HEADER    METAL BINDING PROTEIN                   20-NOV-99   1DFS              
TITLE     SOLUTION STRUCTURE OF THE ALPHA-DOMAIN OF MOUSE METALLOTHIONEIN-1     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METALLOTHIONEIN-1;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: C-TERMINAL DOMAIN (ALPHA);                                 
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET3D                                     
KEYWDS    3-10 HELIX, CD-S CLUSTER, HALF TURN, METAL BINDING PROTEIN            
EXPDTA    SOLUTION NMR                                                          
MDLTYP    MINIMIZED AVERAGE                                                     
AUTHOR    K.ZANGGER,G.OZ,J.D.OTVOS,I.M.ARMITAGE                                 
REVDAT   4   16-FEB-22 1DFS    1       REMARK LINK                              
REVDAT   3   24-FEB-09 1DFS    1       VERSN                                    
REVDAT   2   10-JAN-00 1DFS    1       JRNL   COMPND                            
REVDAT   1   01-DEC-99 1DFS    0                                                
JRNL        AUTH   K.ZANGGER,G.OZ,J.D.OTVOS,I.M.ARMITAGE                        
JRNL        TITL   THREE-DIMENSIONAL SOLUTION STRUCTURE OF MOUSE                
JRNL        TITL 2 [CD7]-METALLOTHIONEIN-1 BY HOMONUCLEAR AND HETERONUCLEAR NMR 
JRNL        TITL 3 SPECTROSCOPY.                                                
JRNL        REF    PROTEIN SCI.                  V.   8  2630 1999              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   10631978                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : VNMR 6.1A, X-PLOR 3.851                              
REMARK   3   AUTHORS     : VARIAN (VNMR), BRUNGER (X-PLOR)                      
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: A TOTAL OF 278 NOE-DERIVED DISTANCE       
REMARK   3  CONSTRAINTS AND 16 CD-S CONNECTIVITIES                              
REMARK   4                                                                      
REMARK   4 1DFS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000010045.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 283; 298                           
REMARK 210  PH                             : 6.5; 6.5                           
REMARK 210  IONIC STRENGTH                 : 15MMKPI; 15MMKPI                   
REMARK 210  PRESSURE                       : AMBIENT; AMBIENT                   
REMARK 210  SAMPLE CONTENTS                : 0.7MM MOUSE-METALLOTHIONEIN-1,     
REMARK 210                                   NATURAL ABUNDANCE, 15MM            
REMARK 210                                   PHOSPHATE BUFFER NA                
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D NOESY; 2D TOCSY; ACCORDION CD   
REMARK 210                                   -H HSQC                            
REMARK 210  SPECTROMETER FIELD STRENGTH    : 800 MHZ; 600 MHZ                   
REMARK 210  SPECTROMETER MODEL             : UNITY INOVA                        
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : X-PLOR 3.851                       
REMARK 210   METHOD USED                   : HYBRID DISTANCE GEOMETRY           
REMARK 210                                   -DYNAMICAL SIMULATED ANNEALING     
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 50                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : MINIMIZED AVERAGE STRUCTURE        
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL                
REMARK 210                                                                      
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D              
REMARK 210  HOMONUCLEAR TECHNIQUES AND AN ACCORDION CD-H HSQC                   
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: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS A   1   N     LYS A   1   CA      0.160                       
REMARK 500    LYS A   1   CA    LYS A   1   CB      0.162                       
REMARK 500    SER A   2   N     SER A   2   CA      0.166                       
REMARK 500    SER A   2   CA    SER A   2   CB      0.111                       
REMARK 500    SER A   2   C     CYS A   3   N       0.143                       
REMARK 500    CYS A   3   N     CYS A   3   CA      0.182                       
REMARK 500    CYS A   3   CA    CYS A   3   CB      0.158                       
REMARK 500    CYS A   4   N     CYS A   4   CA      0.157                       
REMARK 500    CYS A   4   CA    CYS A   4   CB      0.166                       
REMARK 500    SER A   5   N     SER A   5   CA      0.174                       
REMARK 500    SER A   5   CA    SER A   5   CB      0.100                       
REMARK 500    SER A   5   CA    SER A   5   C       0.177                       
REMARK 500    CYS A   6   N     CYS A   6   CA      0.179                       
REMARK 500    CYS A   6   CA    CYS A   6   CB      0.149                       
REMARK 500    CYS A   7   N     CYS A   7   CA      0.155                       
REMARK 500    CYS A   7   CA    CYS A   7   CB      0.136                       
REMARK 500    CYS A   7   C     PRO A   8   N       0.153                       
REMARK 500    PRO A   8   N     PRO A   8   CA      0.141                       
REMARK 500    PRO A   8   CD    PRO A   8   N       0.089                       
REMARK 500    PRO A   8   CA    PRO A   8   C       0.170                       
REMARK 500    PRO A   8   C     VAL A   9   N       0.140                       
REMARK 500    VAL A   9   N     VAL A   9   CA      0.192                       
REMARK 500    VAL A   9   CA    VAL A   9   CB      0.176                       
REMARK 500    GLY A  10   N     GLY A  10   CA      0.127                       
REMARK 500    GLY A  10   CA    GLY A  10   C       0.142                       
