           C  
ATOM     98  C   ASN A  14       6.116   3.210   1.915  1.00  3.98           C  
ATOM     99  O   ASN A  14       6.240   3.144   0.684  1.00  6.22           O  
ATOM    100  CB  ASN A  14       8.145   2.404   3.240  1.00  5.81           C  
ATOM    101  CG  ASN A  14       9.555   2.856   3.730  1.00  6.82           C  
ATOM    102  OD1 ASN A  14      10.013   3.895   3.323  1.00  9.43           O  
ATOM    103  ND2 ASN A  14      10.120   1.956   4.539  1.00  8.21           N  
ATOM    104  N   VAL A  15       4.993   2.927   2.571  1.00  3.76           N  
ATOM    105  CA  VAL A  15       3.782   2.599   1.742  1.00  3.98           C  
ATOM    106  C   VAL A  15       3.296   3.871   1.004  1.00  3.80           C  
ATOM    107  O   VAL A  15       2.947   3.817  -0.189  1.00  4.85           O  
ATOM    108  CB  VAL A  15       2.698   1.953   2.608  1.00  4.71           C  
ATOM    109  CG1 VAL A  15       1.384   1.826   1.806  1.00  6.67           C  
ATOM    110  CG2 VAL A  15       3.174   0.533   3.005  1.00  6.26           C  
ATOM    111  N   CYS A  16       3.321   4.987   1.720  1.00  3.79           N  
ATOM    112  CA  CYS A  16       2.890   6.285   1.126  1.00  3.54           C  
ATOM    113  C   CYS A  16       3.687   6.597  -0.111  1.00  3.48           C  
ATOM    114  O   CYS A  16       3.200   7.147  -1.103  1.00  4.63           O  
ATOM    115  CB  CYS A  16       3.039   7.369   2.240  1.00  4.58           C  
ATOM    116  SG  CYS A  16       2.559   9.014   1.649  1.00  5.66           S  
ATOM    117  N   ARG A  17       4.997   6.227  -0.100  1.00  3.99           N  
ATOM    118  CA  ARG A  17       5.895   6.489  -1.213  1.00  3.83           C  
ATOM    119  C   ARG A  17       5.738   5.560  -2.409  1.00  3.79           C  
ATOM    120  O   ARG A  17       6.228   5.901  -3.507  1.00  5.39           O  
ATOM    121  CB  ARG A  17       7.370   6.507  -0.731  1.00  4.11           C  
ATOM    122  CG  ARG A  17       7.717   7.687   0.206  1.00  4.69           C  
ATOM    123  CD  ARG A  17       7.949   8.947  -0.615  1.00  5.10           C  
ATOM    124  NE  ARG A  17       9.212   8.856  -1.337  1.00  4.71           N  
ATOM    125  CZ  ARG A  17       9.537   9.533  -2.431  1.00  5.28           C  
ATOM    126  NH1 ARG A  17       8.659  10.350  -3.032  1.00  6.67           N  
ATOM    127  NH2 ARG A  17      10.793   9.491  -2.899  1.00  6.41           N  
ATOM    128  N   LEU A  18       5.051   4.411  -2.204  1.00  4.70           N  
ATOM    129  CA  LEU A  18       4.933   3.431  -3.326  1.00  5.46           C  
ATOM    130  C   LEU A  18       4.397   4.014  -4.620  1.00  5.13           C  
ATOM    131  O   LEU A  18       4.988   3.755  -5.687  1.00  5.55           O  
ATOM    132  CB  LEU A  18       4.196   2.184  -2.863  1.00  6.47           C  
ATOM    133  CG  LEU A  18       4.960   1.178  -1.991  1.00  7.43           C  
ATOM    134  CD1 LEU A  18       3.907   0.097  -1.634  1.00  8.70           C  
ATOM    135  CD2 LEU A  18       6.129   0.606  -2.768  1.00  9.39           C  
ATOM    136  N   PRO A  19       3.329   4.795  -4.543  1.00  4.28           N  
ATOM    137  CA  PRO A  19       2.792   5.376  -5.797  1.00  5.38           C  
