HEADER    METAL BINDING PROTEIN                   20-NOV-99   1DFT              
TITLE     SOLUTION STRUCTURE OF THE BETA-DOMAIN OF MOUSE METALLOTHIONEIN-1      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METALLOTHIONEIN-1;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN (BETA);                                  
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;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET3D                                     
KEYWDS    HALF TURN, CD-S CLUSTER, 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 1DFT    1       REMARK LINK                              
REVDAT   3   24-FEB-09 1DFT    1       VERSN                                    
REVDAT   2   10-JAN-00 1DFT    1       JRNL   COMPND                            
REVDAT   1   01-DEC-99 1DFT    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 103 NOE-DERIVED DISTANCE       
REMARK   3  CONSTRAINTS AND 12 CD-S CONNECTIVITIES                              
REMARK   4                                                                      
REMARK   4 1DFT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-NOV-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000010046.                                   
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    MET A   1   N     MET A   1   CA      0.155                       
REMARK 500    MET A   1   CA    MET A   1   CB      0.180                       
REMARK 500    ASP A   2   N     ASP A   2   CA      0.161                       
REMARK 500    ASP A   2   CA    ASP A   2   C       0.166                       
REMARK 500    ASP A   2   C     PRO A   3   N       0.166                       
REMARK 500    PRO A   3   N     PRO A   3   CA      0.137                       
REMARK 500    PRO A   3   CA    PRO A   3   C       0.156                       
REMARK 500    ASN A   4   N     ASN A   4   CA      0.151                       
REMARK 500    ASN A   4   C     CYS A   5   N       0.148                       
REMARK 500    CYS A   5   N     CYS A   5   CA      0.169                       
REMARK 500    CYS A   5   CA    CYS A   5   CB      0.139                       
REMARK 500    SER A   6   N     SER A   6   CA      0.160                       
REMARK 500    SER A   6   CA    SER A   6   CB      0.109                       
REMARK 500    SER A   6   CA    SER A   6   C       0.171                       
REMARK 500    CYS A   7   N     CYS A   7   CA      0.199                       
REMARK 500    CYS A   7   CA    CYS A   7   CB      0.156                       
REMARK 500    CYS A   7   CA    CYS A   7   C       0.163                       
REMARK 500    SER A   8   N     SER A   8   CA      0.201                       
REMARK 500    SER A   8   CA    SER A   8   CB      0.124                       
REMARK 500    SER A   8   CA    SER A   8   C       0.158                       
REMARK 500    SER A   8   C     THR A   9   N       0.152                       
REMARK 500    THR A   9   N     THR A   9   CA      0.197                       
REMARK 500    THR A   9   CA    THR A   9   CB      0.182                       
REMARK 500    GLY A  10   N     GLY A  10   CA      0.149                       
REMARK 500    GLY A  10   CA    GLY A  10   C       0.123                       
REMARK 500    GLY A  11   N     GLY A  11   CA      0.125                       
REMARK 500    GLY A  11   CA    GLY A  11   C       0.098                       
REMARK 500    SER A  12   N     SER A  12   CA      0.175                       
REMARK 500    SER A  12   CA    SER A  12   CB      0.121                       
REMARK 500    CYS A  13   N     CYS A  13   CA      0.181                       
REMARK 500    CYS A  13   CA    CYS A  13   C       0.160                       
REMARK 500    THR A  14   N     THR A  14   CA      0.160                       
REMARK 500    THR A  14   CA    THR A  14   CB      0.203                       
REMARK 500    THR A  14   C     CYS A  15   N       0.148                       
REMARK 500    CYS A  15   N     CYS A  15   CA      0.204                       
REMARK 500    CYS A  15   CA    CYS A  15   CB      0.162                       
REMARK 500    CYS A  15   CA    CYS A  15   C       0.167                       
REMARK 500    THR A  16   N     THR A  16   CA      0.185                       
REMARK 500    THR A  16   CA    THR A  16   CB      0.176                       
REMARK 500    SER A  17   N     SER A  17   CA      0.181                       
REMARK 500    SER A  17   CA    SER A  17   CB      0.120                       
REMARK 500    SER A  18   N     SER A  18   CA      0.162                       
REMARK 500    SER A  18   CA    SER A  18   CB      0.111                       
REMARK 500    CYS A  19   N     CYS A  19   CA      0.175                       
REMARK 500    CYS A  19   CA    CYS A  19   CB      0.150                       
REMARK 500    ALA A  20   N     ALA A  20   CA      0.166                       
REMARK 500    CYS A  21   N     CYS A  21   CA      0.165                       
REMARK 500    CYS A  21   CA    CYS A  21   C       0.182                       
REMARK 500    LYS A  22   N     LYS A  22   CA      0.149                       
