HEADER    METAL BINDING PROTEIN                   20-NOV-03   1V50              
TITLE     SOLUTION STRUCTURE OF PHOSPHORYLATED N-TERMINAL FRAGMENT OF S100C/A11 
TITLE    2 PROTEIN                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALGIZZARIN;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL FRAGMENT;                                       
COMPND   5 SYNONYM: S100C PROTEIN, MLN 70, S100C/A11;                           
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 OTHER_DETAILS: THE SEQUENCE OF THE PEPTIDE WAS CHEMICALLY            
SOURCE   4 SYNTHESIZED. THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN HOMO  
SOURCE   5 SAPIENS (HUMAN)                                                      
KEYWDS    ALPHA-HELIX, METAL BINDING PROTEIN                                    
EXPDTA    SOLUTION NMR                                                          
MDLTYP    MINIMIZED AVERAGE                                                     
AUTHOR    T.KOUNO,M.MIZUGUCHI,M.SAKAGUCHI,E.MAKINO,N.HUH,K.KAWANO               
REVDAT   4   27-DEC-23 1V50    1       REMARK                                   
REVDAT   3   02-MAR-22 1V50    1       REMARK SEQADV LINK                       
REVDAT   2   24-FEB-09 1V50    1       VERSN                                    
REVDAT   1   22-MAR-05 1V50    0                                                
JRNL        AUTH   T.KOUNO,M.MIZUGUCHI,M.SAKAGUCHI,E.MAKINO,N.HUH,K.KAWANO      
JRNL        TITL   STUDY ON STRUCTURE-ACTIVITY RELATIONSHIP BETWEEN THE         
JRNL        TITL 2 N-TERMINAL REGION OF S100C PROTEIN AND ITS FUNCTION          
JRNL        REF    PEPTIDE SCIENCE               V.  40   319 2003              
JRNL        REFN                   ISSN 1344-7661                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : NMRPIPE 2.2, X-PLOR 3.1                              
REMARK   3   AUTHORS     : DELAGLIO (NMRPIPE), BRUNGER (X-PLOR)                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1V50 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-NOV-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000006213.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 293                                
REMARK 210  PH                             : 7.0                                
REMARK 210  IONIC STRENGTH                 : 0.12                               
REMARK 210  PRESSURE                       : 1 ATM                              
REMARK 210  SAMPLE CONTENTS                : 2.0MM PEPTIDE, 20MM PHOSPHATE      
REMARK 210                                   BUFFER NA, 5MM DITHIOTHREITOL,     
REMARK 210                                   50% H2O, 50% TRIFLUOROETHANOL-D3;  
REMARK 210                                   2.0MM PEPTIDE, 20MM PHOSPHATE      
REMARK 210                                   BUFFER NA, 5MM DITHIOTHREITOL,     
REMARK 210                                   50% D2O, 50% TRIFLUOROETHANOL-D3   
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D NOESY                           
REMARK 210  SPECTROMETER FIELD STRENGTH    : 500 MHZ                            
REMARK 210  SPECTROMETER MODEL             : DMX                                
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : PIPP 4.3.2                         
REMARK 210   METHOD USED                   : DISTANCE GEOMETRY, SIMULATED       
REMARK 210                                   ANNEALING                          
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : NULL                               