ATOM    138  C   PRO A  19       3.573   6.540  -6.322  1.00  6.30           C  
ATOM    139  O   PRO A  19       3.260   7.045  -7.422  1.00  9.62           O  
ATOM    140  CB  PRO A  19       1.358   5.766  -5.472  1.00  5.87           C  
ATOM    141  CG  PRO A  19       1.223   5.694  -3.993  1.00  6.47           C  
ATOM    142  CD  PRO A  19       2.421   4.941  -3.408  1.00  6.45           C  
ATOM    143  N   GLY A  20       4.565   7.047  -5.559  1.00  4.94           N  
ATOM    144  CA  GLY A  20       5.366   8.191  -6.018  1.00  5.39           C  
ATOM    145  C   GLY A  20       5.007   9.481  -5.280  1.00  5.03           C  
ATOM    146  O   GLY A  20       5.535  10.510  -5.730  1.00  7.34           O  
ATOM    147  N   THR A  21       4.181   9.438  -4.262  1.00  4.10           N  
ATOM    148  CA  THR A  21       3.767  10.609  -3.513  1.00  3.94           C  
ATOM    149  C   THR A  21       5.017  11.397  -3.042  1.00  3.96           C  
ATOM    150  O   THR A  21       5.947  10.757  -2.523  1.00  5.82           O  
ATOM    151  CB  THR A  21       2.992  10.188  -2.225  1.00  4.13           C  
ATOM    152  OG1 THR A  21       2.051   9.144  -2.623  1.00  5.45           O  
ATOM    153  CG2 THR A  21       2.260  11.349  -1.551  1.00  5.41           C  
ATOM    154  N   PRO A  22       4.971  12.703  -3.176  1.00  5.04           N  
ATOM    155  CA  PRO A  22       6.143  13.513  -2.696  1.00  4.69           C  
ATOM    156  C   PRO A  22       6.400  13.233  -1.225  1.00  4.19           C  
ATOM    157  O   PRO A  22       5.485  13.061  -0.382  1.00  4.47           O  
ATOM    158  CB  PRO A  22       5.703  14.969  -2.920  1.00  7.12           C  
ATOM    159  CG  PRO A  22       4.676  14.893  -3.996  1.00  7.03           C  
ATOM    160  CD  PRO A  22       3.964  13.567  -3.811  1.00  4.90           C  
ATOM    161  N   GLU A  23       7.728  13.297  -0.921  1.00  5.16           N  
ATOM    162  CA  GLU A  23       8.114  13.103   0.500  1.00  5.31           C  
ATOM    163  C   GLU A  23       7.427  14.073   1.410  1.00  4.11           C  
ATOM    164  O   GLU A  23       7.036  13.682   2.540  1.00  5.11           O  
ATOM    165  CB  GLU A  23       9.648  13.285   0.660  1.00  6.16           C  
ATOM    166  CG  GLU A  23      10.440  12.093   0.063  1.00  7.48           C  
ATOM    167  CD  GLU A  23      11.941  12.170   0.391  1.00  9.40           C  
ATOM    168  OE1 GLU A  23      12.416  13.225   0.681  1.00 10.40           O  
ATOM    169  OE2 GLU A  23      12.539  11.070   0.292  1.00 13.32           O  
ATOM    170  N   ALA A  24       7.212  15.334   0.966  1.00  4.56           N  
ATOM    171  CA  ALA A  24       6.614  16.317   1.913  1.00  4.49           C  
ATOM    172  C   ALA A  24       5.212  15.936   2.350  1.00  4.10           C  
ATOM    173  O   ALA A  24       4.782  16.166   3.495  1.00  5.64           O  
ATOM    174  CB  ALA A  24       6.605  17.695   1.246  1.00  5.80           C  
ATOM    175  N   ILE A  25       4.445  15.318   1.405  1.00  4.37           N  
ATOM    176  CA  ILE A  25       3.074  14.894   1.756  1.00  5.44           C  