REMARK 500    LYS A  22   CA    LYS A  22   C       0.161                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      68 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   5   CA  -  CB  -  SG  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    CYS A  21   CA  -  CB  -  SG  ANGL. DEV. =   7.4 DEGREES          
REMARK 500    CYS A  24   CA  -  CB  -  SG  ANGL. DEV. =   8.1 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   8     -137.80    113.65                                   
REMARK 500    THR A   9      -42.41   -150.44                                   
REMARK 500    THR A  14      -92.43     86.76                                   
REMARK 500    CYS A  15       70.99     59.75                                   
REMARK 500    THR A  16     -112.18   -104.36                                   
REMARK 500    CYS A  21     -126.29   -123.09                                   
REMARK 500    LYS A  22      -62.44   -132.86                                   
REMARK 500    ASN A  23      -61.84   -133.68                                   
REMARK 500    CYS A  24      151.12     83.42                                   
REMARK 500    LYS A  25       66.71   -105.86                                   
REMARK 500    CYS A  26     -120.45   -116.27                                   
REMARK 500    THR A  27      -82.39   -103.04                                   
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  32  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A   5   SG                                                     
REMARK 620 2 CYS A   7   SG  104.4                                              
REMARK 620 3 CYS A  21   SG  123.6 106.5                                        
REMARK 620 4 CYS A  24   SG  101.1 123.3  99.6                                  
REMARK 620 N                    1     2     3                                   
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   7   SG                                                     
REMARK 620 2 CYS A  13   SG  107.5                                              
REMARK 620 3 CYS A  15   SG  110.4 121.2                                        
REMARK 620 4 CYS A  26   SG  120.2  89.2 107.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A  31  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  15   SG                                                     
REMARK 620 2 CYS A  19   SG  108.6                                              
REMARK 620 3 CYS A  24   SG  120.2  95.5                                        
REMARK 620 4 CYS A  29   SG  112.8 111.8 106.8                                  
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 31                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 32                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 33                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DFS   RELATED DB: PDB                                   
REMARK 900 1DFS CONTAINS THE ALPHA-DOMAIN OF MOUSE METALLOTHIONEIN-1            
DBREF  1DFT A    1    30  UNP    P02802   MT1_MOUSE        1     30             
SEQRES   1 A   30  MET ASP PRO ASN CYS SER CYS SER THR GLY GLY SER CYS          
SEQRES   2 A   30  THR CYS THR SER SER CYS ALA CYS LYS ASN CYS LYS CYS          
SEQRES   3 A   30  THR SER CYS LYS                                              
HET     CD  A  31       1                                                       
HET     CD  A  32       1                                                       
HET     CD  A  33       1                                                       
HETNAM      CD CADMIUM ION                                                      
FORMUL   2   CD    3(CD 2+)                                                     
LINK         SG  CYS A   5                CD    CD A  32     1555   1555  2.57  
LINK         SG  CYS A   7                CD    CD A  32     1555   1555  2.55  
LINK         SG  CYS A   7                CD    CD A  33     1555   1555  2.55  
LINK         SG  CYS A  13                CD    CD A  33     1555   1555  2.54  
LINK         SG  CYS A  15                CD    CD A  31     1555   1555  2.56  
LINK         SG  CYS A  15                CD    CD A  33     1555   1555  2.55  
LINK         SG  CYS A  19                CD    CD A  31     1555   1555  2.54  
LINK         SG  CYS A  21                CD    CD A  32     1555   1555  2.58  
LINK         SG  CYS A  24                CD    CD A  31     1555   1555  2.54  
LINK         SG  CYS A  24                CD    CD A  32     1555   1555  2.54  
LINK         SG  CYS A  26                CD    CD A  33     1555   1555  2.53  
LINK         SG  CYS A  29                CD    CD A  31     1555   1555  2.56  
SITE     1 AC1  4 CYS A  15  CYS A  19  CYS A  24  CYS A  29                    
SITE     1 AC2  4 CYS A   5  CYS A   7  CYS A  21  CYS A  24                    
SITE     1 AC3  4 CYS A   7  CYS A  13  CYS A  15  CYS A  26                    
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   MET A   1      14.266  -0.142   5.537  1.00  2.63           N  
ATOM      2  CA  MET A   1      14.136   1.257   4.743  1.00  2.94           C  
ATOM      3  C   MET A   1      12.657   1.473   4.003  1.00  3.02           C  
ATOM      4  O   MET A   1      12.452   2.526   3.359  1.00  3.53           O  
ATOM      5  CB  MET A   1      15.436   1.453   3.641  1.00  2.66           C  
