CNRS Nantes University UFIP UFIP
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***  Calmodulin  ***

elNémo ID: 20020322283218832

Job options:

ID        	=	 20020322283218832
JOBID     	=	 Calmodulin
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 Calmodulin
HEADER    CALCIUM-BINDING PROTEIN                 29-SEP-92   1CLL              
TITLE     CALMODULIN STRUCTURE REFINED AT 1.7 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: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606                                                 
KEYWDS    CALCIUM-BINDING PROTEIN                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.CHATTOPADHYAYA,F.A.QUIOCHO                                          
REVDAT   3   24-FEB-09 1CLL    1       VERSN                                    
REVDAT   2   01-APR-03 1CLL    1       JRNL                                     
REVDAT   1   31-OCT-93 1CLL    0                                                
JRNL        AUTH   R.CHATTOPADHYAYA,W.E.MEADOR,A.R.MEANS,F.A.QUIOCHO            
JRNL        TITL   CALMODULIN STRUCTURE REFINED AT 1.7 A RESOLUTION.            
JRNL        REF    J.MOL.BIOL.                   V. 228  1177 1992              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   1474585                                                      
JRNL        DOI    10.1016/0022-2836(92)90324-D                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.E.MEADOR,A.R.MEANS,F.A.QUIOCHO                             
REMARK   1  TITL   TARGET ENZYME RECOGNITION BY CALMODULIN: 2.4                 
REMARK   1  TITL 2 ANGSTROMS STRUCTURE OF A CALMODULIN-PEPTIDE COMPLEX          
REMARK   1  REF    SCIENCE                       V. 257  1251 1992              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.S.BABU,C.E.BUGG,W.J.COOK                                   
REMARK   1  TITL   STRUCTURE OF CALMODULIN REFINED AT 2.2 ANGSTROMS             
REMARK   1  TITL 2 RESOLUTION                                                   
REMARK   1  REF    J.MOL.BIOL.                   V. 204   191 1988              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.500                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 14469                          
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) : 0.216                           
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            : 1133                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 142                                     
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) : 0.009 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.032 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.040 ; 0.060               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.007 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.152 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.199 ; 0.500               
REMARK   3    MULTIPLE TORSION                (A) : 0.304 ; 0.500               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : 0.281 ; 0.500               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 1.600 ; 3.000               
REMARK   3    STAGGERED                 (DEGREES) : 21.400; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 2.000 ; 4.000               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 2.500 ; 5.000               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 3.000 ; 5.000               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 4.200 ; 6.000               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:  CRYSTAL PACKING IS EXTENSIVELY           
REMARK   3  STUDIED IN THE CHATTOPADHYAYA ET AL. PAPER ON CALMODULIN, AND       
REMARK   3  FACILE CRYSTAL GROWTH ALONG THE Z-DIRECTION EXPLAINED. THE          
REMARK   3  AUTHORS ALSO HAVE REPORTED IN DETAIL ABOUT THE HYDROGEN             
REMARK   3  BONDING WITHIN VARIOUS STRUCTURAL ELEMENTS IN THAT                  
REMARK   3  PUBLICATION. HYDRATION IS ALSO DESCRIBED. THESE ARE AREAS           
REMARK   3  WHICH WERE NOT DEALT WITH IN THE BABU ET AL. (1988)                 
REMARK   3  PUBLICATION.                                                        
REMARK   4                                                                      
REMARK   4 1CLL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
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: MERLOT                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
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 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     LYS A   148                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU A   4    CB   CG   CD1  CD2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   203     O    HOH A   205              2.04            
REMARK 500   OE1  GLU A   139     O    HOH A   234              2.05            
REMARK 500   OE2  GLU A    82     NH1  ARG A    86              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   220     O    HOH A   265     1644     1.94            
REMARK 500   OD2  ASP A    22     OD2  ASP A   118     1466     2.12            
REMARK 500   O    GLY A    40     O    HOH A   250     1655     2.13            
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  20   CB  -  CG  -  OD1 ANGL. DEV. =  -8.2 DEGREES          
REMARK 500    ASP A  24   CB  -  CG  -  OD1 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ASP A  24   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    THR A  28   N   -  CA  -  CB  ANGL. DEV. = -17.6 DEGREES          
REMARK 500    THR A  28   OG1 -  CB  -  CG2 ANGL. DEV. =  20.0 DEGREES          
REMARK 500    GLU A  31   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    ASP A  50   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ASP A  58   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A  90   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG A  90   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ARG A 106   CD  -  NE  -  CZ  ANGL. DEV. =  31.6 DEGREES          
REMARK 500    ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 158        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH A 178        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH A 202        DISTANCE =  5.53 ANGSTROMS                       
REMARK 525    HOH A 206        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH A 226        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH A 257        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH A 262        DISTANCE =  7.60 ANGSTROMS                       
REMARK 525    HOH A 274        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH A 279        DISTANCE = 10.12 ANGSTROMS                       
REMARK 525    HOH A 280        DISTANCE = 13.07 ANGSTROMS                       
REMARK 525    HOH A 281        DISTANCE = 10.20 ANGSTROMS                       
REMARK 525    HOH A 282        DISTANCE = 11.49 ANGSTROMS                       
REMARK 525    HOH A 283        DISTANCE =  6.74 ANGSTROMS                       
REMARK 525    HOH A 284        DISTANCE =  7.62 ANGSTROMS                       
REMARK 525    HOH A 285        DISTANCE =  9.04 ANGSTROMS                       
REMARK 525    HOH A 286        DISTANCE =  6.89 ANGSTROMS                       
REMARK 525    HOH A 287        DISTANCE =  6.98 ANGSTROMS                       
REMARK 525    HOH A 291        DISTANCE =  6.62 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     EOH A  153                                                       
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   OD1  85.4                                              
REMARK 620 3 ASP A  22   OD1 161.0  83.9                                        
REMARK 620 4 ASP A  24   OD1  84.1  90.5  80.4                                  
REMARK 620 5 HOH A 181   O   103.5 166.8  84.8  80.8                            
REMARK 620 6 GLU A  31   OE1  75.5 107.9 122.8 150.9  84.1                      
REMARK 620 7 GLU A  31   OE2 124.2  94.6  72.3 151.5  88.5  51.5                
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 240   O                                                      
REMARK 620 2 GLU A  67   OE1  89.5                                              
REMARK 620 3 GLU A  67   OE2  85.7  52.3                                        
REMARK 620 4 ASP A  56   OD1 164.2  99.3  89.4                                  
REMARK 620 5 ASP A  58   OD1  83.9 126.5  74.2  80.3                            
REMARK 620 6 ASN A  60   OD1  81.3 154.5 148.8  95.5  76.4                      
REMARK 620 7 THR A  62   O   102.7  79.1 130.9  91.9 154.0  79.8                
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 GLU A 104   OE1                                                    
REMARK 620 2 ASP A  93   OD1  99.6                                              
REMARK 620 3 ASP A  95   OD1 129.3  84.8                                        
REMARK 620 4 GLU A 104   OE2  51.5  97.5  77.8                                  
REMARK 620 5 ASN A  97   OD1 157.4  95.7  68.4 142.3                            
REMARK 620 6 HOH A 188   O    89.7 167.2  82.5  81.3  78.2                      
REMARK 620 7 TYR A  99   O    82.0  95.6 148.3 133.1  80.0  94.5                
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   OD1                                                    
REMARK 620 2 GLN A 135   O    85.1                                              
REMARK 620 3 GLU A 140   OE1 148.7  78.8                                        
REMARK 620 4 HOH A 233   O    74.8  95.9  80.2                                  
REMARK 620 5 ASP A 131   OD1  73.8 157.6 123.4  85.9                            
REMARK 620 6 GLU A 140   OE2 153.0 121.9  49.8  99.3  79.5                      
REMARK 620 7 ASP A 129   OD1  95.1  91.4 111.9 166.9  83.2  85.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE ANTI-PARALLEL BETA SHEETS ARE EXTREMELY SHORT IN THIS            
REMARK 700 STRUCTURE.  THERE IS ADDITIONAL CONNECTIVITY VIA WATERS              
REMARK 700 BETWEEN THE TWO STRANDS OF EACH SHEET.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 149                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 150                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 151                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 152                  