ATOM    177  C   ILE A  25       3.085  13.643   2.645  1.00  4.32           C  
ATOM    178  O   ILE A  25       2.315  13.523   3.578  1.00  4.72           O  
ATOM    179  CB  ILE A  25       2.204  14.637   0.462  1.00  6.42           C  
ATOM    180  CG1 ILE A  25       1.815  16.048  -0.129  1.00  7.50           C  
ATOM    181  CG2 ILE A  25       0.903  13.864   0.811  1.00  7.65           C  
ATOM    182  CD1 ILE A  25       0.756  16.761   0.757  1.00  7.80           C  
ATOM    183  N   CYS A  26       4.032  12.764   2.313  1.00  3.92           N  
ATOM    184  CA  CYS A  26       4.180  11.549   3.187  1.00  4.37           C  
ATOM    185  C   CYS A  26       4.632  11.944   4.596  1.00  3.95           C  
ATOM    186  O   CYS A  26       4.227  11.252   5.547  1.00  4.74           O  
ATOM    187  CB  CYS A  26       5.038  10.518   2.539  1.00  4.63           C  
ATOM    188  SG  CYS A  26       4.349   9.794   1.022  1.00  5.61           S  
ATOM    189  N   ALA A  27       5.408  13.012   4.694  1.00  3.89           N  
ATOM    190  CA  ALA A  27       5.879  13.502   6.026  1.00  4.43           C  
ATOM    191  C   ALA A  27       4.696  13.908   6.882  1.00  4.26           C  
ATOM    192  O   ALA A  27       4.528  13.422   8.025  1.00  5.44           O  
ATOM    193  CB  ALA A  27       6.880  14.615   5.830  1.00  5.36           C  
ATOM    194  N   THR A  28       3.827  14.802   6.358  1.00  4.53           N  
ATOM    195  CA  THR A  28       2.691  15.221   7.194  1.00  5.08           C  
ATOM    196  C   THR A  28       1.672  14.132   7.434  1.00  4.62           C  
ATOM    197  O   THR A  28       0.947  14.112   8.468  1.00  7.80           O  
ATOM    198  CB  THR A  28       1.986  16.520   6.614  1.00  6.03           C  
ATOM    199  OG1 THR A  28       1.664  16.221   5.230  1.00  7.19           O  
ATOM    200  CG2 THR A  28       2.914  17.739   6.700  1.00  7.34           C  
ATOM    201  N   TYR A  29       1.621  13.190   6.511  1.00  5.01           N  
ATOM    202  CA  TYR A  29       0.715  12.045   6.657  1.00  6.60           C  
ATOM    203  C   TYR A  29       1.125  11.125   7.815  1.00  4.92           C  
ATOM    204  O   TYR A  29       0.286  10.632   8.545  1.00  7.13           O  
ATOM    205  CB  TYR A  29       0.755  11.229   5.322  1.00  9.66           C  
ATOM    206  CG  TYR A  29      -0.203  10.044   5.354  1.00 11.56           C  
ATOM    207  CD1 TYR A  29      -1.547  10.337   5.645  1.00 12.85           C  
ATOM    208  CD2 TYR A  29       0.193   8.750   5.100  1.00 14.44           C  
ATOM    209  CE1 TYR A  29      -2.496   9.329   5.673  1.00 16.61           C  
ATOM    210  CE2 TYR A  29      -0.801   7.705   5.156  1.00 17.11           C  
ATOM    211  CZ  TYR A  29      -2.079   8.031   5.430  1.00 19.99           C  
ATOM    212  OH  TYR A  29      -3.097   7.057   5.458  1.00 28.98           O  
ATOM    213  N   THR A  30       2.470  10.984   7.995  1.00  5.31           N  
ATOM    214  CA  THR A  30       2.986   9.994   8.950  1.00  5.70           C  
ATOM    215  C   THR A  30       3.609  10.505  10.230  1.00  6.28           C  
ATOM    216  O   THR A  30       3.766   9.715  11.186  1.00  8.77           O  