ATOM      6  CG  MET A   1      16.957   1.235   4.160  1.00  3.00           C  
ATOM      7  SD  MET A   1      17.600   2.429   5.489  1.00  3.41           S  
ATOM      8  CE  MET A   1      17.734   1.404   7.000  1.00  4.52           C  
ATOM      9  H1  MET A   1      14.194  -0.971   4.882  1.00  2.70           H  
ATOM     10  H2  MET A   1      13.505  -0.228   6.246  1.00  2.88           H  
ATOM     11  H3  MET A   1      15.168  -0.203   6.065  1.00  2.88           H  
ATOM     12  HA  MET A   1      14.220   2.045   5.480  1.00  3.78           H  
ATOM     13  HB2 MET A   1      15.298   0.729   2.837  1.00  3.03           H  
ATOM     14  HB3 MET A   1      15.372   2.445   3.169  1.00  2.68           H  
ATOM     15  HG2 MET A   1      17.048   0.211   4.494  1.00  3.07           H  
ATOM     16  HG3 MET A   1      17.605   1.330   3.288  1.00  3.64           H  
ATOM     17  HE1 MET A   1      18.270   0.477   6.785  1.00  4.70           H  
ATOM     18  HE2 MET A   1      16.748   1.171   7.368  1.00  5.00           H  
ATOM     19  HE3 MET A   1      18.266   1.963   7.751  1.00  4.95           H  
ATOM     20  N   ASP A   2      11.616   0.442   4.053  1.00  2.85           N  
ATOM     21  CA  ASP A   2      10.166   0.413   3.331  1.00  2.89           C  
ATOM     22  C   ASP A   2      10.323   0.422   1.647  1.00  1.87           C  
ATOM     23  O   ASP A   2       9.686   1.282   0.984  1.00  2.26           O  
ATOM     24  CB  ASP A   2       9.212   1.550   4.062  1.00  3.92           C  
ATOM     25  CG  ASP A   2       7.637   1.440   3.714  1.00  4.27           C  
ATOM     26  OD1 ASP A   2       6.943   0.633   4.342  1.00  4.47           O  
ATOM     27  OD2 ASP A   2       7.180   2.137   2.809  1.00  4.63           O  
ATOM     28  H   ASP A   2      11.811  -0.395   4.545  1.00  2.94           H  
ATOM     29  HA  ASP A   2       9.763  -0.597   3.545  1.00  3.24           H  
ATOM     30  HB2 ASP A   2       9.338   1.453   5.146  1.00  4.54           H  
ATOM     31  HB3 ASP A   2       9.601   2.531   3.778  1.00  4.03           H  
ATOM     32  N   PRO A   3      11.155  -0.647   0.993  1.00  1.17           N  
ATOM     33  CA  PRO A   3      11.331  -0.798  -0.595  1.00  1.02           C  
ATOM     34  C   PRO A   3       9.942  -1.304  -1.394  1.00  0.87           C  
ATOM     35  O   PRO A   3       9.888  -1.120  -2.636  1.00  1.04           O  
ATOM     36  CB  PRO A   3      12.565  -1.820  -0.724  1.00  1.85           C  
ATOM     37  CG  PRO A   3      12.602  -2.623   0.592  1.00  2.21           C  
ATOM     38  CD  PRO A   3      11.989  -1.763   1.675  1.00  1.88           C  
ATOM     39  HA  PRO A   3      11.635   0.167  -1.017  1.00  1.54           H  
ATOM     40  HB2 PRO A   3      12.465  -2.500  -1.580  1.00  2.44           H  
ATOM     41  HB3 PRO A   3      13.501  -1.262  -0.850  1.00  2.12           H  
ATOM     42  HG2 PRO A   3      12.026  -3.549   0.493  1.00  2.63           H  
ATOM     43  HG3 PRO A   3      13.626  -2.872   0.866  1.00  2.81           H  
ATOM     44  HD2 PRO A   3      11.337  -2.348   2.333  1.00  2.59           H  
ATOM     45  HD3 PRO A   3      12.773  -1.303   2.276  1.00  1.95           H  
ATOM     46  N   ASN A   4       8.843  -1.932  -0.647  1.00  0.74           N  
ATOM     47  CA  ASN A   4       7.446  -2.476  -1.235  1.00  0.75           C  
ATOM     48  C   ASN A   4       6.542  -1.318  -1.988  1.00  0.75           C  
ATOM     49  O   ASN A   4       6.158  -1.565  -3.149  1.00  1.37           O  
ATOM     50  CB  ASN A   4       6.607  -3.337  -0.070  1.00  1.03           C  
ATOM     51  CG  ASN A   4       6.040  -2.496   1.222  1.00  1.77           C  
ATOM     52  OD1 ASN A   4       4.872  -2.126   1.241  1.00  2.47           O  
ATOM     53  ND2 ASN A   4       6.794  -2.147   2.271  1.00  2.12           N  
ATOM     54  H   ASN A   4       8.960  -2.040   0.327  1.00  0.78           H  
ATOM     55  HA  ASN A   4       7.717  -3.222  -1.992  1.00  0.90           H  
ATOM     56  HB2 ASN A   4       5.778  -3.847  -0.547  1.00  1.68           H  
ATOM     57  HB3 ASN A   4       7.268  -4.121   0.293  1.00  1.36           H  
ATOM     58 HD21 ASN A   4       7.753  -2.392   2.358  1.00  1.67           H  
ATOM     59 HD22 ASN A   4       6.390  -1.585   2.958  1.00  2.95           H  
ATOM     60  N   CYS A   5       6.159  -0.059  -1.301  1.00  0.60           N  
ATOM     61  CA  CYS A   5       5.201   1.078  -1.963  1.00  0.81           C  
ATOM     62  C   CYS A   5       5.522   2.686  -1.697  1.00  0.74           C  
ATOM     63  O   CYS A   5       6.276   3.025  -0.770  1.00  0.75           O  
ATOM     64  CB  CYS A   5       3.630   0.590  -1.652  1.00  1.17           C  
ATOM     65  SG  CYS A   5       2.585   1.274  -0.300  1.00  0.98           S  
ATOM     66  H   CYS A   5       6.453   0.096  -0.365  1.00  0.93           H  
ATOM     67  HA  CYS A   5       5.334   0.993  -3.053  1.00  1.08           H  
ATOM     68  HB2 CYS A   5       3.122   0.854  -2.494  1.00  1.59           H  
ATOM     69  HB3 CYS A   5       3.571  -0.500  -1.586  1.00  1.44           H  
ATOM     70  HG  CYS A   5       1.683   1.273  -0.571  1.00  1.12           H  
ATOM     71  N   SER A   6       4.819   3.649  -2.558  1.00  0.83           N  
