CNRS Nantes University UFIP UFIP
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***  111  ***

elNémo ID: 21021605484316364

Job options:

ID        	=	 21021605484316364
JOBID     	=	 111
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 111

HEADER    CALCIUM BINDING PROTEIN                 11-MAY-88   3CLN              
TITLE     STRUCTURE OF CALMODULIN REFINED AT 2.2 ANGSTROMS RESOLUTION           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS RATTUS;                                  
SOURCE   3 ORGANISM_COMMON: BLACK RAT;                                          
SOURCE   4 ORGANISM_TAXID: 10117                                                
KEYWDS    CALCIUM BINDING PROTEIN                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.S.BABU,C.E.BUGG,W.J.COOK                                            
REVDAT   5   29-NOV-17 3CLN    1       HELIX                                    
REVDAT   4   24-FEB-09 3CLN    1       VERSN                                    
REVDAT   3   01-APR-03 3CLN    1       JRNL                                     
REVDAT   2   09-JAN-89 3CLN    1       JRNL                                     
REVDAT   1   16-JUL-88 3CLN    0                                                
SPRSDE     16-JUL-88 3CLN      1CLN                                             
JRNL        AUTH   Y.S.BABU,C.E.BUGG,W.J.COOK                                   
JRNL        TITL   STRUCTURE OF CALMODULIN REFINED AT 2.2 A RESOLUTION.         
JRNL        REF    J.MOL.BIOL.                   V. 204   191 1988              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   3145979                                                      
JRNL        DOI    10.1016/0022-2836(88)90608-0                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   Y.S.BABU,J.S.SACK,T.J.GREENHOUGH,C.E.BUGG,A.R.MEANS,W.J.COOK 
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF CALMODULIN                    
REMARK   1  REF    NATURE                        V. 315    37 1985              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   W.J.COOK,J.S.SACK                                            
REMARK   1  TITL   PREPARATION OF CALMODULIN CRYSTALS                           
REMARK   1  REF    METHODS ENZYMOL.              V. 102   143 1983              
REMARK   1  REFN                   ISSN 0076-6879                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   J.A.PUTKEY,K.F.TS'UI,T.TANAKA,L.LAGACE,J.P.STEIN,E.C.LAI,    
REMARK   1  AUTH 2 A.R.MEANS                                                    
REMARK   1  TITL   CHICKEN CALMODULIN GENES. A SPECIES COMPARISON OF C/DNA      
REMARK   1  TITL 2 SEQUENCES AND ISOLATION OF A GENOMIC CLONE                   
REMARK   1  REF    J.BIOL.CHEM.                  V. 258 11864 1983              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   W.J.COOK,J.R.DEDMAN,A.R.MEANS,C.E.BUGG                       
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY INVESTIGATION OF       
REMARK   1  TITL 2 CALMODULIN                                                   
REMARK   1  REF    J.BIOL.CHEM.                  V. 255  8152 1980              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1126                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 69                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.016 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.034 ; 0.030               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.044 ; 0.040               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.012 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.162 ; 0.130               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.206 ; 0.400               
REMARK   3    MULTIPLE TORSION                (A) : 0.274 ; 0.400               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : 0.180 ; 0.400               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 2.300 ; 5.000               
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 1.300 ; 1.500               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 2.000 ; 2.000               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 2.410 ; 2.000               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 3.710 ; 3.000               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3CLN 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_1000178914.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     LYS A   148                                                      
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    VAL A    91     NH1  ARG A   126     1556     2.01            
REMARK 500   NH2  ARG A    37     OE1  GLU A   114     1566     2.11            
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    ASP A  22   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ASP A  22   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ASP A  24   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    THR A  28   N   -  CA  -  CB  ANGL. DEV. = -11.6 DEGREES          
REMARK 500    ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG A  86   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A  90   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  42       76.11   -116.87                                   
REMARK 500    ASP A  56       94.19    -56.55                                   
REMARK 500    ALA A  73      -72.91    -54.27                                   
REMARK 500    SER A  81      -63.09    -93.64                                   
REMARK 500    ASP A 131        3.01    -67.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 149  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  26   O                                                      
REMARK 620 2 ASP A  20   OD2  83.3                                              
REMARK 620 3 HOH A 153   O   101.7 161.7                                        
REMARK 620 4 ASP A  22   OD1 156.9  87.5  81.2                                  
REMARK 620 5 ASP A  24   OD2  81.3  85.6  77.9  76.9                            
REMARK 620 6 GLU A  31   OE2  77.4 110.0  88.3 125.7 151.6                      
REMARK 620 7 GLU A  31   OE1 128.9  99.0  91.6  73.5 149.8  53.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 150  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 154   O                                                      
REMARK 620 2 ASP A  56   OD2 156.6                                              
REMARK 620 3 ASP A  58   OD2  76.9  81.8                                        
REMARK 620 4 ASN A  60   OD1  91.5  94.4  80.2                                  
REMARK 620 5 THR A  62   O   121.0  82.3 154.5  81.3                            
REMARK 620 6 GLU A  67   OE1  84.3  99.7 123.7 153.7  78.7                      
REMARK 620 7 GLU A  67   OE2  74.1  89.9  71.1 150.0 128.7  52.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 151  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  95   OD2                                                    
REMARK 620 2 GLU A 104   OE2  78.0                                              
REMARK 620 3 ASN A  97   OD1  71.7 149.0                                        
REMARK 620 4 TYR A  99   O   151.7 130.3  80.3                                  
REMARK 620 5 ASP A  93   OD2  93.2  95.4  92.7  84.3                            
REMARK 620 6 HOH A 155   O    82.7  77.8  91.8 102.2 172.7                      
REMARK 620 7 GLU A 104   OE1 126.6  48.9 158.5  81.7  97.0  80.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 152  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 133   OD2                                                    
REMARK 620 2 GLN A 135   O    82.2                                              
REMARK 620 3 ASP A 131   OD2  79.4 158.9                                        
REMARK 620 4 GLU A 140   OE1 141.6  69.6 131.5                                  
REMARK 620 5 GLU A 140   OE2 164.5 113.0  85.1  52.2                            
REMARK 620 6 HOH A 156   O    75.6 100.7  84.6  84.5 103.5                      
REMARK 620 7 ASN A 129   OD1  94.6  82.6  88.7 106.5  84.6 169.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: EF1                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: calcium binding site                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EF2                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: calcium binding site                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EF3                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: calcium binding site                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EF4                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: calcium binding site                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 149                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 150                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 151                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 152                  
DBREF  3CLN A    1   148  UNP    P02593   CALM_HUMANX      1    148             
SEQRES   1 A  148  ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS          
SEQRES   2 A  148  GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR          
SEQRES   3 A  148  ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU          
SEQRES   4 A  148  GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE          
SEQRES   5 A  148  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE          
SEQRES   6 A  148  PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP          
SEQRES   7 A  148  THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL          
SEQRES   8 A  148  PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU          
SEQRES   9 A  148  LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR          
SEQRES  10 A  148  ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASN ILE          
SEQRES  11 A  148  ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN          
SEQRES  12 A  148  MET MET THR ALA LYS                                          
HET     CA  A 149       1                                                       
HET     CA  A 150       1                                                       
HET     CA  A 151       1                                                       
HET     CA  A 152       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   2   CA    4(CA 2+)                                                     
FORMUL   6  HOH   *69(H2 O)                                                     
HELIX    1  H1 THR A    5  PHE A   19  1                                  15    
HELIX    2  H2 THR A   29  SER A   38  1                                  10    
HELIX    3  H3 GLU A   45  VAL A   55  1                                  11    
HELIX    4  H4 PHE A   65  PHE A   92  1                                  28    
HELIX    5  H5 ALA A  102  ASN A  111  1                                  10    
HELIX    6  H6 ASP A  118  ALA A  128  1                                  11    
HELIX    7  H7 TYR A  138  ALA A  147  1                                  10    
SHEET    1  B1 2 THR A  26  THR A  28  0                                        
SHEET    2  B1 2 THR A  62  ASP A  64 -1                                        
SHEET    1  B2 2 TYR A  99  SER A 101  0                                        
SHEET    2  B2 2 GLN A 135  ASN A 137 -1                                        
LINK        CA    CA A 149                 O   THR A  26     1555   1555  2.46  
LINK        CA    CA A 149                 OD2 ASP A  20     1555   1555  2.34  
LINK        CA    CA A 149                 O   HOH A 153     1555   1555  2.42  
LINK        CA    CA A 149                 OD1 ASP A  22     1555   1555  2.42  
LINK        CA    CA A 149                 OD2 ASP A  24     1555   1555  2.61  
LINK        CA    CA A 149                 OE2 GLU A  31     1555   1555  2.38  
LINK        CA    CA A 149                 OE1 GLU A  31     1555   1555  2.28  
LINK        CA    CA A 150                 O   HOH A 154     1555   1555  2.37  
LINK        CA    CA A 150                 OD2 ASP A  56     1555   1555  2.21  
LINK        CA    CA A 150                 OD2 ASP A  58     1555   1555  2.48  
LINK        CA    CA A 150                 OD1 ASN A  60     1555   1555  2.46  
LINK        CA    CA A 150                 O   THR A  62     1555   1555  2.17  
LINK        CA    CA A 150                 OE1 GLU A  67     1555   1555  2.49  
LINK        CA    CA A 150                 OE2 GLU A  67     1555   1555  2.31  
LINK        CA    CA A 151                 OD2 ASP A  95     1555   1555  2.22  
LINK        CA    CA A 151                 OE2 GLU A 104     1555   1555  2.76  
LINK        CA    CA A 151                 OD1 ASN A  97     1555   1555  2.39  
LINK        CA    CA A 151                 O   TYR A  99     1555   1555  2.06  
LINK        CA    CA A 151                 OD2 ASP A  93     1555   1555  2.14  
LINK        CA    CA A 151                 O   HOH A 155     1555   1555  2.01  
LINK        CA    CA A 151                 OE1 GLU A 104     1555   1555  2.32  
LINK        CA    CA A 152                 OD2 ASP A 133     1555   1555  2.07  
LINK        CA    CA A 152                 O   GLN A 135     1555   1555  2.38  
LINK        CA    CA A 152                 OD2 ASP A 131     1555   1555  2.56  
LINK        CA    CA A 152                 OE1 GLU A 140     1555   1555  2.57  
LINK        CA    CA A 152                 OE2 GLU A 140     1555   1555  2.32  
LINK        CA    CA A 152                 O   HOH A 156     1555   1555  2.63  
LINK        CA    CA A 152                 OD1 ASN A 129     1555   1555  2.17  
SITE     1 EF1 12 ASP A  20  LYS A  21  ASP A  22  GLY A  23                    
SITE     2 EF1 12 ASP A  24  GLY A  25  THR A  26  ILE A  27                    
SITE     3 EF1 12 THR A  28  THR A  29  LYS A  30  GLU A  31                    
SITE     1 EF2 12 ASP A  56  ALA A  57  ASP A  58  GLY A  59                    
SITE     2 EF2 12 ASN A  60  GLY A  61  THR A  62  ILE A  63                    
SITE     3 EF2 12 ASP A  64  PHE A  65  PRO A  66  GLU A  67                    
SITE     1 EF3 12 ASP A  93  LYS A  94  ASP A  95  GLY A  96                    