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : NULL                               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;                   
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                            
REMARK 465     RES C SSSEQI                                                     
REMARK 465     MET A    -1                                                      
REMARK 465     ALA A     0                                                      
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    SER A   3      -63.11     71.19                                   
REMARK 500    SER A   4       89.87     59.17                                   
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    ARG A  10         0.32    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1V4Z   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN                                                     
DBREF  1V50 A   -1    17  UNP    P31949   S10AB_HUMAN      1     19             
SEQADV 1V50 TPO A    8  UNP  P31949    THR    10 MODIFIED RESIDUE               
SEQRES   1 A   19  MET ALA LYS ILE SER SER PRO THR GLU TPO GLU ARG CYS          
SEQRES   2 A   19  ILE GLU SER LEU ILE ALA                                      
MODRES 1V50 TPO A    8  THR  PHOSPHOTHREONINE                                   
HET    TPO  A   8      17                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    C4 H10 N O6 P                                                
HELIX    1   1 GLU A    7  ALA A   17  1                                  11    
LINK         C   GLU A   7                 N   TPO A   8     1555   1555  1.32  
LINK         C   TPO A   8                 N   GLU A   9     1555   1555  1.32  
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                         
ATOM      1  N   LYS A   1     -15.419   1.749  -4.803  1.00  4.10           N  
ATOM      2  CA  LYS A   1     -14.899   3.083  -4.357  1.00  3.69           C  
ATOM      3  C   LYS A   1     -14.506   3.048  -2.868  1.00  2.85           C  
ATOM      4  O   LYS A   1     -14.750   3.986  -2.130  1.00  3.20           O  
ATOM      5  CB  LYS A   1     -16.049   4.077  -4.602  1.00  4.42           C  
ATOM      6  CG  LYS A   1     -17.289   3.674  -3.789  1.00  5.16           C  
ATOM      7  CD  LYS A   1     -17.696   4.826  -2.865  1.00  6.00           C  
ATOM      8  CE  LYS A   1     -19.213   4.800  -2.651  1.00  6.70           C  
ATOM      9  NZ  LYS A   1     -19.455   5.669  -1.463  1.00  7.47           N  
ATOM     10  H   LYS A   1     -14.622   1.102  -4.963  1.00  4.40           H  
ATOM     11  HA  LYS A   1     -14.046   3.363  -4.956  1.00  4.10           H  
ATOM     12  HB2 LYS A   1     -15.732   5.066  -4.306  1.00  4.66           H  
ATOM     13  HB3 LYS A   1     -16.298   4.082  -5.652  1.00  4.66           H  
ATOM     14  HG2 LYS A   1     -18.102   3.450  -4.464  1.00  5.35           H  
ATOM     15  HG3 LYS A   1     -17.065   2.802  -3.194  1.00  5.30           H  
ATOM     16  HD2 LYS A   1     -17.195   4.717  -1.914  1.00  6.23           H  
ATOM     17  HD3 LYS A   1     -17.414   5.766  -3.315  1.00  6.23           H  
ATOM     18  HE2 LYS A   1     -19.720   5.197  -3.520  1.00  6.88           H  
ATOM     19  HE3 LYS A   1     -19.546   3.794  -2.447  1.00  6.79           H  
ATOM     20  HZ1 LYS A   1     -19.087   6.623  -1.648  1.00  7.72           H  
ATOM     21  HZ2 LYS A   1     -18.974   5.265  -0.633  1.00  7.77           H  
ATOM     22  HZ3 LYS A   1     -20.477   5.724  -1.278  1.00  7.74           H  