ATOM     72  CA  SER A   6       4.858   5.267  -2.505  1.00  0.94           C  
ATOM     73  C   SER A   6       3.289   5.902  -2.606  1.00  1.07           C  
ATOM     74  O   SER A   6       3.000   6.810  -3.443  1.00  1.62           O  
ATOM     75  CB  SER A   6       5.902   5.771  -3.657  1.00  1.19           C  
ATOM     76  OG  SER A   6       7.223   5.177  -3.472  1.00  1.60           O  
ATOM     77  H   SER A   6       4.209   3.268  -3.244  1.00  0.91           H  
ATOM     78  HA  SER A   6       5.244   5.579  -1.543  1.00  0.94           H  
ATOM     79  HB2 SER A   6       5.516   5.513  -4.642  1.00  1.70           H  
ATOM     80  HB3 SER A   6       5.989   6.860  -3.592  1.00  1.68           H  
ATOM     81  HG  SER A   6       7.756   5.305  -4.264  1.00  1.90           H  
ATOM     82  N   CYS A   7       2.284   5.392  -1.683  1.00  0.94           N  
ATOM     83  CA  CYS A   7       0.698   5.862  -1.576  1.00  1.07           C  
ATOM     84  C   CYS A   7       0.488   7.427  -0.978  1.00  1.28           C  
ATOM     85  O   CYS A   7      -0.626   7.958  -1.178  1.00  1.84           O  
ATOM     86  CB  CYS A   7      -0.135   4.752  -0.610  1.00  1.04           C  
ATOM     87  SG  CYS A   7      -0.790   3.189  -1.417  1.00  1.19           S  
ATOM     88  H   CYS A   7       2.586   4.701  -1.036  1.00  1.13           H  
ATOM     89  HA  CYS A   7       0.283   5.868  -2.593  1.00  1.18           H  
ATOM     90  HB2 CYS A   7       0.492   4.458   0.208  1.00  1.11           H  
ATOM     91  HB3 CYS A   7      -0.983   5.234  -0.161  1.00  1.18           H  
ATOM     92  HG  CYS A   7      -0.670   2.462  -0.796  1.00  1.52           H  
ATOM     93  N   SER A   8       1.550   8.123  -0.239  1.00  1.52           N  
ATOM     94  CA  SER A   8       1.625   9.618   0.478  1.00  1.77           C  
ATOM     95  C   SER A   8       1.759   9.465   2.149  1.00  1.49           C  
ATOM     96  O   SER A   8       2.616   8.624   2.544  1.00  1.80           O  
ATOM     97  CB  SER A   8       0.537  10.716  -0.096  1.00  2.12           C  
ATOM     98  OG  SER A   8       0.979  12.082   0.160  1.00  2.32           O  
ATOM     99  H   SER A   8       2.398   7.616  -0.125  1.00  1.92           H  
ATOM    100  HA  SER A   8       2.618   9.999   0.175  1.00  2.32           H  
ATOM    101  HB2 SER A   8       0.424  10.582  -1.172  1.00  2.46           H  
ATOM    102  HB3 SER A   8      -0.433  10.535   0.373  1.00  2.63           H  
ATOM    103  HG  SER A   8       0.359  12.712  -0.250  1.00  2.89           H  
ATOM    104  N   THR A   9       1.038  10.284   3.161  1.00  1.79           N  
ATOM    105  CA  THR A   9       1.253  10.179   4.800  1.00  1.95           C  
ATOM    106  C   THR A   9      -0.106  10.565   5.703  1.00  1.66           C  
ATOM    107  O   THR A   9      -0.293   9.899   6.732  1.00  2.28           O  
ATOM    108  CB  THR A   9       2.568  11.181   5.239  1.00  3.03           C  
ATOM    109  OG1 THR A   9       3.671  11.124   4.259  1.00  3.81           O  
ATOM    110  CG2 THR A   9       3.263  10.837   6.664  1.00  3.79           C  
ATOM    111  H   THR A   9       0.419  10.987   2.840  1.00  2.33           H  
ATOM    112  HA  THR A   9       1.516   9.135   5.033  1.00  2.29           H  
ATOM    113  HB  THR A   9       2.222  12.226   5.294  1.00  3.22           H  
ATOM    114  HG1 THR A   9       3.559  11.805   3.575  1.00  4.21           H  
ATOM    115 HG21 THR A   9       2.538  10.954   7.461  1.00  4.37           H  
ATOM    116 HG22 THR A   9       4.090  11.514   6.859  1.00  4.24           H  
ATOM    117 HG23 THR A   9       3.636   9.815   6.671  1.00  3.78           H  
ATOM    118  N   GLY A  10      -0.934  11.699   5.348  1.00  1.71           N  
ATOM    119  CA  GLY A  10      -2.196  12.331   6.112  1.00  2.35           C  
ATOM    120  C   GLY A  10      -3.344  11.370   6.775  1.00  2.50           C  
ATOM    121  O   GLY A  10      -3.001  10.632   7.721  1.00  3.27           O  
ATOM    122  H   GLY A  10      -0.658  12.225   4.565  1.00  1.99           H  
ATOM    123  HA2 GLY A  10      -1.801  12.944   6.911  1.00  2.66           H  
ATOM    124  HA3 GLY A  10      -2.679  13.018   5.415  1.00  2.98           H  
ATOM    125  N   GLY A  11      -4.715  11.446   6.321  1.00  2.26           N  
ATOM    126  CA  GLY A  11      -5.946  10.642   6.903  1.00  2.82           C  
ATOM    127  C   GLY A  11      -6.329   9.347   6.023  1.00  2.40           C  
ATOM    128  O   GLY A  11      -6.273   8.231   6.592  1.00  2.92           O  
ATOM    129  H   GLY A  11      -4.943  12.095   5.594  1.00  2.12           H  
ATOM    130  HA2 GLY A  11      -5.776  10.358   7.950  1.00  3.24           H  
ATOM    131  HA3 GLY A  11      -6.801  11.306   6.900  1.00  3.39           H  
ATOM    132  N   SER A  12      -6.747   9.498   4.646  1.00  1.86           N  
ATOM    133  CA  SER A  12      -7.215   8.292   3.648  1.00  1.65           C  
ATOM    134  C   SER A  12      -6.363   8.227   2.221  1.00  1.42           C  
ATOM    135  O   SER A  12      -6.079   9.302   1.637  1.00  1.55           O  
ATOM    136  CB  SER A  12      -8.831   8.495   3.409  1.00  1.98           C  
ATOM    137  OG  SER A  12      -9.430   7.345   2.721  1.00  2.53           O  
ATOM    138  H   SER A  12      -6.774  10.436   4.263  1.00  1.99           H  