REMARK 500    CYS A  11   N     CYS A  11   CA      0.209                       
REMARK 500    CYS A  11   CA    CYS A  11   CB      0.164                       
REMARK 500    CYS A  11   CA    CYS A  11   C       0.179                       
REMARK 500    SER A  12   N     SER A  12   CA      0.167                       
REMARK 500    SER A  12   CA    SER A  12   CB      0.104                       
REMARK 500    LYS A  13   N     LYS A  13   CA      0.154                       
REMARK 500    CYS A  14   N     CYS A  14   CA      0.151                       
REMARK 500    CYS A  14   CA    CYS A  14   CB      0.147                       
REMARK 500    CYS A  14   CA    CYS A  14   C       0.175                       
REMARK 500    ALA A  15   N     ALA A  15   CA      0.196                       
REMARK 500    GLN A  16   N     GLN A  16   CA      0.172                       
REMARK 500    GLY A  17   N     GLY A  17   CA      0.146                       
REMARK 500    GLY A  17   CA    GLY A  17   C       0.098                       
REMARK 500    CYS A  18   N     CYS A  18   CA      0.186                       
REMARK 500    CYS A  18   CA    CYS A  18   CB      0.141                       
REMARK 500    CYS A  18   CA    CYS A  18   C       0.166                       
REMARK 500    VAL A  19   N     VAL A  19   CA      0.168                       
REMARK 500    VAL A  19   CA    VAL A  19   CB      0.187                       
REMARK 500    VAL A  19   CB    VAL A  19   CG1     0.148                       
REMARK 500    VAL A  19   CA    VAL A  19   C       0.157                       
REMARK 500    CYS A  20   N     CYS A  20   CA      0.161                       
REMARK 500    CYS A  20   CA    CYS A  20   CB      0.149                       
REMARK 500    LYS A  21   N     LYS A  21   CA      0.177                       
REMARK 500    LYS A  21   CD    LYS A  21   CE      0.158                       
REMARK 500    GLY A  22   N     GLY A  22   CA      0.162                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      66 BOND DEVIATIONS.                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    CYS A   3   CA  -  CB  -  SG  ANGL. DEV. =   6.7 DEGREES          
REMARK 500    CYS A   6   CA  -  CB  -  SG  ANGL. DEV. =   7.3 DEGREES          
REMARK 500    CYS A  27   CA  -  CB  -  SG  ANGL. DEV. =   7.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A   2      -92.99   -119.00                                   
REMARK 500    CYS A   3      -45.26   -145.51                                   
REMARK 500    PRO A   8       38.59    -85.59                                   
REMARK 500    VAL A   9      -64.17     70.59                                   
REMARK 500    CYS A  11      171.01    -49.28                                   
REMARK 500    ALA A  23      -48.03     72.73                                   
REMARK 500    ASP A  25      -64.83   -135.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A  33  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A   3   SG                                                     
REMARK 620 2 CYS A   4   SG  112.7                                              
REMARK 620 3 CYS A  14   SG  115.0 120.1                                        
REMARK 620 4 CYS A  18   SG   94.1 100.6 109.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A  35  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A   4   SG                                                     
REMARK 620 2 CYS A   6   SG  105.5                                              
REMARK 620 3 CYS A   7   SG  119.1 121.4                                        
REMARK 620 4 CYS A  20   SG   97.2  99.7 109.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A  34  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A   7   SG                                                     
REMARK 620 2 CYS A  11   SG  100.7                                              
REMARK 620 3 CYS A  14   SG  115.0 121.4                                        
REMARK 620 4 CYS A  30   SG  101.4 102.7 112.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A  32  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  20   SG                                                     
REMARK 620 2 CYS A  27   SG   95.5                                              
REMARK 620 3 CYS A  29   SG  103.1 115.5                                        
REMARK 620 4 CYS A  30   SG  117.3 112.6 111.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 32                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 33                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 34                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 35                   
DBREF  1DFS A    1    31  UNP    P02802   MT1_MOUSE       31     61             
SEQRES   1 A   31  LYS SER CYS CYS SER CYS CYS PRO VAL GLY CYS SER LYS          
SEQRES   2 A   31  CYS ALA GLN GLY CYS VAL CYS LYS GLY ALA ALA ASP LYS          
SEQRES   3 A   31  CYS THR CYS CYS ALA                                          
HET     CD  A  32       1                                                       
HET     CD  A  33       1                                                       
HET     CD  A  34       1                                                       
HET     CD  A  35       1                                                       
HETNAM      CD CADMIUM ION                                                      
FORMUL   2   CD    4(CD 2+)                                                     
LINK         SG  CYS A   3                CD    CD A  33     1555   1555  2.55  
LINK         SG  CYS A   4                CD    CD A  33     1555   1555  2.53  
LINK         SG  CYS A   4                CD    CD A  35     1555   1555  2.52  
