CNRS Nantes University US2B US2B
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***  HYDROLASE 01-FEB-75 1LYZ  ***

elNémo ID: 2404221630241904959

Job options:

ID        	=	 2404221630241904959
JOBID     	=	 HYDROLASE 01-FEB-75 1LYZ
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    HYDROLASE                               01-FEB-75   1LYZ              
TITLE     REAL-SPACE REFINEMENT OF THE STRUCTURE OF HEN EGG-WHITE LYSOZYME      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEN EGG WHITE LYSOZYME;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.2.1.17;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GALLUS GALLUS                                   
KEYWDS    HYDROLASE (O-GLYCOSYL), HYDROLASE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.DIAMOND,D.C.PHILLIPS,C.C.F.BLAKE,A.C.T.NORTH                        
REVDAT  12   29-NOV-17 1LYZ    1       HELIX                                    
REVDAT  11   24-FEB-09 1LYZ    1       VERSN                                    
REVDAT  10   16-OCT-87 1LYZ    1       FTNOTE TURN                              
REVDAT   9   25-APR-86 1LYZ    3       SOURCE SEQRES ATOM                       
REVDAT   8   07-FEB-84 1LYZ    1       FTNOTE                                   
REVDAT   7   30-SEP-83 1LYZ    1       REVDAT                                   
REVDAT   6   01-MAR-82 1LYZ    1       REMARK                                   
REVDAT   5   20-APR-81 1LYZ    1       SHEET                                    
REVDAT   4   31-DEC-80 1LYZ    1       REMARK                                   
REVDAT   3   01-NOV-77 1LYZ    1       COMPND SOURCE AUTHOR JRNL                
REVDAT   3 2                   1       REMARK FORMUL SSBOND                     
REVDAT   2   16-MAY-77 1LYZ    3       SEQRES ATOM                              
REVDAT   1   12-APR-77 1LYZ    0                                                
JRNL        AUTH   R.DIAMOND                                                    
JRNL        TITL   REAL-SPACE REFINEMENT OF THE STRUCTURE OF HEN EGG-WHITE      
JRNL        TITL 2 LYSOZYME.                                                    
JRNL        REF    J.MOL.BIOL.                   V.  82   371 1974              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   4856347                                                      
JRNL        DOI    10.1016/0022-2836(74)90598-1                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   D.C.PHILLIPS                                                 
REMARK   1  TITL   CRYSTALLOGRAPHIC STUDIES OF LYSOZYME AND ITS INTERACTIONS    
REMARK   1  TITL 2 WITH INHIBITORS AND SUBSTRATES                               
REMARK   1  EDIT   E.F.OSSERMAN, R.F.CANFIELD, S.BEYCHOK                        
REMARK   1  REF    LYSOZYME                                 9 1974              
REMARK   1  PUBL   ACADEMIC PRESS,NEW YORK                                      
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   T.IMOTO,L.N.JOHNSON,A.C.T.NORTH,D.C.PHILLIPS,J.A.RUPLEY      
REMARK   1  TITL   VERTEBRATE LYSOZYMES                                         
REMARK   1  EDIT   P.BOYER                                                      
REMARK   1  REF    THE ENZYMES,THIRD EDITION     V.   7   665 1972              
REMARK   1  PUBL   ACADEMIC PRESS,NEW YORK                                      
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   C.R.BEDDELL,C.C.F.BLAKE,S.J.OATLEY                           
REMARK   1  TITL   AN X-RAY STUDY OF THE STRUCTURE AND BINDING PROPERTIES OF    
REMARK   1  TITL 2 IODINE-INACTIVATED LYSOZYME                                  
REMARK   1  REF    J.MOL.BIOL.                   V.  97   643 1975              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   M.LEVITT                                                     
REMARK   1  TITL   ENERGY REFINEMENT OF HEN EGG-WHITE LYSOZYME                  
REMARK   1  REF    J.MOL.BIOL.                   V.  82   393 1974              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   C.C.F.BLAKE,G.A.MAIR,A.C.T.NORTH,D.C.PHILLIPS,V.R.SARMA      
REMARK   1  TITL   ON THE CONFORMATION OF THE HEN EGG-WHITE LYSOZYME MOLECULE   
REMARK   1  REF    PROC.R.SOC.LONDON,SER.B       V. 167   365 1967              
REMARK   1  REFN                   ISSN 0080-4649                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   C.C.F.BLAKE,L.N.JOHNSON,G.A.MAIR,A.C.T.NORTH,D.C.PHILLIPS,   
REMARK   1  AUTH 2 V.R.SARMA                                                    
REMARK   1  TITL   CRYSTALLOGRAPHIC STUDIES OF THE ACTIVITY OF HEN EGG-WHITE    
REMARK   1  TITL 2 LYSOZYME                                                     
REMARK   1  REF    PROC.R.SOC.LONDON,SER.B       V. 167   378 1967              
REMARK   1  REFN                   ISSN 0080-4649                               
REMARK   1 REFERENCE 7                                                          
REMARK   1  AUTH   D.C.PHILLIPS                                                 
REMARK   1  TITL   THE THREE-DIMENSIONAL STRUCTURE OF AN ENZYME MOLECULE        
REMARK   1  REF    SCI.AM.                       V. 215    78 1966              
REMARK   1  REFN                   ISSN 0036-8733                               
REMARK   1 REFERENCE 8                                                          
REMARK   1  AUTH   C.C.F.BLAKE,D.F.KOENIG,G.A.MAIR,A.C.T.NORTH,D.C.PHILLIPS,    
REMARK   1  AUTH 2 V.R.SARMA                                                    
REMARK   1  TITL   STRUCTURE OF HEN EGG-WHITE LYSOZYME, A THREE-DIMENSIONAL     
REMARK   1  TITL 2 FOURIER SYNTHESIS AT 2 ANGSTROMS RESOLUTION                  
REMARK   1  REF    NATURE                        V. 206   757 1965              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1 REFERENCE 9                                                          
REMARK   1  AUTH   L.N.JOHNSON,D.C.PHILLIPS                                     
REMARK   1  TITL   STRUCTURE OF SOME CRYSTALLINE LYSOZYME-INHIBITOR COMPLEXES   
REMARK   1  TITL 2 DETERMINED BY X-RAY ANALYSIS AT 6 ANGSTROMS RESOLUTION       
REMARK   1  REF    NATURE                        V. 206   761 1965              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1 REFERENCE 10                                                         
REMARK   1  EDIT   R.J.FELDMANN                                                 
REMARK   1  REF    ATLAS OF MACROMOLECULAR                492 1976              
REMARK   1  REF  2 STRUCTURE ON MICROFICHE                                      
REMARK   1  PUBL   TRACOR JITCO INC.,ROCKVILLE,MD.                              
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 11                                                         
REMARK   1  EDIT   M.O.DAYHOFF                                                  
REMARK   1  REF    ATLAS OF PROTEIN SEQUENCE     V.   5   138 1972              
REMARK   1  REF  2 AND STRUCTURE (DATA SECTION)                                 
REMARK   1  PUBL   NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER SPRING,MD.   
REMARK   1  REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : NULL                                                 
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1001                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 101                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE TEMPERATURE FACTOR FIELDS OF THIS     
REMARK   3  ENTRY CONTAIN ELECTRON COUNTS INSTEAD, IN THE FORM THEY WERE        
REMARK   3  DEPOSITED.                                                          
REMARK   4                                                                      
REMARK   4 1LYZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000174873.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       18.95000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       39.55000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       39.55000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       28.42500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       39.55000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       39.55000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        9.47500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       39.55000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       39.55000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       28.42500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       39.55000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       39.55000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        9.47500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       18.95000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 218  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CB   ALA A   122     NH1  ARG A   125              1.36            
REMARK 500   NE2  GLN A   121     O    HOH A   144              1.39            
REMARK 500   OD1  ASP A   101     O    HOH A   228              1.58            
REMARK 500   O    LYS A    97     OD1  ASP A   101              1.60            
REMARK 500   O    ALA A    10     N    ALA A    11              1.66            
REMARK 500   OD1  ASP A   119     NH2  ARG A   125              1.67            
REMARK 500   O    CYS A    30     N    ALA A    31              1.76            
REMARK 500   CD   GLN A   121     O    HOH A   144              1.86            
REMARK 500   OG   SER A    24     O    HOH A   153              1.95            
REMARK 500   O    ASN A   106     NH2  ARG A   112              2.01            
REMARK 500   NH1  ARG A     5     O    TRP A   123              2.01            
REMARK 500   CB   ALA A   122     CZ   ARG A   125              2.02            
REMARK 500   CB   ASP A   101     O    HOH A   227              2.02            
REMARK 500   CA   ALA A   122     NE   ARG A   125              2.08            
REMARK 500   O    HOH A   186     O    HOH A   187A             2.08            
REMARK 500   CD1  TRP A    63     O    HOH A   206              2.12            
REMARK 500   O    HOH A   226     O    HOH A   227              2.12            
REMARK 500   O    HOH A   161     O    HOH A   163              2.12            
REMARK 500   O    HOH A   156     O    HOH A   157              2.13            
REMARK 500   O    HOH A   159     O    HOH A   160              2.18            
REMARK 500   CA   ALA A   122     CZ   ARG A   125              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   193     O    HOH A   213     6456     0.06            
REMARK 500   O    HOH A   141     O    HOH A   185     8555     0.13            
REMARK 500   O    HOH A   138A    O    HOH A   220     4454     0.16            
REMARK 500   CD   ARG A   128     O    HOH A   186     8555     0.89            
REMARK 500   NE   ARG A   128     O    HOH A   186     8555     1.69            
REMARK 500   CG2  THR A    47     NE   ARG A   128     3555     2.03            
REMARK 500   CG2  THR A    47     NH2  ARG A   128     3555     2.19            
REMARK 500   CG   ARG A   128     O    HOH A   186     8555     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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     -0.139                       
REMARK 500    LYS A   1   CA    LYS A   1   CB      0.485                       
REMARK 500    LYS A   1   CB    LYS A   1   CG     -0.575                       
REMARK 500    LYS A   1   CA    LYS A   1   C       0.364                       
REMARK 500    LYS A   1   C     VAL A   2   N       0.300                       
REMARK 500    VAL A   2   CB    VAL A   2   CG1    -0.127                       
REMARK 500    VAL A   2   C     VAL A   2   O      -0.119                       
REMARK 500    VAL A   2   C     PHE A   3   N       0.202                       
REMARK 500    PHE A   3   N     PHE A   3   CA     -0.169                       
REMARK 500    PHE A   3   CB    PHE A   3   CG     -0.587                       
REMARK 500    PHE A   3   CG    PHE A   3   CD2    -0.257                       
REMARK 500    PHE A   3   CG    PHE A   3   CD1     0.466                       
REMARK 500    PHE A   3   CD1   PHE A   3   CE1    -0.221                       
REMARK 500    PHE A   3   CZ    PHE A   3   CE2     0.338                       
REMARK 500    PHE A   3   CA    PHE A   3   C       0.311                       
REMARK 500    PHE A   3   C     PHE A   3   O      -0.385                       
REMARK 500    PHE A   3   C     GLY A   4   N       0.243                       
REMARK 500    GLY A   4   N     GLY A   4   CA     -0.124                       
REMARK 500    GLY A   4   CA    GLY A   4   C       0.328                       
REMARK 500    ARG A   5   N     ARG A   5   CA     -0.294                       
REMARK 500    ARG A   5   CA    ARG A   5   CB     -0.134                       
REMARK 500    ARG A   5   CG    ARG A   5   CD     -0.229                       
REMARK 500    ARG A   5   NE    ARG A   5   CZ     -0.510                       
REMARK 500    ARG A   5   CZ    ARG A   5   NH2     0.593                       
REMARK 500    ARG A   5   CA    ARG A   5   C      -0.298                       
REMARK 500    ARG A   5   C     CYS A   6   N       0.274                       
REMARK 500    CYS A   6   N     CYS A   6   CA      0.222                       
REMARK 500    CYS A   6   CA    CYS A   6   CB     -0.255                       
REMARK 500    CYS A   6   CB    CYS A   6   SG      0.144                       
REMARK 500    CYS A   6   CA    CYS A   6   C       0.331                       
REMARK 500    CYS A   6   C     CYS A   6   O      -0.229                       
REMARK 500    CYS A   6   C     GLU A   7   N       0.214                       
REMARK 500    GLU A   7   CA    GLU A   7   CB     -0.458                       
REMARK 500    GLU A   7   CB    GLU A   7   CG      0.296                       
REMARK 500    GLU A   7   CD    GLU A   7   OE1     0.269                       
REMARK 500    GLU A   7   CD    GLU A   7   OE2     0.094                       
REMARK 500    GLU A   7   C     LEU A   8   N      -0.209                       
REMARK 500    LEU A   8   CB    LEU A   8   CG     -0.535                       
REMARK 500    LEU A   8   CG    LEU A   8   CD1     0.361                       
REMARK 500    LEU A   8   CG    LEU A   8   CD2     0.292                       
REMARK 500    LEU A   8   CA    LEU A   8   C      -0.264                       
REMARK 500    ALA A   9   N     ALA A   9   CA     -0.232                       
REMARK 500    ALA A   9   CA    ALA A   9   CB     -0.150                       
REMARK 500    ALA A   9   CA    ALA A   9   C      -0.319                       
REMARK 500    ALA A  10   N     ALA A  10   CA      0.171                       
REMARK 500    ALA A  10   CA    ALA A  10   CB      0.289                       
REMARK 500    ALA A  10   C     ALA A  11   N      -0.598                       
REMARK 500    MET A  12   C     MET A  12   O       0.381                       
REMARK 500    LYS A  13   N     LYS A  13   CA      0.166                       
REMARK 500    LYS A  13   CA    LYS A  13   CB      0.234                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     444 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    LYS A   1   CB  -  CA  -  C   ANGL. DEV. = -25.9 DEGREES          
REMARK 500    LYS A   1   N   -  CA  -  CB  ANGL. DEV. =  42.6 DEGREES          
REMARK 500    LYS A   1   CA  -  CB  -  CG  ANGL. DEV. =  28.1 DEGREES          
REMARK 500    LYS A   1   CD  -  CE  -  NZ  ANGL. DEV. =  22.7 DEGREES          
REMARK 500    LYS A   1   CA  -  C   -  O   ANGL. DEV. = -15.0 DEGREES          
REMARK 500    LYS A   1   CA  -  C   -  N   ANGL. DEV. =  18.4 DEGREES          
REMARK 500    VAL A   2   CB  -  CA  -  C   ANGL. DEV. =  13.0 DEGREES          
REMARK 500    VAL A   2   N   -  CA  -  CB  ANGL. DEV. = -29.7 DEGREES          
REMARK 500    VAL A   2   CA  -  CB  -  CG1 ANGL. DEV. = -15.9 DEGREES          
REMARK 500    VAL A   2   CA  -  C   -  N   ANGL. DEV. = -14.6 DEGREES          
REMARK 500    PHE A   3   CB  -  CA  -  C   ANGL. DEV. =  25.9 DEGREES          
REMARK 500    PHE A   3   CA  -  CB  -  CG  ANGL. DEV. =  23.5 DEGREES          
REMARK 500    PHE A   3   CB  -  CG  -  CD2 ANGL. DEV. =  24.1 DEGREES          
REMARK 500    PHE A   3   CB  -  CG  -  CD1 ANGL. DEV. = -20.8 DEGREES          
REMARK 500    PHE A   3   CG  -  CD2 -  CE2 ANGL. DEV. =  13.4 DEGREES          
REMARK 500    PHE A   3   CD1 -  CE1 -  CZ  ANGL. DEV. = -10.7 DEGREES          
REMARK 500    PHE A   3   CZ  -  CE2 -  CD2 ANGL. DEV. = -13.3 DEGREES          
REMARK 500    PHE A   3   CA  -  C   -  N   ANGL. DEV. = -21.1 DEGREES          
REMARK 500    PHE A   3   O   -  C   -  N   ANGL. DEV. =  15.3 DEGREES          
REMARK 500    GLY A   4   C   -  N   -  CA  ANGL. DEV. = -14.4 DEGREES          
REMARK 500    GLY A   4   CA  -  C   -  O   ANGL. DEV. = -31.2 DEGREES          
REMARK 500    GLY A   4   O   -  C   -  N   ANGL. DEV. =  38.7 DEGREES          
REMARK 500    ARG A   5   CB  -  CA  -  C   ANGL. DEV. = -17.5 DEGREES          
REMARK 500    ARG A   5   CG  -  CD  -  NE  ANGL. DEV. =  23.6 DEGREES          
REMARK 500    ARG A   5   NH1 -  CZ  -  NH2 ANGL. DEV. = -36.7 DEGREES          
REMARK 500    ARG A   5   NE  -  CZ  -  NH1 ANGL. DEV. =  22.6 DEGREES          
REMARK 500    ARG A   5   NE  -  CZ  -  NH2 ANGL. DEV. =  10.8 DEGREES          
REMARK 500    ARG A   5   N   -  CA  -  C   ANGL. DEV. = -18.5 DEGREES          
REMARK 500    ARG A   5   CA  -  C   -  O   ANGL. DEV. =  23.7 DEGREES          
REMARK 500    ARG A   5   O   -  C   -  N   ANGL. DEV. = -29.0 DEGREES          
REMARK 500    CYS A   6   CA  -  CB  -  SG  ANGL. DEV. = -10.8 DEGREES          
REMARK 500    CYS A   6   CA  -  C   -  O   ANGL. DEV. =  33.5 DEGREES          
REMARK 500    CYS A   6   O   -  C   -  N   ANGL. DEV. = -27.3 DEGREES          
REMARK 500    GLU A   7   OE1 -  CD  -  OE2 ANGL. DEV. = -37.4 DEGREES          
REMARK 500    GLU A   7   CG  -  CD  -  OE1 ANGL. DEV. =  23.4 DEGREES          
REMARK 500    GLU A   7   O   -  C   -  N   ANGL. DEV. = -18.3 DEGREES          
REMARK 500    LEU A   8   C   -  N   -  CA  ANGL. DEV. =  32.7 DEGREES          
REMARK 500    LEU A   8   N   -  CA  -  CB  ANGL. DEV. =  19.5 DEGREES          
REMARK 500    LEU A   8   CD1 -  CG  -  CD2 ANGL. DEV. = -20.8 DEGREES          
REMARK 500    LEU A   8   CB  -  CG  -  CD2 ANGL. DEV. =  21.0 DEGREES          
REMARK 500    ALA A  10   CB  -  CA  -  C   ANGL. DEV. = -12.9 DEGREES          
REMARK 500    ALA A  11   N   -  CA  -  CB  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    ALA A  11   CA  -  C   -  N   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ALA A  11   O   -  C   -  N   ANGL. DEV. =  16.2 DEGREES          
REMARK 500    LYS A  13   CB  -  CA  -  C   ANGL. DEV. =  13.8 DEGREES          
REMARK 500    LYS A  13   N   -  CA  -  CB  ANGL. DEV. = -23.0 DEGREES          
REMARK 500    LYS A  13   CA  -  CB  -  CG  ANGL. DEV. = -20.8 DEGREES          
REMARK 500    LYS A  13   CD  -  CE  -  NZ  ANGL. DEV. = -28.0 DEGREES          
REMARK 500    LYS A  13   N   -  CA  -  C   ANGL. DEV. =  31.0 DEGREES          
REMARK 500    LYS A  13   CA  -  C   -  N   ANGL. DEV. = -26.6 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     400 ANGLE DEVIATIONS.                             