ATOM    139  HA  SER A  12      -7.088   7.321   4.160  1.00  1.78           H  
ATOM    140  HB2 SER A  12      -9.333   8.590   4.373  1.00  2.42           H  
ATOM    141  HB3 SER A  12      -9.021   9.423   2.842  1.00  2.19           H  
ATOM    142  HG  SER A  12     -10.371   7.509   2.550  1.00  2.75           H  
ATOM    143  N   CYS A  13      -6.056   6.928   1.651  1.00  1.24           N  
ATOM    144  CA  CYS A  13      -5.322   6.599   0.222  1.00  1.27           C  
ATOM    145  C   CYS A  13      -6.329   5.859  -0.909  1.00  1.48           C  
ATOM    146  O   CYS A  13      -5.940   5.829  -2.097  1.00  1.97           O  
ATOM    147  CB  CYS A  13      -3.899   5.780   0.500  1.00  0.96           C  
ATOM    148  SG  CYS A  13      -3.947   3.994   1.084  1.00  1.08           S  
ATOM    149  H   CYS A  13      -6.365   6.123   2.153  1.00  1.24           H  
ATOM    150  HA  CYS A  13      -5.033   7.559  -0.234  1.00  1.57           H  
ATOM    151  HB2 CYS A  13      -3.342   5.772  -0.420  1.00  1.35           H  
ATOM    152  HB3 CYS A  13      -3.307   6.357   1.209  1.00  1.34           H  
ATOM    153  HG  CYS A  13      -4.124   4.008   2.025  1.00  1.60           H  
ATOM    154  N   THR A  14      -7.591   5.234  -0.518  1.00  1.74           N  
ATOM    155  CA  THR A  14      -8.700   4.430  -1.381  1.00  1.92           C  
ATOM    156  C   THR A  14      -8.285   2.834  -1.468  1.00  1.53           C  
ATOM    157  O   THR A  14      -8.691   2.104  -0.544  1.00  2.30           O  
ATOM    158  CB  THR A  14      -9.215   5.169  -2.860  1.00  2.55           C  
ATOM    159  OG1 THR A  14      -8.724   6.533  -3.062  1.00  3.07           O  
ATOM    160  CG2 THR A  14     -10.804   5.263  -3.013  1.00  3.08           C  
ATOM    161  H   THR A  14      -7.815   5.257   0.439  1.00  2.16           H  
ATOM    162  HA  THR A  14      -9.582   4.440  -0.700  1.00  2.08           H  
ATOM    163  HB  THR A  14      -8.871   4.560  -3.703  1.00  2.85           H  
ATOM    164  HG1 THR A  14      -7.899   6.516  -3.567  1.00  3.67           H  
ATOM    165 HG21 THR A  14     -11.210   5.970  -2.295  1.00  3.16           H  
ATOM    166 HG22 THR A  14     -11.256   4.303  -2.844  1.00  3.62           H  
ATOM    167 HG23 THR A  14     -11.065   5.588  -4.016  1.00  3.48           H  
ATOM    168  N   CYS A  15      -7.481   2.247  -2.568  1.00  0.87           N  
ATOM    169  CA  CYS A  15      -7.029   0.661  -2.781  1.00  0.86           C  
ATOM    170  C   CYS A  15      -8.421  -0.295  -2.892  1.00  1.29           C  
ATOM    171  O   CYS A  15      -8.788  -0.978  -1.899  1.00  1.70           O  
ATOM    172  CB  CYS A  15      -5.912   0.213  -1.584  1.00  0.85           C  
ATOM    173  SG  CYS A  15      -4.121   0.689  -1.870  1.00  1.18           S  
ATOM    174  H   CYS A  15      -7.186   2.861  -3.285  1.00  1.25           H  
ATOM    175  HA  CYS A  15      -6.559   0.596  -3.772  1.00  1.19           H  
ATOM    176  HB2 CYS A  15      -6.218   0.648  -0.643  1.00  0.97           H  
ATOM    177  HB3 CYS A  15      -5.936  -0.875  -1.463  1.00  1.25           H  
ATOM    178  HG  CYS A  15      -3.897   0.447  -2.771  1.00  1.33           H  
ATOM    179  N   THR A  16      -9.237  -0.189  -4.086  1.00  1.56           N  
ATOM    180  CA  THR A  16     -10.703  -0.886  -4.347  1.00  2.13           C  
ATOM    181  C   THR A  16     -10.613  -2.196  -5.357  1.00  1.96           C  
ATOM    182  O   THR A  16     -10.032  -3.205  -4.897  1.00  2.34           O  
ATOM    183  CB  THR A  16     -11.780   0.361  -4.785  1.00  2.87           C  
ATOM    184  OG1 THR A  16     -11.254   1.066  -5.988  1.00  3.52           O  
ATOM    185  CG2 THR A  16     -12.064   1.457  -3.627  1.00  3.11           C  
ATOM    186  H   THR A  16      -8.929   0.442  -4.809  1.00  1.59           H  
ATOM    187  HA  THR A  16     -11.083  -1.313  -3.399  1.00  2.53           H  
ATOM    188  HB  THR A  16     -12.744  -0.115  -5.046  1.00  3.41           H  
ATOM    189  HG1 THR A  16     -11.964   1.289  -6.627  1.00  3.78           H  
ATOM    190 HG21 THR A  16     -12.656   1.012  -2.843  1.00  3.60           H  
ATOM    191 HG22 THR A  16     -12.603   2.304  -4.033  1.00  3.33           H  
ATOM    192 HG23 THR A  16     -11.130   1.822  -3.203  1.00  3.22           H  
ATOM    193  N   SER A  17     -11.186  -2.228  -6.709  1.00  1.95           N  
ATOM    194  CA  SER A  17     -11.179  -3.506  -7.737  1.00  2.10           C  
ATOM    195  C   SER A  17      -9.686  -3.875  -8.344  1.00  1.56           C  
ATOM    196  O   SER A  17      -9.427  -5.087  -8.535  1.00  1.93           O  
ATOM    197  CB  SER A  17     -12.248  -3.201  -8.950  1.00  2.84           C  
ATOM    198  OG  SER A  17     -13.619  -3.019  -8.448  1.00  3.40           O  
ATOM    199  H   SER A  17     -11.635  -1.413  -7.038  1.00  2.21           H  
ATOM    200  HA  SER A  17     -11.563  -4.383  -7.190  1.00  2.56           H  
ATOM    201  HB2 SER A  17     -11.957  -2.306  -9.501  1.00  3.19           H  
ATOM    202  HB3 SER A  17     -12.255  -4.037  -9.654  1.00  3.22           H  
ATOM    203  HG  SER A  17     -13.775  -2.093  -8.173  1.00  3.69           H  
ATOM    204  N   SER A  18      -8.736  -2.820  -8.676  1.00  1.37           N  