LINK         SG  CYS A   6                CD    CD A  35     1555   1555  2.53  
LINK         SG  CYS A   7                CD    CD A  34     1555   1555  2.52  
LINK         SG  CYS A   7                CD    CD A  35     1555   1555  2.53  
LINK         SG  CYS A  11                CD    CD A  34     1555   1555  2.57  
LINK         SG  CYS A  14                CD    CD A  33     1555   1555  2.56  
LINK         SG  CYS A  14                CD    CD A  34     1555   1555  2.58  
LINK         SG  CYS A  18                CD    CD A  33     1555   1555  2.52  
LINK         SG  CYS A  20                CD    CD A  32     1555   1555  2.52  
LINK         SG  CYS A  20                CD    CD A  35     1555   1555  2.49  
LINK         SG  CYS A  27                CD    CD A  32     1555   1555  2.52  
LINK         SG  CYS A  29                CD    CD A  32     1555   1555  2.53  
LINK         SG  CYS A  30                CD    CD A  32     1555   1555  2.54  
LINK         SG  CYS A  30                CD    CD A  34     1555   1555  2.55  
SITE     1 AC1  4 CYS A  20  CYS A  27  CYS A  29  CYS A  30                    
SITE     1 AC2  4 CYS A   3  CYS A   4  CYS A  14  CYS A  18                    
SITE     1 AC3  4 CYS A   7  CYS A  11  CYS A  14  CYS A  30                    
SITE     1 AC4  4 CYS A   4  CYS A   6  CYS A   7  CYS A  20                    
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      12.638   6.231  -2.198  1.00  3.40           N  
ATOM      2  CA  LYS A   1      11.033   6.019  -2.164  1.00  2.57           C  
ATOM      3  C   LYS A   1      10.527   4.513  -2.683  1.00  1.62           C  
ATOM      4  O   LYS A   1      11.332   3.798  -3.325  1.00  2.23           O  
ATOM      5  CB  LYS A   1      10.259   7.248  -3.041  1.00  3.26           C  
ATOM      6  CG  LYS A   1      10.184   8.719  -2.308  1.00  4.14           C  
ATOM      7  CD  LYS A   1       9.360   9.906  -3.111  1.00  4.99           C  
ATOM      8  CE  LYS A   1      10.095  10.486  -4.473  1.00  5.84           C  
ATOM      9  NZ  LYS A   1       9.237  11.554  -5.224  1.00  6.55           N  
ATOM     10  H1  LYS A   1      13.124   5.480  -1.647  1.00  3.79           H  
ATOM     11  H2  LYS A   1      12.900   7.147  -1.764  1.00  3.87           H  
ATOM     12  H3  LYS A   1      13.014   6.206  -3.190  1.00  3.64           H  
ATOM     13  HA  LYS A   1      10.747   6.090  -1.109  1.00  2.85           H  
ATOM     14  HB2 LYS A   1      10.768   7.366  -3.987  1.00  3.61           H  
ATOM     15  HB3 LYS A   1       9.231   6.945  -3.267  1.00  3.39           H  
ATOM     16  HG2 LYS A   1       9.683   8.586  -1.351  1.00  4.42           H  
ATOM     17  HG3 LYS A   1      11.195   9.063  -2.102  1.00  4.35           H  
ATOM     18  HD2 LYS A   1       8.359   9.551  -3.363  1.00  5.17           H  
ATOM     19  HD3 LYS A   1       9.236  10.732  -2.422  1.00  5.24           H  
ATOM     20  HE2 LYS A   1      11.036  10.942  -4.196  1.00  6.16           H  
ATOM     21  HE3 LYS A   1      10.295   9.661  -5.162  1.00  5.95           H  
ATOM     22  HZ1 LYS A   1       8.316  11.161  -5.539  1.00  6.68           H  
ATOM     23  HZ2 LYS A   1       9.758  11.862  -6.082  1.00  6.97           H  
ATOM     24  HZ3 LYS A   1       9.073  12.402  -4.635  1.00  6.79           H  
ATOM     25  N   SER A   2       9.156   4.068  -2.398  1.00  0.89           N  
ATOM     26  CA  SER A   2       8.492   2.654  -2.844  1.00  1.10           C  
ATOM     27  C   SER A   2       7.162   2.878  -3.846  1.00  1.02           C  
ATOM     28  O   SER A   2       7.402   2.904  -5.075  1.00  1.92           O  
ATOM     29  CB  SER A   2       8.251   1.759  -1.496  1.00  1.88           C  
ATOM     30  OG  SER A   2       7.883   0.380  -1.832  1.00  2.90           O  
ATOM     31  H   SER A   2       8.561   4.702  -1.890  1.00  1.41           H  
ATOM     32  HA  SER A   2       9.237   2.092  -3.444  1.00  1.93           H  
ATOM     33  HB2 SER A   2       9.155   1.720  -0.909  1.00  2.22           H  
ATOM     34  HB3 SER A   2       7.467   2.220  -0.895  1.00  2.16           H  
ATOM     35  HG  SER A   2       7.599  -0.101  -1.041  1.00  3.33           H  
ATOM     36  N   CYS A   3       5.766   2.960  -3.364  1.00  0.64           N  
ATOM     37  CA  CYS A   3       4.409   3.066  -4.280  1.00  0.46           C  
ATOM     38  C   CYS A   3       3.150   3.985  -3.665  1.00  0.60           C  
ATOM     39  O   CYS A   3       2.487   4.675  -4.469  1.00  1.07           O  
ATOM     40  CB  CYS A   3       3.898   1.490  -4.630  1.00  0.62           C  
ATOM     41  SG  CYS A   3       3.409   0.288  -3.236  1.00  0.52           S  
ATOM     42  H   CYS A   3       5.604   2.875  -2.405  1.00  1.26           H  
ATOM     43  HA  CYS A   3       4.682   3.510  -5.250  1.00  0.44           H  
ATOM     44  HB2 CYS A   3       3.056   1.530  -5.296  1.00  0.81           H  
ATOM     45  HB3 CYS A   3       4.700   1.021  -5.185  1.00  0.82           H  
ATOM     46  HG  CYS A   3       4.166  -0.272  -3.035  1.00  1.05           H  
ATOM     47  N   CYS A   4       2.774   3.829  -2.281  1.00  0.47           N  
ATOM     48  CA  CYS A   4       1.464   4.448  -1.565  1.00  0.62           C  
ATOM     49  C   CYS A   4       1.708   5.721  -0.541  1.00  0.46           C  
ATOM     50  O   CYS A   4       2.736   5.755   0.180  1.00  1.36           O  
ATOM     51  CB  CYS A   4       0.763   3.184  -0.669  1.00  1.37           C  
ATOM     52  SG  CYS A   4      -0.148   1.830  -1.547  1.00  0.71           S  
ATOM     53  H   CYS A   4       3.313   3.214  -1.723  1.00  0.62           H  
ATOM     54  HA  CYS A   4       0.749   4.759  -2.320  1.00  1.02           H  
ATOM     55  HB2 CYS A   4       1.528   2.700  -0.079  1.00  2.18           H  