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    ARG A   5      -77.02    -56.42                                   
REMARK 500    CYS A   6      -46.50    -29.81                                   
REMARK 500    LYS A  13      -73.21    -42.04                                   
REMARK 500    ARG A  14      -56.52    -16.22                                   
REMARK 500    ASN A  19       -0.51     59.08                                   
REMARK 500    LEU A  25      -26.71    -36.37                                   
REMARK 500    PHE A  38       -3.98     82.80                                   
REMARK 500    ASN A  46     -142.28    -98.36                                   
REMARK 500    ASP A  48       35.44    -92.64                                   
REMARK 500    SER A  50      105.36      9.91                                   
REMARK 500    GLN A  57       51.88     35.45                                   
REMARK 500    TRP A  62      -41.75   -136.24                                   
REMARK 500    ASP A  66       23.96   -159.98                                   
REMARK 500    CYS A  80      -67.99    -10.62                                   
REMARK 500    ILE A  88        3.00    -57.06                                   
REMARK 500    THR A  89      -73.63    -47.30                                   
REMARK 500    ALA A  90      -78.47     -9.16                                   
REMARK 500    ALA A 107      -14.95    -45.07                                   
REMARK 500    CYS A 115      -36.50   -136.72                                   
REMARK 500    ASP A 119       75.54   -102.08                                   
REMARK 500    ARG A 128       99.14    -68.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 MET A   12     LYS A   13                  148.32                    
REMARK 500 LYS A   13     ARG A   14                  144.85                    
REMARK 500 LEU A   17     ASP A   18                 -147.18                    
REMARK 500 TYR A   20     ARG A   21                 -149.87                    
REMARK 500 TYR A   23     SER A   24                  139.93                    
REMARK 500 ALA A   31     ALA A   32                 -128.44                    
REMARK 500 TYR A   53     GLY A   54                  146.26                    
REMARK 500 ILE A   55     LEU A   56                 -145.42                    
REMARK 500 ASP A   66     GLY A   67                  134.64                    
REMARK 500 CYS A   76     ASN A   77                  148.07                    
REMARK 500 SER A   85     SER A   86                 -137.42                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A   5         0.09    SIDE CHAIN                              
REMARK 500    GLU A   7         0.15    SIDE CHAIN                              
REMARK 500    TYR A  20         0.11    SIDE CHAIN                              
REMARK 500    ARG A  21         0.18    SIDE CHAIN                              
REMARK 500    PHE A  34         0.07    SIDE CHAIN                              
REMARK 500    GLU A  35         0.07    SIDE CHAIN                              
REMARK 500    PHE A  38         0.09    SIDE CHAIN                              
REMARK 500    ASN A  44         0.10    SIDE CHAIN                              
REMARK 500    TYR A  53         0.08    SIDE CHAIN                              
REMARK 500    ARG A  61         0.12    SIDE CHAIN                              
REMARK 500    ASN A 103         0.08    SIDE CHAIN                              
REMARK 500    ARG A 114         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    LYS A   1         12.40                                           
REMARK 500    VAL A   2        -11.76                                           
REMARK 500    ARG A   5         15.03                                           
REMARK 500    GLU A   7        -12.76                                           
REMARK 500    MET A  12        -10.79                                           
REMARK 500    ARG A  14        -16.75                                           
REMARK 500    LEU A  17         27.10                                           
REMARK 500    ASP A  18         20.28                                           
REMARK 500    TYR A  20         16.16                                           
REMARK 500    GLY A  22        -10.46                                           
REMARK 500    TYR A  23        -29.62                                           
REMARK 500    SER A  24         15.76                                           
REMARK 500    CYS A  30        -29.88                                           
REMARK 500    ASN A  37        -16.46                                           
REMARK 500    ALA A  42         13.05                                           
REMARK 500    ASN A  46        -31.79                                           
REMARK 500    SER A  50         16.27                                           
REMARK 500    ASP A  52         18.81                                           
REMARK 500    TYR A  53        -18.56                                           
REMARK 500    LEU A  56        -13.41                                           
REMARK 500    SER A  60        -14.12                                           
REMARK 500    ASP A  66        -27.26                                           
REMARK 500    PRO A  70        -15.78                                           
REMARK 500    ARG A  73         16.03                                           
REMARK 500    CYS A  76        -17.06                                           
REMARK 500    SER A  85         26.49                                           
REMARK 500    SER A  86        -11.42                                           
REMARK 500    ASP A  87         15.62                                           
REMARK 500    ASN A  93        -12.63                                           
REMARK 500    ALA A  95         11.64                                           
REMARK 500    LYS A  96        -16.88                                           
REMARK 500    SER A 100        -14.14                                           
REMARK 500    GLN A 121        -10.40                                           
REMARK 500    TRP A 123         19.59                                           
REMARK 500    CYS A 127         12.84                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1LYZ A    1   129  UNP    P00698   LYSC_CHICK      19    147             
SEQRES   1 A  129  LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS          
SEQRES   2 A  129  ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY          
SEQRES   3 A  129  ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN          
SEQRES   4 A  129  THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP          
SEQRES   5 A  129  TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN          
SEQRES   6 A  129  ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE          
SEQRES   7 A  129  PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER          
SEQRES   8 A  129  VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY          
SEQRES   9 A  129  MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY          
SEQRES  10 A  129  THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU              
FORMUL   2  HOH   *101(H2 O)                                                    
HELIX    1   A ARG A    5  HIS A   15  1                                  11    
HELIX    2   B LEU A   25  GLU A   35  1                                  11    
HELIX    3   C CYS A   80  LEU A   84  5                                   5    
HELIX    4   D THR A   89  LYS A   96  1                                   8    
SHEET    1  S1 2 LYS A   1  PHE A   3  0                                        
SHEET    2  S1 2 PHE A  38  THR A  40 -1  N  THR A  40   O  LYS A   1           
SHEET    1  S2 3 ALA A  42  ASN A  46  0                                        
SHEET    2  S2 3 SER A  50  GLY A  54 -1  N  ASN A  46   O  SER A  50           
SHEET    3  S2 3 GLN A  57  SER A  60 -1  N  TYR A  53   O  ILE A  58           
SSBOND   1 CYS A    6    CYS A  127                          1555   1555  2.06  
SSBOND   2 CYS A   30    CYS A  115                          1555   1555  2.42  
SSBOND   3 CYS A   64    CYS A   80                          1555   1555  2.34  
SSBOND   4 CYS A   76    CYS A   94                          1555   1555  2.22  
CRYST1   79.100   79.100   37.900  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.517067  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.517067  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.583113        0.00000                         
SCALE1      0.012642  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012642  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.026385        0.00000                         
ATOM      1  N   LYS A   1       3.296   9.888  10.739  1.00  7.00           N  
ATOM      2  CA  LYS A   1       2.439  10.217   9.791  1.00  6.00           C  
ATOM      3  C   LYS A   1       2.439  11.997   9.160  1.00  6.00           C  
ATOM      4  O   LYS A   1       2.637  12.656  10.107  1.00  8.00           O  
ATOM      5  CB  LYS A   1       0.659  10.086   8.844  1.00  6.00           C  
ATOM      6  CG  LYS A   1       0.198  10.415   8.086  1.00  6.00           C  
ATOM      7  CD  LYS A   1      -1.187  10.086   8.212  1.00  6.00           C  
ATOM      8  CE  LYS A   1      -2.175  10.086   7.264  1.00  6.00           C  
ATOM      9  NZ  LYS A   1      -3.527   9.869   7.288  1.00  7.00           N  
ATOM     10  N   VAL A   2       2.637  12.722   7.707  1.00  7.00           N  
ATOM     11  CA  VAL A   2       2.307  14.172   7.580  1.00  6.00           C  
ATOM     12  C   VAL A   2       0.857  14.041   6.949  1.00  6.00           C  
ATOM     13  O   VAL A   2       0.659  13.843   5.875  1.00  8.00           O  
ATOM     14  CB  VAL A   2       3.625  14.172   6.759  1.00  6.00           C  
ATOM     15  CG1 VAL A   2       3.494  15.491   6.317  1.00  6.00           C  
ATOM     16  CG2 VAL A   2       4.746  13.843   7.580  1.00  6.00           C  
ATOM     17  N   PHE A   3       0.000  14.898   7.896  1.00  7.00           N  
ATOM     18  CA  PHE A   3      -1.187  15.293   7.580  1.00  6.00           C  
ATOM     19  C   PHE A   3      -0.989  16.611   6.317  1.00  6.00           C  
ATOM     20  O   PHE A   3      -0.330  17.139   6.317  1.00  8.00           O  
ATOM     21  CB  PHE A   3      -1.846  15.161   8.844  1.00  6.00           C  
ATOM     22  CG  PHE A   3      -1.978  14.502   9.475  1.00  6.00           C  
ATOM     23  CD1 PHE A   3      -3.757  14.107   9.160  1.00  6.00           C  
ATOM     24  CD2 PHE A   3      -1.582  14.041  10.423  1.00  6.00           C  
ATOM     25  CE1 PHE A   3      -4.417  13.381   9.791  1.00  6.00           C  
ATOM     26  CE2 PHE A   3      -2.109  13.316  11.370  1.00  6.00           C  
ATOM     27  CZ  PHE A   3      -3.691  12.920  10.865  1.00  6.00           C  
ATOM     28  N   GLY A   4      -2.505  16.611   5.875  1.00  7.00           N  
ATOM     29  CA  GLY A   4      -2.637  17.468   4.864  1.00  6.00           C  
ATOM     30  C   GLY A   4      -3.626  18.787   5.685  1.00  6.00           C  
ATOM     31  O   GLY A   4      -3.955  17.930   6.633  1.00  8.00           O  
ATOM     32  N   ARG A   5      -3.494  19.841   5.054  1.00  7.00           N  
ATOM     33  CA  ARG A   5      -3.823  20.764   5.685  1.00  6.00           C  
ATOM     34  C   ARG A   5      -4.944  20.303   5.875  1.00  6.00           C  
ATOM     35  O   ARG A   5      -5.801  20.237   6.633  1.00  8.00           O  
ATOM     36  CB  ARG A   5      -4.285  21.687   4.738  1.00  6.00           C  
ATOM     37  CG  ARG A   5      -4.482  23.005   5.054  1.00  6.00           C  
ATOM     38  CD  ARG A   5      -4.482  23.994   4.232  1.00  6.00           C  
ATOM     39  NE  ARG A   5      -5.273  24.390   3.158  1.00  7.00           N  
ATOM     40  CZ  ARG A   5      -6.065  24.588   3.158  1.00  6.00           C  
ATOM     41  NH1 ARG A   5      -7.119  24.851   3.980  1.00  7.00           N  
ATOM     42  NH2 ARG A   5      -7.119  25.576   1.895  1.00  7.00           N  
ATOM     43  N   CYS A   6      -5.933  20.435   4.611  1.00  7.00           N  
ATOM     44  CA  CYS A   6      -7.581  20.105   4.611  1.00  6.00           C  
ATOM     45  C   CYS A   6      -7.910  18.787   5.875  1.00  6.00           C  
ATOM     46  O   CYS A   6      -8.240  18.457   6.759  1.00  8.00           O  
ATOM     47  CB  CYS A   6      -8.042  19.775   3.474  1.00  6.00           C  
ATOM     48  SG  CYS A   6      -8.899  21.423   2.843  1.00 16.00           S  
ATOM     49  N   GLU A   7      -6.856  17.666   5.685  1.00  7.00           N  
ATOM     50  CA  GLU A   7      -7.119  16.414   6.191  1.00  6.00           C  
ATOM     51  C   GLU A   7      -6.856  16.282   7.580  1.00  6.00           C  
ATOM     52  O   GLU A   7      -7.581  15.689   8.402  1.00  8.00           O  
ATOM     53  CB  GLU A   7      -6.592  15.623   5.685  1.00  6.00           C  
ATOM     54  CG  GLU A   7      -6.262  14.041   6.506  1.00  6.00           C  
ATOM     55  CD  GLU A   7      -5.339  13.184   5.685  1.00  6.00           C  
ATOM     56  OE1 GLU A   7      -3.955  13.184   5.054  1.00  8.00           O  
ATOM     57  OE2 GLU A   7      -4.944  12.063   6.317  1.00  8.00           O  
ATOM     58  N   LEU A   8      -6.196  16.941   8.212  1.00  7.00           N  
ATOM     59  CA  LEU A   8      -5.735  17.534   9.475  1.00  6.00           C  
ATOM     60  C   LEU A   8      -6.724  17.996  10.107  1.00  6.00           C  
ATOM     61  O   LEU A   8      -7.053  17.798  11.370  1.00  8.00           O  
ATOM     62  CB  LEU A   8      -4.482  18.193   9.791  1.00  6.00           C  
ATOM     63  CG  LEU A   8      -4.417  18.457  10.739  1.00  6.00           C  
ATOM     64  CD1 LEU A   8      -4.482  17.073  12.002  1.00  6.00           C  