SITE     2 EF3 12 ASN A  97  GLY A  98  TYR A  99  ILE A 100                    
SITE     3 EF3 12 SER A 101  ALA A 102  ALA A 103  GLU A 104                    
SITE     1 EF4 12 ASN A 129  ILE A 130  ASP A 131  GLY A 132                    
SITE     2 EF4 12 ASP A 133  GLY A 134  GLN A 135  VAL A 136                    
SITE     3 EF4 12 ASN A 137  TYR A 138  GLU A 139  GLU A 140                    
SITE     1 AC1  6 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC1  6 GLU A  31  HOH A 153                                          
SITE     1 AC2  6 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC2  6 GLU A  67  HOH A 154                                          
SITE     1 AC3  6 ASP A  93  ASP A  95  ASN A  97  TYR A  99                    
SITE     2 AC3  6 GLU A 104  HOH A 155                                          
SITE     1 AC4  6 ASN A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC4  6 GLU A 140  HOH A 156                                          
CRYST1   29.710   53.790   24.990  94.13  97.57  89.46 P 1           1          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.033660 -0.000320  0.004460        0.00000                         
SCALE2      0.000000  0.018590  0.001330        0.00000                         
SCALE3      0.000000  0.000000  0.040470        0.00000                         
ATOM      1  N   THR A   5     -22.499  29.260  32.164  1.00 41.62           N  
ATOM      2  CA  THR A   5     -22.134  30.524  31.536  1.00 40.62           C  
ATOM      3  C   THR A   5     -22.164  31.628  32.593  1.00 39.94           C  
ATOM      4  O   THR A   5     -21.295  32.505  32.549  1.00 39.67           O  
ATOM      5  CB  THR A   5     -22.984  30.878  30.265  1.00 41.50           C  
ATOM      6  OG1 THR A   5     -24.243  30.139  30.376  1.00 42.80           O  
ATOM      7  CG2 THR A   5     -22.318  30.640  28.917  1.00 41.46           C  
ATOM      8  N   GLU A   6     -23.098  31.565  33.508  1.00 39.55           N  
ATOM      9  CA  GLU A   6     -23.237  32.552  34.591  1.00 40.34           C  
ATOM     10  C   GLU A   6     -21.904  32.841  35.263  1.00 39.60           C  
ATOM     11  O   GLU A   6     -21.498  34.011  35.421  1.00 39.48           O  
ATOM     12  CB  GLU A   6     -24.247  32.129  35.645  1.00 44.96           C  
ATOM     13  CG  GLU A   6     -25.308  33.074  36.124  1.00 49.43           C  
ATOM     14  CD  GLU A   6     -25.960  32.929  37.448  1.00 53.72           C  
ATOM     15  OE1 GLU A   6     -25.933  33.803  38.324  1.00 56.08           O  
ATOM     16  OE2 GLU A   6     -26.589  31.865  37.662  1.00 54.86           O  
ATOM     17  N   GLU A   7     -21.204  31.809  35.668  1.00 38.31           N  
ATOM     18  CA  GLU A   7     -19.898  31.887  36.322  1.00 38.02           C  
ATOM     19  C   GLU A   7     -18.797  32.213  35.318  1.00 37.50           C  
ATOM     20  O   GLU A   7     -17.659  32.571  35.694  1.00 37.96           O  
ATOM     21  CB  GLU A   7     -19.551  30.620  37.067  1.00 39.11           C  
ATOM     22  CG  GLU A   7     -18.149  30.097  37.247  1.00 41.05           C  
ATOM     23  CD  GLU A   7     -18.087  28.751  37.939  1.00 44.21           C  
ATOM     24  OE1 GLU A   7     -18.670  27.732  37.604  1.00 43.30           O  
ATOM     25  OE2 GLU A   7     -17.330  28.792  38.939  1.00 47.23           O  
ATOM     26  N   GLN A   8     -19.132  32.106  34.051  1.00 36.37           N  
ATOM     27  CA  GLN A   8     -18.223  32.421  32.939  1.00 35.01           C  
ATOM     28  C   GLN A   8     -18.261  33.914  32.646  1.00 34.47           C  
ATOM     29  O   GLN A   8     -17.200  34.553  32.513  1.00 35.38           O  
ATOM     30  CB  GLN A   8     -18.445  31.540  31.734  1.00 32.45           C  
ATOM     31  CG  GLN A   8     -17.535  30.294  31.794  1.00 32.46           C  
ATOM     32  CD  GLN A   8     -17.685  29.431  30.576  1.00 31.72           C  
ATOM     33  OE1 GLN A   8     -18.786  29.066  30.177  1.00 33.68           O  
ATOM     34  NE2 GLN A   8     -16.570  29.083  29.965  1.00 32.40           N  
ATOM     35  N   ILE A   9     -19.436  34.501  32.617  1.00 34.54           N  
ATOM     36  CA  ILE A   9     -19.502  35.971  32.394  1.00 35.29           C  
ATOM     37  C   ILE A   9     -18.862  36.731  33.553  1.00 34.13           C  
ATOM     38  O   ILE A   9     -18.210  37.783  33.357  1.00 33.98           O  
ATOM     39  CB  ILE A   9     -20.918  36.381  31.915  1.00 37.77           C  
ATOM     40  CG1 ILE A   9     -21.520  37.473  32.823  1.00 39.46           C  
ATOM     41  CG2 ILE A   9     -21.839  35.168  31.631  1.00 36.59           C  
ATOM     42  CD1 ILE A   9     -23.025  37.251  33.169  1.00 43.00           C  
ATOM     43  N   ALA A  10     -19.018  36.230  34.746  1.00 33.63           N  
ATOM     44  CA  ALA A  10     -18.466  36.763  35.983  1.00 34.39           C  
ATOM     45  C   ALA A  10     -16.949  36.828  35.824  1.00 34.25           C  
ATOM     46  O   ALA A  10     -16.326  37.875  36.051  1.00 34.21           O  
ATOM     47  CB  ALA A  10     -18.924  35.972  37.211  1.00 33.08           C  
ATOM     48  N   GLU A  11     -16.373  35.720  35.400  1.00 35.29           N  
ATOM     49  CA  GLU A  11     -14.901  35.674  35.185  1.00 35.77           C  
ATOM     50  C   GLU A  11     -14.501  36.750  34.198  1.00 35.29           C  
ATOM     51  O   GLU A  11     -13.583  37.555  34.440  1.00 35.50           O  
ATOM     52  CB  GLU A  11     -14.446  34.304  34.713  1.00 40.35           C  
ATOM     53  CG  GLU A  11     -14.428  33.247  35.866  1.00 45.24           C  
ATOM     54  CD  GLU A  11     -14.370  31.828  35.401  1.00 48.66           C  
ATOM     55  OE1 GLU A  11     -15.346  31.187  35.023  1.00 50.72           O  
ATOM     56  OE2 GLU A  11     -13.198  31.368  35.413  1.00 50.58           O  
ATOM     57  N   PHE A  12     -15.228  36.787  33.087  1.00 34.25           N  
ATOM     58  CA  PHE A  12     -15.010  37.780  32.010  1.00 31.94           C  
ATOM     59  C   PHE A  12     -15.205  39.189  32.588  1.00 30.74           C  
ATOM     60  O   PHE A  12     -14.379  40.071  32.268  1.00 31.01           O  
ATOM     61  CB  PHE A  12     -15.875  37.528  30.792  1.00 31.85           C  
ATOM     62  CG  PHE A  12     -15.415  36.427  29.895  1.00 33.62           C  
ATOM     63  CD1 PHE A  12     -16.281  35.400  29.532  1.00 33.63           C  
ATOM     64  CD2 PHE A  12     -14.103  36.402  29.432  1.00 34.35           C  
ATOM     65  CE1 PHE A  12     -15.884  34.382  28.683  1.00 33.79           C  
ATOM     66  CE2 PHE A  12     -13.680  35.368  28.571  1.00 34.94           C  
ATOM     67  CZ  PHE A  12     -14.572  34.353  28.214  1.00 34.09           C  
ATOM     68  N   LYS A  13     -16.220  39.358  33.395  1.00 27.69           N  
ATOM     69  CA  LYS A  13     -16.474  40.656  34.032  1.00 27.44           C  
ATOM     70  C   LYS A  13     -15.256  41.170  34.816  1.00 27.49           C  
ATOM     71  O   LYS A  13     -14.863  42.359  34.738  1.00 25.29           O  
ATOM     72  CB  LYS A  13     -17.659  40.565  34.949  1.00 27.81           C  
ATOM     73  CG  LYS A  13     -18.482  41.851  35.030  1.00 28.32           C  
ATOM     74  CD  LYS A  13     -19.924  41.449  35.330  1.00 32.28           C  
ATOM     75  CE  LYS A  13     -20.746  41.197  34.076  1.00 34.08           C  
ATOM     76  NZ  LYS A  13     -22.166  40.938  34.473  1.00 35.89           N  
ATOM     77  N   GLU A  14     -14.645  40.226  35.541  1.00 26.75           N  
ATOM     78  CA  GLU A  14     -13.481  40.484  36.368  1.00 25.96           C  
ATOM     79  C   GLU A  14     -12.346  40.980  35.478  1.00 24.90           C  
ATOM     80  O   GLU A  14     -11.646  41.915  35.844  1.00 25.09           O  
ATOM     81  CB  GLU A  14     -12.975  39.215  37.079  1.00 27.89           C  
ATOM     82  CG  GLU A  14     -13.145  39.041  38.565  1.00 32.90           C  
ATOM     83  CD  GLU A  14     -13.191  37.635  39.102  1.00 37.45           C  
ATOM     84  OE1 GLU A  14     -14.199  36.953  39.319  1.00 40.01           O  
ATOM     85  OE2 GLU A  14     -12.038  37.205  39.307  1.00 39.87           O  
ATOM     86  N   ALA A  15     -12.177  40.294  34.359  1.00 22.90           N  
ATOM     87  CA  ALA A  15     -11.087  40.670  33.422  1.00 24.48           C  
ATOM     88  C   ALA A  15     -11.362  42.070  32.864  1.00 23.66           C  
ATOM     89  O   ALA A  15     -10.435  42.901  32.892  1.00 26.15           O  
ATOM     90  CB  ALA A  15     -10.918  39.603  32.355  1.00 23.65           C  
ATOM     91  N   PHE A  16     -12.576  42.380  32.470  1.00 22.21           N  
ATOM     92  CA  PHE A  16     -13.026  43.677  31.966  1.00 21.00           C  
ATOM     93  C   PHE A  16     -12.746  44.775  32.973  1.00 21.66           C  
ATOM     94  O   PHE A  16     -12.271  45.866  32.563  1.00 23.07           O  
ATOM     95  CB  PHE A  16     -14.505  43.676  31.563  1.00 20.00           C  
ATOM     96  CG  PHE A  16     -15.062  44.910  30.927  1.00 19.19           C  
ATOM     97  CD1 PHE A  16     -15.685  45.888  31.743  1.00 19.49           C  
ATOM     98  CD2 PHE A  16     -14.978  45.135  29.560  1.00 16.35           C  
ATOM     99  CE1 PHE A  16     -16.214  47.058  31.221  1.00 18.26           C  
ATOM    100  CE2 PHE A  16     -15.528  46.274  28.986  1.00 17.46           C  
ATOM    101  CZ  PHE A  16     -16.119  47.257  29.840  1.00 19.94           C  
ATOM    102  N   SER A  17     -13.029  44.539  34.251  1.00 20.70           N  
ATOM    103  CA  SER A  17     -12.792  45.597  35.227  1.00 22.09           C  
ATOM    104  C   SER A  17     -11.352  45.997  35.311  1.00 21.38           C  
ATOM    105  O   SER A  17     -11.231  47.157  35.750  1.00 25.68           O  
ATOM    106  CB  SER A  17     -13.279  45.292  36.682  1.00 24.10           C  
ATOM    107  OG  SER A  17     -14.414  44.466  36.471  1.00 30.63           O  
ATOM    108  N   LEU A  18     -10.367  45.188  35.023  1.00 22.80           N  
ATOM    109  CA  LEU A  18      -8.966  45.631  35.193  1.00 22.03           C  
ATOM    110  C   LEU A  18      -8.671  46.804  34.247  1.00 21.25           C  
ATOM    111  O   LEU A  18      -7.927  47.732  34.597  1.00 21.35           O  
ATOM    112  CB  LEU A  18      -7.978  44.461  35.047  1.00 25.16           C  
ATOM    113  CG  LEU A  18      -6.504  44.927  35.003  1.00 28.76           C  
ATOM    114  CD1 LEU A  18      -6.116  45.444  36.389  1.00 28.40           C  
ATOM    115  CD2 LEU A  18      -5.571  43.802  34.592  1.00 28.09           C  
ATOM    116  N   PHE A  19      -9.234  46.678  33.081  1.00 20.59           N  
ATOM    117  CA  PHE A  19      -9.151  47.628  31.970  1.00 20.73           C  
ATOM    118  C   PHE A  19      -9.984  48.873  32.225  1.00 20.81           C  
ATOM    119  O   PHE A  19      -9.489  49.952  31.998  1.00 22.88           O  
ATOM    120  CB  PHE A  19      -9.570  46.960  30.652  1.00 22.38           C  
ATOM    121  CG  PHE A  19      -8.679  45.872  30.156  1.00 22.39           C  
ATOM    122  CD1 PHE A  19      -7.535  46.212  29.420  1.00 23.82           C  
ATOM    123  CD2 PHE A  19      -8.937  44.536  30.467  1.00 24.25           C  
ATOM    124  CE1 PHE A  19      -6.676  45.228  28.950  1.00 24.66           C  
ATOM    125  CE2 PHE A  19      -8.053  43.525  30.023  1.00 25.58           C  
ATOM    126  CZ  PHE A  19      -6.928  43.886  29.253  1.00 24.05           C  
ATOM    127  N   ASP A  20     -11.226  48.721  32.667  1.00 20.84           N  
ATOM    128  CA  ASP A  20     -12.162  49.791  32.955  1.00 18.43           C  
ATOM    129  C   ASP A  20     -11.827  50.467  34.276  1.00 18.16           C  
ATOM    130  O   ASP A  20     -12.567  50.290  35.225  1.00 17.98           O  
ATOM    131  CB  ASP A  20     -13.602  49.276  32.933  1.00 18.21           C  
ATOM    132  CG  ASP A  20     -14.614  50.399  33.000  1.00 20.51           C  
ATOM    133  OD1 ASP A  20     -15.827  50.153  33.198  1.00 22.05           O  
ATOM    134  OD2 ASP A  20     -14.153  51.558  32.903  1.00 19.79           O  
ATOM    135  N   LYS A  21     -10.776  51.259  34.325  1.00 18.44           N  
ATOM    136  CA  LYS A  21     -10.315  51.935  35.524  1.00 19.31           C  
ATOM    137  C   LYS A  21     -11.300  52.825  36.252  1.00 20.14           C  
ATOM    138  O   LYS A  21     -11.209  52.955  37.515  1.00 19.46           O  
ATOM    139  CB  LYS A  21      -9.056  52.792  35.203  1.00 19.21           C  
ATOM    140  CG  LYS A  21      -7.824  51.957  34.850  1.00 20.11           C  
ATOM    141  CD  LYS A  21      -7.709  50.666  35.640  1.00 19.05           C  
ATOM    142  CE  LYS A  21      -6.259  50.369  35.975  1.00 17.79           C  
ATOM    143  NZ  LYS A  21      -5.949  48.952  35.796  1.00 17.10           N  
ATOM    144  N   ASP A  22     -12.145  53.516  35.465  1.00 20.74           N  
ATOM    145  CA  ASP A  22     -13.104  54.465  36.113  1.00 20.86           C  
ATOM    146  C   ASP A  22     -14.492  53.852  36.222  1.00 21.06           C  
ATOM    147  O   ASP A  22     -15.411  54.604  36.566  1.00 20.51           O  
ATOM    148  CB  ASP A  22     -13.093  55.799  35.412  1.00 22.31           C  
ATOM    149  CG  ASP A  22     -13.650  55.804  34.015  1.00 22.17           C  
ATOM    150  OD1 ASP A  22     -14.036  54.809  33.396  1.00 21.29           O  
ATOM    151  OD2 ASP A  22     -13.702  56.959  33.520  1.00 24.18           O  
ATOM    152  N   GLY A  23     -14.619  52.585  35.854  1.00 19.15           N  
ATOM    153  CA  GLY A  23     -15.839  51.847  35.877  1.00 18.44           C  
ATOM    154  C   GLY A  23     -17.043  52.441  35.191  1.00 18.21           C  
ATOM    155  O   GLY A  23     -18.185  52.235  35.658  1.00 16.72           O  
ATOM    156  N   ASP A  24     -16.846  53.142  34.070  1.00 16.63           N  
ATOM    157  CA  ASP A  24     -18.032  53.715  33.367  1.00 13.85           C  
ATOM    158  C   ASP A  24     -18.610  52.697  32.422  1.00 14.07           C  
ATOM    159  O   ASP A  24     -19.558  53.069  31.682  1.00 16.75           O  
ATOM    160  CB  ASP A  24     -17.682  55.028  32.657  1.00 13.06           C  
ATOM    161  CG  ASP A  24     -16.951  54.752  31.345  1.00 12.45           C  
ATOM    162  OD1 ASP A  24     -17.153  55.450  30.305  1.00 10.31           O  
ATOM    163  OD2 ASP A  24     -16.216  53.754  31.404  1.00  8.35           O  