ATOM     56  HB3 CYS A   4       0.045   3.598   0.035  1.00  2.06           H  
ATOM     57  HG  CYS A   4       0.103   0.988  -1.164  1.00  1.14           H  
ATOM     58  N   SER A   5       0.580   6.621  -0.352  1.00  0.55           N  
ATOM     59  CA  SER A   5       0.422   7.780   0.787  1.00  0.40           C  
ATOM     60  C   SER A   5      -0.571   7.203   2.043  1.00  0.39           C  
ATOM     61  O   SER A   5      -0.608   7.849   3.116  1.00  0.65           O  
ATOM     62  CB  SER A   5      -0.118   9.146   0.091  1.00  0.80           C  
ATOM     63  OG  SER A   5       0.865   9.673  -0.855  1.00  1.25           O  
ATOM     64  H   SER A   5      -0.258   6.416  -0.876  1.00  1.29           H  
ATOM     65  HA  SER A   5       1.401   7.974   1.236  1.00  0.47           H  
ATOM     66  HB2 SER A   5      -1.046   8.953  -0.429  1.00  0.96           H  
ATOM     67  HB3 SER A   5      -0.313   9.900   0.861  1.00  1.11           H  
ATOM     68  HG  SER A   5       0.517  10.469  -1.296  1.00  1.55           H  
ATOM     69  N   CYS A   6      -1.272   5.915   1.911  1.00  0.27           N  
ATOM     70  CA  CYS A   6      -2.170   5.085   3.001  1.00  0.26           C  
ATOM     71  C   CYS A   6      -1.223   4.106   3.939  1.00  0.35           C  
ATOM     72  O   CYS A   6      -1.546   3.942   5.136  1.00  0.82           O  
ATOM     73  CB  CYS A   6      -3.435   4.234   2.285  1.00  0.30           C  
ATOM     74  SG  CYS A   6      -3.127   2.986   0.893  1.00  0.81           S  
ATOM     75  H   CYS A   6      -1.115   5.434   1.090  1.00  0.41           H  
ATOM     76  HA  CYS A   6      -2.633   5.812   3.655  1.00  0.31           H  
ATOM     77  HB2 CYS A   6      -4.002   3.704   3.046  1.00  0.86           H  
ATOM     78  HB3 CYS A   6      -4.102   4.972   1.885  1.00  0.83           H  
ATOM     79  HG  CYS A   6      -3.235   3.447   0.056  1.00  1.35           H  
ATOM     80  N   CYS A   7      -0.079   3.456   3.357  1.00  0.37           N  
ATOM     81  CA  CYS A   7       0.969   2.452   4.064  1.00  0.36           C  
ATOM     82  C   CYS A   7       2.349   3.269   4.510  1.00  0.42           C  
ATOM     83  O   CYS A   7       2.585   4.363   3.935  1.00  0.56           O  
ATOM     84  CB  CYS A   7       1.319   1.162   3.062  1.00  0.38           C  
ATOM     85  SG  CYS A   7      -0.132   0.152   2.474  1.00  0.29           S  
ATOM     86  H   CYS A   7       0.105   3.625   2.429  1.00  0.69           H  
ATOM     87  HA  CYS A   7       0.531   2.069   4.986  1.00  0.39           H  
ATOM     88  HB2 CYS A   7       1.833   1.505   2.179  1.00  0.48           H  
ATOM     89  HB3 CYS A   7       1.991   0.485   3.593  1.00  0.61           H  
ATOM     90  HG  CYS A   7      -0.466  -0.336   3.232  1.00  0.90           H  
ATOM     91  N   PRO A   8       3.271   2.704   5.537  1.00  0.45           N  
ATOM     92  CA  PRO A   8       4.604   3.463   6.023  1.00  0.58           C  
ATOM     93  C   PRO A   8       5.971   3.189   5.061  1.00  0.51           C  
ATOM     94  O   PRO A   8       7.087   3.100   5.624  1.00  0.67           O  
ATOM     95  CB  PRO A   8       4.665   2.922   7.548  1.00  0.73           C  
ATOM     96  CG  PRO A   8       4.050   1.504   7.559  1.00  0.70           C  
ATOM     97  CD  PRO A   8       3.133   1.368   6.336  1.00  0.55           C  
ATOM     98  HA  PRO A   8       4.471   4.543   6.032  1.00  0.70           H  
ATOM     99  HB2 PRO A   8       5.671   2.914   7.952  1.00  0.78           H  
ATOM    100  HB3 PRO A   8       4.054   3.584   8.182  1.00  0.88           H  
ATOM    101  HG2 PRO A   8       4.862   0.757   7.495  1.00  0.71           H  
ATOM    102  HG3 PRO A   8       3.500   1.329   8.471  1.00  0.87           H  
ATOM    103  HD2 PRO A   8       3.437   0.540   5.692  1.00  0.56           H  
ATOM    104  HD3 PRO A   8       2.098   1.215   6.648  1.00  0.66           H  
ATOM    105  N   VAL A   9       5.886   3.095   3.590  1.00  0.45           N  
ATOM    106  CA  VAL A   9       7.086   2.840   2.485  1.00  0.53           C  
ATOM    107  C   VAL A   9       7.640   1.287   2.584  1.00  0.58           C  
ATOM    108  O   VAL A   9       7.465   0.516   1.607  1.00  0.97           O  
ATOM    109  CB  VAL A   9       8.240   4.110   2.578  1.00  0.73           C  
ATOM    110  CG1 VAL A   9       9.648   3.831   1.798  1.00  1.13           C  
ATOM    111  CG2 VAL A   9       7.570   5.563   2.179  1.00  1.53           C  
ATOM    112  H   VAL A   9       5.028   3.223   3.179  1.00  0.51           H  
ATOM    113  HA  VAL A   9       6.611   2.898   1.507  1.00  0.65           H  
ATOM    114  HB  VAL A   9       8.514   4.188   3.618  1.00  1.46           H  
ATOM    115 HG11 VAL A   9      10.317   4.670   1.888  1.00  1.70           H  
ATOM    116 HG12 VAL A   9       9.469   3.614   0.749  1.00  1.78           H  
ATOM    117 HG13 VAL A   9      10.138   2.969   2.252  1.00  1.63           H  
ATOM    118 HG21 VAL A   9       8.263   6.364   2.367  1.00  2.02           H  
ATOM    119 HG22 VAL A   9       6.691   5.751   2.797  1.00  2.20           H  
ATOM    120 HG23 VAL A   9       7.268   5.571   1.131  1.00  1.97           H  
ATOM    121  N   GLY A  10       8.284   0.860   3.786  1.00  0.59           N  
ATOM    122  CA  GLY A  10       8.875  -0.568   4.130  1.00  0.75           C  
ATOM    123  C   GLY A  10       7.792  -1.753   4.537  1.00  0.67           C  
ATOM    124  O   GLY A  10       8.180  -2.630   5.328  1.00  1.03           O  
ATOM    125  H   GLY A  10       8.382   1.532   4.485  1.00  0.80           H  
ATOM    126  HA2 GLY A  10       9.446  -0.923   3.274  1.00  0.87           H  
ATOM    127  HA3 GLY A  10       9.573  -0.425   4.948  1.00  0.91           H  