ATOM     23  N   ILE A   2     -13.894   1.973  -2.425  1.00  2.47           N  
ATOM     24  CA  ILE A   2     -13.480   1.856  -1.010  1.00  2.59           C  
ATOM     25  C   ILE A   2     -12.317   2.803  -0.683  1.00  2.44           C  
ATOM     26  O   ILE A   2     -12.109   3.164   0.460  1.00  3.17           O  
ATOM     27  CB  ILE A   2     -13.060   0.391  -0.905  1.00  3.42           C  
ATOM     28  CG1 ILE A   2     -12.989  -0.009   0.543  1.00  4.14           C  
ATOM     29  CG2 ILE A   2     -11.682   0.175  -1.549  1.00  4.27           C  
ATOM     30  CD1 ILE A   2     -14.399  -0.211   1.105  1.00  5.01           C  
ATOM     31  H   ILE A   2     -13.701   1.229  -3.022  1.00  2.79           H  
ATOM     32  HA  ILE A   2     -14.306   2.048  -0.364  1.00  3.09           H  
ATOM     33  HB  ILE A   2     -13.787  -0.226  -1.409  1.00  3.55           H  
ATOM     34 HG12 ILE A   2     -12.440  -0.922   0.602  1.00  4.66           H  
ATOM     35 HG13 ILE A   2     -12.485   0.762   1.095  1.00  4.00           H  
ATOM     36 HG21 ILE A   2     -10.922   0.641  -0.939  1.00  4.74           H  
ATOM     37 HG22 ILE A   2     -11.668   0.613  -2.536  1.00  4.61           H  
ATOM     38 HG23 ILE A   2     -11.482  -0.884  -1.624  1.00  4.54           H  
ATOM     39 HD11 ILE A   2     -14.987  -0.786   0.404  1.00  5.45           H  
ATOM     40 HD12 ILE A   2     -14.865   0.750   1.263  1.00  5.32           H  
ATOM     41 HD13 ILE A   2     -14.339  -0.741   2.044  1.00  5.29           H  
ATOM     42  N   SER A   3     -11.571   3.190  -1.688  1.00  2.29           N  
ATOM     43  CA  SER A   3     -10.395   4.113  -1.509  1.00  3.00           C  
ATOM     44  C   SER A   3      -9.238   3.392  -0.798  1.00  2.65           C  
ATOM     45  O   SER A   3      -8.175   3.225  -1.365  1.00  3.35           O  
ATOM     46  CB  SER A   3     -10.898   5.302  -0.681  1.00  3.80           C  
ATOM     47  OG  SER A   3     -10.628   6.508  -1.383  1.00  4.16           O  
ATOM     48  H   SER A   3     -11.788   2.861  -2.579  1.00  2.30           H  
ATOM     49  HA  SER A   3     -10.063   4.465  -2.470  1.00  3.69           H  
ATOM     50  HB2 SER A   3     -11.960   5.215  -0.524  1.00  4.36           H  
ATOM     51  HB3 SER A   3     -10.394   5.310   0.273  1.00  4.09           H  
ATOM     52  HG  SER A   3     -10.937   7.240  -0.845  1.00  4.59           H  
ATOM     53  N   SER A   4      -9.440   2.965   0.433  1.00  2.03           N  
ATOM     54  CA  SER A   4      -8.365   2.250   1.199  1.00  2.09           C  
ATOM     55  C   SER A   4      -7.114   3.137   1.342  1.00  1.62           C  
ATOM     56  O   SER A   4      -6.226   3.099   0.509  1.00  1.93           O  
ATOM     57  CB  SER A   4      -8.055   0.983   0.393  1.00  3.00           C  
ATOM     58  OG  SER A   4      -7.487   0.007   1.256  1.00  3.69           O  
ATOM     59  H   SER A   4     -10.309   3.116   0.858  1.00  2.03           H  
ATOM     60  HA  SER A   4      -8.733   1.975   2.175  1.00  2.49           H  
ATOM     61  HB2 SER A   4      -8.964   0.593  -0.033  1.00  3.46           H  
ATOM     62  HB3 SER A   4      -7.361   1.222  -0.402  1.00  3.26           H  
ATOM     63  HG  SER A   4      -7.129  -0.698   0.712  1.00  4.21           H  
ATOM     64  N   PRO A   5      -7.084   3.908   2.409  1.00  1.90           N  
ATOM     65  CA  PRO A   5      -5.932   4.813   2.674  1.00  2.41           C  
ATOM     66  C   PRO A   5      -4.737   4.054   3.293  1.00  2.37           C  