ATOM    164  N   GLY A  25     -18.065  51.507  32.323  1.00 12.14           N  
ATOM    165  CA  GLY A  25     -18.609  50.526  31.347  1.00 12.61           C  
ATOM    166  C   GLY A  25     -17.948  50.491  29.986  1.00 13.62           C  
ATOM    167  O   GLY A  25     -18.464  49.830  29.053  1.00 13.60           O  
ATOM    168  N   THR A  26     -16.807  51.209  29.819  1.00 12.60           N  
ATOM    169  CA  THR A  26     -16.140  51.149  28.517  1.00 11.60           C  
ATOM    170  C   THR A  26     -14.648  51.219  28.695  1.00 12.25           C  
ATOM    171  O   THR A  26     -14.199  51.753  29.724  1.00 11.22           O  
ATOM    172  CB  THR A  26     -16.602  52.313  27.550  1.00 13.20           C  
ATOM    173  OG1 THR A  26     -15.954  53.491  28.082  1.00 10.80           O  
ATOM    174  CG2 THR A  26     -18.132  52.452  27.414  1.00 15.64           C  
ATOM    175  N   ILE A  27     -13.955  50.732  27.669  1.00 12.94           N  
ATOM    176  CA  ILE A  27     -12.493  50.841  27.669  1.00 11.76           C  
ATOM    177  C   ILE A  27     -12.094  51.756  26.506  1.00 13.41           C  
ATOM    178  O   ILE A  27     -12.367  51.607  25.327  1.00 11.54           O  
ATOM    179  CB  ILE A  27     -11.765  49.463  27.545  1.00 13.37           C  
ATOM    180  CG1 ILE A  27     -12.426  48.491  28.557  1.00 12.26           C  
ATOM    181  CG2 ILE A  27     -10.231  49.706  27.617  1.00 10.42           C  
ATOM    182  CD1 ILE A  27     -12.227  47.004  28.226  1.00 13.93           C  
ATOM    183  N   THR A  28     -11.315  52.692  26.908  1.00 13.85           N  
ATOM    184  CA  THR A  28     -10.723  53.815  26.191  1.00 15.52           C  
ATOM    185  C   THR A  28      -9.274  53.538  25.864  1.00 17.02           C  
ATOM    186  O   THR A  28      -8.680  52.685  26.590  1.00 15.17           O  
ATOM    187  CB  THR A  28     -10.892  54.940  27.321  1.00 16.41           C  
ATOM    188  OG1 THR A  28     -11.966  55.820  26.865  1.00 25.49           O  
ATOM    189  CG2 THR A  28      -9.731  55.506  27.960  1.00 16.22           C  
ATOM    190  N   THR A  29      -8.768  54.296  24.880  1.00 17.16           N  
ATOM    191  CA  THR A  29      -7.357  54.115  24.504  1.00 19.26           C  
ATOM    192  C   THR A  29      -6.493  54.499  25.704  1.00 18.50           C  
ATOM    193  O   THR A  29      -5.448  53.870  25.820  1.00 19.41           O  
ATOM    194  CB  THR A  29      -6.840  54.898  23.214  1.00 18.16           C  
ATOM    195  OG1 THR A  29      -7.031  56.301  23.474  1.00 16.15           O  
ATOM    196  CG2 THR A  29      -7.540  54.451  21.938  1.00 18.78           C  
ATOM    197  N   LYS A  30      -6.953  55.421  26.532  1.00 18.81           N  
ATOM    198  CA  LYS A  30      -6.147  55.805  27.717  1.00 19.06           C  
ATOM    199  C   LYS A  30      -6.134  54.738  28.776  1.00 18.15           C  
ATOM    200  O   LYS A  30      -5.086  54.432  29.399  1.00 19.23           O  
ATOM    201  CB  LYS A  30      -6.594  57.124  28.320  1.00 24.93           C  
ATOM    202  CG  LYS A  30      -7.179  58.140  27.344  1.00 27.64           C  
ATOM    203  CD  LYS A  30      -8.665  58.009  27.152  1.00 28.58           C  
ATOM    204  CE  LYS A  30      -9.292  58.745  26.005  1.00 31.14           C  
ATOM    205  NZ  LYS A  30      -9.030  58.028  24.704  1.00 31.99           N  
ATOM    206  N   GLU A  31      -7.247  54.090  29.014  1.00 16.45           N  
ATOM    207  CA  GLU A  31      -7.322  52.995  30.032  1.00 13.49           C  
ATOM    208  C   GLU A  31      -6.517  51.803  29.554  1.00 13.38           C  
ATOM    209  O   GLU A  31      -5.731  51.227  30.320  1.00 12.55           O  
ATOM    210  CB  GLU A  31      -8.807  52.653  30.269  1.00  9.19           C  
ATOM    211  CG  GLU A  31      -9.488  53.737  31.120  1.00  7.76           C  
ATOM    212  CD  GLU A  31     -10.959  53.542  31.367  1.00  9.13           C  
ATOM    213  OE1 GLU A  31     -11.595  53.888  32.345  1.00  9.17           O  
ATOM    214  OE2 GLU A  31     -11.533  52.987  30.447  1.00  6.00           O  
ATOM    215  N   LEU A  32      -6.666  51.452  28.273  1.00 12.88           N  
ATOM    216  CA  LEU A  32      -5.888  50.381  27.651  1.00 15.01           C  
ATOM    217  C   LEU A  32      -4.385  50.714  27.779  1.00 14.27           C  
ATOM    218  O   LEU A  32      -3.553  49.829  28.070  1.00 17.15           O  
ATOM    219  CB  LEU A  32      -6.282  50.184  26.183  1.00 16.84           C  
ATOM    220  CG  LEU A  32      -5.425  49.156  25.462  1.00 17.59           C  
ATOM    221  CD1 LEU A  32      -5.609  47.780  26.100  1.00 17.31           C  
ATOM    222  CD2 LEU A  32      -5.821  49.148  23.988  1.00 14.70           C  
ATOM    223  N   GLY A  33      -4.048  51.947  27.604  1.00 13.17           N  
ATOM    224  CA  GLY A  33      -2.756  52.513  27.734  1.00 13.00           C  
ATOM    225  C   GLY A  33      -2.221  52.291  29.151  1.00 15.21           C  
ATOM    226  O   GLY A  33      -1.038  51.904  29.232  1.00 14.86           O  
ATOM    227  N   THR A  34      -2.968  52.543  30.213  1.00 15.31           N  
ATOM    228  CA  THR A  34      -2.353  52.387  31.559  1.00 16.80           C  
ATOM    229  C   THR A  34      -2.070  50.978  31.967  1.00 16.19           C  
ATOM    230  O   THR A  34      -1.102  50.775  32.731  1.00 17.81           O  
ATOM    231  CB  THR A  34      -3.018  53.270  32.697  1.00 21.32           C  
ATOM    232  OG1 THR A  34      -3.443  52.418  33.791  1.00 21.87           O  
ATOM    233  CG2 THR A  34      -4.074  54.237  32.186  1.00 16.89           C  
ATOM    234  N   VAL A  35      -2.825  50.023  31.498  1.00 16.13           N  
ATOM    235  CA  VAL A  35      -2.695  48.603  31.674  1.00 16.15           C  
ATOM    236  C   VAL A  35      -1.470  48.123  30.889  1.00 18.15           C  
ATOM    237  O   VAL A  35      -0.712  47.316  31.458  1.00 17.84           O  
ATOM    238  CB  VAL A  35      -3.975  47.828  31.272  1.00 14.91           C  
ATOM    239  CG1 VAL A  35      -3.796  46.343  31.294  1.00 12.50           C  
ATOM    240  CG2 VAL A  35      -5.167  48.140  32.173  1.00 14.51           C  
ATOM    241  N   MET A  36      -1.342  48.563  29.634  1.00 19.00           N  
ATOM    242  CA  MET A  36      -0.178  48.111  28.842  1.00 20.95           C  
ATOM    243  C   MET A  36       1.083  48.535  29.635  1.00 21.58           C  
ATOM    244  O   MET A  36       2.053  47.780  29.723  1.00 22.26           O  
ATOM    245  CB  MET A  36      -0.028  48.738  27.475  1.00 25.31           C  
ATOM    246  CG  MET A  36      -1.140  48.443  26.507  1.00 29.88           C  
ATOM    247  SD  MET A  36      -1.315  46.651  26.624  1.00 37.79           S  
ATOM    248  CE  MET A  36      -1.283  46.209  24.873  1.00 38.30           C  
ATOM    249  N   ARG A  37       1.044  49.764  30.099  1.00 20.92           N  
ATOM    250  CA  ARG A  37       2.153  50.354  30.839  1.00 24.06           C  
ATOM    251  C   ARG A  37       2.471  49.618  32.133  1.00 24.97           C  
ATOM    252  O   ARG A  37       3.651  49.399  32.519  1.00 27.86           O  
ATOM    253  CB  ARG A  37       1.834  51.810  31.184  1.00 22.25           C  
ATOM    254  CG  ARG A  37       2.595  52.827  30.372  1.00 27.64           C  
ATOM    255  CD  ARG A  37       1.806  53.682  29.474  1.00 25.80           C  
ATOM    256  NE  ARG A  37       0.993  54.669  30.236  1.00 25.32           N  
ATOM    257  CZ  ARG A  37       0.071  55.355  29.508  1.00 24.63           C  
ATOM    258  NH1 ARG A  37       0.006  55.266  28.193  1.00 20.76           N  
ATOM    259  NH2 ARG A  37      -0.816  56.096  30.157  1.00 26.96           N  
ATOM    260  N   SER A  38       1.397  49.306  32.847  1.00 25.01           N  
ATOM    261  CA  SER A  38       1.571  48.625  34.163  1.00 25.22           C  
ATOM    262  C   SER A  38       2.227  47.290  33.847  1.00 25.89           C  
ATOM    263  O   SER A  38       2.846  46.688  34.727  1.00 26.25           O  
ATOM    264  CB  SER A  38       0.235  48.572  34.877  1.00 25.40           C  
ATOM    265  OG  SER A  38      -0.455  47.437  34.451  1.00 24.74           O  
ATOM    266  N   LEU A  39       2.173  46.884  32.579  1.00 24.98           N  
ATOM    267  CA  LEU A  39       2.786  45.648  32.145  1.00 27.52           C  
ATOM    268  C   LEU A  39       4.192  45.802  31.564  1.00 28.36           C  
ATOM    269  O   LEU A  39       4.716  44.786  31.059  1.00 28.82           O  
ATOM    270  CB  LEU A  39       1.816  44.947  31.168  1.00 30.14           C  
ATOM    271  CG  LEU A  39       0.549  44.370  31.811  1.00 32.82           C  
ATOM    272  CD1 LEU A  39      -0.231  43.483  30.851  1.00 31.77           C  
ATOM    273  CD2 LEU A  39       0.979  43.590  33.057  1.00 31.47           C  
ATOM    274  N   GLY A  40       4.758  46.985  31.568  1.00 28.70           N  
ATOM    275  CA  GLY A  40       6.062  47.300  31.022  1.00 29.32           C  
ATOM    276  C   GLY A  40       6.137  47.493  29.523  1.00 30.36           C  
ATOM    277  O   GLY A  40       7.190  47.237  28.881  1.00 30.67           O  
ATOM    278  N   GLN A  41       5.055  47.961  28.931  1.00 30.29           N  
ATOM    279  CA  GLN A  41       4.986  48.226  27.455  1.00 29.10           C  
ATOM    280  C   GLN A  41       4.359  49.612  27.314  1.00 28.89           C  
ATOM    281  O   GLN A  41       3.287  49.847  27.919  1.00 26.03           O  
ATOM    282  CB  GLN A  41       4.218  47.084  26.850  1.00 32.65           C  
ATOM    283  CG  GLN A  41       4.154  46.902  25.374  1.00 35.17           C  
ATOM    284  CD  GLN A  41       3.675  45.498  25.022  1.00 36.67           C  
ATOM    285  OE1 GLN A  41       3.690  45.140  23.860  1.00 38.00           O  
ATOM    286  NE2 GLN A  41       3.294  44.755  26.054  1.00 36.31           N  
ATOM    287  N   ASN A  42       5.041  50.483  26.561  1.00 27.87           N  
ATOM    288  CA  ASN A  42       4.588  51.890  26.443  1.00 28.08           C  
ATOM    289  C   ASN A  42       4.219  52.170  24.985  1.00 27.25           C  
ATOM    290  O   ASN A  42       4.961  52.806  24.249  1.00 26.74           O  
ATOM    291  CB  ASN A  42       5.631  52.859  26.971  1.00 28.77           C  
ATOM    292  CG  ASN A  42       5.849  52.818  28.464  1.00 32.04           C  
ATOM    293  OD1 ASN A  42       6.377  51.848  29.058  1.00 31.20           O  
ATOM    294  ND2 ASN A  42       5.451  53.913  29.118  1.00 32.27           N  
ATOM    295  N   PRO A  43       3.054  51.653  24.630  1.00 26.70           N  
ATOM    296  CA  PRO A  43       2.580  51.830  23.236  1.00 24.93           C  
ATOM    297  C   PRO A  43       2.337  53.300  22.935  1.00 24.08           C  
ATOM    298  O   PRO A  43       2.091  54.078  23.881  1.00 23.57           O  
ATOM    299  CB  PRO A  43       1.322  50.994  23.187  1.00 24.92           C  
ATOM    300  CG  PRO A  43       0.806  50.991  24.623  1.00 25.87           C  
ATOM    301  CD  PRO A  43       2.078  50.904  25.455  1.00 26.59           C  
ATOM    302  N   THR A  44       2.355  53.656  21.657  1.00 23.02           N  
ATOM    303  CA  THR A  44       2.014  55.053  21.290  1.00 22.23           C  
ATOM    304  C   THR A  44       0.496  55.080  21.154  1.00 23.22           C  
ATOM    305  O   THR A  44      -0.151  54.018  21.173  1.00 23.99           O  
ATOM    306  CB  THR A  44       2.735  55.552  19.994  1.00 21.23           C  
ATOM    307  OG1 THR A  44       2.168  54.796  18.907  1.00 19.46           O  
ATOM    308  CG2 THR A  44       4.281  55.378  20.011  1.00 19.45           C  
ATOM    309  N   GLU A  45      -0.072  56.270  21.065  1.00 24.98           N  
ATOM    310  CA  GLU A  45      -1.515  56.482  20.914  1.00 25.14           C  
ATOM    311  C   GLU A  45      -1.997  55.807  19.645  1.00 23.64           C  
ATOM    312  O   GLU A  45      -3.103  55.247  19.641  1.00 23.74           O  
ATOM    313  CB  GLU A  45      -1.904  57.964  20.877  1.00 29.38           C  
ATOM    314  CG  GLU A  45      -3.385  58.289  20.727  1.00 36.70           C  
ATOM    315  CD  GLU A  45      -4.214  58.342  21.983  1.00 41.76           C  
ATOM    316  OE1 GLU A  45      -5.407  58.091  22.104  1.00 41.93           O  
ATOM    317  OE2 GLU A  45      -3.530  58.708  22.980  1.00 44.85           O  
ATOM    318  N   ALA A  46      -1.179  55.811  18.608  1.00 21.85           N  
ATOM    319  CA  ALA A  46      -1.527  55.213  17.306  1.00 21.89           C  
ATOM    320  C   ALA A  46      -1.685  53.716  17.408  1.00 20.45           C  
ATOM    321  O   ALA A  46      -2.534  53.076  16.782  1.00 20.42           O  
ATOM    322  CB  ALA A  46      -0.487  55.561  16.222  1.00 21.97           C  
ATOM    323  N   GLU A  47      -0.785  53.121  18.176  1.00 20.26           N  
ATOM    324  CA  GLU A  47      -0.834  51.647  18.410  1.00 19.01           C  
ATOM    325  C   GLU A  47      -2.038  51.305  19.299  1.00 17.00           C  
ATOM    326  O   GLU A  47      -2.687  50.262  19.117  1.00 16.78           O  
ATOM    327  CB  GLU A  47       0.429  51.218  19.157  1.00 20.60           C  
ATOM    328  CG  GLU A  47       1.669  51.239  18.252  1.00 21.02           C  
ATOM    329  CD  GLU A  47       2.962  51.049  18.952  1.00 20.98           C  
ATOM    330  OE1 GLU A  47       3.319  51.588  19.981  1.00 22.62           O  
ATOM    331  OE2 GLU A  47       3.640  50.271  18.285  1.00 23.50           O  
ATOM    332  N   LEU A  48      -2.287  52.192  20.229  1.00 16.26           N  
ATOM    333  CA  LEU A  48      -3.457  52.010  21.164  1.00 18.71           C  
ATOM    334  C   LEU A  48      -4.704  52.070  20.267  1.00 19.55           C  
ATOM    335  O   LEU A  48      -5.512  51.154  20.325  1.00 19.40           O  
ATOM    336  CB  LEU A  48      -3.403  53.065  22.224  1.00 20.20           C  
ATOM    337  CG  LEU A  48      -2.908  52.793  23.636  1.00 22.78           C  
ATOM    338  CD1 LEU A  48      -2.047  51.568  23.717  1.00 22.16           C  
ATOM    339  CD2 LEU A  48      -2.070  54.003  24.083  1.00 21.36           C  
ATOM    340  N   GLN A  49      -4.787  53.125  19.447  1.00 19.79           N  
ATOM    341  CA  GLN A  49      -5.944  53.259  18.537  1.00 20.21           C  
ATOM    342  C   GLN A  49      -6.162  52.028  17.694  1.00 18.97           C  