ATOM    128  N   CYS A  11       6.457  -1.794   3.949  1.00  0.36           N  
ATOM    129  CA  CYS A  11       5.239  -2.915   4.156  1.00  0.30           C  
ATOM    130  C   CYS A  11       5.728  -4.537   3.971  1.00  0.27           C  
ATOM    131  O   CYS A  11       6.851  -4.789   3.475  1.00  0.35           O  
ATOM    132  CB  CYS A  11       4.009  -2.528   3.049  1.00  0.27           C  
ATOM    133  SG  CYS A  11       2.223  -2.822   3.483  1.00  0.33           S  
ATOM    134  H   CYS A  11       6.243  -1.063   3.355  1.00  0.49           H  
ATOM    135  HA  CYS A  11       4.878  -2.775   5.159  1.00  0.34           H  
ATOM    136  HB2 CYS A  11       4.037  -1.489   2.813  1.00  0.30           H  
ATOM    137  HB3 CYS A  11       4.204  -3.062   2.133  1.00  0.29           H  
ATOM    138  HG  CYS A  11       1.796  -3.248   2.740  1.00  0.94           H  
ATOM    139  N   SER A  12       4.823  -5.584   4.313  1.00  0.26           N  
ATOM    140  CA  SER A  12       5.037  -7.189   4.165  1.00  0.28           C  
ATOM    141  C   SER A  12       4.246  -7.794   2.839  1.00  0.27           C  
ATOM    142  O   SER A  12       4.778  -8.746   2.229  1.00  0.31           O  
ATOM    143  CB  SER A  12       4.481  -7.875   5.534  1.00  0.34           C  
ATOM    144  OG  SER A  12       5.352  -7.588   6.681  1.00  0.56           O  
ATOM    145  H   SER A  12       3.928  -5.319   4.620  1.00  0.30           H  
ATOM    146  HA  SER A  12       6.101  -7.411   4.077  1.00  0.30           H  
ATOM    147  HB2 SER A  12       3.462  -7.518   5.745  1.00  0.39           H  
ATOM    148  HB3 SER A  12       4.431  -8.952   5.411  1.00  0.45           H  
ATOM    149  HG  SER A  12       5.037  -6.807   7.172  1.00  1.05           H  
ATOM    150  N   LYS A  13       2.985  -7.215   2.401  1.00  0.26           N  
ATOM    151  CA  LYS A  13       2.065  -7.629   1.142  1.00  0.31           C  
ATOM    152  C   LYS A  13       2.554  -6.768  -0.193  1.00  0.29           C  
ATOM    153  O   LYS A  13       2.711  -7.369  -1.276  1.00  0.39           O  
ATOM    154  CB  LYS A  13       0.475  -7.313   1.505  1.00  0.33           C  
ATOM    155  CG  LYS A  13      -0.223  -8.103   2.772  1.00  0.41           C  
ATOM    156  CD  LYS A  13      -0.710  -9.651   2.507  1.00  1.20           C  
ATOM    157  CE  LYS A  13      -1.490 -10.362   3.774  1.00  1.84           C  
ATOM    158  NZ  LYS A  13      -1.953 -11.822   3.446  1.00  2.44           N  
ATOM    159  H   LYS A  13       2.642  -6.435   2.883  1.00  0.26           H  
ATOM    160  HA  LYS A  13       2.170  -8.672   0.958  1.00  0.35           H  
ATOM    161  HB2 LYS A  13       0.403  -6.241   1.736  1.00  0.35           H  
ATOM    162  HB3 LYS A  13      -0.104  -7.495   0.619  1.00  0.38           H  
ATOM    163  HG2 LYS A  13       0.467  -8.089   3.616  1.00  0.72           H  
ATOM    164  HG3 LYS A  13      -1.093  -7.509   3.056  1.00  0.70           H  
ATOM    165  HD2 LYS A  13      -1.380  -9.671   1.650  1.00  1.71           H  
ATOM    166  HD3 LYS A  13       0.164 -10.250   2.270  1.00  1.72           H  
ATOM    167  HE2 LYS A  13      -0.826 -10.404   4.634  1.00  2.21           H  
ATOM    168  HE3 LYS A  13      -2.370  -9.777   4.041  1.00  2.39           H  
ATOM    169  HZ1 LYS A  13      -2.698 -11.829   2.705  1.00  2.82           H  
ATOM    170  HZ2 LYS A  13      -2.364 -12.242   4.310  1.00  2.83           H  
ATOM    171  HZ3 LYS A  13      -1.152 -12.431   3.145  1.00  2.80           H  
ATOM    172  N   CYS A  14       2.833  -5.351  -0.034  1.00  0.23           N  
ATOM    173  CA  CYS A  14       3.377  -4.303  -1.128  1.00  0.26           C  
ATOM    174  C   CYS A  14       5.072  -4.325  -1.261  1.00  0.33           C  
ATOM    175  O   CYS A  14       5.620  -3.436  -1.971  1.00  0.42           O  
ATOM    176  CB  CYS A  14       2.813  -2.779  -0.692  1.00  0.25           C  
ATOM    177  SG  CYS A  14       1.014  -2.366  -0.822  1.00  0.28           S  
ATOM    178  H   CYS A  14       2.716  -4.979   0.863  1.00  0.22           H  
ATOM    179  HA  CYS A  14       2.990  -4.570  -2.076  1.00  0.29           H  
ATOM    180  HB2 CYS A  14       3.058  -2.606   0.295  1.00  0.28           H  
ATOM    181  HB3 CYS A  14       3.336  -2.067  -1.238  1.00  0.30           H  
ATOM    182  HG  CYS A  14       0.783  -1.771  -0.105  1.00  0.90           H  
ATOM    183  N   ALA A  15       5.901  -5.341  -0.609  1.00  0.33           N  
ATOM    184  CA  ALA A  15       7.551  -5.460  -0.640  1.00  0.44           C  
ATOM    185  C   ALA A  15       8.260  -5.557  -2.145  1.00  0.53           C  
ATOM    186  O   ALA A  15       9.317  -4.916  -2.355  1.00  0.63           O  
ATOM    187  CB  ALA A  15       7.991  -6.699   0.311  1.00  0.46           C  
ATOM    188  H   ALA A  15       5.428  -6.033  -0.096  1.00  0.29           H  
ATOM    189  HA  ALA A  15       7.891  -4.571  -0.180  1.00  0.48           H  
ATOM    190  HB1 ALA A  15       7.612  -6.535   1.313  1.00  1.15           H  
ATOM    191  HB2 ALA A  15       9.072  -6.795   0.373  1.00  1.11           H  
ATOM    192  HB3 ALA A  15       7.569  -7.633  -0.068  1.00  1.10           H  
ATOM    193  N   GLN A  16       7.635  -6.349  -3.133  1.00  0.54           N  
ATOM    194  CA  GLN A  16       8.089  -6.589  -4.681  1.00  0.69           C  
ATOM    195  C   GLN A  16       6.893  -6.107  -5.733  1.00  0.41           C  
ATOM    196  O   GLN A  16       7.244  -5.483  -6.768  1.00  0.69           O  
ATOM    197  CB  GLN A  16       8.539  -8.183  -4.801  1.00  1.27           C  
ATOM    198  CG  GLN A  16       9.180  -8.677  -6.243  1.00  1.71           C  
ATOM    199  CD  GLN A  16      10.033 -10.052  -6.140  1.00  2.54           C  
ATOM    200  OE1 GLN A  16       9.461 -11.139  -6.187  1.00  3.19           O  