ATOM     67  O   PRO A   5      -3.915   4.640   3.973  1.00  3.03           O  
ATOM     68  CB  PRO A   5      -6.499   5.815   3.676  1.00  3.44           C  
ATOM     69  CG  PRO A   5      -7.616   5.097   4.370  1.00  3.55           C  
ATOM     70  CD  PRO A   5      -8.116   4.013   3.449  1.00  2.69           C  
ATOM     71  HA  PRO A   5      -5.633   5.325   1.774  1.00  2.67           H  
ATOM     72  HB2 PRO A   5      -5.738   6.105   4.387  1.00  3.95           H  
ATOM     73  HB3 PRO A   5      -6.883   6.682   3.162  1.00  3.89           H  
ATOM     74  HG2 PRO A   5      -7.251   4.658   5.288  1.00  3.87           H  
ATOM     75  HG3 PRO A   5      -8.418   5.787   4.586  1.00  4.26           H  
ATOM     76  HD2 PRO A   5      -8.212   3.079   3.985  1.00  2.97           H  
ATOM     77  HD3 PRO A   5      -9.059   4.297   3.008  1.00  2.83           H  
ATOM     78  N   THR A   6      -4.630   2.763   3.068  1.00  2.17           N  
ATOM     79  CA  THR A   6      -3.489   1.985   3.645  1.00  2.67           C  
ATOM     80  C   THR A   6      -2.231   2.166   2.779  1.00  1.95           C  
ATOM     81  O   THR A   6      -1.969   1.387   1.881  1.00  2.37           O  
ATOM     82  CB  THR A   6      -3.943   0.518   3.644  1.00  3.65           C  
ATOM     83  OG1 THR A   6      -4.722   0.245   2.483  1.00  4.01           O  
ATOM     84  CG2 THR A   6      -4.773   0.254   4.898  1.00  4.11           C  
ATOM     85  H   THR A   6      -5.296   2.306   2.521  1.00  2.14           H  
ATOM     86  HA  THR A   6      -3.301   2.301   4.660  1.00  3.30           H  
ATOM     87  HB  THR A   6      -3.076  -0.125   3.653  1.00  4.28           H  
ATOM     88  HG1 THR A   6      -4.130  -0.066   1.794  1.00  4.43           H  
ATOM     89 HG21 THR A   6      -5.818   0.424   4.682  1.00  4.44           H  
ATOM     90 HG22 THR A   6      -4.454   0.925   5.683  1.00  4.45           H  
ATOM     91 HG23 THR A   6      -4.631  -0.767   5.217  1.00  4.27           H  
ATOM     92  N   GLU A   7      -1.450   3.190   3.042  1.00  1.49           N  
ATOM     93  CA  GLU A   7      -0.207   3.423   2.236  1.00  1.78           C  
ATOM     94  C   GLU A   7       0.884   2.398   2.592  1.00  1.43           C  
ATOM     95  O   GLU A   7       1.860   2.262   1.877  1.00  1.47           O  
ATOM     96  CB  GLU A   7       0.250   4.838   2.599  1.00  2.66           C  
ATOM     97  CG  GLU A   7      -0.568   5.863   1.806  1.00  3.55           C  
ATOM     98  CD  GLU A   7      -1.069   6.962   2.745  1.00  4.51           C  
ATOM     99  OE1 GLU A   7      -2.134   6.788   3.315  1.00  4.97           O  
ATOM    100  OE2 GLU A   7      -0.380   7.961   2.878  1.00  5.12           O  
ATOM    101  H   GLU A   7      -1.681   3.807   3.768  1.00  1.66           H  
ATOM    102  HA  GLU A   7      -0.431   3.373   1.181  1.00  2.33           H  
ATOM    103  HB2 GLU A   7       0.107   5.002   3.658  1.00  2.61           H  
ATOM    104  HB3 GLU A   7       1.296   4.952   2.356  1.00  3.20           H  
ATOM    105  HG2 GLU A   7       0.053   6.300   1.037  1.00  3.83           H  
ATOM    106  HG3 GLU A   7      -1.413   5.371   1.347  1.00  3.70           H  
HETATM  107  N   TPO A   8       0.733   1.677   3.685  1.00  1.84           N  
HETATM  108  CA  TPO A   8       1.762   0.668   4.074  1.00  2.51           C  
HETATM  109  CB  TPO A   8       1.248   0.033   5.373  1.00  3.60           C  
HETATM  110  CG2 TPO A   8       2.334  -0.866   5.940  1.00  4.57           C  
HETATM  111  OG1 TPO A   8       0.934   1.052   6.316  1.00  4.04           O  