ATOM     65  CD2 LEU A   8      -3.098  19.248  11.686  1.00  6.00           C  
ATOM     66  N   ALA A   9      -7.581  19.116   9.160  1.00  7.00           N  
ATOM     67  CA  ALA A   9      -8.372  19.907   9.665  1.00  6.00           C  
ATOM     68  C   ALA A   9      -9.229  19.182  10.107  1.00  6.00           C  
ATOM     69  O   ALA A   9      -9.888  19.248  11.244  1.00  8.00           O  
ATOM     70  CB  ALA A   9      -8.965  20.830   8.844  1.00  6.00           C  
ATOM     71  N   ALA A  10     -10.020  18.128   8.844  1.00  7.00           N  
ATOM     72  CA  ALA A  10     -11.206  17.205   9.475  1.00  6.00           C  
ATOM     73  C   ALA A  10     -10.877  16.150  10.739  1.00  6.00           C  
ATOM     74  O   ALA A  10     -11.536  16.150  11.686  1.00  8.00           O  
ATOM     75  CB  ALA A  10     -11.536  15.952   8.212  1.00  6.00           C  
ATOM     76  N   ALA A  11     -10.217  15.820  10.739  1.00  7.00           N  
ATOM     77  CA  ALA A  11      -9.426  14.963  11.749  1.00  6.00           C  
ATOM     78  C   ALA A  11      -9.756  15.557  13.266  1.00  6.00           C  
ATOM     79  O   ALA A  11     -10.349  14.766  14.087  1.00  8.00           O  
ATOM     80  CB  ALA A  11      -7.910  14.502  11.623  1.00  6.00           C  
ATOM     81  N   MET A  12      -9.229  16.677  13.266  1.00  7.00           N  
ATOM     82  CA  MET A  12      -9.295  17.534  14.529  1.00  6.00           C  
ATOM     83  C   MET A  12     -10.547  18.062  14.908  1.00  6.00           C  
ATOM     84  O   MET A  12     -11.074  17.930  16.424  1.00  8.00           O  
ATOM     85  CB  MET A  12      -8.438  18.721  14.529  1.00  6.00           C  
ATOM     86  CG  MET A  12      -6.921  18.457  14.529  1.00  6.00           C  
ATOM     87  SD  MET A  12      -5.999  19.973  14.529  1.00 16.00           S  
ATOM     88  CE  MET A  12      -6.081  20.438  16.246  1.00  6.00           C  
ATOM     89  N   LYS A  13     -11.272  18.259  13.897  1.00  7.00           N  
ATOM     90  CA  LYS A  13     -12.854  18.062  14.213  1.00  6.00           C  
ATOM     91  C   LYS A  13     -13.843  17.139  14.971  1.00  6.00           C  
ATOM     92  O   LYS A  13     -14.370  17.271  16.298  1.00  8.00           O  
ATOM     93  CB  LYS A  13     -13.184  18.787  12.634  1.00  6.00           C  
ATOM     94  CG  LYS A  13     -14.502  19.314  13.076  1.00  6.00           C  
ATOM     95  CD  LYS A  13     -15.293  19.775  12.002  1.00  6.00           C  
ATOM     96  CE  LYS A  13     -16.480  20.303  12.507  1.00  6.00           C  
ATOM     97  NZ  LYS A  13     -16.941  20.303  10.928  1.00  7.00           N  
ATOM     98  N   ARG A  14     -13.645  16.018  13.897  1.00  7.00           N  
ATOM     99  CA  ARG A  14     -13.645  14.502  14.213  1.00  6.00           C  
ATOM    100  C   ARG A  14     -13.447  14.370  15.792  1.00  6.00           C  
ATOM    101  O   ARG A  14     -14.304  14.304  17.056  1.00  8.00           O  
ATOM    102  CB  ARG A  14     -13.909  13.184  13.771  1.00  6.00           C  
ATOM    103  CG  ARG A  14     -13.711  12.722  12.634  1.00  6.00           C  
ATOM    104  CD  ARG A  14     -14.304  11.272  13.329  1.00  6.00           C  
ATOM    105  NE  ARG A  14     -12.986  10.679  13.771  1.00  7.00           N  
ATOM    106  CZ  ARG A  14     -12.986   9.888  14.845  1.00  6.00           C  
ATOM    107  NH1 ARG A  14     -14.172   9.954  15.603  1.00  7.00           N  
ATOM    108  NH2 ARG A  14     -11.997   9.097  15.287  1.00  7.00           N  
ATOM    109  N   HIS A  15     -12.525  14.832  16.424  1.00  7.00           N  
ATOM    110  CA  HIS A  15     -11.865  14.898  17.814  1.00  6.00           C  
ATOM    111  C   HIS A  15     -12.261  15.952  18.951  1.00  6.00           C  
ATOM    112  O   HIS A  15     -11.997  16.084  19.835  1.00  8.00           O  
ATOM    113  CB  HIS A  15     -10.415  14.634  17.687  1.00  6.00           C  
ATOM    114  CG  HIS A  15     -10.020  13.381  17.498  1.00  6.00           C  
ATOM    115  ND1 HIS A  15      -9.756  12.986  16.234  1.00  7.00           N  
ATOM    116  CD2 HIS A  15      -9.756  12.261  18.319  1.00  6.00           C  
ATOM    117  CE1 HIS A  15      -9.426  11.733  16.234  1.00  6.00           C  
ATOM    118  NE2 HIS A  15      -9.229  11.206  17.498  1.00  7.00           N  
ATOM    119  N   GLY A  16     -13.381  16.809  18.761  1.00  7.00           N  
ATOM    120  CA  GLY A  16     -13.645  17.996  19.772  1.00  6.00           C  
ATOM    121  C   GLY A  16     -12.788  19.446  19.582  1.00  6.00           C  
ATOM    122  O   GLY A  16     -13.184  20.105  20.340  1.00  8.00           O  
ATOM    123  N   LEU A  17     -11.865  19.512  18.824  1.00  7.00           N  
ATOM    124  CA  LEU A  17     -10.877  20.764  18.635  1.00  6.00           C  
ATOM    125  C   LEU A  17     -11.865  21.885  18.382  1.00  6.00           C  
ATOM    126  O   LEU A  17     -11.074  23.071  18.509  1.00  8.00           O  
ATOM    127  CB  LEU A  17      -9.888  20.566  18.130  1.00  6.00           C  
ATOM    128  CG  LEU A  17      -8.833  19.775  18.635  1.00  6.00           C  
ATOM    129  CD1 LEU A  17      -7.449  19.644  18.193  1.00  6.00           C  
ATOM    130  CD2 LEU A  17      -8.569  20.435  20.151  1.00  6.00           C  
ATOM    131  N   ASP A  18     -12.854  21.885  17.435  1.00  7.00           N  
ATOM    132  CA  ASP A  18     -13.184  23.071  16.866  1.00  6.00           C  
ATOM    133  C   ASP A  18     -13.975  23.862  17.877  1.00  6.00           C  
ATOM    134  O   ASP A  18     -14.304  23.335  18.951  1.00  8.00           O  
ATOM    135  CB  ASP A  18     -14.172  22.874  15.792  1.00  6.00           C  
ATOM    136  CG  ASP A  18     -14.502  23.731  15.161  1.00  6.00           C  
ATOM    137  OD1 ASP A  18     -14.416  24.929  15.012  1.00  8.00           O  
ATOM    138  OD2 ASP A  18     -15.437  23.446  13.950  1.00  8.00           O  
ATOM    139  N   ASN A  19     -13.843  25.181  18.130  1.00  7.00           N  
ATOM    140  CA  ASN A  19     -14.172  25.708  19.330  1.00  6.00           C  
ATOM    141  C   ASN A  19     -13.579  25.313  20.593  1.00  6.00           C  
ATOM    142  O   ASN A  19     -14.370  25.972  21.162  1.00  8.00           O  
ATOM    143  CB  ASN A  19     -15.623  26.104  18.951  1.00  6.00           C  
ATOM    144  CG  ASN A  19     -15.491  27.290  17.687  1.00  6.00           C  
ATOM    145  OD1 ASN A  19     -14.963  28.477  17.687  1.00  7.00           O  
ATOM    146  ND2 ASN A  19     -15.952  26.631  16.803  1.00  7.00           N  
ATOM    147  N   TYR A  20     -12.788  24.522  20.720  1.00  7.00           N  
ATOM    148  CA  TYR A  20     -12.656  24.258  21.857  1.00  6.00           C  
ATOM    149  C   TYR A  20     -11.931  25.049  22.741  1.00  6.00           C  
ATOM    150  O   TYR A  20     -11.074  26.104  22.488  1.00  8.00           O  
ATOM    151  CB  TYR A  20     -11.536  22.940  21.730  1.00  6.00           C  
ATOM    152  CG  TYR A  20     -11.602  22.412  23.057  1.00  6.00           C  
ATOM    153  CD1 TYR A  20     -12.656  21.951  23.562  1.00  6.00           C  
ATOM    154  CD2 TYR A  20     -10.086  22.676  24.131  1.00  6.00           C  
ATOM    155  CE1 TYR A  20     -12.656  20.962  24.889  1.00  6.00           C  
ATOM    156  CE2 TYR A  20     -10.086  22.149  25.520  1.00  6.00           C  
ATOM    157  CZ  TYR A  20     -11.074  21.226  25.899  1.00  6.00           C  
ATOM    158  OH  TYR A  20     -10.811  20.698  27.352  1.00  8.00           O  
ATOM    159  N   ARG A  21     -12.393  25.181  23.688  1.00  7.00           N  
ATOM    160  CA  ARG A  21     -12.195  26.697  24.762  1.00  6.00           C  
ATOM    161  C   ARG A  21     -12.393  27.818  23.941  1.00  6.00           C  
ATOM    162  O   ARG A  21     -11.733  28.872  24.004  1.00  8.00           O  
ATOM    163  CB  ARG A  21     -10.547  26.697  25.457  1.00  6.00           C  
ATOM    164  CG  ARG A  21     -10.679  26.038  26.531  1.00  6.00           C  
ATOM    165  CD  ARG A  21     -11.668  26.697  27.731  1.00  6.00           C  
ATOM    166  NE  ARG A  21     -11.008  25.708  28.932  1.00  7.00           N  
ATOM    167  CZ  ARG A  21     -10.877  26.367  30.005  1.00  6.00           C  
ATOM    168  NH1 ARG A  21     -10.217  28.015  29.816  1.00  7.00           N  
ATOM    169  NH2 ARG A  21     -10.679  25.972  31.079  1.00  7.00           N  
ATOM    170  N   GLY A  22     -13.316  28.015  22.867  1.00  7.00           N  
ATOM    171  CA  GLY A  22     -13.513  29.136  22.109  1.00  6.00           C  
ATOM    172  C   GLY A  22     -12.195  29.663  21.162  1.00  6.00           C  
ATOM    173  O   GLY A  22     -12.063  30.586  20.467  1.00  8.00           O  
ATOM    174  N   TYR A  23     -11.404  28.345  20.846  1.00  7.00           N  
ATOM    175  CA  TYR A  23     -10.086  28.609  19.646  1.00  6.00           C  
ATOM    176  C   TYR A  23     -11.206  28.015  18.572  1.00  6.00           C  
ATOM    177  O   TYR A  23     -11.140  26.499  18.509  1.00  8.00           O  
ATOM    178  CB  TYR A  23      -8.965  28.147  20.214  1.00  6.00           C  
ATOM    179  CG  TYR A  23      -8.438  28.674  21.162  1.00  6.00           C  
ATOM    180  CD1 TYR A  23      -7.712  29.993  20.846  1.00  6.00           C  
ATOM    181  CD2 TYR A  23      -8.240  28.477  22.488  1.00  6.00           C  
ATOM    182  CE1 TYR A  23      -7.383  30.652  21.730  1.00  6.00           C  
ATOM    183  CE2 TYR A  23      -7.778  29.400  23.373  1.00  6.00           C  
ATOM    184  CZ  TYR A  23      -7.119  30.586  22.994  1.00  6.00           C  
ATOM    185  OH  TYR A  23      -6.460  31.377  24.004  1.00  8.00           O  
ATOM    186  N   SER A  24     -11.206  28.674  17.182  1.00  7.00           N  
ATOM    187  CA  SER A  24     -11.338  28.147  16.171  1.00  6.00           C  
ATOM    188  C   SER A  24     -10.877  27.158  15.161  1.00  6.00           C  
ATOM    189  O   SER A  24      -9.492  27.422  15.666  1.00  8.00           O  
ATOM    190  CB  SER A  24     -11.074  29.400  15.034  1.00  6.00           C  
ATOM    191  OG  SER A  24     -11.008  28.674  13.771  1.00  8.00           O  
ATOM    192  N   LEU A  25     -11.602  26.170  14.529  1.00  7.00           N  
ATOM    193  CA  LEU A  25     -10.547  25.379  13.897  1.00  6.00           C  
ATOM    194  C   LEU A  25      -9.295  25.576  13.266  1.00  6.00           C  
ATOM    195  O   LEU A  25      -8.108  24.851  13.266  1.00  8.00           O  
ATOM    196  CB  LEU A  25     -11.206  24.456  13.266  1.00  6.00           C  
ATOM    197  CG  LEU A  25     -11.074  23.137  13.266  1.00  6.00           C  
ATOM    198  CD1 LEU A  25     -11.733  22.412  11.876  1.00  6.00           C  
ATOM    199  CD2 LEU A  25      -9.888  22.478  12.255  1.00  6.00           C  
ATOM    200  N   GLY A  26      -8.965  26.433  12.760  1.00  7.00           N  
ATOM    201  CA  GLY A  26      -8.174  27.224  12.002  1.00  6.00           C  
ATOM    202  C   GLY A  26      -7.119  27.488  12.634  1.00  6.00           C  
ATOM    203  O   GLY A  26      -5.867  27.488  12.634  1.00  8.00           O  
ATOM    204  N   ASN A  27      -7.053  27.686  14.024  1.00  7.00           N  
ATOM    205  CA  ASN A  27      -6.262  28.279  15.161  1.00  6.00           C  
ATOM    206  C   ASN A  27      -5.273  27.026  15.224  1.00  6.00           C  
ATOM    207  O   ASN A  27      -3.955  27.554  15.161  1.00  8.00           O  
ATOM    208  CB  ASN A  27      -6.592  28.543  16.424  1.00  6.00           C  
ATOM    209  CG  ASN A  27      -6.790  30.059  16.424  1.00  6.00           C  
ATOM    210  OD1 ASN A  27      -6.460  31.113  16.614  1.00  7.00           O  
ATOM    211  ND2 ASN A  27      -8.569  30.784  16.298  1.00  7.00           N  
ATOM    212  N   TRP A  28      -5.933  25.840  15.287  1.00  7.00           N  
ATOM    213  CA  TRP A  28      -5.603  24.588  15.540  1.00  6.00           C  
ATOM    214  C   TRP A  28      -4.746  23.862  14.403  1.00  6.00           C  
ATOM    215  O   TRP A  28      -3.823  23.203  14.403  1.00  8.00           O  
ATOM    216  CB  TRP A  28      -6.658  23.533  15.792  1.00  6.00           C  
ATOM    217  CG  TRP A  28      -7.449  23.928  17.182  1.00  6.00           C  
ATOM    218  CD1 TRP A  28      -8.504  24.588  17.308  1.00  6.00           C  
ATOM    219  CD2 TRP A  28      -6.856  23.599  18.572  1.00  6.00           C  
ATOM    220  NE1 TRP A  28      -8.701  24.456  18.698  1.00  7.00           N  
ATOM    221  CE2 TRP A  28      -7.910  24.060  19.456  1.00  6.00           C  
ATOM    222  CE3 TRP A  28      -5.801  23.137  18.951  1.00  6.00           C  
ATOM    223  CZ2 TRP A  28      -7.712  24.192  20.846  1.00  6.00           C  
ATOM    224  CZ3 TRP A  28      -5.471  23.269  20.404  1.00  6.00           C  
ATOM    225  CH2 TRP A  28      -6.526  23.533  21.288  1.00  6.00           C  
ATOM    226  N   VAL A  29      -5.076  24.192  13.266  1.00  7.00           N  
ATOM    227  CA  VAL A  29      -4.614  23.731  11.876  1.00  6.00           C  
ATOM    228  C   VAL A  29      -3.362  24.588  11.560  1.00  6.00           C  
ATOM    229  O   VAL A  29      -2.241  24.258  11.244  1.00  8.00           O  
ATOM    230  CB  VAL A  29      -5.801  23.731  10.802  1.00  6.00           C  
ATOM    231  CG1 VAL A  29      -4.944  23.599   9.665  1.00  6.00           C  
ATOM    232  CG2 VAL A  29      -6.724  22.676  11.244  1.00  6.00           C  
ATOM    233  N   CYS A  30      -3.362  25.840  11.686  1.00  7.00           N  
ATOM    234  CA  CYS A  30      -2.109  26.697  11.560  1.00  6.00           C  
ATOM    235  C   CYS A  30      -1.318  26.631  12.571  1.00  6.00           C  
ATOM    236  O   CYS A  30       0.000  26.367  12.507  1.00  8.00           O  
ATOM    237  CB  CYS A  30      -2.703  28.345  11.497  1.00  6.00           C  
ATOM    238  SG  CYS A  30      -1.450  29.465  11.560  1.00 16.00           S  
ATOM    239  N   ALA A  31      -1.318  26.104  13.645  1.00  7.00           N  