ATOM    343  O   GLN A  49      -7.354  51.615  17.513  1.00 19.33           O  
ATOM    344  CB  GLN A  49      -5.927  54.497  17.622  1.00 22.83           C  
ATOM    345  CG  GLN A  49      -7.314  54.647  16.995  1.00 25.25           C  
ATOM    346  CD  GLN A  49      -8.372  55.048  17.970  1.00 26.63           C  
ATOM    347  OE1 GLN A  49      -9.515  54.615  17.918  1.00 29.29           O  
ATOM    348  NE2 GLN A  49      -8.006  55.882  18.936  1.00 26.87           N  
ATOM    349  N   ASP A  50      -5.120  51.415  17.170  1.00 18.19           N  
ATOM    350  CA  ASP A  50      -5.342  50.170  16.352  1.00 16.88           C  
ATOM    351  C   ASP A  50      -5.870  49.055  17.265  1.00 16.18           C  
ATOM    352  O   ASP A  50      -6.612  48.189  16.792  1.00 14.26           O  
ATOM    353  CB  ASP A  50      -4.094  49.723  15.615  1.00 18.42           C  
ATOM    354  CG  ASP A  50      -3.669  50.575  14.435  1.00 20.98           C  
ATOM    355  OD1 ASP A  50      -4.473  51.051  13.632  1.00 20.52           O  
ATOM    356  OD2 ASP A  50      -2.435  50.780  14.324  1.00 23.34           O  
ATOM    357  N   MET A  51      -5.371  49.008  18.503  1.00 15.84           N  
ATOM    358  CA  MET A  51      -5.851  47.874  19.389  1.00 17.33           C  
ATOM    359  C   MET A  51      -7.360  48.048  19.587  1.00 17.43           C  
ATOM    360  O   MET A  51      -8.122  47.052  19.478  1.00 19.72           O  
ATOM    361  CB  MET A  51      -5.024  47.781  20.635  1.00 17.86           C  
ATOM    362  CG  MET A  51      -3.553  47.404  20.423  1.00 23.63           C  
ATOM    363  SD  MET A  51      -2.766  47.359  22.083  1.00 28.19           S  
ATOM    364  CE  MET A  51      -1.262  48.276  21.816  1.00 29.31           C  
ATOM    365  N   ILE A  52      -7.858  49.235  19.860  1.00 17.07           N  
ATOM    366  CA  ILE A  52      -9.295  49.484  20.059  1.00 16.64           C  
ATOM    367  C   ILE A  52     -10.116  49.206  18.800  1.00 18.33           C  
ATOM    368  O   ILE A  52     -11.222  48.537  18.944  1.00 17.31           O  
ATOM    369  CB  ILE A  52      -9.612  50.886  20.633  1.00 17.05           C  
ATOM    370  CG1 ILE A  52      -9.744  50.954  22.144  1.00 19.66           C  
ATOM    371  CG2 ILE A  52     -11.018  51.398  20.074  1.00 17.94           C  
ATOM    372  CD1 ILE A  52      -8.641  50.785  23.132  1.00 19.43           C  
ATOM    373  N   ASN A  53      -9.678  49.708  17.663  1.00 17.55           N  
ATOM    374  CA  ASN A  53     -10.446  49.527  16.397  1.00 21.58           C  
ATOM    375  C   ASN A  53     -10.775  48.082  16.050  1.00 21.59           C  
ATOM    376  O   ASN A  53     -11.809  47.712  15.453  1.00 23.82           O  
ATOM    377  CB  ASN A  53      -9.678  50.148  15.213  1.00 23.87           C  
ATOM    378  CG  ASN A  53      -9.724  51.663  15.248  1.00 26.92           C  
ATOM    379  OD1 ASN A  53      -9.084  52.331  14.405  1.00 28.28           O  
ATOM    380  ND2 ASN A  53     -10.435  52.160  16.234  1.00 26.81           N  
ATOM    381  N   GLU A  54      -9.793  47.254  16.335  1.00 22.80           N  
ATOM    382  CA  GLU A  54      -9.940  45.815  16.074  1.00 23.50           C  
ATOM    383  C   GLU A  54     -11.120  45.244  16.832  1.00 22.87           C  
ATOM    384  O   GLU A  54     -11.788  44.374  16.269  1.00 24.01           O  
ATOM    385  CB  GLU A  54      -8.648  45.116  16.497  1.00 28.16           C  
ATOM    386  CG  GLU A  54      -8.269  43.842  15.802  1.00 34.68           C  
ATOM    387  CD  GLU A  54      -7.453  42.840  16.542  1.00 38.35           C  
ATOM    388  OE1 GLU A  54      -7.731  41.635  16.493  1.00 42.97           O  
ATOM    389  OE2 GLU A  54      -6.509  43.354  17.159  1.00 38.95           O  
ATOM    390  N   VAL A  55     -11.384  45.697  18.052  1.00 22.62           N  
ATOM    391  CA  VAL A  55     -12.457  45.134  18.907  1.00 21.95           C  
ATOM    392  C   VAL A  55     -13.713  45.940  18.857  1.00 21.03           C  
ATOM    393  O   VAL A  55     -14.836  45.419  18.876  1.00 22.43           O  
ATOM    394  CB  VAL A  55     -11.892  44.903  20.333  1.00 23.39           C  
ATOM    395  CG1 VAL A  55     -10.419  44.520  20.347  1.00 22.18           C  
ATOM    396  CG2 VAL A  55     -12.056  46.110  21.205  1.00 28.30           C  
ATOM    397  N   ASP A  56     -13.574  47.239  18.682  1.00 22.18           N  
ATOM    398  CA  ASP A  56     -14.735  48.151  18.586  1.00 22.44           C  
ATOM    399  C   ASP A  56     -15.690  47.749  17.476  1.00 23.40           C  
ATOM    400  O   ASP A  56     -15.539  48.132  16.313  1.00 25.10           O  
ATOM    401  CB  ASP A  56     -14.185  49.554  18.495  1.00 20.65           C  
ATOM    402  CG  ASP A  56     -15.313  50.572  18.593  1.00 21.64           C  
ATOM    403  OD1 ASP A  56     -15.070  51.680  18.103  1.00 20.26           O  
ATOM    404  OD2 ASP A  56     -16.348  50.152  19.195  1.00 19.29           O  
ATOM    405  N   ALA A  57     -16.747  46.972  17.744  1.00 24.02           N  
ATOM    406  CA  ALA A  57     -17.664  46.585  16.658  1.00 23.15           C  
ATOM    407  C   ALA A  57     -18.567  47.668  16.140  1.00 23.34           C  
ATOM    408  O   ALA A  57     -18.909  47.559  14.932  1.00 25.58           O  
ATOM    409  CB  ALA A  57     -18.506  45.377  17.071  1.00 25.33           C  
ATOM    410  N   ASP A  58     -19.047  48.621  16.899  1.00 22.66           N  
ATOM    411  CA  ASP A  58     -20.001  49.631  16.463  1.00 21.42           C  
ATOM    412  C   ASP A  58     -19.400  50.981  16.142  1.00 21.12           C  
ATOM    413  O   ASP A  58     -20.151  51.943  15.943  1.00 22.98           O  
ATOM    414  CB  ASP A  58     -21.130  49.760  17.524  1.00 19.72           C  
ATOM    415  CG  ASP A  58     -20.645  50.228  18.867  1.00 17.91           C  
ATOM    416  OD1 ASP A  58     -21.427  50.432  19.849  1.00 19.58           O  
ATOM    417  OD2 ASP A  58     -19.409  50.361  18.987  1.00 13.58           O  
ATOM    418  N   GLY A  59     -18.109  51.161  16.214  1.00 22.19           N  
ATOM    419  CA  GLY A  59     -17.344  52.341  15.929  1.00 18.46           C  
ATOM    420  C   GLY A  59     -17.532  53.520  16.769  1.00 19.88           C  
ATOM    421  O   GLY A  59     -17.250  54.649  16.329  1.00 21.43           O  
ATOM    422  N   ASN A  60     -18.043  53.365  18.016  1.00 19.83           N  
ATOM    423  CA  ASN A  60     -18.184  54.574  18.860  1.00 17.34           C  
ATOM    424  C   ASN A  60     -16.782  54.918  19.335  1.00 16.56           C  
ATOM    425  O   ASN A  60     -16.743  55.983  20.007  1.00 17.44           O  
ATOM    426  CB  ASN A  60     -19.178  54.546  19.999  1.00 17.31           C  
ATOM    427  CG  ASN A  60     -19.018  53.422  20.980  1.00 17.91           C  
ATOM    428  OD1 ASN A  60     -18.106  52.599  20.835  1.00 17.75           O  
ATOM    429  ND2 ASN A  60     -19.894  53.329  22.012  1.00 20.17           N  
ATOM    430  N   GLY A  61     -15.779  54.076  19.115  1.00 15.39           N  
ATOM    431  CA  GLY A  61     -14.439  54.515  19.616  1.00 16.04           C  
ATOM    432  C   GLY A  61     -13.997  53.991  20.921  1.00 16.80           C  
ATOM    433  O   GLY A  61     -12.844  54.241  21.393  1.00 17.54           O  
ATOM    434  N   THR A  62     -14.873  53.200  21.579  1.00 17.20           N  
ATOM    435  CA  THR A  62     -14.579  52.517  22.836  1.00 14.69           C  
ATOM    436  C   THR A  62     -15.148  51.112  22.805  1.00 15.42           C  
ATOM    437  O   THR A  62     -16.039  50.722  22.002  1.00 12.35           O  
ATOM    438  CB  THR A  62     -15.125  53.283  24.101  1.00 18.05           C  
ATOM    439  OG1 THR A  62     -16.580  53.288  24.042  1.00 17.65           O  
ATOM    440  CG2 THR A  62     -14.562  54.724  24.209  1.00 17.50           C  
ATOM    441  N   ILE A  63     -14.601  50.352  23.781  1.00 14.25           N  
ATOM    442  CA  ILE A  63     -15.070  48.964  23.936  1.00 13.53           C  
ATOM    443  C   ILE A  63     -15.835  48.775  25.235  1.00 12.84           C  
ATOM    444  O   ILE A  63     -15.439  49.182  26.345  1.00 10.53           O  
ATOM    445  CB  ILE A  63     -13.957  47.910  23.617  1.00 18.50           C  
ATOM    446  CG1 ILE A  63     -14.024  46.863  24.751  1.00 15.59           C  
ATOM    447  CG2 ILE A  63     -12.502  48.366  23.369  1.00 16.66           C  
ATOM    448  CD1 ILE A  63     -14.787  45.622  24.345  1.00 20.10           C  
ATOM    449  N   ASP A  64     -17.010  48.187  25.027  1.00 13.61           N  
ATOM    450  CA  ASP A  64     -17.969  47.847  26.075  1.00 12.51           C  
ATOM    451  C   ASP A  64     -17.865  46.337  26.357  1.00 13.54           C  
ATOM    452  O   ASP A  64     -17.200  45.584  25.647  1.00 11.74           O  
ATOM    453  CB  ASP A  64     -19.357  48.323  25.651  1.00 11.65           C  
ATOM    454  CG  ASP A  64     -19.927  47.510  24.514  1.00 14.89           C  
ATOM    455  OD1 ASP A  64     -21.000  47.883  23.974  1.00 15.16           O  
ATOM    456  OD2 ASP A  64     -19.300  46.488  24.165  1.00 12.98           O  
ATOM    457  N   PHE A  65     -18.582  45.867  27.368  1.00 14.05           N  
ATOM    458  CA  PHE A  65     -18.560  44.466  27.775  1.00 14.53           C  
ATOM    459  C   PHE A  65     -18.863  43.464  26.722  1.00 13.47           C  
ATOM    460  O   PHE A  65     -18.098  42.490  26.488  1.00 14.44           O  
ATOM    461  CB  PHE A  65     -19.472  44.316  29.036  1.00 17.98           C  
ATOM    462  CG  PHE A  65     -19.137  42.977  29.648  1.00 18.04           C  
ATOM    463  CD1 PHE A  65     -20.170  42.038  29.789  1.00 20.65           C  
ATOM    464  CD2 PHE A  65     -17.846  42.700  30.033  1.00 17.67           C  
ATOM    465  CE1 PHE A  65     -19.886  40.785  30.344  1.00 19.56           C  
ATOM    466  CE2 PHE A  65     -17.533  41.443  30.592  1.00 19.78           C  
ATOM    467  CZ  PHE A  65     -18.580  40.525  30.724  1.00 17.87           C  
ATOM    468  N   PRO A  66     -20.004  43.576  26.047  1.00 13.52           N  
ATOM    469  CA  PRO A  66     -20.359  42.667  24.954  1.00 14.49           C  
ATOM    470  C   PRO A  66     -19.289  42.558  23.878  1.00 16.22           C  
ATOM    471  O   PRO A  66     -19.057  41.435  23.321  1.00 18.19           O  
ATOM    472  CB  PRO A  66     -21.667  43.180  24.373  1.00 13.79           C  
ATOM    473  CG  PRO A  66     -22.162  44.237  25.312  1.00 13.77           C  
ATOM    474  CD  PRO A  66     -21.019  44.638  26.198  1.00 14.93           C  
ATOM    475  N   GLU A  67     -18.653  43.658  23.512  1.00 16.80           N  
ATOM    476  CA  GLU A  67     -17.574  43.705  22.486  1.00 17.11           C  
ATOM    477  C   GLU A  67     -16.343  42.973  23.015  1.00 18.63           C  
ATOM    478  O   GLU A  67     -15.774  42.127  22.281  1.00 19.47           O  
ATOM    479  CB  GLU A  67     -17.173  45.128  22.142  1.00 16.83           C  
ATOM    480  CG  GLU A  67     -18.045  45.924  21.149  1.00 15.51           C  
ATOM    481  CD  GLU A  67     -17.878  47.402  21.119  1.00 14.60           C  
ATOM    482  OE1 GLU A  67     -17.202  47.995  21.937  1.00 16.02           O  
ATOM    483  OE2 GLU A  67     -18.502  48.046  20.243  1.00 13.27           O  
ATOM    484  N   PHE A  68     -15.900  43.257  24.198  1.00 18.30           N  
ATOM    485  CA  PHE A  68     -14.777  42.604  24.913  1.00 20.47           C  
ATOM    486  C   PHE A  68     -15.008  41.087  24.996  1.00 21.88           C  
ATOM    487  O   PHE A  68     -14.187  40.259  24.573  1.00 21.18           O  
ATOM    488  CB  PHE A  68     -14.644  43.152  26.341  1.00 18.61           C  
ATOM    489  CG  PHE A  68     -13.578  42.590  27.212  1.00 21.39           C  
ATOM    490  CD1 PHE A  68     -12.270  43.078  27.159  1.00 21.36           C  
ATOM    491  CD2 PHE A  68     -13.861  41.518  28.096  1.00 20.00           C  
ATOM    492  CE1 PHE A  68     -11.271  42.563  27.985  1.00 21.58           C  
ATOM    493  CE2 PHE A  68     -12.893  41.001  28.930  1.00 19.74           C  
ATOM    494  CZ  PHE A  68     -11.584  41.506  28.859  1.00 21.30           C  
ATOM    495  N   LEU A  69     -16.148  40.767  25.542  1.00 24.10           N  
ATOM    496  CA  LEU A  69     -16.624  39.386  25.794  1.00 28.28           C  
ATOM    497  C   LEU A  69     -16.543  38.552  24.520  1.00 30.40           C  
ATOM    498  O   LEU A  69     -16.079  37.396  24.576  1.00 29.47           O  
ATOM    499  CB  LEU A  69     -17.992  39.551  26.431  1.00 30.14           C  
ATOM    500  CG  LEU A  69     -18.841  38.480  27.019  1.00 33.02           C  
ATOM    501  CD1 LEU A  69     -18.978  37.313  26.051  1.00 35.33           C  
ATOM    502  CD2 LEU A  69     -18.226  37.997  28.343  1.00 32.95           C  
ATOM    503  N   THR A  70     -17.001  39.149  23.424  1.00 31.75           N  
ATOM    504  CA  THR A  70     -17.019  38.495  22.112  1.00 34.26           C  
ATOM    505  C   THR A  70     -15.616  38.433  21.539  1.00 35.41           C  
ATOM    506  O   THR A  70     -15.326  37.414  20.872  1.00 37.68           O  
ATOM    507  CB  THR A  70     -18.055  39.077  21.088  1.00 35.58           C  
ATOM    508  OG1 THR A  70     -17.445  40.286  20.527  1.00 40.24           O  
ATOM    509  CG2 THR A  70     -19.422  39.455  21.643  1.00 35.83           C  
ATOM    510  N   MET A  71     -14.768  39.402  21.777  1.00 36.62           N  
ATOM    511  CA  MET A  71     -13.371  39.368  21.286  1.00 37.56           C  
ATOM    512  C   MET A  71     -12.680  38.171  21.989  1.00 38.04           C  
ATOM    513  O   MET A  71     -12.071  37.323  21.394  1.00 36.30           O  
ATOM    514  CB  MET A  71     -12.598  40.651  21.527  1.00 37.42           C  
ATOM    515  CG  MET A  71     -11.092  40.459  21.456  1.00 41.09           C  
ATOM    516  SD  MET A  71     -10.375  40.674  23.127  1.00 46.36           S  
ATOM    517  CE  MET A  71      -8.810  39.854  23.000  1.00 43.62           C  
ATOM    518  N   MET A  72     -12.829  38.198  23.299  1.00 40.20           N  
ATOM    519  CA  MET A  72     -12.293  37.280  24.289  1.00 41.15           C  
ATOM    520  C   MET A  72     -12.668  35.826  24.011  1.00 40.53           C  
ATOM    521  O   MET A  72     -11.787  34.974  24.063  1.00 40.39           O  