DBREF  1CLL A    1   148  UNP    P62158   CALM_HUMAN       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 ASP 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                                                       
HET    EOH  A 153       3                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     EOH ETHANOL                                                          
FORMUL   2   CA    4(CA 2+)                                                     
FORMUL   6  EOH    C2 H6 O                                                      
FORMUL   7  HOH   *139(H2 O)                                                    
HELIX    1   I THR A    5  PHE A   19  1                                  15    
HELIX    2  II THR A   29  ARG A   37  1                                   9    
HELIX    3 III GLU A   45  VAL A   55  1                                  11    
HELIX    4  IV PHE A   65  PHE A   92  1SEE REMARK 6                      28    
HELIX    5   V ALA A  102  ASN A  111  1                                  10    
HELIX    6  VI ASP A  118  ALA A  128  1                                  11    
HELIX    7 VII TYR A  138  THR A  146  1                                   9    
SHEET    1  S1 2 ILE A  27  THR A  29  0                                        
SHEET    2  S1 2 ILE A  63  PHE A  65 -1  N  ILE A  63   O  ILE A  27           
SHEET    1  S2 2 ILE A 100  ALA A 102  0                                        
SHEET    2  S2 2 VAL A 136  TYR A 138 -1  N  VAL A 136   O  ILE A 100           
LINK        CA    CA A 149                 O   THR A  26     1555   1555  2.35  
LINK        CA    CA A 149                 OD1 ASP A  20     1555   1555  2.42  
LINK        CA    CA A 149                 OD1 ASP A  22     1555   1555  2.50  
LINK        CA    CA A 149                 OD1 ASP A  24     1555   1555  2.39  
LINK        CA    CA A 149                 O   HOH A 181     1555   1555  2.62  
LINK        CA    CA A 149                 OE1 GLU A  31     1555   1555  2.43  
LINK        CA    CA A 149                 OE2 GLU A  31     1555   1555  2.38  
LINK        CA    CA A 150                 O   HOH A 240     1555   1555  2.30  
LINK        CA    CA A 150                 OE1 GLU A  67     1555   1555  2.55  
LINK        CA    CA A 150                 OE2 GLU A  67     1555   1555  2.40  
LINK        CA    CA A 150                 OD1 ASP A  56     1555   1555  2.13  
LINK        CA    CA A 150                 OD1 ASP A  58     1555   1555  2.30  
LINK        CA    CA A 150                 OD1 ASN A  60     1555   1555  2.38  
LINK        CA    CA A 150                 O   THR A  62     1555   1555  2.29  
LINK        CA    CA A 151                 OE1 GLU A 104     1555   1555  2.44  
LINK        CA    CA A 151                 OD1 ASP A  93     1555   1555  2.23  
LINK        CA    CA A 151                 OD1 ASP A  95     1555   1555  2.53  
LINK        CA    CA A 151                 OE2 GLU A 104     1555   1555  2.60  
LINK        CA    CA A 151                 OD1 ASN A  97     1555   1555  2.35  
LINK        CA    CA A 151                 O   HOH A 188     1555   1555  2.60  
LINK        CA    CA A 151                 O   TYR A  99     1555   1555  2.20  
LINK        CA    CA A 152                 OD1 ASP A 133     1555   1555  2.30  
LINK        CA    CA A 152                 O   GLN A 135     1555   1555  2.30  
LINK        CA    CA A 152                 OE1 GLU A 140     1555   1555  2.57  
LINK        CA    CA A 152                 O   HOH A 233     1555   1555  2.63  
LINK        CA    CA A 152                 OD1 ASP A 131     1555   1555  2.45  
LINK        CA    CA A 152                 OE2 GLU A 140     1555   1555  2.55  
LINK        CA    CA A 152                 OD1 ASP A 129     1555   1555  2.31  
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 181                                          
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 240                                          
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 188                                          
SITE     1 AC4  6 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC4  6 GLU A 140  HOH A 233                                          
CRYST1   30.170   53.600   25.140  93.62  97.30  89.17 P 1           1          
ORIGX1      0.033146 -0.000480  0.004224        0.00000                         
ORIGX2      0.000000  0.018659  0.001155        0.00000                         
ORIGX3      0.000000  0.000000  0.040179        0.00000                         
SCALE1      0.033146 -0.000480  0.004224        0.00000                         
SCALE2      0.000000  0.018659  0.001155        0.00000                         
SCALE3      0.000000  0.000000  0.040179        0.00000                         
ATOM      1  N   LEU A   4      -6.873  21.082  25.312  1.00 49.53           N  
ATOM      2  CA  LEU A   4      -6.696  22.003  26.447  1.00 48.82           C  
ATOM      3  C   LEU A   4      -6.318  23.391  25.929  1.00 46.50           C  
ATOM      4  O   LEU A   4      -5.313  23.981  26.352  1.00 45.72           O  
ATOM      5  N   THR A   5      -7.147  23.871  25.013  1.00 46.77           N  
ATOM      6  CA  THR A   5      -6.891  25.193  24.428  1.00 46.84           C  
ATOM      7  C   THR A   5      -6.801  26.228  25.543  1.00 45.36           C  
ATOM      8  O   THR A   5      -5.829  26.999  25.561  1.00 47.41           O  
ATOM      9  CB  THR A   5      -7.923  25.626  23.323  1.00 46.33           C  
ATOM     10  OG1 THR A   5      -9.238  25.386  23.908  1.00 48.28           O  
ATOM     11  CG2 THR A   5      -7.704  24.943  21.974  1.00 44.31           C  
ATOM     12  N   GLU A   6      -7.781  26.217  26.419  1.00 46.42           N  
ATOM     13  CA  GLU A   6      -7.858  27.154  27.557  1.00 45.65           C  
ATOM     14  C   GLU A   6      -6.502  27.343  28.224  1.00 44.22           C  
ATOM     15  O   GLU A   6      -6.040  28.483  28.423  1.00 42.97           O  
ATOM     16  CB  GLU A   6      -8.881  26.726  28.592  1.00 50.13           C  
ATOM     17  CG  GLU A   6      -9.358  27.699  29.657  1.00 55.79           C  
ATOM     18  CD  GLU A   6     -10.322  27.149  30.668  1.00 58.96           C  
ATOM     19  OE1 GLU A   6     -10.775  26.034  30.334  1.00 62.89           O  
ATOM     20  OE2 GLU A   6     -10.648  27.701  31.706  1.00 60.58           O  
ATOM     21  N   GLU A   7      -5.878  26.224  28.555  1.00 41.38           N  
ATOM     22  CA  GLU A   7      -4.554  26.201  29.194  1.00 39.78           C  
ATOM     23  C   GLU A   7      -3.488  26.654  28.194  1.00 36.82           C  
ATOM     24  O   GLU A   7      -2.492  27.284  28.575  1.00 35.19           O  
ATOM     25  CB  GLU A   7      -4.220  24.818  29.707  1.00 41.74           C  
ATOM     26  CG  GLU A   7      -2.859  24.477  30.277  1.00 45.41           C  
ATOM     27  CD  GLU A   7      -2.755  23.096  30.867  1.00 47.19           C  
ATOM     28  OE1 GLU A   7      -3.096  22.069  30.304  1.00 45.58           O  
ATOM     29  OE2 GLU A   7      -2.284  23.115  32.029  1.00 49.85           O  
ATOM     30  N   GLN A   8      -3.742  26.335  26.934  1.00 34.23           N  
ATOM     31  CA  GLN A   8      -2.874  26.663  25.797  1.00 32.23           C  
ATOM     32  C   GLN A   8      -2.838  28.187  25.588  1.00 33.49           C  
ATOM     33  O   GLN A   8      -1.732  28.749  25.518  1.00 32.07           O  
ATOM     34  CB  GLN A   8      -3.273  25.955  24.510  1.00 30.73           C  
ATOM     35  CG  GLN A   8      -2.731  24.544  24.361  1.00 29.84           C  
ATOM     36  CD  GLN A   8      -2.980  23.970  22.985  1.00 28.64           C  
ATOM     37  OE1 GLN A   8      -4.082  23.858  22.452  1.00 29.29           O  
ATOM     38  NE2 GLN A   8      -1.893  23.581  22.335  1.00 26.48           N  
ATOM     39  N   ILE A   9      -4.017  28.772  25.488  1.00 32.05           N  
ATOM     40  CA  ILE A   9      -4.118  30.226  25.284  1.00 35.87           C  
ATOM     41  C   ILE A   9      -3.405  30.916  26.444  1.00 33.10           C  
ATOM     42  O   ILE A   9      -2.686  31.909  26.240  1.00 32.76           O  
ATOM     43  CB  ILE A   9      -5.569  30.720  25.011  1.00 38.25           C  
ATOM     44  CG1 ILE A   9      -6.249  31.153  26.340  1.00 42.51           C  
ATOM     45  CG2 ILE A   9      -6.441  29.697  24.231  1.00 38.25           C  
ATOM     46  CD1 ILE A   9      -7.719  31.624  26.165  1.00 46.23           C  
ATOM     47  N   ALA A  10      -3.568  30.386  27.641  1.00 32.29           N  
ATOM     48  CA  ALA A  10      -2.933  30.933  28.846  1.00 29.35           C  
ATOM     49  C   ALA A  10      -1.427  31.094  28.677  1.00 29.52           C  
ATOM     50  O   ALA A  10      -0.849  32.120  29.060  1.00 29.04           O  
ATOM     51  CB  ALA A  10      -3.281  30.070  30.058  1.00 32.99           C  
ATOM     52  N   GLU A  11      -0.787  30.084  28.107  1.00 30.70           N  
ATOM     53  CA  GLU A  11       0.670  30.102  27.900  1.00 31.69           C  
ATOM     54  C   GLU A  11       1.098  31.116  26.852  1.00 29.24           C  
ATOM     55  O   GLU A  11       2.183  31.704  26.957  1.00 32.68           O  
ATOM     56  CB  GLU A  11       1.191  28.718  27.487  1.00 37.43           C  
ATOM     57  CG  GLU A  11       0.859  27.630  28.520  1.00 40.07           C  
ATOM     58  CD  GLU A  11       1.277  26.245  28.139  1.00 42.15           C  
ATOM     59  OE1 GLU A  11       2.451  26.028  28.517  1.00 48.12           O  
ATOM     60  OE2 GLU A  11       0.584  25.440  27.547  1.00 44.80           O  
ATOM     61  N   PHE A  12       0.223  31.283  25.879  1.00 28.97           N  
ATOM     62  CA  PHE A  12       0.462  32.236  24.777  1.00 26.93           C  
ATOM     63  C   PHE A  12       0.271  33.672  25.299  1.00 24.14           C  
ATOM     64  O   PHE A  12       1.002  34.532  24.826  1.00 26.06           O  
ATOM     65  CB  PHE A  12      -0.393  31.969  23.550  1.00 28.76           C  
ATOM     66  CG  PHE A  12       0.066  30.867  22.641  1.00 30.67           C  
ATOM     67  CD1 PHE A  12       1.328  30.920  22.046  1.00 32.84           C  
ATOM     68  CD2 PHE A  12      -0.767  29.774  22.377  1.00 28.68           C  
ATOM     69  CE1 PHE A  12       1.752  29.891  21.185  1.00 33.43           C  
ATOM     70  CE2 PHE A  12      -0.369  28.755  21.524  1.00 32.88           C  
ATOM     71  CZ  PHE A  12       0.893  28.813  20.931  1.00 29.64           C  
ATOM     72  N   LYS A  13      -0.659  33.857  26.203  1.00 20.89           N  