ATOM    240  CA  ALA A  31      -0.791  25.840  14.718  1.00  6.00           C  
ATOM    241  C   ALA A  31       0.198  24.588  14.655  1.00  6.00           C  
ATOM    242  O   ALA A  31       1.318  24.851  14.971  1.00  8.00           O  
ATOM    243  CB  ALA A  31      -1.187  25.708  16.677  1.00  6.00           C  
ATOM    244  N   ALA A  32      -0.198  23.665  14.087  1.00  7.00           N  
ATOM    245  CA  ALA A  32      -0.198  22.478  14.592  1.00  6.00           C  
ATOM    246  C   ALA A  32       0.989  22.742  12.634  1.00  6.00           C  
ATOM    247  O   ALA A  32       2.043  21.819  12.381  1.00  8.00           O  
ATOM    248  CB  ALA A  32      -0.725  21.160  13.897  1.00  6.00           C  
ATOM    249  N   LYS A  33       0.659  23.599  11.876  1.00  7.00           N  
ATOM    250  CA  LYS A  33       1.384  23.467  10.612  1.00  6.00           C  
ATOM    251  C   LYS A  33       2.834  23.862  10.865  1.00  6.00           C  
ATOM    252  O   LYS A  33       3.955  23.599  10.612  1.00  8.00           O  
ATOM    253  CB  LYS A  33       0.791  24.653   9.854  1.00  6.00           C  
ATOM    254  CG  LYS A  33       1.912  25.049   8.781  1.00  6.00           C  
ATOM    255  CD  LYS A  33       1.846  24.653   7.454  1.00  6.00           C  
ATOM    256  CE  LYS A  33       2.900  24.917   6.506  1.00  6.00           C  
ATOM    257  NZ  LYS A  33       3.098  24.522   5.306  1.00  7.00           N  
ATOM    258  N   PHE A  34       2.966  25.379  11.370  1.00  7.00           N  
ATOM    259  CA  PHE A  34       3.955  25.906  11.749  1.00  6.00           C  
ATOM    260  C   PHE A  34       4.614  25.247  12.887  1.00  6.00           C  
ATOM    261  O   PHE A  34       5.801  25.379  12.887  1.00  8.00           O  
ATOM    262  CB  PHE A  34       3.494  27.356  12.002  1.00  6.00           C  
ATOM    263  CG  PHE A  34       3.362  27.949  10.612  1.00  6.00           C  
ATOM    264  CD1 PHE A  34       2.241  29.004  10.297  1.00  6.00           C  
ATOM    265  CD2 PHE A  34       4.614  27.949   9.728  1.00  6.00           C  
ATOM    266  CE1 PHE A  34       1.978  29.663   9.160  1.00  6.00           C  
ATOM    267  CE2 PHE A  34       4.417  28.674   8.402  1.00  6.00           C  
ATOM    268  CZ  PHE A  34       3.164  29.400   8.212  1.00  6.00           C  
ATOM    269  N   GLU A  35       3.889  24.653  13.771  1.00  7.00           N  
ATOM    270  CA  GLU A  35       4.680  23.796  14.971  1.00  6.00           C  
ATOM    271  C   GLU A  35       5.273  22.412  14.529  1.00  6.00           C  
ATOM    272  O   GLU A  35       6.526  22.149  14.845  1.00  8.00           O  
ATOM    273  CB  GLU A  35       4.087  23.599  15.982  1.00  6.00           C  
ATOM    274  CG  GLU A  35       3.757  23.665  17.308  1.00  6.00           C  
ATOM    275  CD  GLU A  35       4.680  24.522  17.940  1.00  6.00           C  
ATOM    276  OE1 GLU A  35       5.603  24.588  17.687  1.00  8.00           O  
ATOM    277  OE2 GLU A  35       4.153  25.642  18.509  1.00  8.00           O  
ATOM    278  N   SER A  36       4.680  21.687  13.834  1.00  7.00           N  
ATOM    279  CA  SER A  36       4.878  20.435  13.455  1.00  6.00           C  
ATOM    280  C   SER A  36       5.142  20.039  11.876  1.00  6.00           C  
ATOM    281  O   SER A  36       5.669  18.919  11.370  1.00  8.00           O  
ATOM    282  CB  SER A  36       4.285  19.446  14.024  1.00  6.00           C  
ATOM    283  OG  SER A  36       2.966  19.116  13.266  1.00  8.00           O  
ATOM    284  N   ASN A  37       4.614  20.896  11.118  1.00  7.00           N  
ATOM    285  CA  ASN A  37       4.680  20.632   9.665  1.00  6.00           C  
ATOM    286  C   ASN A  37       3.691  19.380   9.096  1.00  6.00           C  
ATOM    287  O   ASN A  37       3.691  19.380   7.959  1.00  8.00           O  
ATOM    288  CB  ASN A  37       5.735  20.896   9.033  1.00  6.00           C  
ATOM    289  CG  ASN A  37       5.867  21.687   7.707  1.00  6.00           C  
ATOM    290  OD1 ASN A  37       5.273  22.478   7.391  1.00  7.00           O  
ATOM    291  ND2 ASN A  37       6.790  21.358   7.075  1.00  7.00           N  
ATOM    292  N   PHE A  38       2.637  18.984   9.854  1.00  7.00           N  
ATOM    293  CA  PHE A  38       1.780  18.062   9.475  1.00  6.00           C  
ATOM    294  C   PHE A  38       1.978  16.743   9.602  1.00  6.00           C  
ATOM    295  O   PHE A  38       1.318  15.952   9.602  1.00  8.00           O  
ATOM    296  CB  PHE A  38       0.791  18.457   7.959  1.00  6.00           C  
ATOM    297  CG  PHE A  38       0.132  19.644   7.959  1.00  6.00           C  
ATOM    298  CD1 PHE A  38       0.000  20.303   9.160  1.00  6.00           C  
ATOM    299  CD2 PHE A  38       0.000  20.303   6.759  1.00  6.00           C  
ATOM    300  CE1 PHE A  38      -0.989  21.687   9.096  1.00  6.00           C  
ATOM    301  CE2 PHE A  38      -0.989  21.687   6.696  1.00  6.00           C  
ATOM    302  CZ  PHE A  38      -1.187  22.017   7.833  1.00  6.00           C  
ATOM    303  N   ASN A  39       3.296  16.941  10.107  1.00  7.00           N  
ATOM    304  CA  ASN A  39       4.021  15.754  10.676  1.00  6.00           C  
ATOM    305  C   ASN A  39       4.153  15.557  12.192  1.00  6.00           C  
ATOM    306  O   ASN A  39       4.680  16.150  13.076  1.00  8.00           O  
ATOM    307  CB  ASN A  39       5.801  15.820  10.423  1.00  6.00           C  
ATOM    308  CG  ASN A  39       6.460  14.634  10.360  1.00  6.00           C  
ATOM    309  OD1 ASN A  39       5.933  13.316  10.739  1.00  7.00           O  
ATOM    310  ND2 ASN A  39       7.581  14.634   9.981  1.00  7.00           N  
ATOM    311  N   THR A  40       3.230  14.502  12.318  1.00  7.00           N  
ATOM    312  CA  THR A  40       2.966  13.843  13.771  1.00  6.00           C  
ATOM    313  C   THR A  40       4.482  12.986  14.529  1.00  6.00           C  
ATOM    314  O   THR A  40       4.285  12.854  15.476  1.00  8.00           O  
ATOM    315  CB  THR A  40       1.978  12.722  13.645  1.00  6.00           C  
ATOM    316  OG1 THR A  40       2.373  11.799  12.571  1.00  8.00           O  
ATOM    317  CG2 THR A  40       0.725  12.986  13.392  1.00  6.00           C  
ATOM    318  N   GLN A  41       5.142  12.854  13.834  1.00  7.00           N  
ATOM    319  CA  GLN A  41       6.724  12.063  14.339  1.00  6.00           C  
ATOM    320  C   GLN A  41       7.581  12.788  14.782  1.00  6.00           C  
ATOM    321  O   GLN A  41       8.438  13.052  15.666  1.00  8.00           O  
ATOM    322  CB  GLN A  41       7.251  11.206  13.202  1.00  6.00           C  
ATOM    323  CG  GLN A  41       6.724   9.822  12.950  1.00  6.00           C  
ATOM    324  CD  GLN A  41       7.581   8.965  12.128  1.00  6.00           C  
ATOM    325  OE1 GLN A  41       7.581   8.965  11.055  1.00  7.00           O  
ATOM    326  NE2 GLN A  41       8.438   8.240  12.760  1.00  7.00           N  
ATOM    327  N   ALA A  42       7.581  14.304  14.213  1.00  7.00           N  
ATOM    328  CA  ALA A  42       8.569  15.293  14.339  1.00  6.00           C  
ATOM    329  C   ALA A  42       8.767  15.425  15.919  1.00  6.00           C  
ATOM    330  O   ALA A  42       8.042  15.029  16.740  1.00  8.00           O  
ATOM    331  CB  ALA A  42       7.910  16.545  13.771  1.00  6.00           C  
ATOM    332  N   THR A  43      10.151  15.491  16.298  1.00  7.00           N  
ATOM    333  CA  THR A  43      10.481  15.623  17.751  1.00  6.00           C  
ATOM    334  C   THR A  43      11.536  16.941  17.687  1.00  6.00           C  
ATOM    335  O   THR A  43      12.063  17.139  16.993  1.00  8.00           O  
ATOM    336  CB  THR A  43      11.206  14.370  17.814  1.00  6.00           C  
ATOM    337  OG1 THR A  43      12.590  14.238  16.803  1.00  8.00           O  
ATOM    338  CG2 THR A  43      10.415  12.986  17.561  1.00  6.00           C  
ATOM    339  N   ASN A  44      11.733  17.666  18.951  1.00  7.00           N  
ATOM    340  CA  ASN A  44      12.195  18.787  19.077  1.00  6.00           C  
ATOM    341  C   ASN A  44      12.854  18.984  20.530  1.00  6.00           C  
ATOM    342  O   ASN A  44      12.393  19.116  21.035  1.00  8.00           O  
ATOM    343  CB  ASN A  44      11.931  20.303  18.572  1.00  6.00           C  
ATOM    344  CG  ASN A  44      12.195  20.105  17.056  1.00  6.00           C  
ATOM    345  OD1 ASN A  44      12.854  20.435  16.550  1.00  7.00           O  
ATOM    346  ND2 ASN A  44      10.877  20.105  16.298  1.00  7.00           N  
ATOM    347  N   ARG A  45      14.370  19.116  20.656  1.00  7.00           N  
ATOM    348  CA  ARG A  45      14.766  19.248  21.857  1.00  6.00           C  
ATOM    349  C   ARG A  45      15.293  20.698  22.109  1.00  6.00           C  
ATOM    350  O   ARG A  45      15.886  21.292  21.351  1.00  8.00           O  
ATOM    351  CB  ARG A  45      16.348  18.457  21.920  1.00  6.00           C  
ATOM    352  CG  ARG A  45      17.007  18.128  23.246  1.00  6.00           C  
ATOM    353  CD  ARG A  45      17.798  16.809  23.562  1.00  6.00           C  
ATOM    354  NE  ARG A  45      17.930  16.216  24.762  1.00  7.00           N  
ATOM    355  CZ  ARG A  45      18.589  15.293  24.952  1.00  6.00           C  
ATOM    356  NH1 ARG A  45      19.446  14.700  23.815  1.00  7.00           N  
ATOM    357  NH2 ARG A  45      18.984  14.832  26.215  1.00  7.00           N  
ATOM    358  N   ASN A  46      14.898  21.226  23.373  1.00  7.00           N  
ATOM    359  CA  ASN A  46      15.161  22.676  23.499  1.00  6.00           C  
ATOM    360  C   ASN A  46      16.677  22.742  24.383  1.00  6.00           C  
ATOM    361  O   ASN A  46      17.139  21.423  24.889  1.00  8.00           O  
ATOM    362  CB  ASN A  46      13.513  23.071  23.815  1.00  6.00           C  
ATOM    363  CG  ASN A  46      12.656  22.676  23.183  1.00  6.00           C  
ATOM    364  OD1 ASN A  46      11.997  21.951  23.752  1.00  7.00           O  
ATOM    365  ND2 ASN A  46      12.393  23.071  22.741  1.00  7.00           N  
ATOM    366  N   THR A  47      17.271  23.401  25.268  1.00  7.00           N  
ATOM    367  CA  THR A  47      18.589  23.071  26.026  1.00  6.00           C  
ATOM    368  C   THR A  47      18.457  22.280  27.542  1.00  6.00           C  
ATOM    369  O   THR A  47      19.446  21.885  27.794  1.00  8.00           O  
ATOM    370  CB  THR A  47      19.116  24.522  26.152  1.00  6.00           C  
ATOM    371  OG1 THR A  47      18.457  25.049  25.394  1.00  8.00           O  
ATOM    372  CG2 THR A  47      20.567  24.390  25.710  1.00  6.00           C  
ATOM    373  N   ASP A  48      17.139  22.544  27.921  1.00  7.00           N  
ATOM    374  CA  ASP A  48      17.007  21.819  29.500  1.00  6.00           C  
ATOM    375  C   ASP A  48      16.545  20.501  29.626  1.00  6.00           C  
ATOM    376  O   ASP A  48      15.886  20.303  30.637  1.00  8.00           O  
ATOM    377  CB  ASP A  48      15.754  22.874  30.005  1.00  6.00           C  
ATOM    378  CG  ASP A  48      14.634  22.544  29.563  1.00  6.00           C  
ATOM    379  OD1 ASP A  48      14.436  22.412  28.553  1.00  7.00           O  
ATOM    380  OD2 ASP A  48      13.645  22.346  30.511  1.00  7.00           O  
ATOM    381  N   GLY A  49      16.809  19.512  28.742  1.00  7.00           N  
ATOM    382  CA  GLY A  49      16.480  17.930  28.805  1.00  6.00           C  
ATOM    383  C   GLY A  49      15.227  18.128  27.794  1.00  6.00           C  
ATOM    384  O   GLY A  49      15.293  17.732  26.847  1.00  8.00           O  
ATOM    385  N   SER A  50      14.370  18.457  28.237  1.00  7.00           N  
ATOM    386  CA  SER A  50      13.184  18.787  27.605  1.00  6.00           C  
ATOM    387  C   SER A  50      12.854  18.457  25.899  1.00  6.00           C  
ATOM    388  O   SER A  50      14.041  19.116  25.268  1.00  8.00           O  
ATOM    389  CB  SER A  50      12.393  19.907  27.921  1.00  6.00           C  
ATOM    390  OG  SER A  50      11.865  20.435  26.847  1.00  8.00           O  
ATOM    391  N   THR A  51      12.524  18.062  25.710  1.00  7.00           N  
ATOM    392  CA  THR A  51      11.931  17.798  24.257  1.00  6.00           C  
ATOM    393  C   THR A  51      10.547  17.864  24.004  1.00  6.00           C  
ATOM    394  O   THR A  51       9.756  17.732  24.636  1.00  8.00           O  
ATOM    395  CB  THR A  51      12.524  16.150  24.067  1.00  6.00           C  
ATOM    396  OG1 THR A  51      13.777  15.952  24.004  1.00  8.00           O  
ATOM    397  CG2 THR A  51      11.865  15.820  22.867  1.00  6.00           C  
ATOM    398  N   ASP A  52      10.020  17.996  22.741  1.00  7.00           N  
ATOM    399  CA  ASP A  52       8.899  18.457  22.109  1.00  6.00           C  
ATOM    400  C   ASP A  52       8.569  17.468  20.972  1.00  6.00           C  
ATOM    401  O   ASP A  52       9.426  17.139  20.404  1.00  8.00           O  
ATOM    402  CB  ASP A  52       9.097  19.841  21.351  1.00  6.00           C  
ATOM    403  CG  ASP A  52       8.965  20.830  22.172  1.00  6.00           C  
ATOM    404  OD1 ASP A  52       8.965  20.830  23.373  1.00  8.00           O  
ATOM    405  OD2 ASP A  52       9.031  22.083  21.857  1.00  8.00           O  
ATOM    406  N   TYR A  53       7.581  16.545  21.035  1.00  7.00           N  
ATOM    407  CA  TYR A  53       6.987  15.623  20.277  1.00  6.00           C  
ATOM    408  C   TYR A  53       5.933  15.820  19.519  1.00  6.00           C  
ATOM    409  O   TYR A  53       4.614  16.216  20.151  1.00  8.00           O  
ATOM    410  CB  TYR A  53       6.724  14.502  21.225  1.00  6.00           C  
ATOM    411  CG  TYR A  53       7.910  13.975  22.046  1.00  6.00           C  
ATOM    412  CD1 TYR A  53       8.767  12.920  21.604  1.00  6.00           C  
ATOM    413  CD2 TYR A  53       8.108  14.502  23.183  1.00  6.00           C  