ATOM    205  CA  SER A  18      -7.257  -3.005  -9.313  1.00  1.71           C  
ATOM    206  C   SER A  18      -6.128  -2.008  -8.591  1.00  1.37           C  
ATOM    207  O   SER A  18      -6.409  -0.783  -8.464  1.00  1.89           O  
ATOM    208  CB  SER A  18      -7.419  -2.779 -10.925  1.00  2.64           C  
ATOM    209  OG  SER A  18      -6.218  -3.200 -11.648  1.00  3.13           O  
ATOM    210  H   SER A  18      -9.013  -1.884  -8.519  1.00  1.61           H  
ATOM    211  HA  SER A  18      -6.941  -4.033  -9.149  1.00  2.02           H  
ATOM    212  HB2 SER A  18      -8.258  -3.387 -11.285  1.00  3.00           H  
ATOM    213  HB3 SER A  18      -7.651  -1.728 -11.134  1.00  2.81           H  
ATOM    214  HG  SER A  18      -6.363  -3.143 -12.607  1.00  3.51           H  
ATOM    215  N   CYS A  19      -4.870  -2.546  -8.151  1.00  0.93           N  
ATOM    216  CA  CYS A  19      -3.654  -1.721  -7.436  1.00  0.81           C  
ATOM    217  C   CYS A  19      -2.398  -1.547  -8.509  1.00  0.84           C  
ATOM    218  O   CYS A  19      -2.069  -2.546  -9.204  1.00  1.12           O  
ATOM    219  CB  CYS A  19      -3.259  -2.547  -6.021  1.00  1.10           C  
ATOM    220  SG  CYS A  19      -2.235  -1.625  -4.744  1.00  1.15           S  
ATOM    221  H   CYS A  19      -4.710  -3.524  -8.316  1.00  1.19           H  
ATOM    222  HA  CYS A  19      -4.015  -0.711  -7.167  1.00  1.04           H  
ATOM    223  HB2 CYS A  19      -4.171  -2.841  -5.508  1.00  1.92           H  
ATOM    224  HB3 CYS A  19      -2.730  -3.470  -6.276  1.00  1.63           H  
ATOM    225  HG  CYS A  19      -1.505  -2.193  -4.495  1.00  1.45           H  
ATOM    226  N   ALA A  20      -1.662  -0.306  -8.554  1.00  0.90           N  
ATOM    227  CA  ALA A  20      -0.359  -0.007  -9.477  1.00  1.09           C  
ATOM    228  C   ALA A  20       0.985   0.228  -8.530  1.00  1.03           C  
ATOM    229  O   ALA A  20       1.768   1.206  -8.726  1.00  1.22           O  
ATOM    230  CB  ALA A  20      -0.762   1.154 -10.527  1.00  1.37           C  
ATOM    231  H   ALA A  20      -1.920   0.417  -7.914  1.00  1.03           H  
ATOM    232  HA  ALA A  20      -0.125  -0.887 -10.065  1.00  1.22           H  
ATOM    233  HB1 ALA A  20      -1.019   2.076 -10.011  1.00  1.91           H  
ATOM    234  HB2 ALA A  20      -1.607   0.835 -11.126  1.00  1.73           H  
ATOM    235  HB3 ALA A  20       0.071   1.341 -11.198  1.00  1.63           H  
ATOM    236  N   CYS A  21       1.227  -0.740  -7.484  1.00  0.85           N  
ATOM    237  CA  CYS A  21       2.460  -0.762  -6.428  1.00  0.91           C  
ATOM    238  C   CYS A  21       3.265  -2.259  -6.581  1.00  0.93           C  
ATOM    239  O   CYS A  21       3.638  -2.580  -7.730  1.00  1.00           O  
ATOM    240  CB  CYS A  21       1.798  -0.470  -4.933  1.00  0.86           C  
ATOM    241  SG  CYS A  21       0.959   1.163  -4.529  1.00  0.96           S  
ATOM    242  H   CYS A  21       0.555  -1.487  -7.378  1.00  0.77           H  
ATOM    243  HA  CYS A  21       3.193   0.013  -6.658  1.00  1.06           H  
ATOM    244  HB2 CYS A  21       1.089  -1.256  -4.712  1.00  0.73           H  
ATOM    245  HB3 CYS A  21       2.602  -0.594  -4.238  1.00  0.99           H  
ATOM    246  HG  CYS A  21       0.042   0.989  -4.303  1.00  1.14           H  
ATOM    247  N   LYS A  22       3.516  -3.154  -5.446  1.00  0.96           N  
ATOM    248  CA  LYS A  22       4.194  -4.612  -5.447  1.00  1.04           C  
ATOM    249  C   LYS A  22       3.196  -5.597  -4.511  1.00  0.83           C  
ATOM    250  O   LYS A  22       2.595  -6.537  -5.072  1.00  0.81           O  
ATOM    251  CB  LYS A  22       5.756  -4.426  -4.901  1.00  1.26           C  
ATOM    252  CG  LYS A  22       6.755  -5.691  -5.235  1.00  1.57           C  
ATOM    253  CD  LYS A  22       8.092  -5.840  -4.304  1.00  1.74           C  
ATOM    254  CE  LYS A  22       9.134  -7.049  -4.694  1.00  2.38           C  
ATOM    255  NZ  LYS A  22       9.786  -6.911  -6.116  1.00  3.01           N  
ATOM    256  H   LYS A  22       3.236  -2.857  -4.565  1.00  0.95           H  
ATOM    257  HA  LYS A  22       4.197  -5.001  -6.468  1.00  1.20           H  
ATOM    258  HB2 LYS A  22       6.185  -3.534  -5.380  1.00  1.42           H  
ATOM    259  HB3 LYS A  22       5.721  -4.221  -3.828  1.00  1.20           H  
ATOM    260  HG2 LYS A  22       6.194  -6.621  -5.155  1.00  1.94           H  
ATOM    261  HG3 LYS A  22       7.061  -5.570  -6.273  1.00  1.72           H  
ATOM    262  HD2 LYS A  22       8.658  -4.920  -4.320  1.00  1.68           H  
ATOM    263  HD3 LYS A  22       7.771  -6.021  -3.278  1.00  2.18           H  
ATOM    264  HE2 LYS A  22       9.933  -7.029  -3.965  1.00  2.87           H  
ATOM    265  HE3 LYS A  22       8.631  -8.010  -4.616  1.00  2.47           H  
ATOM    266  HZ1 LYS A  22       9.063  -6.921  -6.877  1.00  3.69           H  
ATOM    267  HZ2 LYS A  22      10.420  -7.725  -6.269  1.00  3.03           H  
ATOM    268  HZ3 LYS A  22      10.360  -6.034  -6.189  1.00  3.23           H  
ATOM    269  N   ASN A  23       3.002  -5.284  -3.089  1.00  0.80           N  
ATOM    270  CA  ASN A  23       2.032  -6.037  -2.040  1.00  0.74           C  