ATOM    522  CB  MET A  72     -12.723  37.736  25.687  1.00 44.20           C  
ATOM    523  CG  MET A  72     -11.536  37.990  26.575  1.00 48.40           C  
ATOM    524  SD  MET A  72     -10.334  38.886  25.517  1.00 54.90           S  
ATOM    525  CE  MET A  72      -9.208  39.466  26.828  1.00 53.32           C  
ATOM    526  N   ALA A  73     -13.922  35.577  23.724  1.00 41.07           N  
ATOM    527  CA  ALA A  73     -14.453  34.240  23.434  1.00 42.68           C  
ATOM    528  C   ALA A  73     -13.624  33.624  22.303  1.00 44.67           C  
ATOM    529  O   ALA A  73     -12.754  32.738  22.557  1.00 44.92           O  
ATOM    530  CB  ALA A  73     -15.944  34.343  23.226  1.00 39.68           C  
ATOM    531  N   ARG A  74     -13.798  34.100  21.094  1.00 45.81           N  
ATOM    532  CA  ARG A  74     -13.068  33.718  19.893  1.00 46.94           C  
ATOM    533  C   ARG A  74     -11.580  33.470  20.112  1.00 47.42           C  
ATOM    534  O   ARG A  74     -11.047  32.405  19.733  1.00 47.79           O  
ATOM    535  CB  ARG A  74     -13.180  34.851  18.840  1.00 48.50           C  
ATOM    536  CG  ARG A  74     -14.285  34.649  17.818  1.00 50.87           C  
ATOM    537  CD  ARG A  74     -14.073  35.447  16.567  1.00 53.34           C  
ATOM    538  NE  ARG A  74     -14.485  36.840  16.744  1.00 55.02           N  
ATOM    539  CZ  ARG A  74     -15.751  37.121  17.107  1.00 56.42           C  
ATOM    540  NH1 ARG A  74     -16.653  36.155  17.259  1.00 56.08           N  
ATOM    541  NH2 ARG A  74     -16.086  38.392  17.329  1.00 57.71           N  
ATOM    542  N   LYS A  75     -10.889  34.443  20.688  1.00 47.17           N  
ATOM    543  CA  LYS A  75      -9.463  34.351  20.961  1.00 48.29           C  
ATOM    544  C   LYS A  75      -9.086  33.314  22.020  1.00 49.44           C  
ATOM    545  O   LYS A  75      -7.882  32.940  22.089  1.00 49.19           O  
ATOM    546  CB  LYS A  75      -8.790  35.673  21.381  1.00 46.65           C  
ATOM    547  CG  LYS A  75      -7.348  35.401  21.825  1.00 46.31           C  
ATOM    548  CD  LYS A  75      -6.688  36.543  22.529  1.00 47.98           C  
ATOM    549  CE  LYS A  75      -5.934  37.415  21.525  1.00 50.15           C  
ATOM    550  NZ  LYS A  75      -4.896  36.550  20.879  1.00 51.83           N  
ATOM    551  N   MET A  76     -10.043  32.886  22.831  1.00 50.11           N  
ATOM    552  CA  MET A  76      -9.673  31.878  23.853  1.00 51.53           C  
ATOM    553  C   MET A  76      -9.583  30.534  23.129  1.00 51.52           C  
ATOM    554  O   MET A  76      -8.791  29.680  23.593  1.00 51.55           O  
ATOM    555  CB  MET A  76     -10.529  31.932  25.091  1.00 54.86           C  
ATOM    556  CG  MET A  76     -10.367  33.180  25.927  1.00 57.16           C  
ATOM    557  SD  MET A  76      -9.321  32.874  27.392  1.00 60.69           S  
ATOM    558  CE  MET A  76      -7.722  32.562  26.636  1.00 57.92           C  
ATOM    559  N   LYS A  77     -10.306  30.376  22.032  1.00 51.25           N  
ATOM    560  CA  LYS A  77     -10.293  29.138  21.240  1.00 52.19           C  
ATOM    561  C   LYS A  77      -8.939  28.880  20.557  1.00 52.51           C  
ATOM    562  O   LYS A  77      -8.403  27.759  20.584  1.00 52.84           O  
ATOM    563  CB  LYS A  77     -11.340  29.066  20.133  1.00 51.30           C  
ATOM    564  CG  LYS A  77     -12.702  29.620  20.470  1.00 52.25           C  
ATOM    565  CD  LYS A  77     -13.724  28.604  20.904  1.00 53.76           C  
ATOM    566  CE  LYS A  77     -14.375  27.866  19.756  1.00 55.65           C  
ATOM    567  NZ  LYS A  77     -15.073  28.822  18.851  1.00 56.25           N  
ATOM    568  N   ASP A  78      -8.431  29.919  19.943  1.00 52.78           N  
ATOM    569  CA  ASP A  78      -7.196  29.999  19.190  1.00 52.77           C  
ATOM    570  C   ASP A  78      -5.934  29.862  20.046  1.00 52.72           C  
ATOM    571  O   ASP A  78      -4.843  29.652  19.482  1.00 52.65           O  
ATOM    572  CB  ASP A  78      -7.172  31.305  18.364  1.00 52.21           C  
ATOM    573  CG  ASP A  78      -8.403  31.429  17.497  1.00 52.40           C  
ATOM    574  OD1 ASP A  78      -8.485  32.304  16.622  1.00 52.15           O  
ATOM    575  OD2 ASP A  78      -9.312  30.591  17.738  1.00 52.77           O  
ATOM    576  N   THR A  79      -6.073  29.985  21.328  1.00 52.91           N  
ATOM    577  CA  THR A  79      -4.917  29.856  22.249  1.00 54.95           C  
ATOM    578  C   THR A  79      -4.913  28.451  22.854  1.00 55.01           C  
ATOM    579  O   THR A  79      -3.950  27.977  23.481  1.00 54.95           O  
ATOM    580  CB  THR A  79      -4.947  31.021  23.305  1.00 55.63           C  
ATOM    581  OG1 THR A  79      -4.007  30.655  24.363  1.00 57.46           O  
ATOM    582  CG2 THR A  79      -6.363  31.300  23.816  1.00 55.61           C  
ATOM    583  N   ASP A  80      -6.038  27.789  22.617  1.00 55.15           N  
ATOM    584  CA  ASP A  80      -6.314  26.410  23.052  1.00 55.30           C  
ATOM    585  C   ASP A  80      -5.974  25.448  21.895  1.00 54.57           C  
ATOM    586  O   ASP A  80      -5.973  24.224  22.004  1.00 54.07           O  
ATOM    587  CB  ASP A  80      -7.760  26.300  23.537  1.00 56.76           C  
ATOM    588  CG  ASP A  80      -7.890  26.789  24.978  1.00 58.40           C  
ATOM    589  OD1 ASP A  80      -8.953  27.301  25.357  1.00 59.28           O  
ATOM    590  OD2 ASP A  80      -6.876  26.633  25.696  1.00 58.57           O  
ATOM    591  N   SER A  81      -5.715  26.099  20.784  1.00 53.97           N  
ATOM    592  CA  SER A  81      -5.287  25.541  19.503  1.00 52.82           C  
ATOM    593  C   SER A  81      -3.754  25.583  19.457  1.00 51.91           C  
ATOM    594  O   SER A  81      -3.087  24.537  19.440  1.00 52.35           O  
ATOM    595  CB  SER A  81      -5.913  26.303  18.354  1.00 52.57           C  
ATOM    596  OG  SER A  81      -7.220  25.849  18.062  1.00 51.82           O  
ATOM    597  N   GLU A  82      -3.208  26.783  19.496  1.00 51.05           N  
ATOM    598  CA  GLU A  82      -1.752  26.960  19.484  1.00 51.06           C  
ATOM    599  C   GLU A  82      -1.106  26.087  20.556  1.00 51.10           C  
ATOM    600  O   GLU A  82       0.077  25.698  20.472  1.00 51.41           O  
ATOM    601  CB  GLU A  82      -1.366  28.395  19.796  1.00 51.80           C  
ATOM    602  CG  GLU A  82       0.103  28.780  19.795  1.00 52.84           C  
ATOM    603  CD  GLU A  82       0.795  28.784  18.459  1.00 53.57           C  
ATOM    604  OE1 GLU A  82       1.992  29.041  18.344  1.00 53.66           O  
ATOM    605  OE2 GLU A  82       0.031  28.483  17.507  1.00 53.77           O  
ATOM    606  N   GLU A  83      -1.890  25.820  21.601  1.00 50.47           N  
ATOM    607  CA  GLU A  83      -1.380  25.033  22.740  1.00 49.30           C  
ATOM    608  C   GLU A  83      -1.411  23.548  22.476  1.00 47.62           C  
ATOM    609  O   GLU A  83      -0.467  22.842  22.897  1.00 47.29           O  
ATOM    610  CB  GLU A  83      -1.966  25.470  24.069  1.00 51.89           C  
ATOM    611  CG  GLU A  83      -1.236  26.697  24.704  1.00 54.78           C  
ATOM    612  CD  GLU A  83      -1.545  26.912  26.155  1.00 57.88           C  
ATOM    613  OE1 GLU A  83      -2.697  26.886  26.596  1.00 59.91           O  
ATOM    614  OE2 GLU A  83      -0.559  27.110  26.898  1.00 58.20           O  
ATOM    615  N   GLU A  84      -2.370  23.053  21.733  1.00 46.24           N  
ATOM    616  CA  GLU A  84      -2.444  21.640  21.347  1.00 45.32           C  
ATOM    617  C   GLU A  84      -1.265  21.361  20.393  1.00 43.82           C  
ATOM    618  O   GLU A  84      -0.517  20.391  20.553  1.00 43.79           O  
ATOM    619  CB  GLU A  84      -3.742  21.292  20.645  1.00 48.82           C  
ATOM    620  CG  GLU A  84      -4.838  20.604  21.450  1.00 52.86           C  
ATOM    621  CD  GLU A  84      -6.255  20.976  21.152  1.00 55.90           C  
ATOM    622  OE1 GLU A  84      -6.732  22.092  21.380  1.00 57.32           O  
ATOM    623  OE2 GLU A  84      -6.925  20.026  20.673  1.00 57.34           O  
ATOM    624  N   ILE A  85      -1.118  22.281  19.442  1.00 40.87           N  
ATOM    625  CA  ILE A  85      -0.060  22.227  18.451  1.00 38.05           C  
ATOM    626  C   ILE A  85       1.278  22.422  19.144  1.00 36.85           C  
ATOM    627  O   ILE A  85       2.210  21.759  18.686  1.00 38.32           O  
ATOM    628  CB  ILE A  85      -0.253  23.201  17.245  1.00 35.83           C  
ATOM    629  CG1 ILE A  85      -1.501  22.796  16.433  1.00 34.51           C  
ATOM    630  CG2 ILE A  85       0.994  23.286  16.317  1.00 37.67           C  
ATOM    631  CD1 ILE A  85      -1.975  23.926  15.459  1.00 35.09           C  
ATOM    632  N   ARG A  86       1.364  23.231  20.169  1.00 35.82           N  
ATOM    633  CA  ARG A  86       2.673  23.415  20.837  1.00 35.37           C  
ATOM    634  C   ARG A  86       3.074  22.131  21.572  1.00 34.02           C  
ATOM    635  O   ARG A  86       4.263  21.883  21.856  1.00 32.56           O  
ATOM    636  CB  ARG A  86       2.698  24.640  21.712  1.00 39.18           C  
ATOM    637  CG  ARG A  86       3.124  25.951  21.055  1.00 42.48           C  
ATOM    638  CD  ARG A  86       3.127  27.062  22.056  1.00 47.06           C  
ATOM    639  NE  ARG A  86       4.110  28.071  21.812  1.00 49.67           N  
ATOM    640  CZ  ARG A  86       4.115  29.127  21.006  1.00 51.73           C  
ATOM    641  NH1 ARG A  86       3.103  29.484  20.210  1.00 51.45           N  
ATOM    642  NH2 ARG A  86       5.229  29.891  21.010  1.00 51.52           N  
ATOM    643  N   GLU A  87       2.080  21.316  21.850  1.00 32.47           N  
ATOM    644  CA  GLU A  87       2.212  20.042  22.545  1.00 30.68           C  
ATOM    645  C   GLU A  87       2.824  18.973  21.651  1.00 28.28           C  
ATOM    646  O   GLU A  87       3.886  18.433  21.953  1.00 27.65           O  
ATOM    647  CB  GLU A  87       0.856  19.502  23.025  1.00 33.05           C  
ATOM    648  CG  GLU A  87       0.578  19.778  24.488  1.00 37.42           C  
ATOM    649  CD  GLU A  87      -0.716  19.341  25.093  1.00 39.62           C  
ATOM    650  OE1 GLU A  87      -1.035  19.812  26.182  1.00 40.26           O  
ATOM    651  OE2 GLU A  87      -1.383  18.487  24.459  1.00 40.11           O  
ATOM    652  N   ALA A  88       2.099  18.715  20.577  1.00 27.12           N  
ATOM    653  CA  ALA A  88       2.520  17.735  19.571  1.00 26.50           C  
ATOM    654  C   ALA A  88       3.974  18.020  19.216  1.00 25.85           C  
ATOM    655  O   ALA A  88       4.801  17.109  19.172  1.00 26.83           O  
ATOM    656  CB  ALA A  88       1.585  17.788  18.396  1.00 26.59           C  
ATOM    657  N   PHE A  89       4.311  19.272  19.025  1.00 26.05           N  
ATOM    658  CA  PHE A  89       5.685  19.677  18.663  1.00 25.40           C  
ATOM    659  C   PHE A  89       6.685  19.077  19.632  1.00 26.45           C  
ATOM    660  O   PHE A  89       7.762  18.567  19.283  1.00 26.96           O  
ATOM    661  CB  PHE A  89       5.889  21.196  18.507  1.00 24.71           C  
ATOM    662  CG  PHE A  89       7.239  21.547  17.908  1.00 23.54           C  
ATOM    663  CD1 PHE A  89       7.409  21.469  16.528  1.00 23.85           C  
ATOM    664  CD2 PHE A  89       8.308  21.893  18.691  1.00 23.54           C  
ATOM    665  CE1 PHE A  89       8.613  21.757  15.920  1.00 24.16           C  
ATOM    666  CE2 PHE A  89       9.554  22.158  18.125  1.00 23.98           C  
ATOM    667  CZ  PHE A  89       9.700  22.094  16.720  1.00 24.42           C  
ATOM    668  N   ARG A  90       6.372  19.177  20.906  1.00 27.51           N  
ATOM    669  CA  ARG A  90       7.228  18.748  22.030  1.00 25.31           C  
ATOM    670  C   ARG A  90       7.405  17.241  22.098  1.00 24.20           C  
ATOM    671  O   ARG A  90       8.431  16.746  22.587  1.00 23.34           O  
ATOM    672  CB  ARG A  90       6.557  19.308  23.281  1.00 29.17           C  
ATOM    673  CG  ARG A  90       7.410  20.190  24.173  1.00 32.87           C  
ATOM    674  CD  ARG A  90       6.533  20.850  25.184  1.00 35.26           C  
ATOM    675  NE  ARG A  90       6.498  22.289  25.015  1.00 36.79           N  
ATOM    676  CZ  ARG A  90       5.371  22.972  25.326  1.00 35.53           C  
ATOM    677  NH1 ARG A  90       4.317  22.347  25.817  1.00 33.01           N  
ATOM    678  NH2 ARG A  90       5.380  24.279  25.077  1.00 35.93           N  
ATOM    679  N   VAL A  91       6.375  16.507  21.720  1.00 25.01           N  
ATOM    680  CA  VAL A  91       6.472  15.037  21.731  1.00 26.13           C  
ATOM    681  C   VAL A  91       7.302  14.664  20.488  1.00 25.63           C  
ATOM    682  O   VAL A  91       8.161  13.795  20.613  1.00 26.21           O  
ATOM    683  CB  VAL A  91       5.200  14.271  21.950  1.00 27.85           C  
ATOM    684  CG1 VAL A  91       4.009  15.127  22.357  1.00 30.40           C  
ATOM    685  CG2 VAL A  91       4.863  13.237  20.893  1.00 26.50           C  
ATOM    686  N   PHE A  92       7.073  15.363  19.389  1.00 25.62           N  
ATOM    687  CA  PHE A  92       7.887  15.081  18.187  1.00 26.07           C  
ATOM    688  C   PHE A  92       9.353  15.407  18.477  1.00 25.59           C  
ATOM    689  O   PHE A  92      10.210  14.575  18.163  1.00 26.73           O  
ATOM    690  CB  PHE A  92       7.405  15.794  16.946  1.00 27.76           C  
ATOM    691  CG  PHE A  92       6.316  15.166  16.154  1.00 29.87           C  
ATOM    692  CD1 PHE A  92       6.623  14.258  15.138  1.00 32.55           C  
ATOM    693  CD2 PHE A  92       4.986  15.496  16.365  1.00 30.05           C  
ATOM    694  CE1 PHE A  92       5.640  13.693  14.349  1.00 31.99           C  
ATOM    695  CE2 PHE A  92       3.974  14.931  15.612  1.00 31.98           C  
ATOM    696  CZ  PHE A  92       4.304  14.029  14.592  1.00 33.48           C  
ATOM    697  N   ASP A  93       9.657  16.549  19.036  1.00 25.32           N  
ATOM    698  CA  ASP A  93      11.015  17.016  19.296  1.00 26.46           C  
ATOM    699  C   ASP A  93      11.696  16.350  20.481  1.00 29.23           C  
ATOM    700  O   ASP A  93      12.063  17.019  21.486  1.00 29.69           O  