ATOM     73  CA  LYS A  13      -0.987  35.159  26.817  1.00 22.33           C  
ATOM     74  C   LYS A  13       0.192  35.621  27.656  1.00 20.70           C  
ATOM     75  O   LYS A  13       0.613  36.788  27.776  1.00 16.13           O  
ATOM     76  CB  LYS A  13      -2.217  34.930  27.661  1.00 28.79           C  
ATOM     77  CG  LYS A  13      -3.041  36.094  28.154  1.00 32.48           C  
ATOM     78  CD  LYS A  13      -4.442  35.589  28.530  1.00 36.44           C  
ATOM     79  CE  LYS A  13      -5.276  35.366  27.283  1.00 40.40           C  
ATOM     80  NZ  LYS A  13      -6.424  34.469  27.572  1.00 41.12           N  
ATOM     81  N   GLU A  14       0.774  34.606  28.303  1.00 21.57           N  
ATOM     82  CA  GLU A  14       1.948  34.832  29.154  1.00 21.36           C  
ATOM     83  C   GLU A  14       3.092  35.346  28.288  1.00 22.09           C  
ATOM     84  O   GLU A  14       3.746  36.313  28.684  1.00 20.70           O  
ATOM     85  CB  GLU A  14       2.402  33.605  29.926  1.00 27.25           C  
ATOM     86  CG  GLU A  14       1.881  33.442  31.347  1.00 35.30           C  
ATOM     87  CD  GLU A  14       2.032  32.070  31.947  1.00 39.45           C  
ATOM     88  OE1 GLU A  14       3.185  31.613  31.795  1.00 41.02           O  
ATOM     89  OE2 GLU A  14       1.111  31.490  32.497  1.00 42.94           O  
ATOM     90  N   ALA A  15       3.312  34.709  27.151  1.00 20.13           N  
ATOM     91  CA  ALA A  15       4.375  35.089  26.210  1.00 20.94           C  
ATOM     92  C   ALA A  15       4.146  36.506  25.665  1.00 17.60           C  
ATOM     93  O   ALA A  15       5.108  37.285  25.635  1.00 18.43           O  
ATOM     94  CB  ALA A  15       4.499  34.020  25.123  1.00 17.73           C  
ATOM     95  N   PHE A  16       2.934  36.813  25.287  1.00 20.02           N  
ATOM     96  CA  PHE A  16       2.482  38.106  24.744  1.00 15.27           C  
ATOM     97  C   PHE A  16       2.771  39.212  25.755  1.00 15.45           C  
ATOM     98  O   PHE A  16       3.341  40.248  25.376  1.00 16.92           O  
ATOM     99  CB  PHE A  16       1.002  38.123  24.378  1.00 13.77           C  
ATOM    100  CG  PHE A  16       0.463  39.353  23.734  1.00 16.36           C  
ATOM    101  CD1 PHE A  16       0.534  39.540  22.365  1.00 14.23           C  
ATOM    102  CD2 PHE A  16      -0.115  40.359  24.545  1.00 14.21           C  
ATOM    103  CE1 PHE A  16       0.050  40.703  21.750  1.00 16.13           C  
ATOM    104  CE2 PHE A  16      -0.589  41.541  23.975  1.00 16.04           C  
ATOM    105  CZ  PHE A  16      -0.506  41.686  22.584  1.00 18.35           C  
ATOM    106  N   SER A  17       2.398  38.968  27.017  1.00 14.55           N  
ATOM    107  CA  SER A  17       2.620  40.003  28.044  1.00 18.34           C  
ATOM    108  C   SER A  17       4.065  40.424  28.164  1.00 15.87           C  
ATOM    109  O   SER A  17       4.281  41.596  28.542  1.00 20.17           O  
ATOM    110  CB  SER A  17       2.054  39.565  29.403  1.00 18.71           C  
ATOM    111  OG  SER A  17       0.694  39.178  29.164  1.00 29.11           O  
ATOM    112  N   LEU A  18       5.017  39.537  27.863  1.00 16.90           N  
ATOM    113  CA  LEU A  18       6.429  39.916  27.972  1.00 13.77           C  
ATOM    114  C   LEU A  18       6.760  41.054  26.994  1.00 11.96           C  
ATOM    115  O   LEU A  18       7.580  41.947  27.290  1.00 12.75           O  
ATOM    116  CB  LEU A  18       7.292  38.669  27.689  1.00 26.24           C  
ATOM    117  CG  LEU A  18       8.757  38.900  27.325  1.00 29.37           C  
ATOM    118  CD1 LEU A  18       9.628  39.178  28.545  1.00 23.47           C  
ATOM    119  CD2 LEU A  18       9.288  37.653  26.611  1.00 29.36           C  
ATOM    120  N   PHE A  19       6.091  41.007  25.852  1.00 16.90           N  
ATOM    121  CA  PHE A  19       6.326  42.020  24.806  1.00 13.01           C  
ATOM    122  C   PHE A  19       5.501  43.313  24.966  1.00 15.56           C  
ATOM    123  O   PHE A  19       6.055  44.390  24.697  1.00 10.27           O  
ATOM    124  CB  PHE A  19       6.018  41.441  23.420  1.00 16.88           C  
ATOM    125  CG  PHE A  19       6.985  40.410  22.937  1.00 15.97           C  
ATOM    126  CD1 PHE A  19       8.160  40.772  22.278  1.00 16.90           C  
ATOM    127  CD2 PHE A  19       6.650  39.067  23.164  1.00 14.82           C  
ATOM    128  CE1 PHE A  19       9.036  39.782  21.827  1.00 22.16           C  
ATOM    129  CE2 PHE A  19       7.537  38.059  22.738  1.00 19.54           C  
ATOM    130  CZ  PHE A  19       8.705  38.449  22.071  1.00 15.11           C  
ATOM    131  N   ASP A  20       4.266  43.121  25.376  1.00 14.41           N  
ATOM    132  CA  ASP A  20       3.304  44.245  25.573  1.00 11.59           C  
ATOM    133  C   ASP A  20       3.670  44.929  26.900  1.00 14.74           C  
ATOM    134  O   ASP A  20       2.889  44.743  27.823  1.00 18.73           O  
ATOM    135  CB  ASP A  20       1.892  43.688  25.483  1.00  9.57           C  
ATOM    136  CG  ASP A  20       0.838  44.766  25.732  1.00 12.80           C  
ATOM    137  OD1 ASP A  20       1.362  45.900  25.680  1.00 15.48           O  
ATOM    138  OD2 ASP A  20      -0.327  44.468  26.038  1.00 14.91           O  
ATOM    139  N   LYS A  21       4.728  45.693  26.942  1.00 17.60           N  
ATOM    140  CA  LYS A  21       5.293  46.400  28.082  1.00 17.11           C  
ATOM    141  C   LYS A  21       4.294  47.280  28.828  1.00 18.92           C  
ATOM    142  O   LYS A  21       4.315  47.311  30.060  1.00 17.29           O  
ATOM    143  CB  LYS A  21       6.503  47.292  27.783  1.00 13.27           C  
ATOM    144  CG  LYS A  21       7.799  46.588  27.382  1.00 17.02           C  
ATOM    145  CD  LYS A  21       7.997  45.345  28.241  1.00 12.36           C  
ATOM    146  CE  LYS A  21       9.432  44.873  28.246  1.00 14.04           C  
ATOM    147  NZ  LYS A  21       9.466  43.420  28.594  1.00 12.84           N  
ATOM    148  N   ASP A  22       3.444  47.960  28.072  1.00 16.55           N  
ATOM    149  CA  ASP A  22       2.467  48.811  28.776  1.00 15.05           C  
ATOM    150  C   ASP A  22       1.114  48.178  28.881  1.00 12.96           C  
ATOM    151  O   ASP A  22       0.189  48.826  29.396  1.00 14.58           O  
ATOM    152  CB  ASP A  22       2.549  50.211  28.151  1.00 12.16           C  
ATOM    153  CG  ASP A  22       1.791  50.191  26.830  1.00 19.80           C  
ATOM    154  OD1 ASP A  22       1.480  49.126  26.287  1.00 12.67           O  
ATOM    155  OD2 ASP A  22       1.487  51.294  26.337  1.00 14.63           O  
ATOM    156  N   GLY A  23       0.901  46.928  28.470  1.00 11.59           N  
ATOM    157  CA  GLY A  23      -0.417  46.341  28.589  1.00 12.59           C  
ATOM    158  C   GLY A  23      -1.603  46.932  27.878  1.00 15.04           C  
ATOM    159  O   GLY A  23      -2.725  46.782  28.403  1.00 19.45           O  
ATOM    160  N   ASP A  24      -1.454  47.546  26.710  1.00 15.63           N  
ATOM    161  CA  ASP A  24      -2.616  48.079  25.966  1.00 13.63           C  
ATOM    162  C   ASP A  24      -3.219  47.054  25.040  1.00 15.51           C  
ATOM    163  O   ASP A  24      -4.213  47.333  24.351  1.00 11.21           O  
ATOM    164  CB  ASP A  24      -2.213  49.407  25.299  1.00 16.34           C  
ATOM    165  CG  ASP A  24      -1.522  49.054  23.983  1.00 17.21           C  
ATOM    166  OD1 ASP A  24      -0.647  48.198  24.144  1.00  6.33           O  
ATOM    167  OD2 ASP A  24      -1.796  49.554  22.920  1.00 11.82           O  
ATOM    168  N   GLY A  25      -2.631  45.860  24.931  1.00  6.69           N  
ATOM    169  CA  GLY A  25      -3.185  44.822  24.047  1.00 11.58           C  
ATOM    170  C   GLY A  25      -2.510  44.785  22.651  1.00  2.00           C  
ATOM    171  O   GLY A  25      -3.040  44.051  21.780  1.00 10.63           O  
ATOM    172  N   THR A  26      -1.468  45.522  22.517  1.00  5.29           N  
ATOM    173  CA  THR A  26      -0.742  45.570  21.225  1.00  7.60           C  
ATOM    174  C   THR A  26       0.732  45.703  21.494  1.00  9.51           C  
ATOM    175  O   THR A  26       1.230  46.259  22.472  1.00 11.31           O  
ATOM    176  CB  THR A  26      -1.250  46.702  20.252  1.00 13.05           C  
ATOM    177  OG1 THR A  26      -0.824  47.960  20.889  1.00 11.71           O  
ATOM    178  CG2 THR A  26      -2.752  46.752  19.973  1.00 15.35           C  
ATOM    179  N   ILE A  27       1.487  45.176  20.498  1.00 10.83           N  
ATOM    180  CA  ILE A  27       2.948  45.226  20.545  1.00 10.53           C  
ATOM    181  C   ILE A  27       3.373  46.196  19.430  1.00  9.58           C  
ATOM    182  O   ILE A  27       2.968  46.058  18.283  1.00  7.93           O  
ATOM    183  CB  ILE A  27       3.631  43.828  20.356  1.00 12.73           C  
ATOM    184  CG1 ILE A  27       3.061  42.772  21.322  1.00  9.70           C  
ATOM    185  CG2 ILE A  27       5.170  44.038  20.518  1.00 20.43           C  
ATOM    186  CD1 ILE A  27       3.357  41.298  20.894  1.00 16.56           C  
ATOM    187  N   THR A  28       4.130  47.187  19.784  1.00  8.69           N  
ATOM    188  CA  THR A  28       4.614  48.231  18.848  1.00 13.66           C  
ATOM    189  C   THR A  28       6.066  48.039  18.487  1.00 16.31           C  
ATOM    190  O   THR A  28       6.709  47.194  19.149  1.00 14.73           O  
ATOM    191  CB  THR A  28       4.397  49.407  19.926  1.00  8.84           C  
ATOM    192  OG1 THR A  28       3.328  50.261  19.465  1.00 23.63           O  
ATOM    193  CG2 THR A  28       5.697  49.759  20.563  1.00  4.75           C  
ATOM    194  N   THR A  29       6.625  48.793  17.551  1.00 17.87           N  
ATOM    195  CA  THR A  29       8.042  48.661  17.186  1.00 20.41           C  
ATOM    196  C   THR A  29       8.972  48.898  18.370  1.00 20.52           C  
ATOM    197  O   THR A  29      10.010  48.216  18.477  1.00 22.52           O  
ATOM    198  CB  THR A  29       8.475  49.654  16.036  1.00 16.79           C  
ATOM    199  OG1 THR A  29       8.236  51.000  16.543  1.00 23.49           O  
ATOM    200  CG2 THR A  29       7.730  49.451  14.729  1.00 17.84           C  
ATOM    201  N   LYS A  30       8.620  49.865  19.204  1.00 19.91           N  
ATOM    202  CA  LYS A  30       9.395  50.247  20.386  1.00 17.77           C  