ATOM    217  CB  THR A  30       4.076   9.103   8.225  1.00  6.55           C  
ATOM    218  OG1 THR A  30       5.125  10.027   7.824  1.00  6.57           O  
ATOM    219  CG2 THR A  30       3.493   8.324   7.035  1.00  7.29           C  
ATOM    220  N   GLY A  31       3.984  11.764  10.241  1.00  4.99           N  
ATOM    221  CA  GLY A  31       4.769  12.336  11.360  1.00  5.50           C  
ATOM    222  C   GLY A  31       6.255  12.243  11.106  1.00  4.19           C  
ATOM    223  O   GLY A  31       7.037  12.750  11.954  1.00  6.12           O  
ATOM    224  N   CYS A  32       6.710  11.631   9.992  1.00  4.30           N  
ATOM    225  CA  CYS A  32       8.140  11.694   9.635  1.00  4.89           C  
ATOM    226  C   CYS A  32       8.500  13.141   9.206  1.00  5.50           C  
ATOM    227  O   CYS A  32       7.581  13.949   8.944  1.00  5.82           O  
ATOM    228  CB  CYS A  32       8.504  10.686   8.530  1.00  4.66           C  
ATOM    229  SG  CYS A  32       8.048   8.987   8.881  1.00  5.33           S  
ATOM    230  N   ILE A  33       9.793  13.410   9.173  1.00  6.02           N  
ATOM    231  CA  ILE A  33      10.280  14.760   8.823  1.00  5.24           C  
ATOM    232  C   ILE A  33      11.346  14.658   7.743  1.00  5.16           C  
ATOM    233  O   ILE A  33      11.971  13.583   7.552  1.00  7.19           O  
ATOM    234  CB  ILE A  33      10.790  15.535  10.085  1.00  5.49           C  
ATOM    235  CG1 ILE A  33      12.059  14.803  10.671  1.00  6.85           C  
ATOM    236  CG2 ILE A  33       9.684  15.686  11.138  1.00  6.45           C  
ATOM    237  CD1 ILE A  33      12.733  15.676  11.781  1.00  8.94           C  
ATOM    238  N   ILE A  34      11.490  15.773   7.038  1.00  5.52           N  
ATOM    239  CA  ILE A  34      12.552  15.877   6.036  1.00  6.82           C  
ATOM    240  C   ILE A  34      13.590  16.917   6.560  1.00  6.92           C  
ATOM    241  O   ILE A  34      13.168  18.006   6.945  1.00  9.22           O  
ATOM    242  CB  ILE A  34      11.987  16.360   4.681  1.00  8.11           C  
ATOM    243  CG1 ILE A  34      10.914  15.338   4.163  1.00  9.59           C  
ATOM    244  CG2 ILE A  34      13.131  16.517   3.629  1.00  9.73           C  
ATOM    245  CD1 ILE A  34      10.151  16.024   2.938  1.00 13.41           C  
ATOM    246  N   ILE A  35      14.856  16.493   6.536  1.00  7.06           N  
ATOM    247  CA  ILE A  35      15.930  17.454   6.941  1.00  7.52           C  
ATOM    248  C   ILE A  35      16.913  17.550   5.819  1.00  6.63           C  
ATOM    249  O   ILE A  35      17.097  16.660   4.970  1.00  7.90           O  
ATOM    250  CB  ILE A  35      16.622  16.995   8.285  1.00  8.07           C  
ATOM    251  CG1 ILE A  35      17.360  15.651   8.067  1.00  9.41           C  
ATOM    252  CG2 ILE A  35      15.592  16.974   9.434  1.00  9.46           C  
ATOM    253  CD1 ILE A  35      18.298  15.206   9.219  1.00  9.85           C  
ATOM    254  N   PRO A  36      17.664  18.669   5.806  1.00  8.07           N  
ATOM    255  CA  PRO A  36      18.635  18.861   4.738  1.00  8.78           C  
ATOM    256  C   PRO A  36      19.925  18.042   4.949  1.00  8.31           C  