ATOM    414  CE1 TYR A  53       9.756  12.524  22.362  1.00  6.00           C  
ATOM    415  CE2 TYR A  53       9.163  14.304  24.004  1.00  6.00           C  
ATOM    416  CZ  TYR A  53      10.020  13.184  23.499  1.00  6.00           C  
ATOM    417  OH  TYR A  53      11.338  12.920  24.257  1.00  8.00           O  
ATOM    418  N   GLY A  54       5.405  15.425  18.319  1.00  7.00           N  
ATOM    419  CA  GLY A  54       4.087  15.161  17.687  1.00  6.00           C  
ATOM    420  C   GLY A  54       3.757  16.480  17.119  1.00  6.00           C  
ATOM    421  O   GLY A  54       4.285  17.600  17.182  1.00  8.00           O  
ATOM    422  N   ILE A  55       2.637  16.282  16.424  1.00  7.00           N  
ATOM    423  CA  ILE A  55       1.846  17.600  15.413  1.00  6.00           C  
ATOM    424  C   ILE A  55       1.912  18.391  16.424  1.00  6.00           C  
ATOM    425  O   ILE A  55       1.780  19.775  15.919  1.00  8.00           O  
ATOM    426  CB  ILE A  55       0.527  16.875  15.161  1.00  6.00           C  
ATOM    427  CG1 ILE A  55      -0.264  17.600  13.897  1.00  6.00           C  
ATOM    428  CG2 ILE A  55      -0.659  17.007  16.424  1.00  6.00           C  
ATOM    429  CD1 ILE A  55       0.395  17.139  12.634  1.00  6.00           C  
ATOM    430  N   LEU A  56       1.912  18.457  17.687  1.00  7.00           N  
ATOM    431  CA  LEU A  56       1.187  19.775  18.319  1.00  6.00           C  
ATOM    432  C   LEU A  56       2.175  20.237  19.456  1.00  6.00           C  
ATOM    433  O   LEU A  56       1.978  21.094  19.961  1.00  8.00           O  
ATOM    434  CB  LEU A  56       0.000  19.578  18.951  1.00  6.00           C  
ATOM    435  CG  LEU A  56      -0.989  20.303  18.951  1.00  6.00           C  
ATOM    436  CD1 LEU A  56      -1.187  21.094  17.561  1.00  6.00           C  
ATOM    437  CD2 LEU A  56      -2.769  19.973  18.951  1.00  6.00           C  
ATOM    438  N   GLN A  57       3.494  19.775  19.203  1.00  7.00           N  
ATOM    439  CA  GLN A  57       4.746  19.907  20.025  1.00  6.00           C  
ATOM    440  C   GLN A  57       4.548  19.841  21.478  1.00  6.00           C  
ATOM    441  O   GLN A  57       5.273  20.764  21.920  1.00  8.00           O  
ATOM    442  CB  GLN A  57       5.735  20.632  19.140  1.00  6.00           C  
ATOM    443  CG  GLN A  57       6.196  20.566  17.687  1.00  6.00           C  
ATOM    444  CD  GLN A  57       7.119  19.644  18.066  1.00  6.00           C  
ATOM    445  OE1 GLN A  57       8.108  19.841  18.572  1.00  7.00           O  
ATOM    446  NE2 GLN A  57       6.987  18.259  17.687  1.00  7.00           N  
ATOM    447  N   ILE A  58       3.889  18.853  21.983  1.00  7.00           N  
ATOM    448  CA  ILE A  58       3.889  18.853  23.373  1.00  6.00           C  
ATOM    449  C   ILE A  58       5.010  18.655  24.004  1.00  6.00           C  
ATOM    450  O   ILE A  58       5.801  17.666  23.436  1.00  8.00           O  
ATOM    451  CB  ILE A  58       2.769  18.128  23.815  1.00  6.00           C  
ATOM    452  CG1 ILE A  58       1.780  18.193  22.867  1.00  6.00           C  
ATOM    453  CG2 ILE A  58       2.373  18.457  25.394  1.00  6.00           C  
ATOM    454  CD1 ILE A  58       0.659  17.139  22.994  1.00  6.00           C  
ATOM    455  N   ASN A  59       5.537  19.578  25.268  1.00  7.00           N  
ATOM    456  CA  ASN A  59       6.724  19.248  25.899  1.00  6.00           C  
ATOM    457  C   ASN A  59       6.658  18.128  26.973  1.00  6.00           C  
ATOM    458  O   ASN A  59       5.933  17.930  27.415  1.00  8.00           O  
ATOM    459  CB  ASN A  59       7.119  20.566  26.531  1.00  6.00           C  
ATOM    460  CG  ASN A  59       8.174  20.830  27.163  1.00  6.00           C  
ATOM    461  OD1 ASN A  59       8.240  20.698  28.426  1.00  7.00           O  
ATOM    462  ND2 ASN A  59       9.097  21.226  26.342  1.00  7.00           N  
ATOM    463  N   SER A  60       7.844  17.798  27.163  1.00  7.00           N  
ATOM    464  CA  SER A  60       8.042  16.611  28.426  1.00  6.00           C  
ATOM    465  C   SER A  60       8.569  16.941  29.690  1.00  6.00           C  
ATOM    466  O   SER A  60       8.372  16.018  30.511  1.00  8.00           O  
ATOM    467  CB  SER A  60       8.965  15.820  28.237  1.00  6.00           C  
ATOM    468  OG  SER A  60      10.283  16.282  27.921  1.00  8.00           O  
ATOM    469  N   ARG A  61       8.701  18.325  29.942  1.00  7.00           N  
ATOM    470  CA  ARG A  61       8.701  18.655  31.332  1.00  6.00           C  
ATOM    471  C   ARG A  61       7.449  18.655  32.027  1.00  6.00           C  
ATOM    472  O   ARG A  61       7.581  18.655  33.038  1.00  8.00           O  
ATOM    473  CB  ARG A  61       9.558  19.775  31.332  1.00  6.00           C  
ATOM    474  CG  ARG A  61       9.690  20.435  33.038  1.00  6.00           C  
ATOM    475  CD  ARG A  61      10.679  21.423  33.227  1.00  6.00           C  
ATOM    476  NE  ARG A  61      10.942  21.555  34.743  1.00  7.00           N  
ATOM    477  CZ  ARG A  61      11.997  21.951  35.122  1.00  6.00           C  
ATOM    478  NH1 ARG A  61      12.986  22.214  34.238  1.00  7.00           N  
ATOM    479  NH2 ARG A  61      11.997  22.544  36.386  1.00  7.00           N  
ATOM    480  N   TRP A  62       6.064  18.721  31.458  1.00  7.00           N  
ATOM    481  CA  TRP A  62       4.812  18.787  32.090  1.00  6.00           C  
ATOM    482  C   TRP A  62       3.955  17.930  31.458  1.00  6.00           C  
ATOM    483  O   TRP A  62       3.296  17.468  31.964  1.00  8.00           O  
ATOM    484  CB  TRP A  62       4.285  20.435  32.216  1.00  6.00           C  
ATOM    485  CG  TRP A  62       5.405  21.423  32.216  1.00  6.00           C  
ATOM    486  CD1 TRP A  62       6.064  21.951  31.269  1.00  6.00           C  
ATOM    487  CD2 TRP A  62       5.933  22.083  33.480  1.00  6.00           C  
ATOM    488  NE1 TRP A  62       7.251  23.071  31.585  1.00  7.00           N  
ATOM    489  CE2 TRP A  62       6.987  23.203  32.974  1.00  6.00           C  
ATOM    490  CE3 TRP A  62       5.462  21.754  34.554  1.00  6.00           C  
ATOM    491  CZ2 TRP A  62       7.401  23.829  33.946  1.00  6.00           C  
ATOM    492  CZ3 TRP A  62       6.067  22.590  35.516  1.00  6.00           C  
ATOM    493  CH2 TRP A  62       6.962  23.607  35.217  1.00  6.00           C  
ATOM    494  N   TRP A  63       3.757  17.666  30.195  1.00  7.00           N  
ATOM    495  CA  TRP A  63       2.703  16.875  29.563  1.00  6.00           C  
ATOM    496  C   TRP A  63       2.966  15.359  29.311  1.00  6.00           C  
ATOM    497  O   TRP A  63       1.978  14.832  29.437  1.00  8.00           O  
ATOM    498  CB  TRP A  63       2.175  17.600  28.047  1.00  6.00           C  
ATOM    499  CG  TRP A  63       1.978  19.182  28.426  1.00  6.00           C  
ATOM    500  CD1 TRP A  63       2.966  20.039  27.731  1.00  6.00           C  
ATOM    501  CD2 TRP A  63       1.121  19.512  29.437  1.00  6.00           C  
ATOM    502  NE1 TRP A  63       2.505  21.226  28.426  1.00  7.00           N  
ATOM    503  CE2 TRP A  63       1.450  21.028  29.311  1.00  6.00           C  
ATOM    504  CE3 TRP A  63       0.264  18.984  30.384  1.00  6.00           C  
ATOM    505  CZ2 TRP A  63       0.923  21.819  30.321  1.00  6.00           C  
ATOM    506  CZ3 TRP A  63      -0.461  19.973  31.269  1.00  6.00           C  
ATOM    507  CH2 TRP A  63      -0.132  21.160  31.206  1.00  6.00           C  
ATOM    508  N   CYS A  64       3.955  14.700  28.932  1.00  7.00           N  
ATOM    509  CA  CYS A  64       4.153  13.579  28.805  1.00  6.00           C  
ATOM    510  C   CYS A  64       5.801  13.118  29.184  1.00  6.00           C  
ATOM    511  O   CYS A  64       6.394  13.843  29.184  1.00  8.00           O  
ATOM    512  CB  CYS A  64       4.285  13.315  27.289  1.00  6.00           C  
ATOM    513  SG  CYS A  64       4.944  14.041  26.405  1.00 16.00           S  
ATOM    514  N   ASN A  65       5.603  11.865  29.690  1.00  7.00           N  
ATOM    515  CA  ASN A  65       6.921  11.470  30.195  1.00  6.00           C  
ATOM    516  C   ASN A  65       7.844  10.547  29.058  1.00  6.00           C  
ATOM    517  O   ASN A  65       6.921  10.020  28.173  1.00  8.00           O  
ATOM    518  CB  ASN A  65       6.724  10.283  31.142  1.00  6.00           C  
ATOM    519  CG  ASN A  65       8.042   9.756  31.711  1.00  6.00           C  
ATOM    520  OD1 ASN A  65       8.833  10.217  31.964  1.00  8.00           O  
ATOM    521  ND2 ASN A  65       7.910   8.438  31.837  1.00  8.00           N  
ATOM    522  N   ASP A  66       9.031  10.547  29.058  1.00  7.00           N  
ATOM    523  CA  ASP A  66       9.954  10.151  27.858  1.00  6.00           C  
ATOM    524  C   ASP A  66      11.074   9.888  28.426  1.00  6.00           C  
ATOM    525  O   ASP A  66      11.865   9.229  27.794  1.00  8.00           O  
ATOM    526  CB  ASP A  66      10.020  11.668  27.100  1.00  6.00           C  
ATOM    527  CG  ASP A  66      10.877  12.524  27.984  1.00  6.00           C  
ATOM    528  OD1 ASP A  66      11.206  12.524  28.932  1.00  7.00           O  
ATOM    529  OD2 ASP A  66      11.602  13.447  27.226  1.00  7.00           O  
ATOM    530  N   GLY A  67      11.536   9.492  29.690  1.00  7.00           N  
ATOM    531  CA  GLY A  67      12.195   8.833  30.321  1.00  6.00           C  
ATOM    532  C   GLY A  67      13.184   9.229  30.511  1.00  6.00           C  
ATOM    533  O   GLY A  67      14.238   8.701  31.206  1.00  8.00           O  
ATOM    534  N   ARG A  68      13.909  10.679  29.816  1.00  7.00           N  
ATOM    535  CA  ARG A  68      15.029  11.404  30.005  1.00  6.00           C  
ATOM    536  C   ARG A  68      14.963  12.722  30.321  1.00  6.00           C  
ATOM    537  O   ARG A  68      15.952  13.381  30.069  1.00  8.00           O  
ATOM    538  CB  ARG A  68      16.150  11.206  28.679  1.00  6.00           C  
ATOM    539  CG  ARG A  68      15.293  11.865  27.731  1.00  6.00           C  
ATOM    540  CD  ARG A  68      16.480  12.195  26.657  1.00  6.00           C  
ATOM    541  NE  ARG A  68      15.820  12.524  25.268  1.00  7.00           N  
ATOM    542  CZ  ARG A  68      16.480  12.920  24.383  1.00  6.00           C  
ATOM    543  NH1 ARG A  68      17.798  12.986  24.573  1.00  7.00           N  
ATOM    544  NH2 ARG A  68      15.952  13.381  23.246  1.00  7.00           N  
ATOM    545  N   THR A  69      13.975  13.315  30.763  1.00  7.00           N  
ATOM    546  CA  THR A  69      13.843  14.700  31.079  1.00  6.00           C  
ATOM    547  C   THR A  69      13.513  14.700  32.659  1.00  6.00           C  
ATOM    548  O   THR A  69      12.195  14.700  32.722  1.00  8.00           O  
ATOM    549  CB  THR A  69      12.524  15.161  30.321  1.00  6.00           C  
ATOM    550  OG1 THR A  69      12.920  15.095  28.932  1.00  8.00           O  
ATOM    551  CG2 THR A  69      12.327  16.809  30.763  1.00  6.00           C  
ATOM    552  N   PRO A  70      14.370  14.700  33.353  1.00  7.00           N  
ATOM    553  CA  PRO A  70      14.172  14.832  34.869  1.00  6.00           C  
ATOM    554  C   PRO A  70      13.250  15.754  35.627  1.00  6.00           C  
ATOM    555  O   PRO A  70      12.524  15.161  36.512  1.00  8.00           O  
ATOM    556  CB  PRO A  70      15.359  14.963  35.501  1.00  6.00           C  
ATOM    557  CG  PRO A  70      16.018  14.832  34.364  1.00  6.00           C  
ATOM    558  CD  PRO A  70      15.623  14.832  33.038  1.00  6.00           C  
ATOM    559  N   GLY A  71      12.854  16.809  35.122  1.00  7.00           N  
ATOM    560  CA  GLY A  71      11.865  17.666  35.754  1.00  6.00           C  
ATOM    561  C   GLY A  71      10.547  17.139  35.754  1.00  6.00           C  
ATOM    562  O   GLY A  71       9.888  17.798  36.449  1.00  8.00           O  
ATOM    563  N   SER A  72      10.547  16.150  35.059  1.00  7.00           N  
ATOM    564  CA  SER A  72       9.229  15.623  34.806  1.00  6.00           C  
ATOM    565  C   SER A  72       8.042  15.029  36.007  1.00  6.00           C  
ATOM    566  O   SER A  72       8.306  14.502  36.891  1.00  8.00           O  
ATOM    567  CB  SER A  72       9.426  14.172  33.985  1.00  6.00           C  
ATOM    568  OG  SER A  72       9.558  14.832  32.848  1.00  8.00           O  
ATOM    569  N   ARG A  73       6.987  15.689  35.627  1.00  7.00           N  
ATOM    570  CA  ARG A  73       5.867  15.689  36.259  1.00  6.00           C  
ATOM    571  C   ARG A  73       4.944  15.293  34.996  1.00  6.00           C  
ATOM    572  O   ARG A  73       5.273  15.491  33.985  1.00  8.00           O  
ATOM    573  CB  ARG A  73       5.273  17.139  36.891  1.00  6.00           C  
ATOM    574  CG  ARG A  73       5.933  17.798  38.533  1.00  6.00           C  
ATOM    575  CD  ARG A  73       6.021  18.812  38.399  1.00  6.00           C  
ATOM    576  NE  ARG A  73       6.762  19.228  39.600  1.00  7.00           N  
ATOM    577  CZ  ARG A  73       7.185  20.494  39.810  1.00  6.00           C  
ATOM    578  NH1 ARG A  73       7.090  21.419  38.847  1.00  7.00           N  
ATOM    579  NH2 ARG A  73       7.692  20.811  40.987  1.00  7.00           N  
ATOM    580  N   ASN A  74       4.021  14.041  35.059  1.00  7.00           N  
ATOM    581  CA  ASN A  74       3.757  13.711  33.985  1.00  6.00           C  
ATOM    582  C   ASN A  74       1.780  13.975  34.111  1.00  6.00           C  
ATOM    583  O   ASN A  74       0.791  13.052  34.238  1.00  8.00           O  
ATOM    584  CB  ASN A  74       3.691  11.931  33.796  1.00  6.00           C  
ATOM    585  CG  ASN A  74       3.230  11.536  32.216  1.00  6.00           C  
ATOM    586  OD1 ASN A  74       3.296  10.679  32.090  1.00  7.00           O  
ATOM    587  ND2 ASN A  74       2.505  12.524  31.585  1.00  7.00           N  
ATOM    588  N   LEU A  75       1.846  15.491  33.669  1.00  7.00           N  