ATOM    203  C   LYS A  30       9.359  49.163  21.449  1.00 16.00           C  
ATOM    204  O   LYS A  30      10.371  48.918  22.116  1.00 21.31           O  
ATOM    205  CB  LYS A  30       8.937  51.528  21.076  1.00 18.19           C  
ATOM    206  CG  LYS A  30       8.271  52.555  20.162  1.00 24.44           C  
ATOM    207  CD  LYS A  30       6.755  52.484  20.356  1.00 31.34           C  
ATOM    208  CE  LYS A  30       6.009  52.925  19.112  1.00 33.74           C  
ATOM    209  NZ  LYS A  30       6.597  52.282  17.907  1.00 34.76           N  
ATOM    210  N   GLU A  31       8.220  48.516  21.601  1.00 15.72           N  
ATOM    211  CA  GLU A  31       8.160  47.434  22.629  1.00 15.49           C  
ATOM    212  C   GLU A  31       8.991  46.269  22.136  1.00 13.09           C  
ATOM    213  O   GLU A  31       9.814  45.682  22.880  1.00 13.15           O  
ATOM    214  CB  GLU A  31       6.723  47.039  22.947  1.00  8.61           C  
ATOM    215  CG  GLU A  31       5.971  48.075  23.781  1.00 15.46           C  
ATOM    216  CD  GLU A  31       4.517  47.919  23.975  1.00 10.77           C  
ATOM    217  OE1 GLU A  31       3.830  47.450  23.067  1.00  9.39           O  
ATOM    218  OE2 GLU A  31       3.900  48.247  24.996  1.00 17.00           O  
ATOM    219  N   LEU A  32       8.798  45.896  20.886  1.00 11.34           N  
ATOM    220  CA  LEU A  32       9.571  44.776  20.282  1.00 10.72           C  
ATOM    221  C   LEU A  32      11.036  45.115  20.443  1.00 10.76           C  
ATOM    222  O   LEU A  32      11.821  44.226  20.767  1.00 13.29           O  
ATOM    223  CB  LEU A  32       9.120  44.561  18.821  1.00 11.99           C  
ATOM    224  CG  LEU A  32       9.953  43.533  18.037  1.00 13.38           C  
ATOM    225  CD1 LEU A  32       9.856  42.168  18.694  1.00 21.91           C  
ATOM    226  CD2 LEU A  32       9.355  43.529  16.621  1.00 15.76           C  
ATOM    227  N   GLY A  33      11.399  46.370  20.252  1.00  7.66           N  
ATOM    228  CA  GLY A  33      12.770  46.883  20.366  1.00 16.31           C  
ATOM    229  C   GLY A  33      13.356  46.657  21.755  1.00 16.66           C  
ATOM    230  O   GLY A  33      14.485  46.150  21.904  1.00 16.41           O  
ATOM    231  N   THR A  34      12.624  47.005  22.805  1.00 15.62           N  
ATOM    232  CA  THR A  34      13.153  46.797  24.169  1.00 19.19           C  
ATOM    233  C   THR A  34      13.268  45.312  24.446  1.00 15.87           C  
ATOM    234  O   THR A  34      14.269  44.943  25.120  1.00 20.23           O  
ATOM    235  CB  THR A  34      12.510  47.726  25.272  1.00 24.30           C  
ATOM    236  OG1 THR A  34      12.010  46.918  26.379  1.00 29.42           O  
ATOM    237  CG2 THR A  34      11.505  48.704  24.702  1.00 19.41           C  
ATOM    238  N   VAL A  35      12.361  44.497  23.923  1.00 12.65           N  
ATOM    239  CA  VAL A  35      12.557  43.050  24.184  1.00 19.28           C  
ATOM    240  C   VAL A  35      13.859  42.548  23.547  1.00 21.94           C  
ATOM    241  O   VAL A  35      14.644  41.851  24.241  1.00 21.37           O  
ATOM    242  CB  VAL A  35      11.356  42.183  23.826  1.00 22.99           C  
ATOM    243  CG1 VAL A  35      11.666  40.694  23.973  1.00 23.97           C  
ATOM    244  CG2 VAL A  35      10.130  42.550  24.637  1.00 25.21           C  
ATOM    245  N   MET A  36      14.089  42.856  22.295  1.00 22.58           N  
ATOM    246  CA  MET A  36      15.291  42.403  21.571  1.00 24.04           C  
ATOM    247  C   MET A  36      16.574  42.876  22.235  1.00 25.85           C  
ATOM    248  O   MET A  36      17.509  42.058  22.382  1.00 30.54           O  
ATOM    249  CB  MET A  36      15.271  42.783  20.095  1.00 24.39           C  
ATOM    250  CG  MET A  36      14.010  42.360  19.406  1.00 27.42           C  
ATOM    251  SD  MET A  36      13.933  40.545  19.279  1.00 37.60           S  
ATOM    252  CE  MET A  36      14.898  40.274  17.785  1.00 37.79           C  
ATOM    253  N   ARG A  37      16.621  44.134  22.599  1.00 22.30           N  
ATOM    254  CA  ARG A  37      17.784  44.748  23.248  1.00 24.72           C  
ATOM    255  C   ARG A  37      18.127  44.071  24.577  1.00 25.68           C  
ATOM    256  O   ARG A  37      19.310  44.062  24.976  1.00 30.14           O  
ATOM    257  CB  ARG A  37      17.570  46.244  23.418  1.00 21.50           C  
ATOM    258  CG  ARG A  37      17.629  47.108  22.183  1.00 22.38           C  
ATOM    259  CD  ARG A  37      17.810  48.548  22.459  1.00 29.01           C  
ATOM    260  NE  ARG A  37      16.577  49.120  23.014  1.00 33.11           N  
ATOM    261  CZ  ARG A  37      15.634  49.620  22.208  1.00 32.22           C  
ATOM    262  NH1 ARG A  37      15.800  49.648  20.889  1.00 30.61           N  
ATOM    263  NH2 ARG A  37      14.504  50.069  22.751  1.00 33.35           N  
ATOM    264  N   SER A  38      17.130  43.532  25.237  1.00 24.69           N  
ATOM    265  CA  SER A  38      17.351  42.851  26.531  1.00 30.18           C  
ATOM    266  C   SER A  38      17.960  41.476  26.233  1.00 32.47           C  
ATOM    267  O   SER A  38      18.483  40.814  27.143  1.00 36.66           O  
ATOM    268  CB  SER A  38      16.109  42.734  27.380  1.00 28.75           C  
ATOM    269  OG  SER A  38      15.277  41.685  26.924  1.00 30.47           O  
ATOM    270  N   LEU A  39      17.885  41.105  24.961  1.00 32.02           N  
ATOM    271  CA  LEU A  39      18.426  39.820  24.495  1.00 30.40           C  
ATOM    272  C   LEU A  39      19.841  39.972  23.945  1.00 30.27           C  
ATOM    273  O   LEU A  39      20.410  38.948  23.530  1.00 31.46           O  
ATOM    274  CB  LEU A  39      17.456  39.202  23.487  1.00 29.34           C  
ATOM    275  CG  LEU A  39      16.059  38.816  23.920  1.00 32.36           C  
ATOM    276  CD1 LEU A  39      15.269  38.185  22.783  1.00 34.54           C  
ATOM    277  CD2 LEU A  39      16.137  37.838  25.090  1.00 33.87           C  
ATOM    278  N   GLY A  40      20.405  41.168  23.943  1.00 26.01           N  
ATOM    279  CA  GLY A  40      21.774  41.366  23.425  1.00 28.44           C  
ATOM    280  C   GLY A  40      21.797  41.652  21.924  1.00 25.97           C  
ATOM    281  O   GLY A  40      22.816  41.594  21.213  1.00 26.68           O  
ATOM    282  N   GLN A  41      20.638  42.015  21.427  1.00 26.26           N  
ATOM    283  CA  GLN A  41      20.442  42.345  19.998  1.00 24.93           C  
ATOM    284  C   GLN A  41      19.920  43.775  19.921  1.00 28.39           C  
ATOM    285  O   GLN A  41      18.896  44.034  20.578  1.00 28.96           O  
ATOM    286  CB  GLN A  41      19.403  41.374  19.495  1.00 28.97           C  
ATOM    287  CG  GLN A  41      19.511  40.733  18.149  1.00 36.53           C  
ATOM    288  CD  GLN A  41      19.014  39.301  18.263  1.00 38.83           C  
ATOM    289  OE1 GLN A  41      18.387  38.761  17.367  1.00 41.03           O  
ATOM    290  NE2 GLN A  41      19.300  38.714  19.428  1.00 42.41           N  
ATOM    291  N   ASN A  42      20.600  44.625  19.179  1.00 27.74           N  
ATOM    292  CA  ASN A  42      20.142  46.026  19.052  1.00 26.58           C  
ATOM    293  C   ASN A  42      19.797  46.268  17.576  1.00 26.15           C  
ATOM    294  O   ASN A  42      20.572  46.811  16.765  1.00 28.12           O  
ATOM    295  CB  ASN A  42      21.138  46.955  19.722  1.00 20.72           C  
ATOM    296  CG  ASN A  42      21.331  46.776  21.220  1.00 26.76           C  
ATOM    297  OD1 ASN A  42      21.697  45.729  21.775  1.00 22.91           O  
ATOM    298  ND2 ASN A  42      21.116  47.842  22.006  1.00 15.27           N  
ATOM    299  N   PRO A  43      18.587  45.850  17.223  1.00 27.74           N  
ATOM    300  CA  PRO A  43      18.069  46.009  15.859  1.00 27.47           C  
ATOM    301  C   PRO A  43      17.816  47.480  15.568  1.00 28.41           C  
ATOM    302  O   PRO A  43      17.657  48.313  16.486  1.00 27.47           O  
ATOM    303  CB  PRO A  43      16.778  45.193  15.807  1.00 29.27           C  
ATOM    304  CG  PRO A  43      16.311  45.200  17.250  1.00 29.04           C  
ATOM    305  CD  PRO A  43      17.583  45.217  18.091  1.00 29.78           C  
ATOM    306  N   THR A  44      17.786  47.780  14.276  1.00 27.75           N  
ATOM    307  CA  THR A  44      17.541  49.173  13.853  1.00 25.78           C  
ATOM    308  C   THR A  44      16.027  49.337  13.701  1.00 25.42           C  
ATOM    309  O   THR A  44      15.334  48.317  13.644  1.00 24.39           O  
ATOM    310  CB  THR A  44      18.321  49.490  12.526  1.00 23.72           C  
ATOM    311  OG1 THR A  44      17.668  48.675  11.496  1.00 24.67           O  
ATOM    312  CG2 THR A  44      19.820  49.177  12.561  1.00 24.35           C  
ATOM    313  N   GLU A  45      15.558  50.570  13.614  1.00 27.78           N  
ATOM    314  CA  GLU A  45      14.113  50.802  13.422  1.00 27.10           C  
ATOM    315  C   GLU A  45      13.674  50.087  12.148  1.00 25.32           C  
ATOM    316  O   GLU A  45      12.604  49.451  12.118  1.00 26.16           O  
ATOM    317  CB  GLU A  45      13.777  52.287  13.415  1.00 31.88           C  
ATOM    318  CG  GLU A  45      12.330  52.725  13.430  1.00 38.44           C  
ATOM    319  CD  GLU A  45      11.457  52.597  14.634  1.00 42.72           C  
ATOM    320  OE1 GLU A  45      12.059  52.647  15.735  1.00 43.65           O  
ATOM    321  OE2 GLU A  45      10.234  52.468  14.557  1.00 43.30           O  
ATOM    322  N   ALA A  46      14.472  50.099  11.093  1.00 24.71           N  
ATOM    323  CA  ALA A  46      14.141  49.427   9.828  1.00 20.95           C  
ATOM    324  C   ALA A  46      13.881  47.943   9.998  1.00 21.64           C  
ATOM    325  O   ALA A  46      12.939  47.338   9.458  1.00 19.18           O  
ATOM    326  CB  ALA A  46      15.248  49.641   8.791  1.00 23.64           C  
ATOM    327  N   GLU A  47      14.771  47.307  10.752  1.00 19.51           N  
ATOM    328  CA  GLU A  47      14.658  45.869  11.023  1.00 20.53           C  
ATOM    329  C   GLU A  47      13.432  45.643  11.912  1.00 15.29           C  
ATOM    330  O   GLU A  47      12.753  44.655  11.678  1.00 14.12           O  
ATOM    331  CB  GLU A  47      15.904  45.297  11.693  1.00 23.05           C  
ATOM    332  CG  GLU A  47      17.102  45.115  10.752  1.00 24.45           C  