ATOM    701  CB  ASP A  93      11.007  18.564  19.411  1.00 24.95           C  
ATOM    702  CG  ASP A  93      12.436  19.049  19.574  1.00 26.14           C  
ATOM    703  OD1 ASP A  93      12.724  20.092  20.169  1.00 26.27           O  
ATOM    704  OD2 ASP A  93      13.313  18.284  19.079  1.00 25.89           O  
ATOM    705  N   LYS A  94      11.908  15.057  20.362  1.00 31.24           N  
ATOM    706  CA  LYS A  94      12.497  14.190  21.353  1.00 33.24           C  
ATOM    707  C   LYS A  94      13.696  14.763  22.085  1.00 34.46           C  
ATOM    708  O   LYS A  94      13.841  14.412  23.286  1.00 35.31           O  
ATOM    709  CB  LYS A  94      12.814  12.774  20.799  1.00 34.63           C  
ATOM    710  CG  LYS A  94      13.493  11.891  21.848  1.00 37.73           C  
ATOM    711  CD  LYS A  94      13.079  10.439  21.921  1.00 39.67           C  
ATOM    712  CE  LYS A  94      13.680   9.755  23.156  1.00 42.07           C  
ATOM    713  NZ  LYS A  94      12.656   8.910  23.878  1.00 42.47           N  
ATOM    714  N   ASP A  95      14.540  15.568  21.489  1.00 34.76           N  
ATOM    715  CA  ASP A  95      15.732  16.121  22.164  1.00 35.22           C  
ATOM    716  C   ASP A  95      15.566  17.594  22.527  1.00 36.20           C  
ATOM    717  O   ASP A  95      16.595  18.314  22.554  1.00 38.51           O  
ATOM    718  CB  ASP A  95      16.976  15.883  21.312  1.00 35.51           C  
ATOM    719  CG  ASP A  95      17.150  16.709  20.057  1.00 35.52           C  
ATOM    720  OD1 ASP A  95      18.141  16.471  19.302  1.00 37.30           O  
ATOM    721  OD2 ASP A  95      16.327  17.598  19.757  1.00 30.91           O  
ATOM    722  N   GLY A  96      14.368  18.052  22.770  1.00 35.42           N  
ATOM    723  CA  GLY A  96      14.054  19.448  23.070  1.00 35.38           C  
ATOM    724  C   GLY A  96      15.115  20.401  22.539  1.00 35.29           C  
ATOM    725  O   GLY A  96      15.722  21.158  23.326  1.00 36.72           O  
ATOM    726  N   ASN A  97      15.369  20.346  21.240  1.00 34.60           N  
ATOM    727  CA  ASN A  97      16.412  21.228  20.674  1.00 32.77           C  
ATOM    728  C   ASN A  97      15.823  22.292  19.759  1.00 30.62           C  
ATOM    729  O   ASN A  97      16.582  23.130  19.267  1.00 31.21           O  
ATOM    730  CB  ASN A  97      17.544  20.389  20.083  1.00 35.04           C  
ATOM    731  CG  ASN A  97      17.270  19.993  18.647  1.00 35.76           C  
ATOM    732  OD1 ASN A  97      16.081  19.835  18.263  1.00 35.79           O  
ATOM    733  ND2 ASN A  97      18.367  19.874  17.902  1.00 35.63           N  
ATOM    734  N   GLY A  98      14.534  22.304  19.572  1.00 28.61           N  
ATOM    735  CA  GLY A  98      13.790  23.244  18.782  1.00 27.92           C  
ATOM    736  C   GLY A  98      13.438  22.756  17.395  1.00 28.50           C  
ATOM    737  O   GLY A  98      12.622  23.373  16.710  1.00 28.94           O  
ATOM    738  N   TYR A  99      14.059  21.664  16.990  1.00 29.81           N  
ATOM    739  CA  TYR A  99      13.925  21.042  15.674  1.00 28.03           C  
ATOM    740  C   TYR A  99      13.589  19.557  15.656  1.00 26.08           C  
ATOM    741  O   TYR A  99      14.140  18.763  16.433  1.00 25.69           O  
ATOM    742  CB  TYR A  99      15.313  21.115  14.973  1.00 29.27           C  
ATOM    743  CG  TYR A  99      15.812  22.552  14.918  1.00 31.59           C  
ATOM    744  CD1 TYR A  99      16.926  22.908  15.679  1.00 34.02           C  
ATOM    745  CD2 TYR A  99      15.194  23.506  14.142  1.00 29.78           C  
ATOM    746  CE1 TYR A  99      17.424  24.235  15.633  1.00 33.85           C  
ATOM    747  CE2 TYR A  99      15.675  24.808  14.082  1.00 30.50           C  
ATOM    748  CZ  TYR A  99      16.783  25.155  14.830  1.00 31.43           C  
ATOM    749  OH  TYR A  99      17.239  26.434  14.785  1.00 33.87           O  
ATOM    750  N   ILE A 100      12.711  19.258  14.725  1.00 23.80           N  
ATOM    751  CA  ILE A 100      12.281  17.894  14.440  1.00 22.98           C  
ATOM    752  C   ILE A 100      13.151  17.317  13.304  1.00 22.05           C  
ATOM    753  O   ILE A 100      12.820  17.683  12.171  1.00 24.45           O  
ATOM    754  CB  ILE A 100      10.776  17.841  14.012  1.00 20.38           C  
ATOM    755  CG1 ILE A 100       9.853  18.254  15.207  1.00 19.21           C  
ATOM    756  CG2 ILE A 100      10.410  16.415  13.494  1.00 19.27           C  
ATOM    757  CD1 ILE A 100       8.369  18.437  14.684  1.00 20.06           C  
ATOM    758  N   SER A 101      14.058  16.447  13.542  1.00 21.23           N  
ATOM    759  CA  SER A 101      14.920  15.873  12.492  1.00 21.42           C  
ATOM    760  C   SER A 101      14.292  14.580  11.987  1.00 22.34           C  
ATOM    761  O   SER A 101      13.267  14.136  12.539  1.00 22.38           O  
ATOM    762  CB  SER A 101      16.315  15.693  13.031  1.00 21.44           C  
ATOM    763  OG  SER A 101      16.264  14.689  14.058  1.00 26.69           O  
ATOM    764  N   ALA A 102      14.832  14.006  10.948  1.00 21.18           N  
ATOM    765  CA  ALA A 102      14.314  12.795  10.319  1.00 23.62           C  
ATOM    766  C   ALA A 102      14.259  11.601  11.264  1.00 23.14           C  
ATOM    767  O   ALA A 102      13.290  10.824  11.264  1.00 23.23           O  
ATOM    768  CB  ALA A 102      15.123  12.470   9.058  1.00 23.52           C  
ATOM    769  N   ALA A 103      15.287  11.485  12.063  1.00 23.25           N  
ATOM    770  CA  ALA A 103      15.453  10.440  13.083  1.00 22.67           C  
ATOM    771  C   ALA A 103      14.288  10.496  14.064  1.00 22.32           C  
ATOM    772  O   ALA A 103      13.735   9.415  14.405  1.00 23.79           O  
ATOM    773  CB  ALA A 103      16.781  10.688  13.804  1.00 19.74           C  
ATOM    774  N   GLU A 104      13.943  11.707  14.464  1.00 20.78           N  
ATOM    775  CA  GLU A 104      12.850  11.993  15.399  1.00 22.25           C  
ATOM    776  C   GLU A 104      11.478  11.713  14.823  1.00 22.43           C  
ATOM    777  O   GLU A 104      10.690  10.994  15.506  1.00 23.28           O  
ATOM    778  CB  GLU A 104      12.904  13.416  15.979  1.00 20.41           C  
ATOM    779  CG  GLU A 104      14.169  13.576  16.888  1.00 23.03           C  
ATOM    780  CD  GLU A 104      14.374  14.938  17.460  1.00 23.80           C  
ATOM    781  OE1 GLU A 104      14.063  15.928  16.839  1.00 24.34           O  
ATOM    782  OE2 GLU A 104      14.887  15.027  18.597  1.00 23.40           O  
ATOM    783  N   LEU A 105      11.178  12.191  13.633  1.00 20.64           N  
ATOM    784  CA  LEU A 105       9.881  11.946  13.000  1.00 20.68           C  
ATOM    785  C   LEU A 105       9.713  10.471  12.706  1.00 20.98           C  
ATOM    786  O   LEU A 105       8.586   9.935  12.696  1.00 23.25           O  
ATOM    787  CB  LEU A 105       9.809  12.786  11.686  1.00 18.83           C  
ATOM    788  CG  LEU A 105       8.522  12.577  10.876  1.00 19.08           C  
ATOM    789  CD1 LEU A 105       7.359  13.148  11.667  1.00 16.86           C  
ATOM    790  CD2 LEU A 105       8.606  13.313   9.535  1.00 18.27           C  
ATOM    791  N   ARG A 106      10.823   9.818  12.384  1.00 21.26           N  
ATOM    792  CA  ARG A 106      10.773   8.368  12.077  1.00 21.22           C  
ATOM    793  C   ARG A 106      10.446   7.633  13.407  1.00 21.33           C  
ATOM    794  O   ARG A 106       9.501   6.832  13.356  1.00 20.58           O  
ATOM    795  CB  ARG A 106      11.976   7.813  11.404  1.00 21.01           C  
ATOM    796  CG  ARG A 106      11.814   6.426  10.757  1.00 25.66           C  
ATOM    797  CD  ARG A 106      13.053   6.096   9.931  1.00 26.49           C  
ATOM    798  NE  ARG A 106      13.887   5.101  10.604  1.00 32.27           N  
ATOM    799  CZ  ARG A 106      15.092   5.395  11.098  1.00 33.89           C  
ATOM    800  NH1 ARG A 106      15.657   6.595  10.957  1.00 36.84           N  
ATOM    801  NH2 ARG A 106      15.778   4.502  11.795  1.00 35.15           N  
ATOM    802  N   HIS A 107      11.165   7.861  14.461  1.00 21.78           N  
ATOM    803  CA  HIS A 107      10.869   7.219  15.761  1.00 25.24           C  
ATOM    804  C   HIS A 107       9.392   7.368  16.129  1.00 26.72           C  
ATOM    805  O   HIS A 107       8.684   6.376  16.270  1.00 28.82           O  
ATOM    806  CB  HIS A 107      11.624   7.787  16.957  1.00 26.54           C  
ATOM    807  CG  HIS A 107      11.505   6.984  18.221  1.00 31.91           C  
ATOM    808  ND1 HIS A 107      11.925   5.682  18.368  1.00 33.04           N  
ATOM    809  CD2 HIS A 107      11.058   7.386  19.449  1.00 32.21           C  
ATOM    810  CE1 HIS A 107      11.723   5.325  19.643  1.00 34.61           C  
ATOM    811  NE2 HIS A 107      11.217   6.335  20.311  1.00 33.66           N  
ATOM    812  N   VAL A 108       8.930   8.615  16.278  1.00 27.17           N  
ATOM    813  CA  VAL A 108       7.512   8.783  16.616  1.00 26.18           C  
ATOM    814  C   VAL A 108       6.597   8.239  15.564  1.00 25.36           C  
ATOM    815  O   VAL A 108       5.501   7.737  15.936  1.00 25.49           O  
ATOM    816  CB  VAL A 108       7.210  10.212  17.159  1.00 26.85           C  
ATOM    817  CG1 VAL A 108       8.345  11.169  17.118  1.00 24.59           C  
ATOM    818  CG2 VAL A 108       5.930  10.759  16.556  1.00 27.13           C  
ATOM    819  N   MET A 109       6.963   8.272  14.285  1.00 25.53           N  
ATOM    820  CA  MET A 109       5.998   7.736  13.245  1.00 24.50           C  
ATOM    821  C   MET A 109       5.773   6.245  13.476  1.00 24.22           C  
ATOM    822  O   MET A 109       4.667   5.681  13.265  1.00 20.61           O  
ATOM    823  CB  MET A 109       6.466   8.172  11.891  1.00 26.74           C  
ATOM    824  CG  MET A 109       5.414   8.645  10.959  1.00 30.19           C  
ATOM    825  SD  MET A 109       4.337   9.966  11.688  1.00 30.88           S  
ATOM    826  CE  MET A 109       2.972   9.789  10.531  1.00 30.94           C  
ATOM    827  N   THR A 110       6.833   5.584  13.977  1.00 22.82           N  
ATOM    828  CA  THR A 110       6.769   4.154  14.259  1.00 25.63           C  
ATOM    829  C   THR A 110       5.875   3.850  15.457  1.00 26.49           C  
ATOM    830  O   THR A 110       5.111   2.853  15.376  1.00 26.61           O  
ATOM    831  CB  THR A 110       8.144   3.384  14.184  1.00 25.36           C  
ATOM    832  OG1 THR A 110       8.291   2.656  15.437  1.00 29.07           O  
ATOM    833  CG2 THR A 110       9.351   4.215  13.856  1.00 21.63           C  
ATOM    834  N   ASN A 111       5.837   4.707  16.450  1.00 28.28           N  
ATOM    835  CA  ASN A 111       4.940   4.588  17.601  1.00 30.53           C  
ATOM    836  C   ASN A 111       3.469   4.852  17.205  1.00 30.69           C  
ATOM    837  O   ASN A 111       2.599   4.502  18.001  1.00 32.60           O  
ATOM    838  CB  ASN A 111       5.300   5.496  18.770  1.00 32.34           C  
ATOM    839  CG  ASN A 111       6.627   5.169  19.390  1.00 35.66           C  
ATOM    840  OD1 ASN A 111       7.371   6.121  19.697  1.00 39.23           O  
ATOM    841  ND2 ASN A 111       6.950   3.892  19.564  1.00 35.15           N  
ATOM    842  N   LEU A 112       3.206   5.482  16.100  1.00 30.07           N  
ATOM    843  CA  LEU A 112       1.869   5.768  15.597  1.00 28.23           C  
ATOM    844  C   LEU A 112       1.402   4.617  14.716  1.00 26.61           C  
ATOM    845  O   LEU A 112       0.287   4.682  14.169  1.00 27.63           O  
ATOM    846  CB  LEU A 112       1.843   7.130  14.870  1.00 29.78           C  
ATOM    847  CG  LEU A 112       1.459   8.291  15.799  1.00 31.39           C  
ATOM    848  CD1 LEU A 112       2.153   8.111  17.162  1.00 31.44           C  
ATOM    849  CD2 LEU A 112       1.894   9.606  15.182  1.00 32.38           C  
ATOM    850  N   GLY A 113       2.279   3.639  14.579  1.00 24.50           N  
ATOM    851  CA  GLY A 113       2.030   2.437  13.838  1.00 22.55           C  
ATOM    852  C   GLY A 113       2.455   2.420  12.394  1.00 21.93           C  
ATOM    853  O   GLY A 113       2.029   1.497  11.659  1.00 19.26           O  
ATOM    854  N   GLU A 114       3.301   3.349  12.004  1.00 21.68           N  
ATOM    855  CA  GLU A 114       3.803   3.360  10.602  1.00 22.05           C  
ATOM    856  C   GLU A 114       5.316   3.253  10.567  1.00 21.37           C  
ATOM    857  O   GLU A 114       5.992   4.190  11.048  1.00 20.72           O  
ATOM    858  CB  GLU A 114       3.471   4.704   9.933  1.00 24.29           C  
ATOM    859  CG  GLU A 114       1.990   4.999   9.662  1.00 26.70           C  
ATOM    860  CD  GLU A 114       1.490   4.231   8.455  1.00 28.16           C  
ATOM    861  OE1 GLU A 114       2.243   3.901   7.537  1.00 27.63           O  
ATOM    862  OE2 GLU A 114       0.266   4.022   8.554  1.00 28.00           O  
ATOM    863  N   LYS A 115       5.819   2.198  10.003  1.00 21.64           N  
ATOM    864  CA  LYS A 115       7.297   1.989   9.843  1.00 21.12           C  
ATOM    865  C   LYS A 115       7.640   2.392   8.389  1.00 20.12           C  
ATOM    866  O   LYS A 115       7.323   1.806   7.330  1.00 17.54           O  
ATOM    867  CB  LYS A 115       7.655   0.590  10.229  1.00 24.33           C  
ATOM    868  CG  LYS A 115       6.880  -0.042  11.395  1.00 26.90           C  
ATOM    869  CD  LYS A 115       7.205  -1.574  11.425  1.00 28.99           C  
ATOM    870  CE  LYS A 115       8.688  -1.781  11.621  1.00 30.16           C  
ATOM    871  NZ  LYS A 115       9.183  -3.166  11.475  1.00 29.27           N  
ATOM    872  N   LEU A 116       8.214   3.568   8.342  1.00 20.01           N  
ATOM    873  CA  LEU A 116       8.649   4.371   7.195  1.00 18.57           C  
ATOM    874  C   LEU A 116      10.173   4.237   6.979  1.00 17.70           C  
ATOM    875  O   LEU A 116      10.887   4.254   7.980  1.00 14.86           O  
ATOM    876  CB  LEU A 116       8.394   5.839   7.587  1.00 19.68           C  
ATOM    877  CG  LEU A 116       7.142   6.533   7.122  1.00 25.82           C  
ATOM    878  CD1 LEU A 116       5.930   5.627   7.053  1.00 25.03           C  
ATOM    879  CD2 LEU A 116       6.918   7.725   8.064  1.00 26.27           C  