ATOM    257  O   PRO A  36      20.593  17.742   3.945  1.00  9.09           O  
ATOM    258  CB  PRO A  36      18.945  20.364   4.783  1.00  9.67           C  
ATOM    259  CG  PRO A  36      18.238  20.937   5.908  1.00 10.15           C  
ATOM    260  CD  PRO A  36      17.371  19.900   6.596  1.00  9.53           C  
ATOM    261  N   GLY A  37      20.172  17.730   6.217  1.00  8.48           N  
ATOM    262  CA  GLY A  37      21.452  16.969   6.513  1.00  9.20           C  
ATOM    263  C   GLY A  37      21.143  15.478   6.427  1.00 10.41           C  
ATOM    264  O   GLY A  37      20.138  15.023   5.878  1.00 12.06           O  
ATOM    265  N   ALA A  38      22.055  14.701   7.032  1.00  9.24           N  
ATOM    266  CA  ALA A  38      22.019  13.242   7.020  1.00  9.24           C  
ATOM    267  C   ALA A  38      21.944  12.628   8.396  1.00  9.60           C  
ATOM    268  O   ALA A  38      21.869  11.387   8.435  1.00 13.65           O  
ATOM    269  CB  ALA A  38      23.246  12.697   6.275  1.00 10.43           C  
ATOM    270  N   THR A  39      21.894  13.435   9.436  1.00  8.70           N  
ATOM    271  CA  THR A  39      21.936  12.911  10.809  1.00  9.46           C  
ATOM    272  C   THR A  39      20.615  13.191  11.521  1.00  8.32           C  
ATOM    273  O   THR A  39      20.357  14.317  11.948  1.00  9.89           O  
ATOM    274  CB  THR A  39      23.131  13.601  11.593  1.00 10.72           C  
ATOM    275  OG1 THR A  39      24.284  13.401  10.709  1.00 11.66           O  
ATOM    276  CG2 THR A  39      23.340  12.935  12.962  1.00 11.81           C  
ATOM    277  N   CYS A  40      19.827  12.110  11.642  1.00  7.64           N  
ATOM    278  CA  CYS A  40      18.504  12.312  12.298  1.00  8.05           C  
ATOM    279  C   CYS A  40      18.684  12.451  13.784  1.00  7.63           C  
ATOM    280  O   CYS A  40      19.533  11.718  14.362  1.00  9.64           O  
ATOM    281  CB  CYS A  40      17.582  11.117  11.996  1.00  7.80           C  
ATOM    282  SG  CYS A  40      17.199  10.929  10.237  1.00  7.30           S  
ATOM    283  N   PRO A  41      17.880  13.266  14.426  1.00  8.00           N  
ATOM    284  CA  PRO A  41      17.924  13.421  15.877  1.00  8.96           C  
ATOM    285  C   PRO A  41      17.392  12.206  16.594  1.00  9.06           C  
ATOM    286  O   PRO A  41      16.652  11.368  16.033  1.00  8.82           O  
ATOM    287  CB  PRO A  41      17.076  14.658  16.145  1.00 10.39           C  
ATOM    288  CG  PRO A  41      16.098  14.689  14.997  1.00 10.99           C  
ATOM    289  CD  PRO A  41      16.859  14.150  13.779  1.00 10.49           C  
ATOM    290  N   GLY A  42      17.728  12.124  17.884  1.00  7.55           N  
ATOM    291  CA  GLY A  42      17.334  10.956  18.691  1.00  8.00           C  
ATOM    292  C   GLY A  42      15.875  10.688  18.871  1.00  7.22           C  
ATOM    293  O   GLY A  42      15.434   9.550  19.166  1.00  8.41           O  
ATOM    294  N   ASP A  43      15.036  11.747  18.715  1.00  5.54           N  
ATOM    295  CA  ASP A  43      13.564  11.573  18.836  1.00  5.85           C  
ATOM    296  C   ASP A  43      12.936  11.227  17.470  1.00  5.87           C  