ATOM    333  CD  GLU A  47      18.461  45.177  11.384  1.00 28.74           C  
ATOM    334  OE1 GLU A  47      18.727  45.739  12.437  1.00 28.22           O  
ATOM    335  OE2 GLU A  47      19.328  44.616  10.672  1.00 23.62           O  
ATOM    336  N   LEU A  48      13.181  46.544  12.845  1.00 13.15           N  
ATOM    337  CA  LEU A  48      12.024  46.429  13.766  1.00 10.72           C  
ATOM    338  C   LEU A  48      10.755  46.492  12.915  1.00 11.70           C  
ATOM    339  O   LEU A  48       9.849  45.688  13.089  1.00 13.32           O  
ATOM    340  CB  LEU A  48      12.125  47.492  14.846  1.00 19.61           C  
ATOM    341  CG  LEU A  48      12.428  47.183  16.295  1.00 20.36           C  
ATOM    342  CD1 LEU A  48      13.007  45.806  16.543  1.00 23.93           C  
ATOM    343  CD2 LEU A  48      13.373  48.247  16.860  1.00 21.03           C  
ATOM    344  N   GLN A  49      10.717  47.363  11.909  1.00 14.61           N  
ATOM    345  CA  GLN A  49       9.529  47.460  11.046  1.00 14.47           C  
ATOM    346  C   GLN A  49       9.283  46.208  10.224  1.00 13.88           C  
ATOM    347  O   GLN A  49       8.121  45.751  10.085  1.00 11.99           O  
ATOM    348  CB  GLN A  49       9.607  48.764  10.244  1.00 19.70           C  
ATOM    349  CG  GLN A  49       8.265  49.056   9.587  1.00 28.77           C  
ATOM    350  CD  GLN A  49       7.204  49.395  10.612  1.00 30.35           C  
ATOM    351  OE1 GLN A  49       6.141  48.787  10.645  1.00 33.82           O  
ATOM    352  NE2 GLN A  49       7.530  50.394  11.434  1.00 31.96           N  
ATOM    353  N   ASP A  50      10.320  45.584   9.662  1.00 18.83           N  
ATOM    354  CA  ASP A  50      10.179  44.341   8.880  1.00 14.32           C  
ATOM    355  C   ASP A  50       9.629  43.199   9.746  1.00 11.08           C  
ATOM    356  O   ASP A  50       8.795  42.418   9.293  1.00 13.15           O  
ATOM    357  CB  ASP A  50      11.518  43.946   8.248  1.00 16.77           C  
ATOM    358  CG  ASP A  50      11.792  44.763   6.994  1.00 21.73           C  
ATOM    359  OD1 ASP A  50      10.900  45.179   6.250  1.00 24.00           O  
ATOM    360  OD2 ASP A  50      13.003  44.962   6.817  1.00 22.73           O  
ATOM    361  N   MET A  51      10.105  43.139  10.978  1.00 15.31           N  
ATOM    362  CA  MET A  51       9.613  42.106  11.907  1.00 12.18           C  
ATOM    363  C   MET A  51       8.117  42.253  12.128  1.00  9.57           C  
ATOM    364  O   MET A  51       7.376  41.226  12.098  1.00 14.22           O  
ATOM    365  CB  MET A  51      10.404  42.111  13.206  1.00 16.25           C  
ATOM    366  CG  MET A  51      11.882  41.960  12.974  1.00 25.99           C  
ATOM    367  SD  MET A  51      12.662  41.534  14.575  1.00 31.06           S  
ATOM    368  CE  MET A  51      14.268  42.304  14.343  1.00 33.58           C  
ATOM    369  N   ILE A  52       7.636  43.455  12.372  1.00 15.00           N  
ATOM    370  CA  ILE A  52       6.206  43.697  12.614  1.00  9.92           C  
ATOM    371  C   ILE A  52       5.402  43.465  11.344  1.00  9.44           C  
ATOM    372  O   ILE A  52       4.348  42.828  11.327  1.00 11.75           O  
ATOM    373  CB  ILE A  52       6.011  45.145  13.198  1.00 13.02           C  
ATOM    374  CG1 ILE A  52       6.451  45.096  14.682  1.00 22.03           C  
ATOM    375  CG2 ILE A  52       4.573  45.640  12.915  1.00 14.79           C  
ATOM    376  CD1 ILE A  52       5.499  45.757  15.695  1.00 26.23           C  
ATOM    377  N   ASN A  53       5.949  43.935  10.232  1.00 13.88           N  
ATOM    378  CA  ASN A  53       5.295  43.775   8.930  1.00  7.92           C  
ATOM    379  C   ASN A  53       4.944  42.313   8.654  1.00  6.09           C  
ATOM    380  O   ASN A  53       3.850  41.993   8.201  1.00 12.29           O  
ATOM    381  CB  ASN A  53       6.131  44.298   7.750  1.00 18.24           C  
ATOM    382  CG  ASN A  53       6.012  45.816   7.653  1.00 20.79           C  
ATOM    383  OD1 ASN A  53       6.704  46.424   6.834  1.00 23.91           O  
ATOM    384  ND2 ASN A  53       5.155  46.325   8.517  1.00 16.53           N  
ATOM    385  N   GLU A  54       5.899  41.451   8.898  1.00 12.39           N  
ATOM    386  CA  GLU A  54       5.680  40.017   8.679  1.00 17.61           C  
ATOM    387  C   GLU A  54       4.520  39.397   9.443  1.00 21.44           C  
ATOM    388  O   GLU A  54       3.896  38.441   8.950  1.00 22.19           O  
ATOM    389  CB  GLU A  54       6.980  39.306   9.092  1.00 26.47           C  
ATOM    390  CG  GLU A  54       7.091  37.803   8.955  1.00 37.65           C  
ATOM    391  CD  GLU A  54       8.324  37.167   9.530  1.00 43.96           C  
ATOM    392  OE1 GLU A  54       9.213  38.003   9.794  1.00 48.31           O  
ATOM    393  OE2 GLU A  54       8.439  35.960   9.721  1.00 50.11           O  
ATOM    394  N   VAL A  55       4.220  39.902  10.627  1.00 19.68           N  
ATOM    395  CA  VAL A  55       3.156  39.398  11.506  1.00 18.90           C  
ATOM    396  C   VAL A  55       1.880  40.207  11.501  1.00 10.90           C  
ATOM    397  O   VAL A  55       0.810  39.722  11.892  1.00 14.51           O  
ATOM    398  CB  VAL A  55       3.707  39.303  12.952  1.00 17.13           C  
ATOM    399  CG1 VAL A  55       5.122  38.766  12.957  1.00 14.61           C  
ATOM    400  CG2 VAL A  55       3.649  40.601  13.714  1.00 26.02           C  
ATOM    401  N   ASP A  56       1.965  41.461  11.075  1.00 18.02           N  
ATOM    402  CA  ASP A  56       0.738  42.329  11.068  1.00 14.93           C  
ATOM    403  C   ASP A  56      -0.171  42.108   9.888  1.00 17.89           C  
ATOM    404  O   ASP A  56      -0.065  42.685   8.791  1.00 17.87           O  
ATOM    405  CB  ASP A  56       1.338  43.730  11.207  1.00 14.83           C  
ATOM    406  CG  ASP A  56       0.256  44.800  11.247  1.00 14.70           C  
ATOM    407  OD1 ASP A  56      -0.834  44.378  11.658  1.00  9.18           O  
ATOM    408  OD2 ASP A  56       0.621  45.908  10.829  1.00 14.53           O  
ATOM    409  N   ALA A  57      -1.135  41.207  10.062  1.00 15.88           N  
ATOM    410  CA  ALA A  57      -2.114  40.819   9.062  1.00 20.86           C  
ATOM    411  C   ALA A  57      -3.085  41.892   8.609  1.00 20.68           C  
ATOM    412  O   ALA A  57      -3.364  41.876   7.392  1.00 26.17           O  
ATOM    413  CB  ALA A  57      -2.829  39.552   9.532  1.00 19.58           C  
ATOM    414  N   ASP A  58      -3.542  42.783   9.458  1.00 25.48           N  
ATOM    415  CA  ASP A  58      -4.498  43.838   9.122  1.00 22.06           C  
ATOM    416  C   ASP A  58      -3.865  45.184   8.763  1.00 23.59           C  
ATOM    417  O   ASP A  58      -4.609  46.155   8.577  1.00 23.87           O  
ATOM    418  CB  ASP A  58      -5.501  44.035  10.269  1.00 23.40           C  
ATOM    419  CG  ASP A  58      -4.887  44.551  11.543  1.00 20.37           C  
ATOM    420  OD1 ASP A  58      -3.669  44.751  11.695  1.00 21.72           O  
ATOM    421  OD2 ASP A  58      -5.642  44.742  12.521  1.00 22.23           O  
ATOM    422  N   GLY A  59      -2.563  45.224   8.731  1.00 21.04           N  
ATOM    423  CA  GLY A  59      -1.733  46.342   8.405  1.00 17.64           C  
ATOM    424  C   GLY A  59      -1.950  47.607   9.181  1.00 21.41           C  
ATOM    425  O   GLY A  59      -1.666  48.677   8.614  1.00 22.08           O  
ATOM    426  N   ASN A  60      -2.382  47.482  10.428  1.00 17.37           N  
ATOM    427  CA  ASN A  60      -2.608  48.645  11.292  1.00 16.01           C  
ATOM    428  C   ASN A  60      -1.325  49.102  11.956  1.00 18.56           C  
ATOM    429  O   ASN A  60      -1.383  50.118  12.688  1.00 16.11           O  
ATOM    430  CB  ASN A  60      -3.772  48.467  12.260  1.00 20.56           C  
ATOM    431  CG  ASN A  60      -3.377  47.606  13.445  1.00 16.93           C  
ATOM    432  OD1 ASN A  60      -2.429  46.793  13.325  1.00 14.20           O  
ATOM    433  ND2 ASN A  60      -4.074  47.746  14.552  1.00 19.49           N  
ATOM    434  N   GLY A  61      -0.224  48.406  11.780  1.00 19.98           N  
ATOM    435  CA  GLY A  61       1.053  48.800  12.337  1.00 19.24           C  
ATOM    436  C   GLY A  61       1.474  48.240  13.681  1.00 19.03           C  
ATOM    437  O   GLY A  61       2.604  48.563  14.089  1.00 13.84           O  
ATOM    438  N   THR A  62       0.599  47.451  14.306  1.00 12.39           N  
ATOM    439  CA  THR A  62       0.964  46.893  15.618  1.00  7.64           C  
ATOM    440  C   THR A  62       0.452  45.439  15.558  1.00  2.00           C  
ATOM    441  O   THR A  62      -0.391  45.099  14.724  1.00 14.16           O  
ATOM    442  CB  THR A  62       0.256  47.655  16.807  1.00  9.89           C  
ATOM    443  OG1 THR A  62      -1.157  47.624  16.526  1.00 10.49           O  
ATOM    444  CG2 THR A  62       0.663  49.129  16.976  1.00 11.10           C  
ATOM    445  N   ILE A  63       0.994  44.734  16.558  1.00 13.11           N  
ATOM    446  CA  ILE A  63       0.513  43.331  16.621  1.00 11.54           C  
ATOM    447  C   ILE A  63      -0.367  43.200  17.872  1.00 12.43           C  
ATOM    448  O   ILE A  63       0.015  43.642  18.955  1.00 12.62           O  
ATOM    449  CB  ILE A  63       1.652  42.318  16.352  1.00 19.31           C  
ATOM    450  CG1 ILE A  63       1.563  41.066  17.280  1.00  9.32           C  
ATOM    451  CG2 ILE A  63       3.094  42.803  16.148  1.00 11.65           C  
ATOM    452  CD1 ILE A  63       0.556  40.040  16.713  1.00 22.67           C  
ATOM    453  N   ASP A  64      -1.499  42.592  17.643  1.00 14.08           N  
ATOM    454  CA  ASP A  64      -2.517  42.309  18.661  1.00 11.41           C  
ATOM    455  C   ASP A  64      -2.365  40.817  19.055  1.00 14.01           C  
ATOM    456  O   ASP A  64      -1.551  40.126  18.437  1.00 13.61           O  
ATOM    457  CB  ASP A  64      -3.929  42.651  18.256  1.00 13.48           C  
ATOM    458  CG  ASP A  64      -4.516  41.964  17.054  1.00 11.48           C  
ATOM    459  OD1 ASP A  64      -4.024  40.917  16.573  1.00 19.19           O  
ATOM    460  OD2 ASP A  64      -5.554  42.440  16.561  1.00 19.69           O  
ATOM    461  N   PHE A  65      -3.115  40.401  20.058  1.00 10.75           N  
ATOM    462  CA  PHE A  65      -3.021  38.984  20.513  1.00 16.47           C  