ATOM    201  NE2 GLN A  16      11.379 -10.077  -6.000  1.00  3.15           N  
ATOM    202  H   GLN A  16       6.807  -6.810  -2.846  1.00  0.49           H  
ATOM    203  HA  GLN A  16       8.952  -5.987  -4.883  1.00  1.04           H  
ATOM    204  HB2 GLN A  16       9.279  -8.352  -4.013  1.00  1.54           H  
ATOM    205  HB3 GLN A  16       7.669  -8.814  -4.568  1.00  1.35           H  
ATOM    206  HG2 GLN A  16       8.356  -8.826  -6.942  1.00  1.90           H  
ATOM    207  HG3 GLN A  16       9.820  -7.893  -6.661  1.00  1.98           H  
ATOM    208 HE21 GLN A  16      11.928  -9.246  -5.961  1.00  3.15           H  
ATOM    209 HE22 GLN A  16      11.824 -10.941  -5.917  1.00  3.89           H  
ATOM    210  N   GLY A  17       5.524  -6.429  -5.458  1.00  0.47           N  
ATOM    211  CA  GLY A  17       4.247  -6.071  -6.357  1.00  1.01           C  
ATOM    212  C   GLY A  17       3.027  -5.456  -5.501  1.00  1.02           C  
ATOM    213  O   GLY A  17       2.582  -6.144  -4.544  1.00  1.73           O  
ATOM    214  H   GLY A  17       5.337  -6.940  -4.621  1.00  0.40           H  
ATOM    215  HA2 GLY A  17       4.506  -5.379  -7.166  1.00  1.24           H  
ATOM    216  HA3 GLY A  17       3.900  -6.983  -6.816  1.00  1.34           H  
ATOM    217  N   CYS A  18       2.443  -4.163  -5.854  1.00  0.35           N  
ATOM    218  CA  CYS A  18       1.186  -3.444  -5.074  1.00  0.30           C  
ATOM    219  C   CYS A  18      -0.244  -4.337  -5.206  1.00  0.30           C  
ATOM    220  O   CYS A  18      -0.563  -4.846  -6.303  1.00  0.33           O  
ATOM    221  CB  CYS A  18       1.034  -1.858  -5.594  1.00  0.34           C  
ATOM    222  SG  CYS A  18       0.059  -0.680  -4.502  1.00  0.36           S  
ATOM    223  H   CYS A  18       2.846  -3.672  -6.634  1.00  0.52           H  
ATOM    224  HA  CYS A  18       1.479  -3.432  -4.002  1.00  0.29           H  
ATOM    225  HB2 CYS A  18       2.023  -1.431  -5.675  1.00  0.41           H  
ATOM    226  HB3 CYS A  18       0.606  -1.831  -6.593  1.00  0.37           H  
ATOM    227  HG  CYS A  18      -0.820  -1.043  -4.393  1.00  0.98           H  
ATOM    228  N   VAL A  19      -1.037  -4.432  -4.047  1.00  0.31           N  
ATOM    229  CA  VAL A  19      -2.468  -5.163  -3.795  1.00  0.36           C  
ATOM    230  C   VAL A  19      -3.711  -4.037  -3.665  1.00  0.35           C  
ATOM    231  O   VAL A  19      -4.877  -4.440  -3.865  1.00  0.39           O  
ATOM    232  CB  VAL A  19      -2.292  -6.188  -2.412  1.00  0.42           C  
ATOM    233  CG1 VAL A  19      -1.683  -5.445  -1.044  1.00  0.85           C  
ATOM    234  CG2 VAL A  19      -3.628  -7.079  -2.081  1.00  0.66           C  
ATOM    235  H   VAL A  19      -0.705  -3.949  -3.263  1.00  0.31           H  
ATOM    236  HA  VAL A  19      -2.685  -5.782  -4.654  1.00  0.40           H  
ATOM    237  HB  VAL A  19      -1.527  -6.916  -2.700  1.00  0.85           H  
ATOM    238 HG11 VAL A  19      -1.826  -6.025  -0.141  1.00  1.43           H  
ATOM    239 HG12 VAL A  19      -2.138  -4.478  -0.904  1.00  1.32           H  
ATOM    240 HG13 VAL A  19      -0.615  -5.278  -1.182  1.00  1.49           H  
ATOM    241 HG21 VAL A  19      -3.429  -7.796  -1.289  1.00  1.35           H  
ATOM    242 HG22 VAL A  19      -3.934  -7.630  -2.959  1.00  1.23           H  
ATOM    243 HG23 VAL A  19      -4.444  -6.420  -1.779  1.00  1.31           H  
ATOM    244  N   CYS A  20      -3.421  -2.681  -3.260  1.00  0.32           N  
ATOM    245  CA  CYS A  20      -4.436  -1.449  -2.981  1.00  0.35           C  
ATOM    246  C   CYS A  20      -5.244  -0.918  -4.341  1.00  0.42           C  
ATOM    247  O   CYS A  20      -4.584  -0.610  -5.364  1.00  0.57           O  
ATOM    248  CB  CYS A  20      -3.596  -0.210  -2.209  1.00  0.33           C  
ATOM    249  SG  CYS A  20      -2.847  -0.572  -0.512  1.00  0.29           S  
ATOM    250  H   CYS A  20      -2.492  -2.478  -3.081  1.00  0.32           H  
ATOM    251  HA  CYS A  20      -5.185  -1.801  -2.299  1.00  0.38           H  
ATOM    252  HB2 CYS A  20      -2.767   0.083  -2.844  1.00  0.34           H  
ATOM    253  HB3 CYS A  20      -4.244   0.647  -2.094  1.00  0.38           H  
ATOM    254  HG  CYS A  20      -1.979  -0.947  -0.636  1.00  0.92           H  
ATOM    255  N   LYS A  21      -6.683  -0.785  -4.279  1.00  0.48           N  
ATOM    256  CA  LYS A  21      -7.694  -0.230  -5.439  1.00  0.55           C  
ATOM    257  C   LYS A  21      -8.063   1.363  -5.162  1.00  0.52           C  
ATOM    258  O   LYS A  21      -8.134   2.129  -6.152  1.00  0.70           O  
ATOM    259  CB  LYS A  21      -8.994  -1.263  -5.554  1.00  0.89           C  
ATOM    260  CG  LYS A  21      -8.631  -2.709  -6.290  1.00  1.47           C  
ATOM    261  CD  LYS A  21      -9.720  -3.948  -6.116  1.00  2.02           C  
ATOM    262  CE  LYS A  21     -10.021  -4.870  -7.470  1.00  2.68           C  
ATOM    263  NZ  LYS A  21     -11.383  -4.522  -8.158  1.00  3.33           N  
ATOM    264  H   LYS A  21      -7.127  -1.014  -3.418  1.00  0.57           H  
ATOM    265  HA  LYS A  21      -7.153  -0.243  -6.368  1.00  0.77           H  
ATOM    266  HB2 LYS A  21      -9.382  -1.439  -4.552  1.00  1.09           H  
ATOM    267  HB3 LYS A  21      -9.788  -0.786  -6.134  1.00  1.09           H  
ATOM    268  HG2 LYS A  21      -8.465  -2.489  -7.341  1.00  1.90           H  
ATOM    269  HG3 LYS A  21      -7.671  -3.062  -5.892  1.00  1.79           H  
ATOM    270  HD2 LYS A  21      -9.305  -4.625  -5.363  1.00  2.31           H  
ATOM    271  HD3 LYS A  21     -10.668  -3.585  -5.709  1.00  2.51           H  
ATOM    272  HE2 LYS A  21      -9.229  -4.766  -8.211  1.00  3.07           H  