HETATM  112  P   TPO A   8      -0.453   0.930   7.158  1.00  4.74           P  
HETATM  113  O1P TPO A   8      -0.172   1.599   8.561  1.00  5.27           O  
HETATM  114  O2P TPO A   8      -0.806  -0.622   7.313  1.00  5.23           O  
HETATM  115  O3P TPO A   8      -1.547   1.762   6.319  1.00  5.10           O  
HETATM  116  C   TPO A   8       1.927  -0.396   2.976  1.00  2.05           C  
HETATM  117  O   TPO A   8       3.020  -0.866   2.733  1.00  2.26           O  
HETATM  118  H   TPO A   8      -0.053   1.801   4.250  1.00  2.07           H  
HETATM  119  HA  TPO A   8       2.706   1.156   4.259  1.00  2.96           H  
HETATM  120  HB  TPO A   8       0.369  -0.562   5.176  1.00  3.59           H  
HETATM  121 HG21 TPO A   8       3.063  -0.261   6.456  1.00  4.81           H  
HETATM  122 HG22 TPO A   8       2.811  -1.397   5.131  1.00  4.90           H  
HETATM  123 HG23 TPO A   8       1.894  -1.570   6.628  1.00  5.02           H  
ATOM    124  N   GLU A   9       0.859  -0.770   2.304  1.00  1.97           N  
ATOM    125  CA  GLU A   9       0.975  -1.796   1.216  1.00  2.50           C  
ATOM    126  C   GLU A   9       1.774  -1.234   0.028  1.00  1.87           C  
ATOM    127  O   GLU A   9       2.363  -1.977  -0.734  1.00  2.19           O  
ATOM    128  CB  GLU A   9      -0.469  -2.135   0.806  1.00  3.48           C  
ATOM    129  CG  GLU A   9      -1.131  -0.937   0.107  1.00  4.09           C  
ATOM    130  CD  GLU A   9      -1.425  -1.289  -1.355  1.00  5.19           C  
ATOM    131  OE1 GLU A   9      -0.486  -1.350  -2.133  1.00  5.61           O  
ATOM    132  OE2 GLU A   9      -2.586  -1.489  -1.673  1.00  5.87           O  
ATOM    133  H   GLU A   9      -0.011  -0.371   2.506  1.00  1.97           H  
ATOM    134  HA  GLU A   9       1.459  -2.681   1.598  1.00  3.06           H  
ATOM    135  HB2 GLU A   9      -0.458  -2.979   0.132  1.00  3.83           H  
ATOM    136  HB3 GLU A   9      -1.039  -2.391   1.687  1.00  3.88           H  
ATOM    137  HG2 GLU A   9      -2.055  -0.695   0.611  1.00  4.23           H  
ATOM    138  HG3 GLU A   9      -0.470  -0.085   0.143  1.00  4.09           H  
ATOM    139  N   ARG A  10       1.805   0.071  -0.126  1.00  1.52           N  
ATOM    140  CA  ARG A  10       2.572   0.685  -1.252  1.00  2.15           C  
ATOM    141  C   ARG A  10       4.048   0.832  -0.863  1.00  1.75           C  
ATOM    142  O   ARG A  10       4.931   0.532  -1.643  1.00  2.08           O  
ATOM    143  CB  ARG A  10       1.931   2.057  -1.471  1.00  3.04           C  
ATOM    144  CG  ARG A  10       0.674   1.898  -2.327  1.00  3.94           C  
ATOM    145  CD  ARG A  10       1.016   2.136  -3.801  1.00  5.16           C  
ATOM    146  NE  ARG A  10      -0.300   2.249  -4.493  1.00  6.06           N  
ATOM    147  CZ  ARG A  10      -0.975   1.171  -4.801  1.00  6.46           C  
ATOM    148  NH1 ARG A  10      -0.704   0.524  -5.905  1.00  6.91           N  
ATOM    149  NH2 ARG A  10      -1.921   0.743  -4.004  1.00  6.74           N  
ATOM    150  H   ARG A  10       1.329   0.649   0.505  1.00  1.37           H  
ATOM    151  HA  ARG A  10       2.473   0.088  -2.144  1.00  2.77           H  
ATOM    152  HB2 ARG A  10       1.664   2.489  -0.516  1.00  2.63           H  
ATOM    153  HB3 ARG A  10       2.630   2.706  -1.977  1.00  3.72           H  
ATOM    154  HG2 ARG A  10       0.281   0.900  -2.206  1.00  3.91           H  
ATOM    155  HG3 ARG A  10      -0.064   2.614  -2.011  1.00  4.02           H  