ATOM    463  C   PHE A  65      -3.307  37.947  19.445  1.00 17.70           C  
ATOM    464  O   PHE A  65      -2.552  36.961  19.256  1.00 16.73           O  
ATOM    465  CB  PHE A  65      -3.862  38.793  21.787  1.00 20.98           C  
ATOM    466  CG  PHE A  65      -3.661  37.402  22.350  1.00 13.65           C  
ATOM    467  CD1 PHE A  65      -2.395  36.996  22.758  1.00 15.54           C  
ATOM    468  CD2 PHE A  65      -4.758  36.545  22.427  1.00 19.27           C  
ATOM    469  CE1 PHE A  65      -2.232  35.691  23.248  1.00 19.09           C  
ATOM    470  CE2 PHE A  65      -4.623  35.246  22.905  1.00 20.56           C  
ATOM    471  CZ  PHE A  65      -3.348  34.850  23.318  1.00 20.75           C  
ATOM    472  N   PRO A  66      -4.426  38.042  18.763  1.00 15.37           N  
ATOM    473  CA  PRO A  66      -4.815  37.106  17.708  1.00 20.60           C  
ATOM    474  C   PRO A  66      -3.713  36.956  16.665  1.00 20.83           C  
ATOM    475  O   PRO A  66      -3.427  35.825  16.235  1.00 17.65           O  
ATOM    476  CB  PRO A  66      -6.121  37.648  17.173  1.00 21.18           C  
ATOM    477  CG  PRO A  66      -6.618  38.590  18.221  1.00 17.65           C  
ATOM    478  CD  PRO A  66      -5.408  39.130  18.945  1.00 16.35           C  
ATOM    479  N   GLU A  67      -3.071  38.041  16.275  1.00 15.50           N  
ATOM    480  CA  GLU A  67      -1.981  38.065  15.277  1.00 14.38           C  
ATOM    481  C   GLU A  67      -0.747  37.351  15.814  1.00 17.23           C  
ATOM    482  O   GLU A  67      -0.126  36.532  15.110  1.00 19.20           O  
ATOM    483  CB  GLU A  67      -1.612  39.481  14.839  1.00 17.56           C  
ATOM    484  CG  GLU A  67      -2.504  40.208  13.828  1.00 13.54           C  
ATOM    485  CD  GLU A  67      -2.253  41.700  13.706  1.00 14.36           C  
ATOM    486  OE1 GLU A  67      -1.470  42.217  14.438  1.00 15.62           O  
ATOM    487  OE2 GLU A  67      -2.920  42.249  12.800  1.00 12.60           O  
ATOM    488  N   PHE A  68      -0.387  37.612  17.061  1.00 11.17           N  
ATOM    489  CA  PHE A  68       0.744  36.990  17.758  1.00 15.85           C  
ATOM    490  C   PHE A  68       0.546  35.467  17.855  1.00 17.28           C  
ATOM    491  O   PHE A  68       1.520  34.720  17.636  1.00 18.26           O  
ATOM    492  CB  PHE A  68       0.930  37.563  19.154  1.00 18.11           C  
ATOM    493  CG  PHE A  68       1.923  36.927  20.073  1.00 17.51           C  
ATOM    494  CD1 PHE A  68       1.536  35.888  20.929  1.00 17.02           C  
ATOM    495  CD2 PHE A  68       3.232  37.381  20.100  1.00 17.36           C  
ATOM    496  CE1 PHE A  68       2.478  35.310  21.785  1.00 18.58           C  
ATOM    497  CE2 PHE A  68       4.176  36.829  20.966  1.00 20.93           C  
ATOM    498  CZ  PHE A  68       3.790  35.790  21.817  1.00 16.11           C  
ATOM    499  N   LEU A  69      -0.650  35.101  18.231  1.00 21.02           N  
ATOM    500  CA  LEU A  69      -1.099  33.706  18.420  1.00 23.90           C  
ATOM    501  C   LEU A  69      -0.883  32.918  17.133  1.00 27.92           C  
ATOM    502  O   LEU A  69      -0.170  31.897  17.173  1.00 28.73           O  
ATOM    503  CB  LEU A  69      -2.533  33.804  18.915  1.00 27.45           C  
ATOM    504  CG  LEU A  69      -3.406  32.705  19.438  1.00 31.75           C  
ATOM    505  CD1 LEU A  69      -3.700  31.657  18.375  1.00 32.19           C  
ATOM    506  CD2 LEU A  69      -2.745  32.062  20.657  1.00 31.64           C  
ATOM    507  N   THR A  70      -1.458  33.393  16.043  1.00 28.87           N  
ATOM    508  CA  THR A  70      -1.335  32.723  14.741  1.00 32.11           C  
ATOM    509  C   THR A  70       0.117  32.585  14.291  1.00 33.13           C  
ATOM    510  O   THR A  70       0.464  31.527  13.721  1.00 35.80           O  
ATOM    511  CB  THR A  70      -2.165  33.364  13.562  1.00 31.35           C  
ATOM    512  OG1 THR A  70      -1.271  34.330  12.930  1.00 40.44           O  
ATOM    513  CG2 THR A  70      -3.504  33.972  13.953  1.00 32.27           C  
ATOM    514  N   MET A  71       0.929  33.594  14.517  1.00 31.95           N  
ATOM    515  CA  MET A  71       2.339  33.524  14.102  1.00 35.39           C  
ATOM    516  C   MET A  71       3.116  32.557  14.998  1.00 35.93           C  
ATOM    517  O   MET A  71       3.965  31.788  14.517  1.00 34.06           O  
ATOM    518  CB  MET A  71       2.995  34.897  14.084  1.00 36.46           C  
ATOM    519  CG  MET A  71       4.505  34.765  14.052  1.00 43.44           C  
ATOM    520  SD  MET A  71       5.119  35.236  15.705  1.00 51.18           S  
ATOM    521  CE  MET A  71       6.517  34.125  15.904  1.00 49.00           C  
ATOM    522  N   MET A  72       2.813  32.644  16.275  1.00 34.29           N  
ATOM    523  CA  MET A  72       3.445  31.850  17.332  1.00 35.38           C  
ATOM    524  C   MET A  72       3.260  30.361  17.049  1.00 33.66           C  
ATOM    525  O   MET A  72       4.182  29.553  17.200  1.00 31.68           O  
ATOM    526  CB  MET A  72       2.866  32.226  18.694  1.00 40.65           C  
ATOM    527  CG  MET A  72       3.797  31.783  19.791  1.00 46.00           C  
ATOM    528  SD  MET A  72       5.374  32.645  19.468  1.00 55.43           S  
ATOM    529  CE  MET A  72       6.306  32.163  20.936  1.00 52.35           C  
ATOM    530  N   ALA A  73       2.041  30.069  16.660  1.00 33.28           N  
ATOM    531  CA  ALA A  73       1.613  28.701  16.334  1.00 34.31           C  
ATOM    532  C   ALA A  73       2.460  28.184  15.170  1.00 37.90           C  
ATOM    533  O   ALA A  73       3.214  27.215  15.321  1.00 37.29           O  
ATOM    534  CB  ALA A  73       0.122  28.661  16.028  1.00 32.80           C  
ATOM    535  N   ARG A  74       2.315  28.864  14.047  1.00 38.05           N  
ATOM    536  CA  ARG A  74       3.037  28.517  12.815  1.00 40.00           C  
ATOM    537  C   ARG A  74       4.523  28.377  13.094  1.00 39.52           C  
ATOM    538  O   ARG A  74       5.177  27.479  12.526  1.00 40.32           O  
ATOM    539  CB  ARG A  74       2.755  29.504  11.680  1.00 41.12           C  
ATOM    540  CG  ARG A  74       1.393  29.271  11.026  1.00 47.61           C  
ATOM    541  CD  ARG A  74       1.353  29.771   9.624  1.00 55.76           C  
ATOM    542  NE  ARG A  74       1.195  31.214   9.510  1.00 58.03           N  
ATOM    543  CZ  ARG A  74       0.025  31.856   9.530  1.00 60.60           C  
ATOM    544  NH1 ARG A  74      -1.124  31.195   9.644  1.00 61.96           N  
ATOM    545  NH2 ARG A  74      -0.011  33.190   9.445  1.00 60.54           N  
ATOM    546  N   LYS A  75       5.038  29.234  13.955  1.00 39.34           N  
ATOM    547  CA  LYS A  75       6.459  29.181  14.306  1.00 41.79           C  
ATOM    548  C   LYS A  75       6.750  27.884  15.073  1.00 43.90           C  
ATOM    549  O   LYS A  75       7.796  27.257  14.814  1.00 42.38           O  
ATOM    550  CB  LYS A  75       6.953  30.345  15.152  1.00 44.08           C  
ATOM    551  CG  LYS A  75       8.476  30.366  15.329  1.00 43.84           C  
ATOM    552  CD  LYS A  75       9.134  31.306  14.341  1.00 45.26           C  
ATOM    553  CE  LYS A  75       8.430  31.404  13.012  1.00 45.01           C  
ATOM    554  NZ  LYS A  75       8.563  30.151  12.230  1.00 45.66           N  
ATOM    555  N   MET A  76       5.863  27.528  15.978  1.00 41.59           N  
ATOM    556  CA  MET A  76       6.025  26.315  16.792  1.00 43.47           C  
ATOM    557  C   MET A  76       6.191  25.107  15.871  1.00 41.68           C  
ATOM    558  O   MET A  76       7.226  24.429  15.914  1.00 39.26           O  
ATOM    559  CB  MET A  76       4.879  26.099  17.758  1.00 47.60           C  
ATOM    560  CG  MET A  76       4.724  27.205  18.766  1.00 53.04           C  
ATOM    561  SD  MET A  76       6.184  27.197  19.856  1.00 61.27           S  
ATOM    562  CE  MET A  76       7.402  27.992  18.793  1.00 56.84           C  
ATOM    563  N   LYS A  77       5.159  24.876  15.092  1.00 41.72           N  
ATOM    564  CA  LYS A  77       5.102  23.767  14.134  1.00 44.13           C  
ATOM    565  C   LYS A  77       6.445  23.576  13.420  1.00 44.14           C  
ATOM    566  O   LYS A  77       6.942  22.450  13.256  1.00 45.25           O  
ATOM    567  CB  LYS A  77       4.065  24.007  13.039  1.00 44.78           C  
ATOM    568  CG  LYS A  77       2.658  24.359  13.492  1.00 49.08           C  
ATOM    569  CD  LYS A  77       1.753  23.142  13.589  1.00 51.18           C  
ATOM    570  CE  LYS A  77       0.916  22.930  12.345  1.00 54.27           C  
ATOM    571  NZ  LYS A  77      -0.376  23.664  12.432  1.00 51.55           N  
ATOM    572  N   ASP A  78       6.979  24.702  12.979  1.00 43.17           N  
ATOM    573  CA  ASP A  78       8.249  24.759  12.235  1.00 42.10           C  
ATOM    574  C   ASP A  78       9.459  24.411  13.091  1.00 41.13           C  
ATOM    575  O   ASP A  78      10.384  23.757  12.574  1.00 43.13           O  
ATOM    576  CB  ASP A  78       8.381  26.100  11.513  1.00 43.55           C  
ATOM    577  CG  ASP A  78       7.501  26.198  10.284  1.00 42.36           C  
ATOM    578  OD1 ASP A  78       6.559  25.388  10.202  1.00 45.72           O  
ATOM    579  OD2 ASP A  78       7.744  27.050   9.425  1.00 45.57           O  
ATOM    580  N   THR A  79       9.451  24.827  14.333  1.00 40.84           N  
ATOM    581  CA  THR A  79      10.551  24.555  15.264  1.00 42.20           C  
ATOM    582  C   THR A  79      10.605  23.052  15.565  1.00 43.34           C  
ATOM    583  O   THR A  79      11.682  22.523  15.889  1.00 43.23           O  
ATOM    584  CB  THR A  79      10.488  25.406  16.588  1.00 41.54           C  
ATOM    585  OG1 THR A  79      11.129  26.689  16.292  1.00 40.60           O  
ATOM    586  CG2 THR A  79      11.140  24.746  17.813  1.00 42.06           C  
ATOM    587  N   ASP A  80       9.449  22.426  15.456  1.00 44.63           N  
ATOM    588  CA  ASP A  80       9.281  20.990  15.705  1.00 46.06           C  
ATOM    589  C   ASP A  80       9.852  20.206  14.522  1.00 45.97           C  
ATOM    590  O   ASP A  80      10.441  19.123  14.702  1.00 45.31           O  
ATOM    591  CB  ASP A  80       7.836  20.648  16.046  1.00 51.03           C  
ATOM    592  CG  ASP A  80       7.400  21.131  17.415  1.00 53.74           C  