ATOM    297  O   ASP A  43      11.720  11.040  17.428  1.00  7.29           O  
ATOM    298  CB  ASP A  43      12.933  12.737  19.580  1.00  6.72           C  
ATOM    299  CG  ASP A  43      13.140  14.094  18.958  1.00  8.59           C  
ATOM    300  OD1 ASP A  43      14.109  14.303  18.212  1.00  9.59           O  
ATOM    301  OD2 ASP A  43      12.267  14.963  19.265  1.00 11.45           O  
ATOM    302  N   TYR A  44      13.725  11.174  16.425  1.00  5.22           N  
ATOM    303  CA  TYR A  44      13.257  10.745  15.081  1.00  5.56           C  
ATOM    304  C   TYR A  44      14.275   9.687  14.612  1.00  4.61           C  
ATOM    305  O   TYR A  44      14.930   9.862  13.568  1.00  6.04           O  
ATOM    306  CB  TYR A  44      13.200  11.914  14.071  1.00  5.41           C  
ATOM    307  CG  TYR A  44      12.000  12.819  14.399  1.00  5.34           C  
ATOM    308  CD1 TYR A  44      12.119  13.853  15.332  1.00  6.59           C  
ATOM    309  CD2 TYR A  44      10.775  12.617  13.762  1.00  5.94           C  
ATOM    310  CE1 TYR A  44      11.045  14.675  15.610  1.00  5.97           C  
ATOM    311  CE2 TYR A  44       9.676  13.433  14.048  1.00  5.17           C  
ATOM    312  CZ  TYR A  44       9.802  14.456  14.996  1.00  5.96           C  
ATOM    313  OH  TYR A  44       8.740  15.265  15.269  1.00  8.60           O  
ATOM    314  N   ALA A  45      14.342   8.640  15.422  1.00  4.76           N  
ATOM    315  CA  ALA A  45      15.445   7.667  15.246  1.00  5.89           C  
ATOM    316  C   ALA A  45      15.171   6.533  14.280  1.00  6.67           C  
ATOM    317  O   ALA A  45      16.093   5.705  14.039  1.00  7.56           O  
ATOM    318  CB  ALA A  45      15.680   7.099  16.682  1.00  6.82           C  
ATOM    319  N   ASN A  46      13.966   6.502  13.739  1.00  5.80           N  
ATOM    320  CA  ASN A  46      13.512   5.395  12.878  1.00  6.15           C  
ATOM    321  C   ASN A  46      13.311   5.853  11.455  1.00  6.61           C  
ATOM    322  O   ASN A  46      13.733   6.929  11.026  1.00  7.18           O  
ATOM    323  CB  ASN A  46      12.266   4.769  13.501  1.00  7.27           C  
ATOM    324  CG  ASN A  46      12.538   4.304  14.922  1.00  7.98           C  
ATOM    325  OD1 ASN A  46      11.982   4.849  15.886  1.00 11.00           O  
ATOM    326  ND2 ASN A  46      13.407   3.298  15.015  1.00 10.32           N  
ATOM    327  OXT ASN A  46      12.703   4.973  10.746  1.00  7.86           O  
TER     328      ASN A  46                                                      
CONECT   20  282                                                                
CONECT   26  229                                                                
CONECT  116  188                                                                
CONECT  188  116                                                                
CONECT  229   26                                                                
CONECT  282   20                                                                
MASTER      225    0    0    2    2    0    0    6  327    1    6    4          
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.