ATOM    880  N   THR A 117      10.588   4.172   5.720  1.00 15.15           N  
ATOM    881  CA  THR A 117      12.050   4.085   5.485  1.00 15.18           C  
ATOM    882  C   THR A 117      12.613   5.488   5.633  1.00 16.67           C  
ATOM    883  O   THR A 117      11.800   6.444   5.696  1.00 14.88           O  
ATOM    884  CB  THR A 117      12.279   3.454   4.071  1.00 11.17           C  
ATOM    885  OG1 THR A 117      11.945   4.535   3.187  1.00  9.01           O  
ATOM    886  CG2 THR A 117      11.452   2.199   3.748  1.00 12.22           C  
ATOM    887  N   ASP A 118      13.937   5.615   5.679  1.00 17.80           N  
ATOM    888  CA  ASP A 118      14.577   6.930   5.770  1.00 19.25           C  
ATOM    889  C   ASP A 118      14.152   7.792   4.553  1.00 18.91           C  
ATOM    890  O   ASP A 118      14.156   9.029   4.717  1.00 19.50           O  
ATOM    891  CB  ASP A 118      16.106   6.892   5.818  1.00 24.98           C  
ATOM    892  CG  ASP A 118      16.714   8.300   5.850  1.00 31.41           C  
ATOM    893  OD1 ASP A 118      17.645   8.602   5.075  1.00 33.11           O  
ATOM    894  OD2 ASP A 118      16.220   9.134   6.672  1.00 32.81           O  
ATOM    895  N   GLU A 119      13.882   7.231   3.427  1.00 16.60           N  
ATOM    896  CA  GLU A 119      13.527   7.937   2.234  1.00 18.40           C  
ATOM    897  C   GLU A 119      12.132   8.572   2.316  1.00 18.59           C  
ATOM    898  O   GLU A 119      11.947   9.673   1.795  1.00 17.05           O  
ATOM    899  CB  GLU A 119      13.502   7.056   0.971  1.00 23.48           C  
ATOM    900  CG  GLU A 119      12.795   7.627  -0.242  1.00 29.58           C  
ATOM    901  CD  GLU A 119      13.053   6.986  -1.570  1.00 35.87           C  
ATOM    902  OE1 GLU A 119      12.199   6.538  -2.331  1.00 38.86           O  
ATOM    903  OE2 GLU A 119      14.282   6.938  -1.795  1.00 40.04           O  
ATOM    904  N   GLU A 120      11.198   7.841   2.882  1.00 16.41           N  
ATOM    905  CA  GLU A 120       9.830   8.325   3.044  1.00 17.26           C  
ATOM    906  C   GLU A 120       9.779   9.426   4.065  1.00 19.11           C  
ATOM    907  O   GLU A 120       8.980  10.369   3.831  1.00 20.89           O  
ATOM    908  CB  GLU A 120       8.919   7.165   3.471  1.00 19.59           C  
ATOM    909  CG  GLU A 120       8.770   6.102   2.371  1.00 19.47           C  
ATOM    910  CD  GLU A 120       7.900   4.934   2.716  1.00 20.03           C  
ATOM    911  OE1 GLU A 120       7.073   4.563   1.922  1.00 20.71           O  
ATOM    912  OE2 GLU A 120       8.161   4.426   3.813  1.00 16.50           O  
ATOM    913  N   VAL A 121      10.607   9.403   5.076  1.00 18.54           N  
ATOM    914  CA  VAL A 121      10.669  10.437   6.135  1.00 20.31           C  
ATOM    915  C   VAL A 121      11.329  11.702   5.591  1.00 21.54           C  
ATOM    916  O   VAL A 121      10.965  12.841   5.882  1.00 21.38           O  
ATOM    917  CB  VAL A 121      11.374   9.875   7.373  1.00 20.70           C  
ATOM    918  CG1 VAL A 121      11.969  10.892   8.317  1.00 22.82           C  
ATOM    919  CG2 VAL A 121      10.479   8.888   8.164  1.00 18.50           C  
ATOM    920  N   ASP A 122      12.324  11.499   4.774  1.00 22.81           N  
ATOM    921  CA  ASP A 122      13.075  12.553   4.111  1.00 24.21           C  
ATOM    922  C   ASP A 122      12.095  13.418   3.289  1.00 23.64           C  
ATOM    923  O   ASP A 122      12.221  14.641   3.282  1.00 23.73           O  
ATOM    924  CB  ASP A 122      14.202  11.932   3.252  1.00 28.25           C  
ATOM    925  CG  ASP A 122      15.483  11.953   4.062  1.00 34.52           C  
ATOM    926  OD1 ASP A 122      15.713  12.936   4.802  1.00 37.73           O  
ATOM    927  OD2 ASP A 122      16.238  10.963   3.996  1.00 38.28           O  
ATOM    928  N   GLU A 123      11.213  12.764   2.582  1.00 22.51           N  
ATOM    929  CA  GLU A 123      10.207  13.343   1.730  1.00 23.95           C  
ATOM    930  C   GLU A 123       9.238  14.178   2.548  1.00 24.05           C  
ATOM    931  O   GLU A 123       8.807  15.229   2.003  1.00 24.49           O  
ATOM    932  CB  GLU A 123       9.406  12.350   0.924  1.00 26.77           C  
ATOM    933  CG  GLU A 123       8.497  12.917  -0.163  1.00 35.03           C  
ATOM    934  CD  GLU A 123       7.800  11.855  -0.967  1.00 38.38           C  
ATOM    935  OE1 GLU A 123       6.719  11.946  -1.511  1.00 41.33           O  
ATOM    936  OE2 GLU A 123       8.515  10.817  -0.980  1.00 42.45           O  
ATOM    937  N   MET A 124       8.926  13.751   3.733  1.00 23.42           N  
ATOM    938  CA  MET A 124       8.072  14.439   4.692  1.00 24.68           C  
ATOM    939  C   MET A 124       8.742  15.748   5.139  1.00 24.29           C  
ATOM    940  O   MET A 124       8.097  16.795   5.074  1.00 24.55           O  
ATOM    941  CB  MET A 124       7.685  13.598   5.922  1.00 24.69           C  
ATOM    942  CG  MET A 124       6.754  12.508   5.424  1.00 30.17           C  
ATOM    943  SD  MET A 124       6.342  11.427   6.855  1.00 32.88           S  
ATOM    944  CE  MET A 124       4.856  12.289   7.404  1.00 31.99           C  
ATOM    945  N   ILE A 125       9.961  15.655   5.595  1.00 24.86           N  
ATOM    946  CA  ILE A 125      10.750  16.847   5.993  1.00 26.18           C  
ATOM    947  C   ILE A 125      10.753  17.827   4.804  1.00 27.79           C  
ATOM    948  O   ILE A 125      10.240  18.936   4.902  1.00 28.15           O  
ATOM    949  CB  ILE A 125      12.150  16.370   6.445  1.00 25.69           C  
ATOM    950  CG1 ILE A 125      11.951  15.445   7.699  1.00 26.27           C  
ATOM    951  CG2 ILE A 125      13.202  17.455   6.777  1.00 24.29           C  
ATOM    952  CD1 ILE A 125      11.640  16.154   8.997  1.00 24.12           C  
ATOM    953  N   ARG A 126      11.273  17.412   3.660  1.00 27.56           N  
ATOM    954  CA  ARG A 126      11.371  18.236   2.471  1.00 28.83           C  
ATOM    955  C   ARG A 126      10.121  19.067   2.260  1.00 30.72           C  
ATOM    956  O   ARG A 126      10.175  20.298   2.190  1.00 30.64           O  
ATOM    957  CB  ARG A 126      11.710  17.433   1.195  1.00 26.95           C  
ATOM    958  CG  ARG A 126      13.208  17.047   1.232  1.00 28.29           C  
ATOM    959  CD  ARG A 126      13.658  16.644  -0.132  1.00 27.65           C  
ATOM    960  NE  ARG A 126      13.336  15.262  -0.470  1.00 28.99           N  
ATOM    961  CZ  ARG A 126      12.558  14.944  -1.484  1.00 27.26           C  
ATOM    962  NH1 ARG A 126      11.957  15.891  -2.175  1.00 31.36           N  
ATOM    963  NH2 ARG A 126      12.382  13.716  -1.893  1.00 28.50           N  
ATOM    964  N   GLU A 127       9.022  18.366   2.089  1.00 31.44           N  
ATOM    965  CA  GLU A 127       7.724  18.974   1.862  1.00 33.67           C  
ATOM    966  C   GLU A 127       7.427  20.133   2.806  1.00 34.39           C  
ATOM    967  O   GLU A 127       6.789  21.128   2.376  1.00 36.18           O  
ATOM    968  CB  GLU A 127       6.623  17.917   2.005  1.00 35.25           C  
ATOM    969  CG  GLU A 127       5.184  18.391   1.920  1.00 38.03           C  
ATOM    970  CD  GLU A 127       4.178  17.377   1.517  1.00 39.16           C  
ATOM    971  OE1 GLU A 127       2.973  17.550   1.630  1.00 42.84           O  
ATOM    972  OE2 GLU A 127       4.684  16.354   1.029  1.00 40.62           O  
ATOM    973  N   ALA A 128       7.847  20.078   4.051  1.00 32.57           N  
ATOM    974  CA  ALA A 128       7.571  21.118   5.020  1.00 31.61           C  
ATOM    975  C   ALA A 128       8.742  22.028   5.345  1.00 32.04           C  
ATOM    976  O   ALA A 128       8.500  23.007   6.087  1.00 34.08           O  
ATOM    977  CB  ALA A 128       7.100  20.462   6.330  1.00 30.58           C  
ATOM    978  N   ASN A 129       9.933  21.729   4.922  1.00 30.36           N  
ATOM    979  CA  ASN A 129      11.140  22.484   5.227  1.00 31.50           C  
ATOM    980  C   ASN A 129      11.310  23.710   4.327  1.00 33.93           C  
ATOM    981  O   ASN A 129      11.619  23.618   3.115  1.00 35.63           O  
ATOM    982  CB  ASN A 129      12.269  21.482   5.181  1.00 26.41           C  
ATOM    983  CG  ASN A 129      13.604  22.086   5.542  1.00 25.55           C  
ATOM    984  OD1 ASN A 129      13.666  23.014   6.366  1.00 27.52           O  
ATOM    985  ND2 ASN A 129      14.650  21.555   4.923  1.00 22.00           N  
ATOM    986  N   ILE A 130      11.083  24.868   4.910  1.00 35.18           N  
ATOM    987  CA  ILE A 130      11.162  26.175   4.220  1.00 35.52           C  
ATOM    988  C   ILE A 130      12.560  26.742   4.220  1.00 36.61           C  
ATOM    989  O   ILE A 130      13.161  26.910   3.146  1.00 37.62           O  
ATOM    990  CB  ILE A 130      10.081  27.118   4.843  1.00 34.65           C  
ATOM    991  CG1 ILE A 130       8.695  26.475   4.662  1.00 32.49           C  
ATOM    992  CG2 ILE A 130      10.102  28.572   4.276  1.00 35.48           C  
ATOM    993  CD1 ILE A 130       7.536  27.297   5.275  1.00 34.04           C  
ATOM    994  N   ASP A 131      13.143  26.994   5.374  1.00 37.83           N  
ATOM    995  CA  ASP A 131      14.490  27.585   5.494  1.00 38.66           C  
ATOM    996  C   ASP A 131      15.594  26.660   5.005  1.00 39.22           C  
ATOM    997  O   ASP A 131      16.789  27.007   5.137  1.00 40.58           O  
ATOM    998  CB  ASP A 131      14.704  28.096   6.923  1.00 39.48           C  
ATOM    999  CG  ASP A 131      14.959  26.954   7.889  1.00 39.54           C  
ATOM   1000  OD1 ASP A 131      15.078  27.133   9.112  1.00 40.55           O  
ATOM   1001  OD2 ASP A 131      15.096  25.841   7.343  1.00 39.55           O  
ATOM   1002  N   GLY A 132      15.246  25.509   4.492  1.00 38.31           N  
ATOM   1003  CA  GLY A 132      16.074  24.483   3.963  1.00 36.25           C  
ATOM   1004  C   GLY A 132      17.166  23.967   4.841  1.00 36.24           C  
ATOM   1005  O   GLY A 132      18.301  23.695   4.342  1.00 37.47           O  
ATOM   1006  N   ASP A 133      16.913  23.784   6.118  1.00 35.34           N  
ATOM   1007  CA  ASP A 133      17.961  23.224   7.010  1.00 34.73           C  
ATOM   1008  C   ASP A 133      17.785  21.710   7.061  1.00 34.91           C  
ATOM   1009  O   ASP A 133      18.650  21.089   7.709  1.00 36.08           O  
ATOM   1010  CB  ASP A 133      18.005  23.909   8.348  1.00 36.96           C  
ATOM   1011  CG  ASP A 133      16.755  23.757   9.211  1.00 39.16           C  
ATOM   1012  OD1 ASP A 133      16.821  24.148  10.404  1.00 39.27           O  
ATOM   1013  OD2 ASP A 133      15.730  23.258   8.690  1.00 37.53           O  
ATOM   1014  N   GLY A 134      16.780  21.133   6.419  1.00 33.04           N  
ATOM   1015  CA  GLY A 134      16.597  19.670   6.441  1.00 32.83           C  
ATOM   1016  C   GLY A 134      15.947  19.212   7.759  1.00 33.05           C  
ATOM   1017  O   GLY A 134      15.861  18.001   8.073  1.00 33.07           O  
ATOM   1018  N   GLN A 135      15.437  20.157   8.506  1.00 32.08           N  
ATOM   1019  CA  GLN A 135      14.802  20.011   9.811  1.00 31.24           C  
ATOM   1020  C   GLN A 135      13.467  20.752   9.846  1.00 31.25           C  
ATOM   1021  O   GLN A 135      13.288  21.657   9.023  1.00 30.82           O  
ATOM   1022  CB  GLN A 135      15.673  20.632  10.911  1.00 30.93           C  
ATOM   1023  CG  GLN A 135      16.314  19.613  11.782  1.00 34.94           C  
ATOM   1024  CD  GLN A 135      17.660  20.045  12.294  1.00 38.72           C  
ATOM   1025  OE1 GLN A 135      18.100  21.196  12.192  1.00 40.14           O  
ATOM   1026  NE2 GLN A 135      18.331  19.049  12.877  1.00 39.99           N  
ATOM   1027  N   VAL A 136      12.611  20.379  10.798  1.00 30.57           N  
ATOM   1028  CA  VAL A 136      11.302  21.075  10.853  1.00 31.00           C  
ATOM   1029  C   VAL A 136      11.269  21.767  12.199  1.00 31.45           C  
ATOM   1030  O   VAL A 136      11.462  21.126  13.259  1.00 31.50           O  
ATOM   1031  CB  VAL A 136      10.181  20.115  10.510  1.00 33.07           C  
ATOM   1032  CG1 VAL A 136      10.430  18.753  11.159  1.00 36.69           C  
ATOM   1033  CG2 VAL A 136       8.775  20.607  10.855  1.00 33.74           C  
ATOM   1034  N   ASN A 137      11.103  23.068  12.077  1.00 30.90           N  
ATOM   1035  CA  ASN A 137      11.008  23.901  13.320  1.00 30.91           C  
ATOM   1036  C   ASN A 137       9.526  24.179  13.558  1.00 29.60           C  
ATOM   1037  O   ASN A 137       8.658  23.803  12.742  1.00 28.20           O  
ATOM   1038  CB  ASN A 137      11.962  25.058  13.217  1.00 34.19           C  
ATOM   1039  CG  ASN A 137      11.584  26.158  12.248  1.00 33.42           C  
ATOM   1040  OD1 ASN A 137      12.470  27.027  12.073  1.00 36.95           O  
ATOM   1041  ND2 ASN A 137      10.399  26.183  11.663  1.00 32.72           N  
ATOM   1042  N   TYR A 138       9.269  24.804  14.689  1.00 30.34           N  
ATOM   1043  CA  TYR A 138       7.918  25.107  15.152  1.00 32.03           C  
ATOM   1044  C   TYR A 138       7.099  25.810  14.103  1.00 31.66           C  
ATOM   1045  O   TYR A 138       5.946  25.454  13.771  1.00 31.90           O  
ATOM   1046  CB  TYR A 138       7.924  25.850  16.530  1.00 35.12           C  
ATOM   1047  CG  TYR A 138       6.471  25.985  16.957  1.00 38.66           C  
ATOM   1048  CD1 TYR A 138       5.683  24.845  17.170  1.00 39.42           C  
ATOM   1049  CD2 TYR A 138       5.875  27.239  17.030  1.00 41.46           C  
ATOM   1050  CE1 TYR A 138       4.330  24.958  17.494  1.00 41.80           C  
ATOM   1051  CE2 TYR A 138       4.518  27.370  17.350  1.00 43.42           C  
ATOM   1052  CZ  TYR A 138       3.759  26.229  17.576  1.00 42.93           C  
ATOM   1053  OH  TYR A 138       2.440  26.412  17.876  1.00 44.56           O  
ATOM   1054  N   GLU A 139       7.721  26.830  13.545  1.00 32.34           N  
ATOM   1055  CA  GLU A 139       7.168  27.636  12.441  1.00 32.30           C  
ATOM   1056  C   GLU A 139       6.781  26.763  11.264  1.00 30.85           C  
ATOM   1057  O   GLU A 139       5.631  26.802  10.793  1.00 30.85           O  
ATOM   1058  CB  GLU A 139       8.211  28.645  11.965  1.00 34.81           C  
ATOM   1059  CG  GLU A 139       7.807  29.590  10.863  1.00 36.98           C  