ATOM    593  OD1 ASP A  80       8.299  21.330  18.263  1.00 55.69           O  
ATOM    594  OD2 ASP A  80       6.204  21.324  17.681  1.00 56.11           O  
ATOM    595  N   SER A  81       9.672  20.772  13.345  1.00 46.51           N  
ATOM    596  CA  SER A  81      10.167  20.164  12.093  1.00 44.61           C  
ATOM    597  C   SER A  81      11.690  20.064  12.138  1.00 44.58           C  
ATOM    598  O   SER A  81      12.315  18.996  12.081  1.00 45.14           O  
ATOM    599  CB  SER A  81       9.682  20.961  10.904  1.00 44.23           C  
ATOM    600  OG  SER A  81       8.306  20.685  10.685  1.00 48.47           O  
ATOM    601  N   GLU A  82      12.293  21.219  12.268  1.00 42.93           N  
ATOM    602  CA  GLU A  82      13.731  21.407  12.350  1.00 42.96           C  
ATOM    603  C   GLU A  82      14.450  20.484  13.323  1.00 43.40           C  
ATOM    604  O   GLU A  82      15.501  19.921  12.987  1.00 40.45           O  
ATOM    605  CB  GLU A  82      14.044  22.841  12.820  1.00 45.45           C  
ATOM    606  CG  GLU A  82      15.500  23.272  12.696  1.00 48.19           C  
ATOM    607  CD  GLU A  82      16.077  23.101  11.314  1.00 51.96           C  
ATOM    608  OE1 GLU A  82      15.188  22.973  10.441  1.00 53.84           O  
ATOM    609  OE2 GLU A  82      17.277  23.077  11.083  1.00 50.68           O  
ATOM    610  N   GLU A  83      13.923  20.361  14.530  1.00 43.29           N  
ATOM    611  CA  GLU A  83      14.526  19.525  15.575  1.00 43.44           C  
ATOM    612  C   GLU A  83      14.374  18.042  15.279  1.00 41.00           C  
ATOM    613  O   GLU A  83      15.187  17.245  15.787  1.00 38.42           O  
ATOM    614  CB  GLU A  83      14.068  19.888  16.984  1.00 49.03           C  
ATOM    615  CG  GLU A  83      14.818  21.059  17.624  1.00 56.26           C  
ATOM    616  CD  GLU A  83      14.374  21.638  18.930  1.00 58.86           C  
ATOM    617  OE1 GLU A  83      13.217  21.836  19.266  1.00 60.26           O  
ATOM    618  OE2 GLU A  83      15.334  21.923  19.692  1.00 61.29           O  
ATOM    619  N   GLU A  84      13.392  17.685  14.468  1.00 39.10           N  
ATOM    620  CA  GLU A  84      13.190  16.277  14.094  1.00 41.57           C  
ATOM    621  C   GLU A  84      14.283  15.889  13.091  1.00 41.27           C  
ATOM    622  O   GLU A  84      14.923  14.825  13.233  1.00 42.46           O  
ATOM    623  CB  GLU A  84      11.840  15.978  13.475  1.00 47.51           C  
ATOM    624  CG  GLU A  84      10.590  16.031  14.346  1.00 52.07           C  
ATOM    625  CD  GLU A  84       9.307  15.645  13.661  1.00 54.53           C  
ATOM    626  OE1 GLU A  84       9.369  14.471  13.233  1.00 57.32           O  
ATOM    627  OE2 GLU A  84       8.327  16.361  13.527  1.00 56.57           O  
ATOM    628  N   ILE A  85      14.491  16.744  12.106  1.00 38.06           N  
ATOM    629  CA  ILE A  85      15.497  16.557  11.055  1.00 32.72           C  
ATOM    630  C   ILE A  85      16.899  16.637  11.663  1.00 29.37           C  
ATOM    631  O   ILE A  85      17.793  15.879  11.262  1.00 31.84           O  
ATOM    632  CB  ILE A  85      15.314  17.542   9.858  1.00 32.26           C  
ATOM    633  CG1 ILE A  85      13.910  17.425   9.234  1.00 32.00           C  
ATOM    634  CG2 ILE A  85      16.408  17.315   8.771  1.00 35.02           C  
ATOM    635  CD1 ILE A  85      13.697  18.369   8.009  1.00 36.33           C  
ATOM    636  N   ARG A  86      17.105  17.527  12.606  1.00 28.13           N  
ATOM    637  CA  ARG A  86      18.384  17.699  13.290  1.00 30.21           C  
ATOM    638  C   ARG A  86      18.680  16.426  14.114  1.00 30.09           C  
ATOM    639  O   ARG A  86      19.840  16.031  14.274  1.00 26.39           O  
ATOM    640  CB  ARG A  86      18.434  18.906  14.221  1.00 36.19           C  
ATOM    641  CG  ARG A  86      18.927  20.195  13.579  1.00 39.33           C  
ATOM    642  CD  ARG A  86      19.075  21.296  14.572  1.00 44.30           C  
ATOM    643  NE  ARG A  86      19.944  22.365  14.102  1.00 46.88           N  
ATOM    644  CZ  ARG A  86      19.585  23.389  13.320  1.00 48.12           C  
ATOM    645  NH1 ARG A  86      18.343  23.540  12.880  1.00 45.08           N  
ATOM    646  NH2 ARG A  86      20.503  24.290  12.964  1.00 48.53           N  
ATOM    647  N   GLU A  87      17.623  15.830  14.649  1.00 29.65           N  
ATOM    648  CA  GLU A  87      17.769  14.618  15.451  1.00 28.95           C  
ATOM    649  C   GLU A  87      18.315  13.488  14.565  1.00 26.09           C  
ATOM    650  O   GLU A  87      19.297  12.840  14.901  1.00 24.72           O  
ATOM    651  CB  GLU A  87      16.463  14.048  15.996  1.00 29.47           C  
ATOM    652  CG  GLU A  87      15.920  14.676  17.273  1.00 39.81           C  
ATOM    653  CD  GLU A  87      14.802  13.948  17.960  1.00 41.83           C  
ATOM    654  OE1 GLU A  87      14.324  12.991  17.317  1.00 43.69           O  
ATOM    655  OE2 GLU A  87      14.425  14.297  19.067  1.00 47.72           O  
ATOM    656  N   ALA A  88      17.598  13.309  13.472  1.00 27.38           N  
ATOM    657  CA  ALA A  88      17.940  12.266  12.492  1.00 24.53           C  
ATOM    658  C   ALA A  88      19.318  12.516  11.912  1.00 25.16           C  
ATOM    659  O   ALA A  88      19.913  11.526  11.456  1.00 20.92           O  
ATOM    660  CB  ALA A  88      16.859  12.106  11.439  1.00 20.76           C  
ATOM    661  N   PHE A  89      19.794  13.749  11.912  1.00 21.15           N  
ATOM    662  CA  PHE A  89      21.128  14.041  11.349  1.00 21.69           C  
ATOM    663  C   PHE A  89      22.191  13.489  12.297  1.00 24.27           C  
ATOM    664  O   PHE A  89      23.225  12.941  11.889  1.00 23.21           O  
ATOM    665  CB  PHE A  89      21.349  15.533  11.063  1.00 21.68           C  
ATOM    666  CG  PHE A  89      22.709  15.856  10.513  1.00 23.58           C  
ATOM    667  CD1 PHE A  89      22.911  15.781   9.129  1.00 24.43           C  
ATOM    668  CD2 PHE A  89      23.759  16.218  11.337  1.00 23.55           C  
ATOM    669  CE1 PHE A  89      24.151  16.046   8.569  1.00 26.05           C  
ATOM    670  CE2 PHE A  89      25.024  16.487  10.794  1.00 29.52           C  
ATOM    671  CZ  PHE A  89      25.215  16.402   9.403  1.00 26.27           C  
ATOM    672  N   ARG A  90      21.908  13.650  13.592  1.00 22.01           N  
ATOM    673  CA  ARG A  90      22.797  13.183  14.654  1.00 19.74           C  
ATOM    674  C   ARG A  90      22.953  11.657  14.629  1.00 15.48           C  
ATOM    675  O   ARG A  90      24.067  11.230  14.936  1.00 20.49           O  
ATOM    676  CB  ARG A  90      22.284  13.650  16.013  1.00 27.21           C  
ATOM    677  CG  ARG A  90      23.343  14.214  16.952  1.00 35.75           C  
ATOM    678  CD  ARG A  90      22.694  14.981  18.062  1.00 39.34           C  
ATOM    679  NE  ARG A  90      22.299  16.316  17.708  1.00 39.30           N  
ATOM    680  CZ  ARG A  90      21.139  16.924  17.937  1.00 38.98           C  
ATOM    681  NH1 ARG A  90      20.078  16.358  18.500  1.00 34.23           N  
ATOM    682  NH2 ARG A  90      21.088  18.220  17.606  1.00 36.60           N  
ATOM    683  N   VAL A  91      21.888  10.986  14.293  1.00 20.93           N  
ATOM    684  CA  VAL A  91      21.923   9.511  14.231  1.00 23.12           C  
ATOM    685  C   VAL A  91      22.783   9.031  13.059  1.00 25.01           C  
ATOM    686  O   VAL A  91      23.493   8.007  13.248  1.00 19.16           O  
ATOM    687  CB  VAL A  91      20.540   8.876  14.356  1.00 30.73           C  
ATOM    688  CG1 VAL A  91      19.483   9.494  13.467  1.00 36.19           C  
ATOM    689  CG2 VAL A  91      20.592   7.356  14.154  1.00 30.41           C  
ATOM    690  N   PHE A  92      22.715   9.754  11.951  1.00 20.82           N  
ATOM    691  CA  PHE A  92      23.519   9.409  10.767  1.00 20.32           C  
ATOM    692  C   PHE A  92      24.985   9.744  10.991  1.00 17.27           C  
ATOM    693  O   PHE A  92      25.888   8.980  10.593  1.00 21.58           O  
ATOM    694  CB  PHE A  92      23.053  10.089   9.480  1.00 20.89           C  
ATOM    695  CG  PHE A  92      21.903   9.475   8.753  1.00 23.31           C  
ATOM    696  CD1 PHE A  92      20.597   9.757   9.137  1.00 26.02           C  
ATOM    697  CD2 PHE A  92      22.129   8.603   7.683  1.00 29.61           C  
ATOM    698  CE1 PHE A  92      19.514   9.176   8.477  1.00 25.75           C  
ATOM    699  CE2 PHE A  92      21.071   8.029   6.996  1.00 30.44           C  
ATOM    700  CZ  PHE A  92      19.766   8.321   7.394  1.00 29.21           C  
ATOM    701  N   ASP A  93      25.219  10.909  11.563  1.00 16.35           N  
ATOM    702  CA  ASP A  93      26.597  11.381  11.810  1.00 17.94           C  
ATOM    703  C   ASP A  93      27.157  10.683  13.044  1.00 24.33           C  
ATOM    704  O   ASP A  93      27.335  11.275  14.124  1.00 28.63           O  
ATOM    705  CB  ASP A  93      26.607  12.911  11.857  1.00 22.19           C  
ATOM    706  CG  ASP A  93      27.981  13.442  12.195  1.00 22.47           C  
ATOM    707  OD1 ASP A  93      28.910  12.650  11.917  1.00 28.58           O  
ATOM    708  OD2 ASP A  93      28.169  14.562  12.713  1.00 23.68           O  
ATOM    709  N   LYS A  94      27.449   9.408  12.857  1.00 29.19           N  
ATOM    710  CA  LYS A  94      27.969   8.523  13.903  1.00 30.21           C  
ATOM    711  C   LYS A  94      29.149   9.088  14.654  1.00 32.04           C  
ATOM    712  O   LYS A  94      29.280   8.745  15.859  1.00 34.49           O  
ATOM    713  CB  LYS A  94      28.211   7.127  13.338  1.00 30.56           C  
ATOM    714  CG  LYS A  94      28.552   6.027  14.323  1.00 37.50           C  
ATOM    715  CD  LYS A  94      27.740   4.760  14.094  1.00 41.28           C  
ATOM    716  CE  LYS A  94      28.384   3.546  14.749  1.00 42.61           C  
ATOM    717  NZ  LYS A  94      28.653   3.789  16.190  1.00 44.18           N  
ATOM    718  N   ASP A  95      30.002   9.917  14.069  1.00 31.76           N  
ATOM    719  CA  ASP A  95      31.145  10.443  14.844  1.00 34.26           C  
ATOM    720  C   ASP A  95      31.018  11.935  15.155  1.00 35.78           C  
ATOM    721  O   ASP A  95      32.057  12.530  15.501  1.00 37.81           O  
ATOM    722  CB  ASP A  95      32.481  10.168  14.179  1.00 32.88           C  
ATOM    723  CG  ASP A  95      32.746  10.923  12.895  1.00 29.93           C  