ATOM    589  CA  LEU A  75       0.725  16.018  33.732  1.00  6.00           C  
ATOM    590  C   LEU A  75      -0.264  15.359  32.722  1.00  6.00           C  
ATOM    591  O   LEU A  75      -1.516  14.766  32.848  1.00  8.00           O  
ATOM    592  CB  LEU A  75       0.461  17.798  33.796  1.00  6.00           C  
ATOM    593  CG  LEU A  75       0.791  18.128  34.933  1.00  6.00           C  
ATOM    594  CD1 LEU A  75      -0.198  17.468  36.007  1.00  6.00           C  
ATOM    595  CD2 LEU A  75       2.109  17.600  35.312  1.00  6.00           C  
ATOM    596  N   CYS A  76      -0.132  15.029  31.332  1.00  7.00           N  
ATOM    597  CA  CYS A  76      -1.187  14.107  30.700  1.00  6.00           C  
ATOM    598  C   CYS A  76      -0.791  12.524  30.827  1.00  6.00           C  
ATOM    599  O   CYS A  76      -1.648  11.997  30.258  1.00  8.00           O  
ATOM    600  CB  CYS A  76      -1.384  14.436  29.058  1.00  6.00           C  
ATOM    601  SG  CYS A  76      -1.714  16.150  28.426  1.00 16.00           S  
ATOM    602  N   ASN A  77      -0.132  11.997  31.711  1.00  7.00           N  
ATOM    603  CA  ASN A  77      -0.066  10.942  32.280  1.00  6.00           C  
ATOM    604  C   ASN A  77       0.000   9.888  30.827  1.00  6.00           C  
ATOM    605  O   ASN A  77      -0.659   8.965  30.827  1.00  8.00           O  
ATOM    606  CB  ASN A  77      -1.121  10.415  33.038  1.00  6.00           C  
ATOM    607  CG  ASN A  77      -0.791   9.558  34.048  1.00  6.00           C  
ATOM    608  OD1 ASN A  77      -0.132   8.372  33.985  1.00  7.00           O  
ATOM    609  ND2 ASN A  77      -0.659   9.624  35.375  1.00  7.00           N  
ATOM    610  N   ILE A  78       0.659  10.217  29.942  1.00  7.00           N  
ATOM    611  CA  ILE A  78       0.791   9.492  28.679  1.00  6.00           C  
ATOM    612  C   ILE A  78       2.307   9.492  28.426  1.00  6.00           C  
ATOM    613  O   ILE A  78       3.164  10.415  28.553  1.00  8.00           O  
ATOM    614  CB  ILE A  78       0.132   9.888  27.479  1.00  6.00           C  
ATOM    615  CG1 ILE A  78       0.132   9.097  26.278  1.00  6.00           C  
ATOM    616  CG2 ILE A  78       0.857  11.404  27.163  1.00  6.00           C  
ATOM    617  CD1 ILE A  78      -0.659   7.778  26.531  1.00  6.00           C  
ATOM    618  N   PRO A  79       3.098   8.569  27.858  1.00  7.00           N  
ATOM    619  CA  PRO A  79       4.614   8.569  27.542  1.00  6.00           C  
ATOM    620  C   PRO A  79       4.746   9.426  26.152  1.00  6.00           C  
ATOM    621  O   PRO A  79       3.955   8.899  25.268  1.00  8.00           O  
ATOM    622  CB  PRO A  79       5.010   7.053  27.479  1.00  6.00           C  
ATOM    623  CG  PRO A  79       3.691   6.262  27.479  1.00  6.00           C  
ATOM    624  CD  PRO A  79       2.571   7.317  27.668  1.00  6.00           C  
ATOM    625  N   CYS A  80       5.405  10.151  26.152  1.00  7.00           N  
ATOM    626  CA  CYS A  80       5.933  11.206  24.762  1.00  6.00           C  
ATOM    627  C   CYS A  80       5.405  10.679  23.436  1.00  6.00           C  
ATOM    628  O   CYS A  80       4.746  11.206  22.615  1.00  8.00           O  
ATOM    629  CB  CYS A  80       7.383  11.931  25.268  1.00  6.00           C  
ATOM    630  SG  CYS A  80       7.119  13.184  26.531  1.00 16.00           S  
ATOM    631  N   SER A  81       6.130   9.492  23.309  1.00  7.00           N  
ATOM    632  CA  SER A  81       5.999   8.635  22.299  1.00  6.00           C  
ATOM    633  C   SER A  81       4.746   8.306  21.730  1.00  6.00           C  
ATOM    634  O   SER A  81       4.614   8.306  20.340  1.00  8.00           O  
ATOM    635  CB  SER A  81       6.856   7.515  22.741  1.00  6.00           C  
ATOM    636  OG  SER A  81       5.801   6.130  23.120  1.00  8.00           O  
ATOM    637  N   ALA A  82       3.889   8.108  22.551  1.00  7.00           N  
ATOM    638  CA  ALA A  82       2.307   8.108  22.236  1.00  6.00           C  
ATOM    639  C   ALA A  82       2.043   9.229  21.225  1.00  6.00           C  
ATOM    640  O   ALA A  82       0.989   8.899  20.214  1.00  8.00           O  
ATOM    641  CB  ALA A  82       1.318   8.174  23.373  1.00  6.00           C  
ATOM    642  N   LEU A  83       2.571  10.415  21.604  1.00  7.00           N  
ATOM    643  CA  LEU A  83       2.439  11.536  20.846  1.00  6.00           C  
ATOM    644  C   LEU A  83       2.637  11.470  19.330  1.00  6.00           C  
ATOM    645  O   LEU A  83       1.978  12.195  18.698  1.00  8.00           O  
ATOM    646  CB  LEU A  83       2.966  12.920  21.541  1.00  6.00           C  
ATOM    647  CG  LEU A  83       2.109  12.920  22.867  1.00  6.00           C  
ATOM    648  CD1 LEU A  83       2.637  14.172  23.625  1.00  6.00           C  
ATOM    649  CD2 LEU A  83       0.593  12.986  22.551  1.00  6.00           C  
ATOM    650  N   LEU A  84       3.428  10.679  19.077  1.00  7.00           N  
ATOM    651  CA  LEU A  84       4.021  10.679  17.624  1.00  6.00           C  
ATOM    652  C   LEU A  84       3.428   9.756  16.677  1.00  6.00           C  
ATOM    653  O   LEU A  84       3.625   9.558  15.666  1.00  8.00           O  
ATOM    654  CB  LEU A  84       5.603  10.217  17.056  1.00  6.00           C  
ATOM    655  CG  LEU A  84       6.724  10.547  18.509  1.00  6.00           C  
ATOM    656  CD1 LEU A  84       7.844  10.086  18.003  1.00  6.00           C  
ATOM    657  CD2 LEU A  84       6.460  12.327  18.193  1.00  6.00           C  
ATOM    658  N   SER A  85       2.505   8.899  17.182  1.00  7.00           N  
ATOM    659  CA  SER A  85       1.846   7.910  16.361  1.00  6.00           C  
ATOM    660  C   SER A  85       0.330   8.569  15.413  1.00  6.00           C  
ATOM    661  O   SER A  85       0.330   9.888  15.287  1.00  8.00           O  
ATOM    662  CB  SER A  85       1.055   6.856  17.182  1.00  6.00           C  
ATOM    663  OG  SER A  85       0.000   7.317  18.003  1.00  8.00           O  
ATOM    664  N   SER A  86       0.066   7.976  14.403  1.00  7.00           N  
ATOM    665  CA  SER A  86      -0.264   8.503  13.329  1.00  6.00           C  
ATOM    666  C   SER A  86      -1.780   8.569  13.645  1.00  6.00           C  
ATOM    667  O   SER A  86      -2.439   9.097  13.139  1.00  8.00           O  
ATOM    668  CB  SER A  86      -0.066   7.647  12.002  1.00  6.00           C  
ATOM    669  OG  SER A  86       0.906   7.237  11.514  1.00  8.00           O  
ATOM    670  N   ASP A  87      -2.109   8.306  14.908  1.00  7.00           N  
ATOM    671  CA  ASP A  87      -3.428   8.899  15.413  1.00  6.00           C  
ATOM    672  C   ASP A  87      -3.362   9.954  16.677  1.00  6.00           C  
ATOM    673  O   ASP A  87      -2.505   9.690  17.435  1.00  8.00           O  
ATOM    674  CB  ASP A  87      -3.757   7.778  16.234  1.00  6.00           C  
ATOM    675  CG  ASP A  87      -5.142   7.581  16.424  1.00  6.00           C  
ATOM    676  OD1 ASP A  87      -5.801   8.042  17.056  1.00  8.00           O  
ATOM    677  OD2 ASP A  87      -5.867   6.987  15.729  1.00  8.00           O  
ATOM    678  N   ILE A  88      -3.757  11.008  16.424  1.00  7.00           N  
ATOM    679  CA  ILE A  88      -3.823  12.261  17.182  1.00  6.00           C  
ATOM    680  C   ILE A  88      -4.614  12.063  18.509  1.00  6.00           C  
ATOM    681  O   ILE A  88      -4.417  13.513  18.951  1.00  8.00           O  
ATOM    682  CB  ILE A  88      -3.823  13.645  16.424  1.00  6.00           C  
ATOM    683  CG1 ILE A  88      -5.076  13.645  15.919  1.00  6.00           C  
ATOM    684  CG2 ILE A  88      -2.769  13.513  15.161  1.00  6.00           C  
ATOM    685  CD1 ILE A  88      -5.933  15.029  15.350  1.00  6.00           C  
ATOM    686  N   THR A  89      -5.010  11.074  18.824  1.00  7.00           N  
ATOM    687  CA  THR A  89      -5.933  11.008  19.961  1.00  6.00           C  
ATOM    688  C   THR A  89      -5.405  11.865  21.225  1.00  6.00           C  
ATOM    689  O   THR A  89      -5.933  12.524  21.478  1.00  8.00           O  
ATOM    690  CB  THR A  89      -6.262   9.756  20.214  1.00  6.00           C  
ATOM    691  OG1 THR A  89      -7.251   9.229  19.140  1.00  8.00           O  
ATOM    692  CG2 THR A  89      -7.251   9.888  21.478  1.00  6.00           C  
ATOM    693  N   ALA A  90      -4.482  10.942  21.478  1.00  7.00           N  
ATOM    694  CA  ALA A  90      -3.230  11.668  22.425  1.00  6.00           C  
ATOM    695  C   ALA A  90      -3.164  12.722  22.615  1.00  6.00           C  
ATOM    696  O   ALA A  90      -3.296  13.184  23.373  1.00  8.00           O  
ATOM    697  CB  ALA A  90      -2.307  10.217  22.425  1.00  6.00           C  
ATOM    698  N   SER A  91      -2.703  13.184  21.604  1.00  7.00           N  
ATOM    699  CA  SER A  91      -2.175  14.766  21.478  1.00  6.00           C  
ATOM    700  C   SER A  91      -3.164  15.623  21.730  1.00  6.00           C  
ATOM    701  O   SER A  91      -3.164  16.348  22.425  1.00  8.00           O  
ATOM    702  CB  SER A  91      -1.582  14.963  20.025  1.00  6.00           C  
ATOM    703  OG  SER A  91      -0.396  13.975  19.709  1.00  8.00           O  
ATOM    704  N   VAL A  92      -4.285  15.491  20.846  1.00  7.00           N  
ATOM    705  CA  VAL A  92      -5.339  16.348  20.909  1.00  6.00           C  
ATOM    706  C   VAL A  92      -5.999  16.348  22.362  1.00  6.00           C  
ATOM    707  O   VAL A  92      -6.130  17.007  22.804  1.00  8.00           O  
ATOM    708  CB  VAL A  92      -6.856  15.820  19.961  1.00  6.00           C  
ATOM    709  CG1 VAL A  92      -7.976  15.952  20.088  1.00  6.00           C  
ATOM    710  CG2 VAL A  92      -5.933  16.150  18.445  1.00  6.00           C  
ATOM    711  N   ASN A  93      -5.933  14.963  22.804  1.00  7.00           N  
ATOM    712  CA  ASN A  93      -6.658  14.766  24.257  1.00  6.00           C  
ATOM    713  C   ASN A  93      -5.735  15.293  25.268  1.00  6.00           C  
ATOM    714  O   ASN A  93      -6.262  15.886  26.089  1.00  8.00           O  
ATOM    715  CB  ASN A  93      -6.724  13.118  24.447  1.00  6.00           C  
ATOM    716  CG  ASN A  93      -7.976  12.590  24.194  1.00  6.00           C  
ATOM    717  OD1 ASN A  93      -8.767  13.184  24.004  1.00  7.00           O  
ATOM    718  ND2 ASN A  93      -8.042  11.206  24.383  1.00  7.00           N  
ATOM    719  N   CYS A  94      -4.614  15.425  25.015  1.00  7.00           N  
ATOM    720  CA  CYS A  94      -3.362  16.084  25.836  1.00  6.00           C  
ATOM    721  C   CYS A  94      -3.428  17.600  25.710  1.00  6.00           C  
ATOM    722  O   CYS A  94      -3.428  18.523  26.531  1.00  8.00           O  
ATOM    723  CB  CYS A  94      -2.175  15.754  25.268  1.00  6.00           C  
ATOM    724  SG  CYS A  94      -0.791  16.150  26.405  1.00 16.00           S  
ATOM    725  N   ALA A  95      -3.428  17.930  24.447  1.00  7.00           N  
ATOM    726  CA  ALA A  95      -3.691  19.446  23.941  1.00  6.00           C  
ATOM    727  C   ALA A  95      -4.746  19.973  24.699  1.00  6.00           C  
ATOM    728  O   ALA A  95      -4.746  20.962  24.889  1.00  8.00           O  
ATOM    729  CB  ALA A  95      -3.955  19.182  22.425  1.00  6.00           C  
ATOM    730  N   LYS A  96      -5.933  19.446  24.889  1.00  7.00           N  
ATOM    731  CA  LYS A  96      -7.053  19.710  25.647  1.00  6.00           C  
ATOM    732  C   LYS A  96      -6.592  20.105  27.163  1.00  6.00           C  
ATOM    733  O   LYS A  96      -7.053  21.358  27.415  1.00  8.00           O  
ATOM    734  CB  LYS A  96      -8.108  18.787  25.584  1.00  6.00           C  
ATOM    735  CG  LYS A  96      -8.833  18.787  24.194  1.00  6.00           C  
ATOM    736  CD  LYS A  96     -10.020  18.193  24.131  1.00  6.00           C  
ATOM    737  CE  LYS A  96     -10.679  17.666  22.867  1.00  6.00           C  
ATOM    738  NZ  LYS A  96     -11.206  16.150  23.120  1.00  7.00           N  
ATOM    739  N   LYS A  97      -5.801  19.775  27.794  1.00  7.00           N  
ATOM    740  CA  LYS A  97      -5.273  20.303  29.247  1.00  6.00           C  
ATOM    741  C   LYS A  97      -4.285  21.423  29.121  1.00  6.00           C  
ATOM    742  O   LYS A  97      -4.417  21.951  30.511  1.00  8.00           O  
ATOM    743  CB  LYS A  97      -5.076  19.116  29.879  1.00  6.00           C  
ATOM    744  CG  LYS A  97      -5.801  17.930  30.005  1.00  6.00           C  
ATOM    745  CD  LYS A  97      -5.273  16.941  31.079  1.00  6.00           C  
ATOM    746  CE  LYS A  97      -6.724  16.480  32.153  1.00  6.00           C  
ATOM    747  NZ  LYS A  97      -6.122  15.643  33.146  1.00  7.00           N  
ATOM    748  N   ILE A  98      -3.757  21.489  28.047  1.00  7.00           N  
ATOM    749  CA  ILE A  98      -2.835  22.742  27.921  1.00  6.00           C  
ATOM    750  C   ILE A  98      -3.428  24.060  27.542  1.00  6.00           C  
ATOM    751  O   ILE A  98      -3.164  24.653  27.984  1.00  8.00           O  
ATOM    752  CB  ILE A  98      -1.846  22.412  26.721  1.00  6.00           C  
ATOM    753  CG1 ILE A  98      -1.055  21.094  27.163  1.00  6.00           C  
ATOM    754  CG2 ILE A  98      -0.989  23.731  26.721  1.00  6.00           C  
ATOM    755  CD1 ILE A  98      -0.330  20.105  25.899  1.00  6.00           C  
ATOM    756  N   VAL A  99      -4.482  23.862  26.721  1.00  7.00           N  
ATOM    757  CA  VAL A  99      -5.076  24.851  26.278  1.00  6.00           C  
ATOM    758  C   VAL A  99      -6.262  25.379  27.416  1.00  6.00           C  
ATOM    759  O   VAL A  99      -6.856  26.433  27.289  1.00  8.00           O  
ATOM    760  CB  VAL A  99      -6.328  24.653  25.015  1.00  6.00           C  
ATOM    761  CG1 VAL A  99      -7.449  23.731  25.647  1.00  6.00           C  
ATOM    762  CG2 VAL A  99      -6.724  25.510  24.383  1.00  6.00           C  
ATOM    763  N   SER A 100      -6.262  24.522  28.553  1.00  7.00           N  