ATOM    156  HD2 ARG A  10       1.581   3.052  -3.911  1.00  5.40           H  
ATOM    157  HD3 ARG A  10       1.572   1.301  -4.198  1.00  5.38           H  
ATOM    158  HE  ARG A  10      -0.660   3.133  -4.719  1.00  6.55           H  
ATOM    159 HH11 ARG A  10       0.018   0.852  -6.514  1.00  6.96           H  
ATOM    160 HH12 ARG A  10      -1.220  -0.301  -6.142  1.00  7.42           H  
ATOM    161 HH21 ARG A  10      -2.128   1.240  -3.160  1.00  6.66           H  
ATOM    162 HH22 ARG A  10      -2.438  -0.081  -4.237  1.00  7.26           H  
ATOM    163  N   CYS A  11       4.317   1.286   0.342  1.00  1.72           N  
ATOM    164  CA  CYS A  11       5.736   1.449   0.794  1.00  2.53           C  
ATOM    165  C   CYS A  11       6.392   0.076   0.992  1.00  2.08           C  
ATOM    166  O   CYS A  11       7.538  -0.123   0.638  1.00  2.37           O  
ATOM    167  CB  CYS A  11       5.652   2.204   2.124  1.00  3.41           C  
ATOM    168  SG  CYS A  11       7.281   2.870   2.547  1.00  4.84           S  
ATOM    169  H   CYS A  11       3.582   1.515   0.950  1.00  1.61           H  
ATOM    170  HA  CYS A  11       6.295   2.031   0.075  1.00  3.17           H  
ATOM    171  HB2 CYS A  11       4.945   3.016   2.033  1.00  3.68           H  
ATOM    172  HB3 CYS A  11       5.326   1.529   2.901  1.00  3.17           H  
ATOM    173  HG  CYS A  11       7.337   2.933   3.503  1.00  5.25           H  
ATOM    174  N   ILE A  12       5.672  -0.878   1.541  1.00  1.88           N  
ATOM    175  CA  ILE A  12       6.244  -2.232   1.741  1.00  2.43           C  
ATOM    176  C   ILE A  12       6.565  -2.856   0.374  1.00  1.67           C  
ATOM    177  O   ILE A  12       7.623  -3.421   0.179  1.00  1.90           O  
ATOM    178  CB  ILE A  12       5.127  -2.988   2.465  1.00  3.17           C  
ATOM    179  CG1 ILE A  12       5.151  -2.620   3.959  1.00  4.23           C  
ATOM    180  CG2 ILE A  12       5.301  -4.488   2.279  1.00  3.93           C  
ATOM    181  CD1 ILE A  12       6.204  -3.450   4.704  1.00  5.33           C  
ATOM    182  H   ILE A  12       4.747  -0.710   1.814  1.00  1.79           H  
ATOM    183  HA  ILE A  12       7.128  -2.186   2.358  1.00  3.19           H  
ATOM    184  HB  ILE A  12       4.176  -2.694   2.045  1.00  2.69           H  
ATOM    185 HG12 ILE A  12       5.388  -1.571   4.062  1.00  4.10           H  
ATOM    186 HG13 ILE A  12       4.179  -2.807   4.385  1.00  4.51           H  
ATOM    187 HG21 ILE A  12       4.719  -5.011   3.020  1.00  4.07           H  
ATOM    188 HG22 ILE A  12       6.342  -4.744   2.385  1.00  4.41           H  
ATOM    189 HG23 ILE A  12       4.959  -4.759   1.293  1.00  4.28           H  
ATOM    190 HD11 ILE A  12       7.113  -3.487   4.121  1.00  5.73           H  
ATOM    191 HD12 ILE A  12       5.832  -4.453   4.854  1.00  5.66           H  
ATOM    192 HD13 ILE A  12       6.408  -2.995   5.662  1.00  5.65           H  
ATOM    193  N   GLU A  13       5.664  -2.732  -0.576  1.00  1.27           N  
ATOM    194  CA  GLU A  13       5.920  -3.293  -1.941  1.00  1.74           C  
ATOM    195  C   GLU A  13       7.043  -2.505  -2.631  1.00  1.21           C  
ATOM    196  O   GLU A  13       7.802  -3.056  -3.404  1.00  1.66           O  
ATOM    197  CB  GLU A  13       4.601  -3.133  -2.705  1.00  2.67           C  
ATOM    198  CG  GLU A  13       3.731  -4.377  -2.493  1.00  3.77           C  
ATOM    199  CD  GLU A  13       4.167  -5.482  -3.460  1.00  4.79           C  