ATOM   1060  CD  GLU A 139       8.549  30.924  10.853  1.00 37.77           C  
ATOM   1061  OE1 GLU A 139       8.326  31.646   9.903  1.00 37.85           O  
ATOM   1062  OE2 GLU A 139       9.325  31.166  11.800  1.00 34.45           O  
ATOM   1063  N   GLU A 140       7.732  25.965  10.767  1.00 30.72           N  
ATOM   1064  CA  GLU A 140       7.390  25.044   9.626  1.00 29.98           C  
ATOM   1065  C   GLU A 140       6.327  24.057  10.076  1.00 29.01           C  
ATOM   1066  O   GLU A 140       5.337  23.789   9.351  1.00 28.53           O  
ATOM   1067  CB  GLU A 140       8.647  24.350   9.129  1.00 30.25           C  
ATOM   1068  CG  GLU A 140       9.780  25.306   8.658  1.00 32.90           C  
ATOM   1069  CD  GLU A 140      11.126  24.668   8.574  1.00 33.83           C  
ATOM   1070  OE1 GLU A 140      11.416  23.758   9.341  1.00 36.56           O  
ATOM   1071  OE2 GLU A 140      11.900  25.077   7.693  1.00 31.41           O  
ATOM   1072  N   PHE A 141       6.443  23.555  11.293  1.00 28.49           N  
ATOM   1073  CA  PHE A 141       5.474  22.608  11.866  1.00 30.40           C  
ATOM   1074  C   PHE A 141       4.031  23.091  11.859  1.00 31.15           C  
ATOM   1075  O   PHE A 141       3.147  22.324  11.377  1.00 30.73           O  
ATOM   1076  CB  PHE A 141       5.919  22.132  13.251  1.00 31.29           C  
ATOM   1077  CG  PHE A 141       5.079  21.047  13.866  1.00 32.83           C  
ATOM   1078  CD1 PHE A 141       4.063  21.364  14.756  1.00 33.90           C  
ATOM   1079  CD2 PHE A 141       5.330  19.697  13.583  1.00 32.92           C  
ATOM   1080  CE1 PHE A 141       3.286  20.381  15.357  1.00 33.07           C  
ATOM   1081  CE2 PHE A 141       4.570  18.703  14.186  1.00 33.47           C  
ATOM   1082  CZ  PHE A 141       3.529  19.046  15.063  1.00 31.84           C  
ATOM   1083  N   VAL A 142       3.753  24.276  12.352  1.00 34.10           N  
ATOM   1084  CA  VAL A 142       2.377  24.816  12.411  1.00 37.11           C  
ATOM   1085  C   VAL A 142       1.749  25.007  11.021  1.00 39.75           C  
ATOM   1086  O   VAL A 142       0.534  24.773  10.807  1.00 38.37           O  
ATOM   1087  CB  VAL A 142       2.259  26.081  13.260  1.00 38.73           C  
ATOM   1088  CG1 VAL A 142       3.437  26.416  14.159  1.00 39.30           C  
ATOM   1089  CG2 VAL A 142       1.892  27.286  12.399  1.00 39.11           C  
ATOM   1090  N   GLN A 143       2.568  25.454  10.082  1.00 42.88           N  
ATOM   1091  CA  GLN A 143       2.121  25.667   8.701  1.00 46.79           C  
ATOM   1092  C   GLN A 143       1.809  24.291   8.085  1.00 49.07           C  
ATOM   1093  O   GLN A 143       1.026  24.216   7.123  1.00 49.22           O  
ATOM   1094  CB  GLN A 143       3.125  26.375   7.801  1.00 48.54           C  
ATOM   1095  CG  GLN A 143       4.220  27.124   8.530  1.00 50.96           C  
ATOM   1096  CD  GLN A 143       4.528  28.429   7.811  1.00 53.63           C  
ATOM   1097  OE1 GLN A 143       3.800  28.781   6.881  1.00 54.98           O  
ATOM   1098  NE2 GLN A 143       5.586  29.107   8.245  1.00 54.98           N  
ATOM   1099  N   MET A 144       2.489  23.288   8.659  1.00 50.98           N  
ATOM   1100  CA  MET A 144       2.294  21.909   8.132  1.00 53.05           C  
ATOM   1101  C   MET A 144       1.047  21.289   8.743  1.00 54.18           C  
ATOM   1102  O   MET A 144       0.302  20.566   8.062  1.00 53.97           O  
ATOM   1103  CB  MET A 144       3.548  21.109   8.261  1.00 53.03           C  
ATOM   1104  CG  MET A 144       3.719  19.975   7.335  1.00 55.70           C  
ATOM   1105  SD  MET A 144       3.101  20.167   5.659  1.00 58.32           S  
ATOM   1106  CE  MET A 144       3.990  21.574   5.021  1.00 56.18           C  
ATOM   1107  N   MET A 145       0.826  21.586  10.009  1.00 56.06           N  
ATOM   1108  CA  MET A 145      -0.327  21.086  10.763  1.00 58.00           C  
ATOM   1109  C   MET A 145      -1.631  21.706  10.261  1.00 59.46           C  
ATOM   1110  O   MET A 145      -2.500  21.028   9.684  1.00 60.43           O  
ATOM   1111  CB  MET A 145      -0.166  21.301  12.268  1.00 58.36           C  
ATOM   1112  CG  MET A 145      -0.138  19.941  12.947  1.00 60.17           C  
ATOM   1113  SD  MET A 145       1.527  19.227  12.659  1.00 63.04           S  
ATOM   1114  CE  MET A 145       1.033  17.605  12.029  1.00 62.20           C  
ATOM   1115  N   THR A 146      -1.729  22.987  10.497  1.00 60.38           N  
ATOM   1116  CA  THR A 146      -2.833  23.864  10.177  1.00 61.37           C  
ATOM   1117  C   THR A 146      -3.048  24.133   8.701  1.00 61.74           C  
ATOM   1118  O   THR A 146      -4.185  24.037   8.210  1.00 62.27           O  
ATOM   1119  CB  THR A 146      -2.579  25.269  10.896  1.00 61.80           C  
ATOM   1120  OG1 THR A 146      -1.616  25.931  10.004  1.00 62.48           O  
ATOM   1121  CG2 THR A 146      -2.099  25.108  12.328  1.00 61.07           C  
ATOM   1122  N   ALA A 147      -1.985  24.535   8.027  1.00 62.07           N  
ATOM   1123  CA  ALA A 147      -2.095  24.829   6.582  1.00 62.41           C  
ATOM   1124  C   ALA A 147      -1.250  23.827   5.799  1.00 62.64           C  
ATOM   1125  O   ALA A 147      -1.938  22.966   5.190  1.00 63.20           O  
ATOM   1126  CB  ALA A 147      -1.738  26.270   6.293  1.00 63.07           C  
TER    1127      ALA A 147                                                      
HETATM 1128 CA    CA A 149     -13.638  53.352  31.500  1.00 12.29          CA  
HETATM 1129 CA    CA A 150     -17.797  50.156  20.859  1.00 15.64          CA  
HETATM 1130 CA    CA A 151      15.035  17.711  17.954  1.00 28.17          CA  
HETATM 1131 CA    CA A 152      13.784  23.887   8.345  1.00 29.20          CA  
HETATM 1132  O   HOH A 153     -13.778  55.464  30.321  1.21 24.05           O  
HETATM 1133  O   HOH A 154     -19.894  49.838  21.919  0.81 17.79           O  
HETATM 1134  O   HOH A 155      16.666  16.967  17.051  0.91 41.58           O  
HETATM 1135  O   HOH A 156      14.421  24.967  10.651  0.91 28.87           O  
HETATM 1136  O   HOH A 157     -11.041  31.091  36.589  0.77 47.13           O  
HETATM 1137  O   HOH A 158     -12.366  35.525  41.927  0.82 45.23           O  
HETATM 1138  O   HOH A 159     -17.093  56.520  27.305  1.20 14.68           O  
HETATM 1139  O   HOH A 160     -23.350  49.504  31.087  0.60 30.25           O  
HETATM 1140  O   HOH A 161       0.573  52.219  34.162  0.46 30.16           O  
HETATM 1141  O   HOH A 162     -19.465  45.348  13.131  0.77 40.01           O  
HETATM 1142  O   HOH A 163      -7.045  44.227  20.122  0.63 41.06           O  
HETATM 1143  O   HOH A 164      -2.950  31.829  19.122  0.77 37.43           O  
HETATM 1144  O   HOH A 165       6.128  29.697  25.535  1.10 48.36           O  
HETATM 1145  O   HOH A 166      16.987   9.497  18.405  0.96 42.10           O  
HETATM 1146  O   HOH A 167      16.396  13.372  19.463  0.86 30.10           O  
HETATM 1147  O   HOH A 168      16.327   0.928  11.822  0.67 28.85           O  
HETATM 1148  O   HOH A 169      -0.714   5.840   6.211  0.62 45.21           O  
HETATM 1149  O   HOH A 170       8.092   1.518   4.876  0.64 21.16           O  
HETATM 1150  O   HOH A 171      11.166  -1.160   2.784  0.47 33.99           O  
HETATM 1151  O   HOH A 172       5.722   1.937   1.824  0.42 25.50           O  
HETATM 1152  O   HOH A 173       0.627  17.269   0.901  0.49 41.85           O  
HETATM 1153  O   HOH A 174      13.812  24.259   1.011  0.89 36.14           O  
HETATM 1154  O   HOH A 175     -15.922  58.274  31.632  0.88 28.58           O  
HETATM 1155  O   HOH A 176       8.938  51.956  25.567  0.46 38.91           O  
HETATM 1156  O   HOH A 177     -21.975  39.385  37.146  0.65 44.78           O  
HETATM 1157  O   HOH A 178     -10.076  48.872  37.565  0.75 17.37           O  
HETATM 1158  O   HOH A 179     -20.835  55.472  35.127  0.50 30.55           O  
HETATM 1159  O   HOH A 180     -18.023  55.742  24.938  0.80 12.20           O  
HETATM 1160  O   HOH A 181      15.885  -2.513  14.053  0.49 45.89           O  
HETATM 1161  O   HOH A 182       8.855  -1.406   6.966  0.59 19.85           O  
HETATM 1162  O   HOH A 183     -23.904  51.047  20.170  1.25 12.46           O  
HETATM 1163  O   HOH A 184       9.042  34.751  11.243  0.88 31.45           O  
HETATM 1164  O   HOH A 185      15.137  27.759  13.785  0.72 34.64           O  
HETATM 1165  O   HOH A 186      -2.849   5.607  15.419  0.54 34.36           O  
HETATM 1166  O   HOH A 187       3.549   0.244   9.732  0.71 21.28           O  
HETATM 1167  O   HOH A 188      14.541   6.336  14.185  0.76 27.11           O  
HETATM 1168  O   HOH A 189      11.002   2.826  10.145  0.47 29.41           O  
HETATM 1169  O   HOH A 190     -11.331  55.945  19.770  0.89 29.27           O  
HETATM 1170  O   HOH A 191     -11.065  55.126  23.155  0.76 23.14           O  
HETATM 1171  O   HOH A 192     -15.835  42.898  19.625  0.92 26.67           O  
HETATM 1172  O   HOH A 193     -13.260  45.967  13.864  0.82 29.59           O  
HETATM 1173  O   HOH A 194       4.129  49.311  15.900  0.67 28.94           O  
HETATM 1174  O   HOH A 195       8.645  50.861  28.099  0.72 24.58           O  
HETATM 1175  O   HOH A 196      -2.424  56.273  26.868  0.52 25.18           O  
HETATM 1176  O   HOH A 197       9.762  47.482  29.169  0.93 16.02           O  
HETATM 1177  O   HOH A 198     -28.354  35.633  40.152  0.65 31.63           O  
HETATM 1178  O   HOH A 199     -21.933  52.628  32.415  0.77 28.77           O  
HETATM 1179  O   HOH A 200      11.746   0.231   0.587  0.53 38.97           O  
HETATM 1180  O   HOH A 201       8.687   4.188  -0.266  0.50 42.82           O  
HETATM 1181  O   HOH A 202       9.836  -1.594   0.025  0.79 36.31           O  
HETATM 1182  O   HOH A 203      -3.602  19.501   3.085  0.95 32.22           O  
HETATM 1183  O   HOH A 204     -17.887  28.277  27.371  0.64 34.37           O  
HETATM 1184  O   HOH A 205     -16.207  25.116  26.904  0.71 31.90           O  
HETATM 1185  O   HOH A 206     -22.499  43.524  34.136  0.69 32.05           O  
HETATM 1186  O   HOH A 207     -14.314  48.906  37.516  0.79 28.82           O  
HETATM 1187  O   HOH A 208      -3.214  48.771  35.576  0.82 24.44           O  
HETATM 1188  O   HOH A 209     -13.136  53.920  39.325  0.77 32.38           O  
HETATM 1189  O   HOH A 210      -9.152  53.432  39.194  0.77 30.58           O  
HETATM 1190  O   HOH A 211       2.326  54.639  26.681  0.68 24.92           O  
HETATM 1191  O   HOH A 212       8.090  55.249  28.619  0.86 30.56           O  
HETATM 1192  O   HOH A 213       5.578  55.794  23.736  0.62 31.51           O  
HETATM 1193  O   HOH A 214     -13.301  51.692  14.740  0.65 33.85           O  
HETATM 1194  O   HOH A 215     -14.444  40.388  17.611  0.75 27.38           O  
HETATM 1195  O   HOH A 216       0.604  29.279  29.056  0.55 34.07           O  
HETATM 1196  O   HOH A 217      11.022  18.208  24.091  0.78 26.48           O  
HETATM 1197  O   HOH A 218      14.949   8.685   9.236  0.72 25.08           O  
HETATM 1198  O   HOH A 219       5.100   0.329  14.277  0.65 23.97           O  
HETATM 1199  O   HOH A 220      16.164   5.422  -2.253  0.79 30.34           O  
HETATM 1200  O   HOH A 221      -5.039  20.754  10.530  0.71 28.82           O  
CONECT  134 1128                                                                
CONECT  150 1128                                                                
CONECT  163 1128                                                                
CONECT  171 1128                                                                
CONECT  213 1128                                                                
CONECT  214 1128                                                                
CONECT  404 1129                                                                
CONECT  417 1129                                                                
CONECT  428 1129                                                                
CONECT  437 1129                                                                
CONECT  482 1129                                                                
CONECT  483 1129                                                                
CONECT  704 1130                                                                
CONECT  721 1130                                                                
CONECT  732 1130                                                                
CONECT  741 1130                                                                
CONECT  781 1130                                                                
CONECT  782 1130                                                                
CONECT  984 1131                                                                
CONECT 1001 1131                                                                
CONECT 1013 1131                                                                
CONECT 1021 1131                                                                
CONECT 1070 1131                                                                
CONECT 1071 1131                                                                
CONECT 1128  134  150  163  171                                                 
CONECT 1128  213  214 1132                                                      
CONECT 1129  404  417  428  437                                                 
CONECT 1129  482  483 1133                                                      
CONECT 1130  704  721  732  741                                                 
CONECT 1130  781  782 1134                                                      
CONECT 1131  984 1001 1013 1021                                                 
CONECT 1131 1070 1071 1135                                                      
CONECT 1132 1128                                                                
CONECT 1133 1129                                                                
CONECT 1134 1130                                                                
CONECT 1135 1131                                                                
MASTER      371    0    4    7    4    0   20    6 1199    1   36   12          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.