ATOM    764  CA  SER A 100      -7.581  24.851  29.563  1.00  6.00           C  
ATOM    765  C   SER A 100      -6.724  25.049  30.953  1.00  6.00           C  
ATOM    766  O   SER A 100      -7.449  25.247  31.648  1.00  8.00           O  
ATOM    767  CB  SER A 100      -8.240  24.060  29.816  1.00  6.00           C  
ATOM    768  OG  SER A 100      -9.097  23.203  28.995  1.00  8.00           O  
ATOM    769  N   ASP A 101      -5.537  25.379  30.953  1.00  7.00           N  
ATOM    770  CA  ASP A 101      -4.944  25.313  32.153  1.00  6.00           C  
ATOM    771  C   ASP A 101      -4.746  26.697  32.406  1.00  6.00           C  
ATOM    772  O   ASP A 101      -5.142  27.158  33.353  1.00  8.00           O  
ATOM    773  CB  ASP A 101      -3.626  24.588  32.343  1.00  6.00           C  
ATOM    774  CG  ASP A 101      -3.253  23.268  31.950  1.00  6.00           C  
ATOM    775  OD1 ASP A 101      -4.205  22.509  31.996  1.00  8.00           O  
ATOM    776  OD2 ASP A 101      -2.170  22.841  31.654  1.00  8.00           O  
ATOM    777  N   GLY A 102      -4.417  27.686  31.585  1.00  7.00           N  
ATOM    778  CA  GLY A 102      -4.482  29.004  31.774  1.00  6.00           C  
ATOM    779  C   GLY A 102      -4.219  29.993  30.700  1.00  6.00           C  
ATOM    780  O   GLY A 102      -4.614  30.982  30.700  1.00  8.00           O  
ATOM    781  N   ASN A 103      -3.626  29.597  29.563  1.00  7.00           N  
ATOM    782  CA  ASN A 103      -2.769  30.454  28.679  1.00  6.00           C  
ATOM    783  C   ASN A 103      -3.032  30.520  27.226  1.00  6.00           C  
ATOM    784  O   ASN A 103      -2.439  30.982  26.405  1.00  8.00           O  
ATOM    785  CB  ASN A 103      -1.450  30.322  28.742  1.00  6.00           C  
ATOM    786  CG  ASN A 103      -0.791  30.586  30.321  1.00  6.00           C  
ATOM    787  OD1 ASN A 103      -0.659  31.641  30.448  1.00  8.00           O  
ATOM    788  ND2 ASN A 103      -0.132  29.993  30.953  1.00  8.00           N  
ATOM    789  N   GLY A 104      -4.087  29.729  27.163  1.00  7.00           N  
ATOM    790  CA  GLY A 104      -4.614  29.334  25.899  1.00  6.00           C  
ATOM    791  C   GLY A 104      -3.560  28.806  25.015  1.00  6.00           C  
ATOM    792  O   GLY A 104      -2.637  28.015  25.647  1.00  8.00           O  
ATOM    793  N   MET A 105      -3.823  29.268  23.752  1.00  7.00           N  
ATOM    794  CA  MET A 105      -2.966  28.674  22.741  1.00  6.00           C  
ATOM    795  C   MET A 105      -1.648  29.465  22.741  1.00  6.00           C  
ATOM    796  O   MET A 105      -0.659  29.334  21.920  1.00  8.00           O  
ATOM    797  CB  MET A 105      -3.494  28.740  21.414  1.00  6.00           C  
ATOM    798  CG  MET A 105      -4.614  27.949  21.730  1.00  6.00           C  
ATOM    799  SD  MET A 105      -5.076  27.488  20.025  1.00 16.00           S  
ATOM    800  CE  MET A 105      -3.823  26.367  19.203  1.00  6.00           C  
ATOM    801  N   ASN A 106      -1.450  30.322  23.752  1.00  7.00           N  
ATOM    802  CA  ASN A 106      -0.198  31.311  24.004  1.00  6.00           C  
ATOM    803  C   ASN A 106       0.857  30.388  24.510  1.00  6.00           C  
ATOM    804  O   ASN A 106       1.978  30.718  24.320  1.00  8.00           O  
ATOM    805  CB  ASN A 106      -0.725  32.300  25.015  1.00  6.00           C  
ATOM    806  CG  ASN A 106      -1.187  33.618  24.068  1.00  6.00           C  
ATOM    807  OD1 ASN A 106      -0.659  34.278  23.373  1.00  7.00           O  
ATOM    808  ND2 ASN A 106      -2.241  33.948  24.636  1.00  7.00           N  
ATOM    809  N   ALA A 107       0.659  29.334  25.268  1.00  7.00           N  
ATOM    810  CA  ALA A 107       1.318  28.213  25.647  1.00  6.00           C  
ATOM    811  C   ALA A 107       1.978  27.554  24.447  1.00  6.00           C  
ATOM    812  O   ALA A 107       3.164  26.829  24.573  1.00  8.00           O  
ATOM    813  CB  ALA A 107       0.659  26.829  26.531  1.00  6.00           C  
ATOM    814  N   TRP A 108       1.846  27.686  23.309  1.00  7.00           N  
ATOM    815  CA  TRP A 108       2.373  27.554  22.109  1.00  6.00           C  
ATOM    816  C   TRP A 108       3.164  28.806  21.351  1.00  6.00           C  
ATOM    817  O   TRP A 108       2.373  29.136  20.530  1.00  8.00           O  
ATOM    818  CB  TRP A 108       1.648  26.829  20.909  1.00  6.00           C  
ATOM    819  CG  TRP A 108       1.055  25.510  21.288  1.00  6.00           C  
ATOM    820  CD1 TRP A 108       1.780  24.390  20.972  1.00  6.00           C  
ATOM    821  CD2 TRP A 108      -0.198  24.851  21.920  1.00  6.00           C  
ATOM    822  NE1 TRP A 108       0.791  23.137  21.288  1.00  7.00           N  
ATOM    823  CE2 TRP A 108      -0.132  23.533  21.857  1.00  6.00           C  
ATOM    824  CE3 TRP A 108      -1.187  25.576  22.362  1.00  6.00           C  
ATOM    825  CZ2 TRP A 108      -1.318  22.874  22.299  1.00  6.00           C  
ATOM    826  CZ3 TRP A 108      -2.109  24.851  22.867  1.00  6.00           C  
ATOM    827  CH2 TRP A 108      -2.109  23.467  22.867  1.00  6.00           C  
ATOM    828  N   VAL A 109       4.351  28.806  21.857  1.00  7.00           N  
ATOM    829  CA  VAL A 109       5.273  29.861  21.288  1.00  6.00           C  
ATOM    830  C   VAL A 109       4.944  30.125  19.709  1.00  6.00           C  
ATOM    831  O   VAL A 109       4.614  31.509  19.330  1.00  8.00           O  
ATOM    832  CB  VAL A 109       6.658  29.531  21.351  1.00  6.00           C  
ATOM    833  CG1 VAL A 109       6.995  28.230  20.251  1.00  6.00           C  
ATOM    834  CG2 VAL A 109       7.581  30.652  20.846  1.00  6.00           C  
ATOM    835  N   ALA A 110       4.812  29.268  18.888  1.00  7.00           N  
ATOM    836  CA  ALA A 110       4.482  29.466  17.435  1.00  6.00           C  
ATOM    837  C   ALA A 110       3.164  29.993  17.056  1.00  6.00           C  
ATOM    838  O   ALA A 110       3.032  30.784  16.171  1.00  8.00           O  
ATOM    839  CB  ALA A 110       4.614  27.818  16.487  1.00  6.00           C  
ATOM    840  N   TRP A 111       1.978  29.663  17.435  1.00  7.00           N  
ATOM    841  CA  TRP A 111       0.461  30.322  17.182  1.00  6.00           C  
ATOM    842  C   TRP A 111       0.593  31.707  17.308  1.00  6.00           C  
ATOM    843  O   TRP A 111       0.000  32.630  16.424  1.00  8.00           O  
ATOM    844  CB  TRP A 111      -0.659  29.268  17.940  1.00  6.00           C  
ATOM    845  CG  TRP A 111      -1.846  30.125  18.066  1.00  6.00           C  
ATOM    846  CD1 TRP A 111      -2.637  29.861  17.182  1.00  6.00           C  
ATOM    847  CD2 TRP A 111      -2.175  30.850  19.140  1.00  6.00           C  
ATOM    848  NE1 TRP A 111      -3.889  30.520  17.687  1.00  7.00           N  
ATOM    849  CE2 TRP A 111      -3.691  31.179  18.888  1.00  6.00           C  
ATOM    850  CE3 TRP A 111      -1.780  31.509  20.214  1.00  6.00           C  
ATOM    851  CZ2 TRP A 111      -4.153  31.970  19.709  1.00  6.00           C  
ATOM    852  CZ3 TRP A 111      -2.307  32.036  20.972  1.00  6.00           C  
ATOM    853  CH2 TRP A 111      -3.823  32.300  20.783  1.00  6.00           C  
ATOM    854  N   ARG A 112       1.121  31.839  18.509  1.00  7.00           N  
ATOM    855  CA  ARG A 112       1.318  33.289  19.203  1.00  6.00           C  
ATOM    856  C   ARG A 112       2.175  34.014  18.130  1.00  6.00           C  
ATOM    857  O   ARG A 112       1.648  35.069  17.687  1.00  8.00           O  
ATOM    858  CB  ARG A 112       2.043  33.091  20.467  1.00  6.00           C  
ATOM    859  CG  ARG A 112       2.109  34.739  21.099  1.00  6.00           C  
ATOM    860  CD  ARG A 112       3.032  34.607  22.362  1.00  6.00           C  
ATOM    861  NE  ARG A 112       2.307  33.618  23.373  1.00  7.00           N  
ATOM    862  CZ  ARG A 112       3.019  33.140  24.395  1.00  6.00           C  
ATOM    863  NH1 ARG A 112       4.338  33.335  24.539  1.00  7.00           N  
ATOM    864  NH2 ARG A 112       2.351  32.434  25.289  1.00  7.00           N  
ATOM    865  N   ASN A 113       3.296  33.816  17.814  1.00  7.00           N  
ATOM    866  CA  ASN A 113       4.219  34.673  16.993  1.00  6.00           C  
ATOM    867  C   ASN A 113       3.494  34.739  15.413  1.00  6.00           C  
ATOM    868  O   ASN A 113       3.691  35.794  14.908  1.00  8.00           O  
ATOM    869  CB  ASN A 113       5.537  34.014  17.056  1.00  6.00           C  
ATOM    870  CG  ASN A 113       6.262  34.409  18.445  1.00  6.00           C  
ATOM    871  OD1 ASN A 113       5.867  35.266  18.951  1.00  7.00           O  
ATOM    872  ND2 ASN A 113       7.053  33.421  18.761  1.00  7.00           N  
ATOM    873  N   ARG A 114       3.230  33.552  14.971  1.00  7.00           N  
ATOM    874  CA  ARG A 114       2.769  33.355  13.455  1.00  6.00           C  
ATOM    875  C   ARG A 114       1.252  33.157  13.139  1.00  6.00           C  
ATOM    876  O   ARG A 114       1.055  33.289  12.128  1.00  8.00           O  
ATOM    877  CB  ARG A 114       3.560  32.102  12.823  1.00  6.00           C  
ATOM    878  CG  ARG A 114       4.746  31.970  13.455  1.00  6.00           C  
ATOM    879  CD  ARG A 114       5.735  31.179  12.634  1.00  6.00           C  
ATOM    880  NE  ARG A 114       5.801  31.509  11.181  1.00  7.00           N  
ATOM    881  CZ  ARG A 114       6.460  30.652  10.549  1.00  6.00           C  
ATOM    882  NH1 ARG A 114       7.251  29.663  11.244  1.00  7.00           N  
ATOM    883  NH2 ARG A 114       6.064  30.982   9.286  1.00  7.00           N  
ATOM    884  N   CYS A 115       0.330  33.091  14.150  1.00  7.00           N  
ATOM    885  CA  CYS A 115      -1.121  32.564  13.771  1.00  6.00           C  
ATOM    886  C   CYS A 115      -1.978  33.552  14.529  1.00  6.00           C  
ATOM    887  O   CYS A 115      -2.769  34.080  14.213  1.00  8.00           O  
ATOM    888  CB  CYS A 115      -1.648  31.443  14.213  1.00  6.00           C  
ATOM    889  SG  CYS A 115      -0.857  29.663  13.897  1.00 16.00           S  
ATOM    890  N   LYS A 116      -1.648  34.080  15.792  1.00  7.00           N  
ATOM    891  CA  LYS A 116      -2.373  34.937  16.677  1.00  6.00           C  
ATOM    892  C   LYS A 116      -2.637  36.387  16.045  1.00  6.00           C  
ATOM    893  O   LYS A 116      -1.912  36.980  16.045  1.00  8.00           O  
ATOM    894  CB  LYS A 116      -1.846  35.266  18.193  1.00  6.00           C  
ATOM    895  CG  LYS A 116      -2.439  35.925  19.077  1.00  6.00           C  
ATOM    896  CD  LYS A 116      -2.175  35.662  20.277  1.00  6.00           C  
ATOM    897  CE  LYS A 116      -2.307  36.716  21.288  1.00  6.00           C  
ATOM    898  NZ  LYS A 116      -1.846  36.585  22.615  1.00  7.00           N  
ATOM    899  N   GLY A 117      -3.757  36.585  15.792  1.00  7.00           N  
ATOM    900  CA  GLY A 117      -4.153  37.639  15.224  1.00  6.00           C  
ATOM    901  C   GLY A 117      -4.153  37.639  13.645  1.00  6.00           C  
ATOM    902  O   GLY A 117      -4.087  38.892  13.266  1.00  8.00           O  
ATOM    903  N   THR A 118      -4.087  36.651  12.823  1.00  7.00           N  
ATOM    904  CA  THR A 118      -4.087  36.519  11.370  1.00  6.00           C  
ATOM    905  C   THR A 118      -5.537  35.860  11.055  1.00  6.00           C  
ATOM    906  O   THR A 118      -6.130  35.464  11.876  1.00  8.00           O  
ATOM    907  CB  THR A 118      -2.900  35.596  10.928  1.00  6.00           C  
ATOM    908  OG1 THR A 118      -2.966  34.278  11.244  1.00  8.00           O  
ATOM    909  CG2 THR A 118      -1.582  36.123  11.749  1.00  6.00           C  
ATOM    910  N   ASP A 119      -5.933  35.596   9.854  1.00  7.00           N  
ATOM    911  CA  ASP A 119      -7.185  35.200   9.475  1.00  6.00           C  
ATOM    912  C   ASP A 119      -6.987  33.421   9.223  1.00  6.00           C  
ATOM    913  O   ASP A 119      -6.592  33.091   8.212  1.00  8.00           O  
ATOM    914  CB  ASP A 119      -7.910  35.596   8.212  1.00  6.00           C  
ATOM    915  CG  ASP A 119      -7.383  35.398   6.949  1.00  6.00           C  
ATOM    916  OD1 ASP A 119      -8.042  34.937   6.506  1.00  8.00           O  
ATOM    917  OD2 ASP A 119      -6.592  35.596   6.822  1.00  8.00           O  
ATOM    918  N   VAL A 120      -6.921  32.761  10.486  1.00  7.00           N  
ATOM    919  CA  VAL A 120      -6.592  31.311  10.676  1.00  6.00           C  
ATOM    920  C   VAL A 120      -7.778  30.784   9.854  1.00  6.00           C  
ATOM    921  O   VAL A 120      -7.383  29.663   9.475  1.00  8.00           O  
ATOM    922  CB  VAL A 120      -6.790  31.113  12.192  1.00  6.00           C  
ATOM    923  CG1 VAL A 120      -5.537  31.970  12.887  1.00  6.00           C  
ATOM    924  CG2 VAL A 120      -7.976  31.707  12.760  1.00  6.00           C  
ATOM    925  N   GLN A 121      -8.965  31.113   9.475  1.00  7.00           N  
ATOM    926  CA  GLN A 121      -9.954  30.520   8.591  1.00  6.00           C  
ATOM    927  C   GLN A 121      -9.558  29.993   7.075  1.00  6.00           C  
ATOM    928  O   GLN A 121      -9.888  29.202   6.949  1.00  8.00           O  
ATOM    929  CB  GLN A 121     -11.074  31.443   8.402  1.00  6.00           C  
ATOM    930  CG  GLN A 121     -11.536  32.036   9.475  1.00  6.00           C  
ATOM    931  CD  GLN A 121     -12.650  33.097   9.556  1.00  6.00           C  
ATOM    932  OE1 GLN A 121     -13.394  33.336  10.568  1.00  7.00           O  
ATOM    933  NE2 GLN A 121     -12.737  33.728   8.462  1.00  7.00           N  
ATOM    934  N   ALA A 122      -8.438  30.718   6.696  1.00  7.00           N  
ATOM    935  CA  ALA A 122      -7.844  30.652   5.306  1.00  6.00           C  
ATOM    936  C   ALA A 122      -6.987  29.136   5.243  1.00  6.00           C  
ATOM    937  O   ALA A 122      -6.921  28.674   4.548  1.00  8.00           O  
ATOM    938  CB  ALA A 122      -6.724  31.509   4.864  1.00  6.00           C  