ATOM    200  OE1 GLU A  13       5.086  -6.210  -3.122  1.00  5.37           O  
ATOM    201  OE2 GLU A  13       3.574  -5.581  -4.522  1.00  5.31           O  
ATOM    202  H   GLU A  13       4.826  -2.255  -0.394  1.00  1.26           H  
ATOM    203  HA  GLU A  13       6.185  -4.340  -1.873  1.00  2.39           H  
ATOM    204  HB2 GLU A  13       4.077  -2.259  -2.343  1.00  2.69           H  
ATOM    205  HB3 GLU A  13       4.807  -3.017  -3.758  1.00  3.00           H  
ATOM    206  HG2 GLU A  13       3.841  -4.724  -1.475  1.00  4.13           H  
ATOM    207  HG3 GLU A  13       2.697  -4.127  -2.678  1.00  3.93           H  
ATOM    208  N   SER A  14       7.164  -1.224  -2.342  1.00  1.19           N  
ATOM    209  CA  SER A  14       8.256  -0.409  -2.967  1.00  2.21           C  
ATOM    210  C   SER A  14       9.619  -0.984  -2.549  1.00  1.99           C  
ATOM    211  O   SER A  14      10.543  -1.048  -3.337  1.00  2.29           O  
ATOM    212  CB  SER A  14       8.057   1.021  -2.438  1.00  3.09           C  
ATOM    213  OG  SER A  14       8.828   1.222  -1.259  1.00  3.33           O  
ATOM    214  H   SER A  14       6.547  -0.806  -1.706  1.00  1.05           H  
ATOM    215  HA  SER A  14       8.160  -0.421  -4.041  1.00  2.84           H  
ATOM    216  HB2 SER A  14       8.369   1.729  -3.184  1.00  3.95           H  
ATOM    217  HB3 SER A  14       7.009   1.176  -2.224  1.00  3.05           H  
ATOM    218  HG  SER A  14       8.740   2.142  -1.000  1.00  4.10           H  
ATOM    219  N   LEU A  15       9.731  -1.430  -1.316  1.00  2.02           N  
ATOM    220  CA  LEU A  15      11.012  -2.036  -0.839  1.00  2.55           C  
ATOM    221  C   LEU A  15      11.130  -3.462  -1.395  1.00  1.80           C  
ATOM    222  O   LEU A  15      12.202  -3.908  -1.759  1.00  2.02           O  
ATOM    223  CB  LEU A  15      10.910  -2.062   0.693  1.00  3.55           C  
ATOM    224  CG  LEU A  15      10.840  -0.631   1.238  1.00  4.48           C  
ATOM    225  CD1 LEU A  15      10.299  -0.655   2.669  1.00  5.55           C  
ATOM    226  CD2 LEU A  15      12.241  -0.011   1.233  1.00  5.13           C  
ATOM    227  H   LEU A  15       8.960  -1.385  -0.711  1.00  2.08           H  
ATOM    228  HA  LEU A  15      11.854  -1.437  -1.147  1.00  3.13           H  
ATOM    229  HB2 LEU A  15      10.020  -2.601   0.983  1.00  3.31           H  
ATOM    230  HB3 LEU A  15      11.778  -2.558   1.101  1.00  4.09           H  
ATOM    231  HG  LEU A  15      10.181  -0.042   0.617  1.00  4.13           H  
ATOM    232 HD11 LEU A  15      10.951  -1.251   3.291  1.00  6.06           H  
ATOM    233 HD12 LEU A  15       9.308  -1.085   2.672  1.00  5.88           H  
ATOM    234 HD13 LEU A  15      10.256   0.353   3.055  1.00  5.77           H  
ATOM    235 HD21 LEU A  15      12.627   0.001   0.224  1.00  5.49           H  
ATOM    236 HD22 LEU A  15      12.896  -0.596   1.862  1.00  5.31           H  
ATOM    237 HD23 LEU A  15      12.188   0.999   1.610  1.00  5.40           H  
ATOM    238  N   ILE A  16      10.022  -4.167  -1.473  1.00  1.42           N  
ATOM    239  CA  ILE A  16      10.033  -5.562  -2.019  1.00  2.02           C  
ATOM    240  C   ILE A  16      10.481  -5.541  -3.490  1.00  1.82           C  
ATOM    241  O   ILE A  16      11.261  -6.370  -3.919  1.00  2.26           O  
ATOM    242  CB  ILE A  16       8.578  -6.048  -1.895  1.00  2.81           C  
ATOM    243  CG1 ILE A  16       8.263  -6.349  -0.425  1.00  3.48           C  
ATOM    244  CG2 ILE A  16       8.371  -7.317  -2.728  1.00  3.89           C  