ATOM    273  HE3 LYS A  21     -10.049  -5.913  -7.175  1.00  3.03           H  
ATOM    274  HZ1 LYS A  21     -11.514  -5.148  -8.985  1.00  3.63           H  
ATOM    275  HZ2 LYS A  21     -11.402  -3.532  -8.504  1.00  3.71           H  
ATOM    276  HZ3 LYS A  21     -12.187  -4.685  -7.503  1.00  3.67           H  
ATOM    277  N   GLY A  22      -8.139   1.879  -3.800  1.00  0.65           N  
ATOM    278  CA  GLY A  22      -8.286   3.417  -3.321  1.00  1.12           C  
ATOM    279  C   GLY A  22      -6.866   4.221  -3.656  1.00  1.34           C  
ATOM    280  O   GLY A  22      -6.908   5.227  -4.380  1.00  1.94           O  
ATOM    281  H   GLY A  22      -7.997   1.236  -3.082  1.00  0.54           H  
ATOM    282  HA2 GLY A  22      -9.139   3.889  -3.813  1.00  1.54           H  
ATOM    283  HA3 GLY A  22      -8.454   3.441  -2.244  1.00  1.11           H  
ATOM    284  N   ALA A  23      -5.587   3.618  -3.226  1.00  1.09           N  
ATOM    285  CA  ALA A  23      -4.053   4.056  -3.552  1.00  1.66           C  
ATOM    286  C   ALA A  23      -3.438   5.395  -2.841  1.00  1.03           C  
ATOM    287  O   ALA A  23      -2.268   5.278  -2.391  1.00  1.72           O  
ATOM    288  CB  ALA A  23      -3.797   4.056  -5.173  1.00  2.70           C  
ATOM    289  H   ALA A  23      -5.649   2.751  -2.714  1.00  0.71           H  
ATOM    290  HA  ALA A  23      -3.450   3.214  -3.187  1.00  2.29           H  
ATOM    291  HB1 ALA A  23      -2.747   4.271  -5.422  1.00  3.18           H  
ATOM    292  HB2 ALA A  23      -4.427   4.791  -5.655  1.00  3.19           H  
ATOM    293  HB3 ALA A  23      -4.053   3.079  -5.583  1.00  3.10           H  
ATOM    294  N   ALA A  24      -4.132   6.659  -2.806  1.00  1.04           N  
ATOM    295  CA  ALA A  24      -3.496   8.060  -2.221  1.00  1.53           C  
ATOM    296  C   ALA A  24      -4.126   8.682  -0.814  1.00  1.22           C  
ATOM    297  O   ALA A  24      -3.668   9.806  -0.425  1.00  1.46           O  
ATOM    298  CB  ALA A  24      -3.481   9.098  -3.483  1.00  2.17           C  
ATOM    299  H   ALA A  24      -5.034   6.716  -3.209  1.00  1.64           H  
ATOM    300  HA  ALA A  24      -2.461   7.890  -1.997  1.00  2.10           H  
ATOM    301  HB1 ALA A  24      -2.949  10.009  -3.216  1.00  2.57           H  
ATOM    302  HB2 ALA A  24      -4.486   9.357  -3.784  1.00  2.63           H  
ATOM    303  HB3 ALA A  24      -2.963   8.648  -4.329  1.00  2.52           H  
ATOM    304  N   ASP A  25      -5.133   7.998  -0.008  1.00  0.79           N  
ATOM    305  CA  ASP A  25      -5.783   8.559   1.392  1.00  0.69           C  
ATOM    306  C   ASP A  25      -5.870   7.357   2.543  1.00  0.53           C  
ATOM    307  O   ASP A  25      -5.231   7.496   3.611  1.00  0.72           O  
ATOM    308  CB  ASP A  25      -7.254   9.240   0.968  1.00  0.87           C  
ATOM    309  CG  ASP A  25      -7.894  10.246   2.055  1.00  1.27           C  
ATOM    310  OD1 ASP A  25      -8.599   9.778   2.943  1.00  1.88           O  
ATOM    311  OD2 ASP A  25      -7.637  11.448   1.981  1.00  1.75           O  
ATOM    312  H   ASP A  25      -5.463   7.120  -0.320  1.00  0.67           H  
ATOM    313  HA  ASP A  25      -5.141   9.333   1.803  1.00  0.85           H  
ATOM    314  HB2 ASP A  25      -7.128   9.782   0.038  1.00  1.10           H  
ATOM    315  HB3 ASP A  25      -7.962   8.432   0.754  1.00  0.87           H  
ATOM    316  N   LYS A  26      -6.734   6.218   2.312  1.00  0.50           N  
ATOM    317  CA  LYS A  26      -7.042   4.964   3.329  1.00  0.52           C  
ATOM    318  C   LYS A  26      -7.388   3.517   2.569  1.00  0.60           C  
ATOM    319  O   LYS A  26      -8.132   3.574   1.554  1.00  1.41           O  
ATOM    320  CB  LYS A  26      -8.291   5.453   4.349  1.00  0.59           C  
ATOM    321  CG  LYS A  26      -9.756   5.831   3.655  1.00  0.60           C  
ATOM    322  CD  LYS A  26     -10.879   6.473   4.669  1.00  0.88           C  
ATOM    323  CE  LYS A  26     -12.417   6.505   4.094  1.00  1.60           C  
ATOM    324  NZ  LYS A  26     -13.396   7.277   5.047  1.00  2.18           N  
ATOM    325  H   LYS A  26      -7.240   6.228   1.466  1.00  0.68           H  
ATOM    326  HA  LYS A  26      -6.160   4.803   3.960  1.00  0.54           H  
ATOM    327  HB2 LYS A  26      -8.460   4.675   5.096  1.00  0.69           H  
ATOM    328  HB3 LYS A  26      -7.926   6.327   4.893  1.00  0.65           H  
ATOM    329  HG2 LYS A  26      -9.577   6.555   2.855  1.00  0.60           H  
ATOM    330  HG3 LYS A  26     -10.134   4.917   3.196  1.00  0.65           H  
ATOM    331  HD2 LYS A  26     -10.900   5.918   5.606  1.00  1.32           H  
ATOM    332  HD3 LYS A  26     -10.575   7.494   4.893  1.00  1.31           H  
ATOM    333  HE2 LYS A  26     -12.450   6.983   3.118  1.00  2.13           H  
ATOM    334  HE3 LYS A  26     -12.775   5.482   3.996  1.00  2.12           H  
ATOM    335  HZ1 LYS A  26     -13.123   8.288   5.145  1.00  2.53           H  
ATOM    336  HZ2 LYS A  26     -13.445   6.835   5.997  1.00  2.66           H  
ATOM    337  HZ3 LYS A  26     -14.358   7.246   4.634  1.00  2.54           H  
ATOM    338  N   CYS A  27      -6.909   2.250   3.109  1.00  0.53           N  
ATOM    339  CA  CYS A  27      -7.243   0.771   2.528  1.00  0.50           C  
ATOM    340  C   CYS A  27      -8.017  -0.263   3.587  1.00  0.50           C  
ATOM    341  O   CYS A  27      -7.803  -0.152   4.818  1.00  0.76           O  
ATOM    342  CB  CYS A  27      -5.908   0.090   1.838  1.00  0.60           C  
ATOM    343  SG  CYS A  27      -4.440  -0.464   2.860  1.00  0.55           S  
ATOM    344  H   CYS A  27      -6.352   2.266   3.918  1.00  1.15           H  