ATOM    939  N   TRP A 123      -6.856  28.740   6.506  1.00  7.00           N  
ATOM    940  CA  TRP A 123      -6.262  27.290   6.759  1.00  6.00           C  
ATOM    941  C   TRP A 123      -7.053  26.499   6.317  1.00  6.00           C  
ATOM    942  O   TRP A 123      -6.724  25.049   5.938  1.00  8.00           O  
ATOM    943  CB  TRP A 123      -5.405  27.158   8.149  1.00  6.00           C  
ATOM    944  CG  TRP A 123      -4.153  28.279   8.149  1.00  6.00           C  
ATOM    945  CD1 TRP A 123      -3.823  29.334   8.591  1.00  6.00           C  
ATOM    946  CD2 TRP A 123      -3.230  27.752   7.391  1.00  6.00           C  
ATOM    947  NE1 TRP A 123      -2.703  29.597   8.212  1.00  7.00           N  
ATOM    948  CE2 TRP A 123      -2.307  28.740   7.517  1.00  6.00           C  
ATOM    949  CE3 TRP A 123      -2.900  26.697   6.633  1.00  6.00           C  
ATOM    950  CZ2 TRP A 123      -1.055  28.609   6.885  1.00  6.00           C  
ATOM    951  CZ3 TRP A 123      -1.648  26.565   6.064  1.00  6.00           C  
ATOM    952  CH2 TRP A 123      -0.857  27.422   6.127  1.00  6.00           C  
ATOM    953  N   ILE A 124      -8.569  26.433   6.696  1.00  7.00           N  
ATOM    954  CA  ILE A 124      -9.756  25.576   6.570  1.00  6.00           C  
ATOM    955  C   ILE A 124     -10.415  25.906   5.369  1.00  6.00           C  
ATOM    956  O   ILE A 124     -11.470  25.181   5.054  1.00  8.00           O  
ATOM    957  CB  ILE A 124     -10.415  25.379   7.833  1.00  6.00           C  
ATOM    958  CG1 ILE A 124     -11.206  26.697   8.212  1.00  6.00           C  
ATOM    959  CG2 ILE A 124      -9.888  24.522   8.844  1.00  6.00           C  
ATOM    960  CD1 ILE A 124     -11.865  26.367   9.286  1.00  6.00           C  
ATOM    961  N   ARG A 125     -10.283  26.829   4.611  1.00  7.00           N  
ATOM    962  CA  ARG A 125     -10.877  27.026   3.411  1.00  6.00           C  
ATOM    963  C   ARG A 125     -10.679  25.972   2.337  1.00  6.00           C  
ATOM    964  O   ARG A 125      -9.888  25.708   2.085  1.00  8.00           O  
ATOM    965  CB  ARG A 125     -10.481  28.477   2.779  1.00  6.00           C  
ATOM    966  CG  ARG A 125     -10.439  29.656   3.950  1.00  6.00           C  
ATOM    967  CD  ARG A 125      -9.397  30.695   3.583  1.00  6.00           C  
ATOM    968  NE  ARG A 125      -9.394  31.806   4.549  1.00  7.00           N  
ATOM    969  CZ  ARG A 125      -8.365  32.672   4.678  1.00  6.00           C  
ATOM    970  NH1 ARG A 125      -7.208  32.468   4.033  1.00  7.00           N  
ATOM    971  NH2 ARG A 125      -8.518  33.735   5.448  1.00  7.00           N  
ATOM    972  N   GLY A 126     -11.668  25.510   1.832  1.00  7.00           N  
ATOM    973  CA  GLY A 126     -11.602  24.588   0.695  1.00  6.00           C  
ATOM    974  C   GLY A 126     -11.931  23.137   1.327  1.00  6.00           C  
ATOM    975  O   GLY A 126     -12.195  22.478   0.821  1.00  8.00           O  
ATOM    976  N   CYS A 127     -11.865  23.137   2.716  1.00  7.00           N  
ATOM    977  CA  CYS A 127     -12.327  21.951   3.411  1.00  6.00           C  
ATOM    978  C   CYS A 127     -13.645  21.423   3.601  1.00  6.00           C  
ATOM    979  O   CYS A 127     -14.568  22.280   3.727  1.00  8.00           O  
ATOM    980  CB  CYS A 127     -11.404  21.687   4.738  1.00  6.00           C  
ATOM    981  SG  CYS A 127      -9.558  22.083   4.675  1.00 16.00           S  
ATOM    982  N   ARG A 128     -13.975  20.435   3.348  1.00  7.00           N  
ATOM    983  CA  ARG A 128     -15.359  19.710   3.601  1.00  6.00           C  
ATOM    984  C   ARG A 128     -15.425  19.512   5.054  1.00  6.00           C  
ATOM    985  O   ARG A 128     -14.634  18.589   5.306  1.00  8.00           O  
ATOM    986  CB  ARG A 128     -15.623  18.853   2.653  1.00  6.00           C  
ATOM    987  CG  ARG A 128     -15.233  18.979   1.071  1.00  6.00           C  
ATOM    988  CD  ARG A 128     -14.831  17.707   0.350  1.00  6.00           C  
ATOM    989  NE  ARG A 128     -14.532  17.973  -1.066  1.00  7.00           N  
ATOM    990  CZ  ARG A 128     -13.825  17.126  -1.846  1.00  6.00           C  
ATOM    991  NH1 ARG A 128     -13.214  16.054  -1.321  1.00  7.00           N  
ATOM    992  NH2 ARG A 128     -13.750  17.364  -3.143  1.00  7.00           N  
ATOM    993  N   LEU A 129     -15.952  20.105   5.812  1.00  7.00           N  
ATOM    994  CA  LEU A 129     -15.952  19.907   7.264  1.00  6.00           C  
ATOM    995  C   LEU A 129     -17.402  19.907   7.707  1.00  6.00           C  
ATOM    996  O   LEU A 129     -18.062  19.973   7.138  1.00  8.00           O  
ATOM    997  CB  LEU A 129     -15.227  21.226   7.959  1.00  6.00           C  
ATOM    998  CG  LEU A 129     -13.909  21.423   7.391  1.00  6.00           C  
ATOM    999  CD1 LEU A 129     -13.052  22.412   7.833  1.00  6.00           C  
ATOM   1000  CD2 LEU A 129     -12.854  19.973   7.833  1.00  6.00           C  
ATOM   1001  OXT LEU A 129     -17.864  19.907   8.844  1.00  8.00           O  
TER    1002      LEU A 129                                                      
HETATM 1003  O   HOH A 130       1.437  16.676  19.902  1.00  7.36           O  
HETATM 1004  O   HOH A 131      -0.616  11.133  19.523  1.00  8.12           O  
HETATM 1005  O   HOH A 132      -1.859  12.396   4.827  1.00  5.12           O  
HETATM 1006  O   HOH A 133      -4.156  10.145   2.848  1.00  5.71           O  
HETATM 1007  O   HOH A 134     -11.782  17.733   4.758  1.00  6.95           O  
HETATM 1008  O   HOH A 135       3.243  19.918   5.368  1.00  7.67           O  
HETATM 1009  O   HOH A 136     -14.650  25.062   4.959  1.00  8.62           O  
HETATM 1010  O   HOH A 137     -14.388  26.920   2.787  1.00  9.02           O  
HETATM 1011  O   HOH A 138A    -14.817  29.031   5.604  1.00  8.87           O  
HETATM 1012  O   HOH A 139      -2.283  26.351   3.043  1.00  5.44           O  
HETATM 1013  O   HOH A 140      -5.837  19.355   2.104  1.00  8.42           O  
HETATM 1014  O   HOH A 141      -8.404  16.734   1.291  1.00  3.13           O  
HETATM 1015  O   HOH A 142     -12.544  32.373  13.163  1.00  5.87           O  
HETATM 1016  O   HOH A 143     -14.006  31.452   8.669  1.00  6.10           O  
HETATM 1017  O   HOH A 144     -11.974  34.750   9.022  1.00  4.56           O  
HETATM 1018  O   HOH A 145      -3.488  37.134   7.629  1.00  8.16           O  
HETATM 1019  O   HOH A 146      -0.935  32.866   8.179  1.00  8.06           O  
HETATM 1020  O   HOH A 147       8.083  28.178   8.105  1.00 10.17           O  
HETATM 1021  O   HOH A 148       7.499  23.692   4.296  1.00  6.63           O  
HETATM 1022  O   HOH A 149       6.355  15.951   3.994  1.00  7.31           O  
HETATM 1023  O   HOH A 150       3.643   6.779  10.177  1.00  8.23           O  
HETATM 1024  O   HOH A 151       5.834  11.190   9.364  1.00  8.56           O  
HETATM 1025  O   HOH A 152       6.196  10.517   6.878  1.00  9.68           O  
HETATM 1026  O   HOH A 153     -11.373  28.950  11.880  1.00  6.95           O  
HETATM 1027  O   HOH A 154     -10.186  35.036  12.278  1.00  6.30           O  
HETATM 1028  O   HOH A 155A    -10.492  37.474  13.389  1.00  6.45           O  
HETATM 1029  O   HOH A 156       4.486  33.231   9.936  1.00  8.28           O  
HETATM 1030  O   HOH A 157       2.422  33.719   9.723  1.00  6.58           O  
HETATM 1031  O   HOH A 158       7.321  25.129  11.024  1.00  8.18           O  
HETATM 1032  O   HOH A 159       8.807  22.732  10.368  1.00  7.01           O  
HETATM 1033  O   HOH A 160       8.773  21.508  12.167  1.00  7.49           O  
HETATM 1034  O   HOH A 161      10.270  18.653  12.446  1.00  9.22           O  
HETATM 1035  O   HOH A 162       9.016  20.792  14.248  1.00  6.89           O  
HETATM 1036  O   HOH A 163       9.050  18.423  10.724  1.00  8.09           O  
HETATM 1037  O   HOH A 164       8.892  18.409   7.801  1.00  7.64           O  
HETATM 1038  O   HOH A 165       1.063   4.296  10.283  1.00  7.03           O  
HETATM 1039  O   HOH A 166       0.337  36.004   8.597  1.00  4.43           O  
HETATM 1040  O   HOH A 167       7.675  28.515  14.300  1.00  8.85           O  
HETATM 1041  O   HOH A 168      11.790  13.378  14.714  1.00  7.52           O  
HETATM 1042  O   HOH A 169       3.640   7.823  12.635  1.00  6.37           O  
HETATM 1043  O   HOH A 170      -9.445  10.218  12.204  1.00  6.53           O  
HETATM 1044  O   HOH A 171      -6.642  10.502  13.858  1.00  6.78           O  
HETATM 1045  O   HOH A 172      -8.352   8.342  15.325  1.00  6.10           O  
HETATM 1046  O   HOH A 173     -15.203  19.952  17.200  1.00  7.42           O  
HETATM 1047  O   HOH A 174      -0.280  12.094  16.668  1.00  6.24           O  
HETATM 1048  O   HOH A 175       7.849  31.304  16.993  1.00  9.10           O  
HETATM 1049  O   HOH A 176       4.020  38.457  18.217  1.00  7.91           O  
HETATM 1050  O   HOH A 177       9.866  28.672  17.801  1.00  8.14           O  
HETATM 1051  O   HOH A 178       7.959  26.127  18.003  1.00  7.34           O  
HETATM 1052  O   HOH A 179      -7.029  36.080  14.705  1.00  7.81           O  
HETATM 1053  O   HOH A 180      -1.986   4.781  18.256  1.00  3.13           O  
HETATM 1054  O   HOH A 181       1.193   4.674  15.427  1.00  7.40           O  
HETATM 1055  O   HOH A 182       2.913   5.353  18.397  1.00  7.25           O  
HETATM 1056  O   HOH A 183       3.668   4.569  16.307  1.00  6.62           O  
HETATM 1057  O   HOH A 184      -1.140  40.137  17.624  1.00  2.45           O  
HETATM 1058  O   HOH A 185     -16.611   8.399  17.694  1.00  5.75           O  
HETATM 1059  O   HOH A 186     -17.022  15.334  18.866  1.00  6.34           O  
HETATM 1060  O   HOH A 187A    -17.386  17.070  17.778  1.00  5.50           O  
HETATM 1061  O   HOH A 188       9.171  23.006  19.600  1.00  7.66           O  
HETATM 1062  O   HOH A 189      12.518  23.592  19.879  1.00  5.87           O  
HETATM 1063  O   HOH A 190      11.805  25.700  19.768  1.00  7.07           O  
HETATM 1064  O   HOH A 191      -2.903   8.394  19.893  1.00  6.82           O  
HETATM 1065  O   HOH A 192     -10.705   7.515  18.789  1.00  6.40           O  
HETATM 1066  O   HOH A 193     -18.054  19.827  19.163  1.00  5.31           O  
HETATM 1067  O   HOH A 194      16.507  19.005  18.243  1.00  5.96           O  
HETATM 1068  O   HOH A 195      16.616  21.688  17.758  1.00  8.31           O  
HETATM 1069  O   HOH A 196      -0.442   2.991  20.757  1.00  9.35           O  
HETATM 1070  O   HOH A 197       5.822  23.508  22.833  1.00  6.95           O  
HETATM 1071  O   HOH A 198A      5.587  23.934  25.215  1.00  7.82           O  
HETATM 1072  O   HOH A 199       2.697  23.898  23.970  1.00  7.81           O  
HETATM 1073  O   HOH A 200       6.260  26.555  22.268  1.00  6.56           O  
HETATM 1074  O   HOH A 201       7.740  23.642  24.040  1.00  8.03           O  
HETATM 1075  O   HOH A 202      13.719  26.877  24.205  1.00  6.74           O  
HETATM 1076  O   HOH A 203      19.999  21.494  24.138  1.00  7.27           O  
HETATM 1077  O   HOH A 204     -14.883  14.517  24.305  1.00  7.58           O  
HETATM 1078  O   HOH A 205     -16.707  16.553  21.692  1.00  7.33           O  
HETATM 1079  O   HOH A 206       3.717  21.076  26.042  1.00  7.60           O  
HETATM 1080  O   HOH A 207       7.748  27.790  26.634  1.00  9.63           O  
HETATM 1081  O   HOH A 208      13.889  14.951  26.751  1.00  8.82           O  
HETATM 1082  O   HOH A 209      -4.510   8.787  25.141  1.00  7.40           O  
HETATM 1083  O   HOH A 210       7.236  32.376  25.121  1.00  9.58           O  
HETATM 1084  O   HOH A 211      -2.571  26.932  28.686  1.00  6.90           O  
HETATM 1085  O   HOH A 212       3.010  29.072  30.876  1.00  8.66           O  
HETATM 1086  O   HOH A 213      21.502  19.730  28.267  1.00  6.85           O  
HETATM 1087  O   HOH A 214      17.979  16.390  30.324  1.00  6.39           O  
HETATM 1088  O   HOH A 215      -9.097  19.616  31.367  1.00  6.26           O  
HETATM 1089  O   HOH A 216       0.764  36.101  30.952  1.00  7.53           O  
HETATM 1090  O   HOH A 217     -12.099  23.975  29.968  1.00  7.26           O  
HETATM 1091  O   HOH A 218     -12.554  12.554  28.425  0.50  7.79           O  
HETATM 1092  O   HOH A 219       8.199  26.198  32.854  1.00  8.38           O  
HETATM 1093  O   HOH A 220      10.629  24.833  34.084  1.00  7.70           O  
HETATM 1094  O   HOH A 221       4.504  27.893  34.299  1.00  8.44           O  
HETATM 1095  O   HOH A 222      11.951  12.339  32.724  1.00  9.06           O  
HETATM 1096  O   HOH A 223      -5.010  10.314  32.505  1.00  8.12           O  
HETATM 1097  O   HOH A 224      15.048  22.720  35.229  1.00  7.00           O  
HETATM 1098  O   HOH A 225      -0.828  22.595  35.395  1.00  6.41           O  
HETATM 1099  O   HOH A 226      -1.945  24.463  33.952  1.00  6.93           O  
HETATM 1100  O   HOH A 227      -2.131  25.946  32.449  1.00  7.49           O  
HETATM 1101  O   HOH A 228      -4.626  21.858  33.367  1.00  6.01           O  
HETATM 1102  O   HOH A 229      -4.472  18.437  36.114  1.00  6.67           O  
HETATM 1103  O   HOH A 230      -2.560  14.544  36.556  1.00  6.87           O  
CONECT   48  981                                                                
CONECT  238  889                                                                
CONECT  513  630                                                                
CONECT  601  724                                                                
CONECT  630  513                                                                
CONECT  724  601                                                                
CONECT  889  238                                                                
CONECT  981   48                                                                
MASTER      624    0    0    4    5    0    0    6 1102    1    8   10          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.