ATOM    245  CD1 ILE A  16       6.756  -6.548  -0.247  1.00  4.11           C  
ATOM    246  H   ILE A  16       9.175  -3.770  -1.180  1.00  1.28           H  
ATOM    247  HA  ILE A  16      10.684  -6.192  -1.435  1.00  2.62           H  
ATOM    248  HB  ILE A  16       7.913  -5.276  -2.254  1.00  2.57           H  
ATOM    249 HG12 ILE A  16       8.782  -7.246  -0.123  1.00  4.14           H  
ATOM    250 HG13 ILE A  16       8.588  -5.522   0.188  1.00  3.19           H  
ATOM    251 HG21 ILE A  16       8.525  -7.092  -3.772  1.00  4.25           H  
ATOM    252 HG22 ILE A  16       7.363  -7.678  -2.584  1.00  4.27           H  
ATOM    253 HG23 ILE A  16       9.074  -8.074  -2.413  1.00  4.35           H  
ATOM    254 HD11 ILE A  16       6.253  -5.597  -0.342  1.00  4.51           H  
ATOM    255 HD12 ILE A  16       6.561  -6.962   0.731  1.00  4.39           H  
ATOM    256 HD13 ILE A  16       6.390  -7.225  -1.004  1.00  4.28           H  
ATOM    257  N   ALA A  17       9.994  -4.592  -4.255  1.00  1.95           N  
ATOM    258  CA  ALA A  17      10.387  -4.499  -5.696  1.00  2.87           C  
ATOM    259  C   ALA A  17      11.809  -3.934  -5.826  1.00  2.84           C  
ATOM    260  O   ALA A  17      12.096  -2.936  -5.182  1.00  2.92           O  
ATOM    261  CB  ALA A  17       9.368  -3.545  -6.326  1.00  3.38           C  
ATOM    262  OXT ALA A  17      12.586  -4.512  -6.567  1.00  3.24           O  
ATOM    263  H   ALA A  17       9.371  -3.935  -3.878  1.00  1.87           H  
ATOM    264  HA  ALA A  17      10.322  -5.468  -6.166  1.00  3.60           H  
ATOM    265  HB1 ALA A  17       8.407  -4.034  -6.387  1.00  3.89           H  
ATOM    266  HB2 ALA A  17       9.696  -3.271  -7.318  1.00  3.69           H  
ATOM    267  HB3 ALA A  17       9.281  -2.656  -5.718  1.00  3.49           H  
TER     268      ALA A  17                                                      
CONECT   94  107                                                                
CONECT  107   94  108  118                                                      
CONECT  108  107  109  116  119                                                 
CONECT  109  108  110  111  120                                                 
CONECT  110  109  121  122  123                                                 
CONECT  111  109  112                                                           
CONECT  112  111  113  114  115                                                 
CONECT  113  112                                                                
CONECT  114  112                                                                
CONECT  115  112                                                                
CONECT  116  108  117  124                                                      
CONECT  117  116                                                                
CONECT  118  107                                                                
CONECT  119  108                                                                
CONECT  120  109                                                                
CONECT  121  110                                                                
CONECT  122  110                                                                
CONECT  123  110                                                                
CONECT  124  116                                                                
MASTER      116    0    1    1    0    0    0    6  134    1   19    2          
END