ATOM    271  C   ASN A  23       1.162  -4.893  -1.156  1.00  0.92           C  
ATOM    272  O   ASN A  23      -0.054  -4.878  -1.289  1.00  1.40           O  
ATOM    273  CB  ASN A  23       2.978  -7.056  -1.129  1.00  1.03           C  
ATOM    274  CG  ASN A  23       2.185  -8.335  -0.494  1.00  1.29           C  
ATOM    275  OD1 ASN A  23       2.089  -9.364  -1.148  1.00  2.01           O  
ATOM    276  ND2 ASN A  23       1.570  -8.331   0.712  1.00  1.94           N  
ATOM    277  H   ASN A  23       3.503  -4.498  -2.732  1.00  0.89           H  
ATOM    278  HA  ASN A  23       1.306  -6.625  -2.623  1.00  0.76           H  
ATOM    279  HB2 ASN A  23       3.786  -7.446  -1.753  1.00  1.54           H  
ATOM    280  HB3 ASN A  23       3.455  -6.496  -0.326  1.00  1.71           H  
ATOM    281 HD21 ASN A  23       1.541  -7.528   1.299  1.00  2.32           H  
ATOM    282 HD22 ASN A  23       1.154  -9.163   1.031  1.00  2.52           H  
ATOM    283  N   CYS A  24       1.847  -3.924  -0.300  1.00  0.89           N  
ATOM    284  CA  CYS A  24       1.250  -2.713   0.662  1.00  1.08           C  
ATOM    285  C   CYS A  24       0.768  -3.259   2.158  1.00  1.19           C  
ATOM    286  O   CYS A  24       0.223  -4.381   2.219  1.00  1.55           O  
ATOM    287  CB  CYS A  24      -0.010  -1.728   0.093  1.00  1.00           C  
ATOM    288  SG  CYS A  24      -0.143  -1.237  -1.644  1.00  0.95           S  
ATOM    289  H   CYS A  24       2.839  -3.999  -0.273  1.00  1.04           H  
ATOM    290  HA  CYS A  24       2.108  -2.048   0.830  1.00  1.32           H  
ATOM    291  HB2 CYS A  24      -0.952  -2.146   0.328  1.00  1.03           H  
ATOM    292  HB3 CYS A  24       0.055  -0.801   0.654  1.00  1.13           H  
ATOM    293  HG  CYS A  24      -0.959  -0.739  -1.753  1.00  1.28           H  
ATOM    294  N   LYS A  25       0.823  -2.354   3.315  1.00  1.43           N  
ATOM    295  CA  LYS A  25       0.214  -2.643   4.794  1.00  1.60           C  
ATOM    296  C   LYS A  25      -1.173  -1.684   4.903  1.00  1.47           C  
ATOM    297  O   LYS A  25      -1.173  -0.671   5.655  1.00  1.71           O  
ATOM    298  CB  LYS A  25       1.430  -2.353   5.925  1.00  1.99           C  
ATOM    299  CG  LYS A  25       1.068  -2.807   7.461  1.00  2.45           C  
ATOM    300  CD  LYS A  25       2.167  -2.421   8.646  1.00  2.93           C  
ATOM    301  CE  LYS A  25       2.391  -3.562   9.809  1.00  3.42           C  
ATOM    302  NZ  LYS A  25       3.194  -4.807   9.297  1.00  4.45           N  
ATOM    303  H   LYS A  25       1.173  -1.422   3.148  1.00  1.77           H  
ATOM    304  HA  LYS A  25      -0.101  -3.698   4.873  1.00  1.63           H  
ATOM    305  HB2 LYS A  25       2.319  -2.900   5.625  1.00  2.31           H  
ATOM    306  HB3 LYS A  25       1.670  -1.291   5.908  1.00  2.37           H  
ATOM    307  HG2 LYS A  25       0.123  -2.335   7.738  1.00  2.69           H  
ATOM    308  HG3 LYS A  25       0.899  -3.884   7.446  1.00  2.89           H  
ATOM    309  HD2 LYS A  25       3.149  -2.167   8.230  1.00  3.12           H  
ATOM    310  HD3 LYS A  25       1.803  -1.527   9.145  1.00  3.18           H  
ATOM    311  HE2 LYS A  25       2.949  -3.116  10.624  1.00  3.72           H  
ATOM    312  HE3 LYS A  25       1.429  -3.892  10.206  1.00  3.29           H  
ATOM    313  HZ1 LYS A  25       2.707  -5.275   8.489  1.00  4.67           H  
ATOM    314  HZ2 LYS A  25       3.268  -5.505  10.073  1.00  4.90           H  
ATOM    315  HZ3 LYS A  25       4.170  -4.539   9.012  1.00  4.86           H  
ATOM    316  N   CYS A  26      -2.312  -1.986   4.049  1.00  1.16           N  
ATOM    317  CA  CYS A  26      -3.688  -1.106   3.926  1.00  1.12           C  
ATOM    318  C   CYS A  26      -5.020  -1.985   4.449  1.00  1.21           C  
ATOM    319  O   CYS A  26      -4.985  -2.331   5.654  1.00  1.68           O  
ATOM    320  CB  CYS A  26      -3.728  -0.505   2.354  1.00  0.94           C  
ATOM    321  SG  CYS A  26      -2.498   0.844   1.898  1.00  0.99           S  
ATOM    322  H   CYS A  26      -2.240  -2.765   3.426  1.00  1.04           H  
ATOM    323  HA  CYS A  26      -3.656  -0.243   4.625  1.00  1.28           H  
ATOM    324  HB2 CYS A  26      -3.569  -1.325   1.667  1.00  0.86           H  
ATOM    325  HB3 CYS A  26      -4.718  -0.110   2.165  1.00  1.01           H  
ATOM    326  HG  CYS A  26      -2.430   1.447   2.640  1.00  1.39           H  
ATOM    327  N   THR A  27      -6.201  -2.311   3.621  1.00  1.26           N  
ATOM    328  CA  THR A  27      -7.541  -3.115   4.125  1.00  1.35           C  
ATOM    329  C   THR A  27      -7.474  -4.668   3.570  1.00  1.30           C  
ATOM    330  O   THR A  27      -6.959  -5.511   4.341  1.00  1.85           O  
ATOM    331  CB  THR A  27      -8.935  -2.226   3.726  1.00  1.34           C  
ATOM    332  OG1 THR A  27      -9.218  -2.130   2.272  1.00  1.35           O  
ATOM    333  CG2 THR A  27      -9.034  -0.749   4.393  1.00  1.94           C  
ATOM    334  H   THR A  27      -6.209  -2.005   2.678  1.00  1.58           H  
ATOM    335  HA  THR A  27      -7.523  -3.194   5.220  1.00  1.66           H  
ATOM    336  HB  THR A  27      -9.770  -2.789   4.136  1.00  1.65           H  