ATOM    345  HA  CYS A  27      -7.932   0.911   1.703  1.00  0.57           H  
ATOM    346  HB2 CYS A  27      -6.230  -0.807   1.322  1.00  0.90           H  
ATOM    347  HB3 CYS A  27      -5.559   0.756   1.082  1.00  0.90           H  
ATOM    348  HG  CYS A  27      -4.112   0.287   3.362  1.00  1.06           H  
ATOM    349  N   THR A  28      -8.774  -1.346   3.020  1.00  0.51           N  
ATOM    350  CA  THR A  28      -9.470  -2.581   3.814  1.00  0.55           C  
ATOM    351  C   THR A  28      -8.721  -4.029   3.363  1.00  0.44           C  
ATOM    352  O   THR A  28      -9.383  -5.102   3.396  1.00  0.55           O  
ATOM    353  CB  THR A  28     -11.145  -2.479   3.550  1.00  0.72           C  
ATOM    354  OG1 THR A  28     -11.529  -2.541   2.109  1.00  0.92           O  
ATOM    355  CG2 THR A  28     -11.890  -1.252   4.305  1.00  1.02           C  
ATOM    356  H   THR A  28      -8.798  -1.407   2.017  1.00  0.70           H  
ATOM    357  HA  THR A  28      -9.269  -2.509   4.899  1.00  0.62           H  
ATOM    358  HB  THR A  28     -11.575  -3.382   3.986  1.00  0.89           H  
ATOM    359  HG1 THR A  28     -11.215  -1.772   1.573  1.00  1.07           H  
ATOM    360 HG21 THR A  28     -11.512  -0.302   3.943  1.00  1.44           H  
ATOM    361 HG22 THR A  28     -11.728  -1.317   5.374  1.00  1.49           H  
ATOM    362 HG23 THR A  28     -12.955  -1.303   4.118  1.00  1.62           H  
ATOM    363  N   CYS A  29      -7.302  -4.034   2.968  1.00  0.32           N  
ATOM    364  CA  CYS A  29      -6.385  -5.309   2.505  1.00  0.33           C  
ATOM    365  C   CYS A  29      -5.004  -5.572   3.394  1.00  0.34           C  
ATOM    366  O   CYS A  29      -4.550  -6.752   3.410  1.00  0.50           O  
ATOM    367  CB  CYS A  29      -6.092  -5.186   0.871  1.00  0.38           C  
ATOM    368  SG  CYS A  29      -5.126  -3.727   0.189  1.00  0.83           S  
ATOM    369  H   CYS A  29      -6.807  -3.156   2.968  1.00  0.33           H  
ATOM    370  HA  CYS A  29      -6.977  -6.206   2.635  1.00  0.40           H  
ATOM    371  HB2 CYS A  29      -5.562  -6.070   0.539  1.00  0.80           H  
ATOM    372  HB3 CYS A  29      -7.048  -5.200   0.365  1.00  0.76           H  
ATOM    373  HG  CYS A  29      -4.194  -3.883   0.353  1.00  1.22           H  
ATOM    374  N   CYS A  30      -4.340  -4.489   4.062  1.00  0.35           N  
ATOM    375  CA  CYS A  30      -2.967  -4.573   4.899  1.00  0.40           C  
ATOM    376  C   CYS A  30      -3.257  -4.439   6.545  1.00  0.47           C  
ATOM    377  O   CYS A  30      -2.346  -4.001   7.292  1.00  0.56           O  
ATOM    378  CB  CYS A  30      -1.920  -3.426   4.246  1.00  0.50           C  
ATOM    379  SG  CYS A  30      -1.564  -3.500   2.391  1.00  0.34           S  
ATOM    380  H   CYS A  30      -4.729  -3.604   4.017  1.00  0.44           H  
ATOM    381  HA  CYS A  30      -2.530  -5.547   4.776  1.00  0.43           H  
ATOM    382  HB2 CYS A  30      -2.327  -2.449   4.445  1.00  0.78           H  
ATOM    383  HB3 CYS A  30      -0.981  -3.498   4.766  1.00  0.86           H  
ATOM    384  HG  CYS A  30      -0.748  -3.070   2.216  1.00  0.98           H  
ATOM    385  N   ALA A  31      -4.523  -4.894   7.104  1.00  0.53           N  
ATOM    386  CA  ALA A  31      -4.965  -4.881   8.665  1.00  0.71           C  
ATOM    387  C   ALA A  31      -4.774  -6.330   9.387  1.00  1.48           C  
ATOM    388  O   ALA A  31      -4.913  -7.369   8.731  1.00  2.23           O  
ATOM    389  CB  ALA A  31      -6.491  -4.331   8.761  1.00  1.31           C  
ATOM    390  OXT ALA A  31      -4.532  -6.361  10.598  1.00  2.14           O  
ATOM    391  H   ALA A  31      -5.175  -5.292   6.476  1.00  0.52           H  
ATOM    392  HA  ALA A  31      -4.344  -4.158   9.178  1.00  1.24           H  
ATOM    393  HB1 ALA A  31      -6.546  -3.336   8.337  1.00  1.77           H  
ATOM    394  HB2 ALA A  31      -6.811  -4.259   9.800  1.00  1.81           H  
ATOM    395  HB3 ALA A  31      -7.182  -4.979   8.217  1.00  1.97           H  
TER     396      ALA A  31                                                      
HETATM  397 CD    CD A  32      -3.456  -2.197   1.315  1.00  0.34          CD  
HETATM  398 CD    CD A  33       1.114  -0.245  -2.259  1.00  0.41          CD  
HETATM  399 CD    CD A  34       0.490  -2.166   1.696  1.00  0.25          CD  
HETATM  400 CD    CD A  35      -1.406   1.167   0.534  1.00  0.34          CD  
CONECT   41  398                                                                
CONECT   52  398  400                                                           
CONECT   74  400                                                                
CONECT   85  399  400                                                           
CONECT  133  399                                                                
CONECT  177  398  399                                                           
CONECT  222  398                                                                
CONECT  249  397  400                                                           
CONECT  343  397                                                                
CONECT  368  397                                                                
CONECT  379  397  399                                                           
CONECT  397  249  343  368  379                                                 
CONECT  398   41   52  177  222                                                 
CONECT  399   85  133  177  379                                                 
CONECT  400   52   74   85  249                                                 
MASTER      241    0    4    0    0    0    4    6  202    1   15    3          
END