ATOM    337  HG1 THR A  27      -8.441  -1.885   1.730  1.00  1.66           H  
ATOM    338 HG21 THR A  27      -8.940  -0.809   5.478  1.00  2.19           H  
ATOM    339 HG22 THR A  27      -9.989  -0.300   4.159  1.00  2.36           H  
ATOM    340 HG23 THR A  27      -8.246  -0.121   4.001  1.00  2.53           H  
ATOM    341  N   SER A  28      -7.882  -5.057   2.215  1.00  1.05           N  
ATOM    342  CA  SER A  28      -7.722  -6.571   1.586  1.00  1.30           C  
ATOM    343  C   SER A  28      -6.183  -6.843   0.976  1.00  1.34           C  
ATOM    344  O   SER A  28      -5.923  -7.991   0.530  1.00  1.79           O  
ATOM    345  CB  SER A  28      -8.937  -6.814   0.505  1.00  1.41           C  
ATOM    346  OG  SER A  28      -9.026  -8.219   0.078  1.00  2.01           O  
ATOM    347  H   SER A  28      -8.202  -4.338   1.598  1.00  1.11           H  
ATOM    348  HA  SER A  28      -7.858  -7.303   2.397  1.00  1.59           H  
ATOM    349  HB2 SER A  28      -9.882  -6.578   0.977  1.00  1.56           H  
ATOM    350  HB3 SER A  28      -8.814  -6.150  -0.355  1.00  1.54           H  
ATOM    351  HG  SER A  28      -8.583  -8.346  -0.780  1.00  2.39           H  
ATOM    352  N   CYS A  29      -5.126  -5.820   1.053  1.00  1.04           N  
ATOM    353  CA  CYS A  29      -3.570  -5.949   0.582  1.00  1.22           C  
ATOM    354  C   CYS A  29      -2.813  -6.893   1.742  1.00  1.51           C  
ATOM    355  O   CYS A  29      -2.501  -8.065   1.422  1.00  1.77           O  
ATOM    356  CB  CYS A  29      -2.964  -4.388   0.383  1.00  1.12           C  
ATOM    357  SG  CYS A  29      -3.534  -3.477  -1.182  1.00  0.93           S  
ATOM    358  H   CYS A  29      -5.346  -4.964   1.488  1.00  0.88           H  
ATOM    359  HA  CYS A  29      -3.531  -6.491  -0.379  1.00  1.34           H  
ATOM    360  HB2 CYS A  29      -3.263  -3.775   1.235  1.00  1.15           H  
ATOM    361  HB3 CYS A  29      -1.899  -4.417   0.392  1.00  1.33           H  
ATOM    362  HG  CYS A  29      -4.480  -3.325  -1.104  1.00  0.96           H  
ATOM    363  N   LYS A  30      -2.694  -6.423   3.120  1.00  1.57           N  
ATOM    364  CA  LYS A  30      -2.172  -7.274   4.432  1.00  1.90           C  
ATOM    365  C   LYS A  30      -2.640  -6.564   5.842  1.00  2.52           C  
ATOM    366  O   LYS A  30      -2.462  -5.355   5.988  1.00  2.88           O  
ATOM    367  CB  LYS A  30      -0.536  -7.637   4.380  1.00  2.05           C  
ATOM    368  CG  LYS A  30      -0.058  -8.808   5.459  1.00  2.69           C  
ATOM    369  CD  LYS A  30       1.373  -9.577   5.186  1.00  3.33           C  
ATOM    370  CE  LYS A  30       1.338 -11.192   5.539  1.00  4.14           C  
ATOM    371  NZ  LYS A  30       2.727 -11.880   5.371  1.00  4.90           N  
ATOM    372  OXT LYS A  30      -3.136  -7.272   6.732  1.00  3.22           O  
ATOM    373  H   LYS A  30      -3.071  -5.513   3.301  1.00  1.48           H  
ATOM    374  HA  LYS A  30      -2.717  -8.231   4.373  1.00  2.46           H  
ATOM    375  HB2 LYS A  30      -0.323  -7.987   3.372  1.00  2.34           H  
ATOM    376  HB3 LYS A  30       0.055  -6.740   4.544  1.00  2.35           H  
ATOM    377  HG2 LYS A  30      -0.003  -8.333   6.433  1.00  3.12           H  
ATOM    378  HG3 LYS A  30      -0.858  -9.554   5.517  1.00  2.94           H  
ATOM    379  HD2 LYS A  30       1.686  -9.472   4.148  1.00  3.45           H  
ATOM    380  HD3 LYS A  30       2.133  -9.112   5.806  1.00  3.69           H  
ATOM    381  HE2 LYS A  30       1.025 -11.335   6.573  1.00  4.53           H  
ATOM    382  HE3 LYS A  30       0.616 -11.693   4.885  1.00  4.23           H  
ATOM    383  HZ1 LYS A  30       2.620 -12.902   5.584  1.00  5.37           H  
ATOM    384  HZ2 LYS A  30       3.426 -11.487   6.049  1.00  5.05           H  
ATOM    385  HZ3 LYS A  30       3.098 -11.792   4.390  1.00  5.17           H  
TER     386      LYS A  30                                                      
HETATM  387 CD    CD A  31      -2.609  -1.347  -2.247  1.00  0.72          CD  
HETATM  388 CD    CD A  32       0.642   1.159  -1.972  1.00  0.95          CD  
HETATM  389 CD    CD A  33      -2.806   2.152  -0.247  1.00  0.99          CD  
CONECT   65  388                                                                
CONECT   87  388  389                                                           
CONECT  148  389                                                                
CONECT  173  387  389                                                           
CONECT  220  387                                                                
CONECT  241  388                                                                
CONECT  288  387  388                                                           
CONECT  321  389                                                                
CONECT  357  387                                                                
CONECT  387  173  220  288  357                                                 
CONECT  388   65   87  241  288                                                 
CONECT  389   87  148  173  321                                                 
MASTER      237    0    3    0    0    0    3    6  201    1   12    3          
END