ATOM    724  OD1 ASP A  95      31.951  11.793  12.509  1.00 30.52           O  
ATOM    725  OD2 ASP A  95      33.764  10.619  12.255  1.00 29.45           O  
ATOM    726  N   GLY A  96      29.829  12.459  15.008  1.00 36.02           N  
ATOM    727  CA  GLY A  96      29.543  13.869  15.254  1.00 37.43           C  
ATOM    728  C   GLY A  96      30.671  14.806  14.841  1.00 38.02           C  
ATOM    729  O   GLY A  96      31.108  15.640  15.650  1.00 40.57           O  
ATOM    730  N   ASN A  97      31.125  14.678  13.612  1.00 37.14           N  
ATOM    731  CA  ASN A  97      32.201  15.542  13.076  1.00 33.04           C  
ATOM    732  C   ASN A  97      31.504  16.652  12.280  1.00 31.56           C  
ATOM    733  O   ASN A  97      32.141  17.637  11.872  1.00 32.41           O  
ATOM    734  CB  ASN A  97      33.301  14.765  12.382  1.00 35.73           C  
ATOM    735  CG  ASN A  97      32.981  14.234  10.998  1.00 31.86           C  
ATOM    736  OD1 ASN A  97      31.841  13.851  10.695  1.00 33.10           O  
ATOM    737  ND2 ASN A  97      34.006  14.212  10.147  1.00 36.61           N  
ATOM    738  N   GLY A  98      30.207  16.503  12.098  1.00 27.52           N  
ATOM    739  CA  GLY A  98      29.345  17.442  11.389  1.00 26.51           C  
ATOM    740  C   GLY A  98      29.068  17.043   9.945  1.00 24.98           C  
ATOM    741  O   GLY A  98      28.473  17.800   9.159  1.00 26.16           O  
ATOM    742  N   TYR A  99      29.481  15.839   9.575  1.00 25.86           N  
ATOM    743  CA  TYR A  99      29.231  15.410   8.193  1.00 22.31           C  
ATOM    744  C   TYR A  99      29.024  13.899   8.111  1.00 20.01           C  
ATOM    745  O   TYR A  99      29.733  13.165   8.786  1.00 21.77           O  
ATOM    746  CB  TYR A  99      30.397  15.735   7.272  1.00 31.25           C  
ATOM    747  CG  TYR A  99      31.081  17.063   7.292  1.00 34.85           C  
ATOM    748  CD1 TYR A  99      32.158  17.321   8.149  1.00 35.91           C  
ATOM    749  CD2 TYR A  99      30.686  18.072   6.406  1.00 35.64           C  
ATOM    750  CE1 TYR A  99      32.811  18.554   8.139  1.00 36.59           C  
ATOM    751  CE2 TYR A  99      31.332  19.306   6.381  1.00 36.86           C  
ATOM    752  CZ  TYR A  99      32.392  19.531   7.248  1.00 35.05           C  
ATOM    753  OH  TYR A  99      33.005  20.751   7.193  1.00 38.23           O  
ATOM    754  N   ILE A 100      28.104  13.572   7.240  1.00 19.00           N  
ATOM    755  CA  ILE A 100      27.815  12.157   6.981  1.00 17.02           C  
ATOM    756  C   ILE A 100      28.666  11.617   5.831  1.00 17.92           C  
ATOM    757  O   ILE A 100      28.561  12.059   4.672  1.00 23.03           O  
ATOM    758  CB  ILE A 100      26.313  12.020   6.680  1.00 11.61           C  
ATOM    759  CG1 ILE A 100      25.399  12.544   7.822  1.00 11.00           C  
ATOM    760  CG2 ILE A 100      25.891  10.572   6.349  1.00 12.51           C  
ATOM    761  CD1 ILE A 100      23.937  12.601   7.258  1.00 13.19           C  
ATOM    762  N   SER A 101      29.499  10.655   6.145  1.00 20.33           N  
ATOM    763  CA  SER A 101      30.367   9.981   5.172  1.00 19.64           C  
ATOM    764  C   SER A 101      29.583   8.817   4.570  1.00 22.87           C  
ATOM    765  O   SER A 101      28.454   8.425   4.933  1.00 18.75           O  
ATOM    766  CB  SER A 101      31.656   9.511   5.824  1.00 20.95           C  
ATOM    767  OG  SER A 101      31.360   8.533   6.827  1.00 14.46           O  
ATOM    768  N   ALA A 102      30.237   8.242   3.562  1.00 17.36           N  
ATOM    769  CA  ALA A 102      29.718   7.093   2.817  1.00 18.70           C  
ATOM    770  C   ALA A 102      29.575   5.902   3.781  1.00 14.55           C  
ATOM    771  O   ALA A 102      28.533   5.264   3.788  1.00 21.52           O  
ATOM    772  CB  ALA A 102      30.695   6.745   1.690  1.00 18.13           C  
ATOM    773  N   ALA A 103      30.647   5.685   4.527  1.00 16.08           N  
ATOM    774  CA  ALA A 103      30.728   4.600   5.518  1.00 14.58           C  
ATOM    775  C   ALA A 103      29.633   4.717   6.571  1.00 16.97           C  
ATOM    776  O   ALA A 103      28.985   3.727   6.974  1.00 15.34           O  
ATOM    777  CB  ALA A 103      32.114   4.598   6.147  1.00 13.81           C  
ATOM    778  N   GLU A 104      29.373   5.939   6.996  1.00 11.60           N  
ATOM    779  CA  GLU A 104      28.321   6.203   8.014  1.00 13.51           C  
ATOM    780  C   GLU A 104      26.956   5.928   7.429  1.00 18.49           C  
ATOM    781  O   GLU A 104      26.146   5.190   8.019  1.00 17.83           O  
ATOM    782  CB  GLU A 104      28.448   7.624   8.527  1.00 15.44           C  
ATOM    783  CG  GLU A 104      29.394   7.862   9.704  1.00 22.41           C  
ATOM    784  CD  GLU A 104      29.639   9.306  10.008  1.00 23.25           C  
ATOM    785  OE1 GLU A 104      29.205  10.211   9.326  1.00 26.70           O  
ATOM    786  OE2 GLU A 104      30.346   9.430  11.028  1.00 20.68           O  
ATOM    787  N   LEU A 105      26.686   6.473   6.247  1.00 15.75           N  
ATOM    788  CA  LEU A 105      25.426   6.264   5.550  1.00 17.47           C  
ATOM    789  C   LEU A 105      25.229   4.780   5.296  1.00 12.94           C  
ATOM    790  O   LEU A 105      24.109   4.246   5.523  1.00 12.78           O  
ATOM    791  CB  LEU A 105      25.396   7.210   4.306  1.00 11.48           C  
ATOM    792  CG  LEU A 105      24.202   6.912   3.395  1.00 13.27           C  
ATOM    793  CD1 LEU A 105      22.904   7.265   4.102  1.00 20.40           C  
ATOM    794  CD2 LEU A 105      24.402   7.751   2.135  1.00 20.78           C  
ATOM    795  N   ARG A 106      26.258   4.039   4.881  1.00 14.55           N  
ATOM    796  CA  ARG A 106      26.136   2.598   4.602  1.00 13.48           C  
ATOM    797  C   ARG A 106      25.799   1.745   5.826  1.00 12.65           C  
ATOM    798  O   ARG A 106      25.024   0.770   5.739  1.00 17.09           O  
ATOM    799  CB  ARG A 106      27.407   2.074   3.903  1.00 10.46           C  
ATOM    800  CG  ARG A 106      27.201   0.668   3.323  1.00 15.55           C  
ATOM    801  CD  ARG A 106      28.271   0.377   2.300  1.00 12.53           C  
ATOM    802  NE  ARG A 106      29.532   0.117   2.867  1.00 21.07           N  
ATOM    803  CZ  ARG A 106      30.717   0.423   3.288  1.00 31.60           C  
ATOM    804  NH1 ARG A 106      31.279   1.635   3.203  1.00 36.63           N  
ATOM    805  NH2 ARG A 106      31.420  -0.527   3.930  1.00 35.05           N  
ATOM    806  N   HIS A 107      26.370   2.105   6.949  1.00 17.49           N  
ATOM    807  CA  HIS A 107      26.112   1.398   8.231  1.00 18.44           C  
ATOM    808  C   HIS A 107      24.680   1.661   8.659  1.00 20.32           C  
ATOM    809  O   HIS A 107      23.923   0.708   8.898  1.00 17.09           O  
ATOM    810  CB  HIS A 107      27.122   1.781   9.326  1.00 24.42           C  
ATOM    811  CG  HIS A 107      26.949   0.984  10.590  1.00 30.66           C  
ATOM    812  ND1 HIS A 107      27.278  -0.348  10.724  1.00 33.01           N  
ATOM    813  CD2 HIS A 107      26.458   1.382  11.787  1.00 32.96           C  
ATOM    814  CE1 HIS A 107      26.994  -0.725  11.961  1.00 36.56           C  
ATOM    815  NE2 HIS A 107      26.511   0.301  12.626  1.00 35.22           N  
ATOM    816  N   VAL A 108      24.174   2.897   8.699  1.00 17.89           N  
ATOM    817  CA  VAL A 108      22.765   3.086   9.097  1.00 18.38           C  
ATOM    818  C   VAL A 108      21.804   2.422   8.136  1.00 15.49           C  
ATOM    819  O   VAL A 108      20.718   1.898   8.475  1.00 16.73           O  
ATOM    820  CB  VAL A 108      22.442   4.569   9.388  1.00 20.05           C  
ATOM    821  CG1 VAL A 108      23.531   5.328  10.110  1.00 20.07           C  
ATOM    822  CG2 VAL A 108      22.010   5.321   8.151  1.00 24.53           C  
ATOM    823  N   MET A 109      22.129   2.379   6.854  1.00 17.22           N  
ATOM    824  CA  MET A 109      21.273   1.761   5.834  1.00 17.85           C  
ATOM    825  C   MET A 109      21.113   0.266   6.093  1.00 10.47           C  
ATOM    826  O   MET A 109      20.050  -0.359   5.886  1.00 14.11           O  
ATOM    827  CB  MET A 109      21.909   2.144   4.505  1.00 22.24           C  
ATOM    828  CG  MET A 109      20.979   2.621   3.457  1.00 29.60           C  
ATOM    829  SD  MET A 109      19.894   3.984   4.029  1.00 32.18           S  
ATOM    830  CE  MET A 109      18.527   3.674   2.904  1.00 33.27           C  
ATOM    831  N   THR A 110      22.191  -0.363   6.558  1.00 17.98           N  
ATOM    832  CA  THR A 110      22.121  -1.826   6.819  1.00 22.31           C  
ATOM    833  C   THR A 110      21.151  -2.012   7.994  1.00 22.14           C  
ATOM    834  O   THR A 110      20.346  -2.952   7.952  1.00 26.54           O  
ATOM    835  CB  THR A 110      23.510  -2.540   6.922  1.00 21.86           C  
ATOM    836  OG1 THR A 110      23.953  -2.589   8.315  1.00 33.28           O  
ATOM    837  CG2 THR A 110      24.612  -1.981   6.033  1.00 19.63           C  
ATOM    838  N   ASN A 111      21.248  -1.106   8.950  1.00 25.65           N  
ATOM    839  CA  ASN A 111      20.368  -1.121  10.142  1.00 21.59           C  
ATOM    840  C   ASN A 111      18.913  -0.904   9.751  1.00 25.07           C  
ATOM    841  O   ASN A 111      18.005  -1.294  10.505  1.00 27.22           O  
ATOM    842  CB  ASN A 111      20.877  -0.158  11.210  1.00 28.26           C  
ATOM    843  CG  ASN A 111      22.088  -0.707  11.942  1.00 28.57           C  
ATOM    844  OD1 ASN A 111      22.764   0.053  12.638  1.00 34.57           O  
ATOM    845  ND2 ASN A 111      22.392  -1.990  11.802  1.00 28.88           N  
ATOM    846  N   LEU A 112      18.684  -0.286   8.606  1.00 22.38           N  
ATOM    847  CA  LEU A 112      17.353  -0.012   8.074  1.00 21.94           C  
ATOM    848  C   LEU A 112      16.818  -1.139   7.223  1.00 20.89           C  
ATOM    849  O   LEU A 112      15.662  -1.110   6.757  1.00 24.83           O  
ATOM    850  CB  LEU A 112      17.409   1.361   7.367  1.00 28.40           C  
ATOM    851  CG  LEU A 112      16.985   2.575   8.181  1.00 32.53           C  
ATOM    852  CD1 LEU A 112      17.316   2.403   9.662  1.00 33.72           C  
ATOM    853  CD2 LEU A 112      17.701   3.814   7.648  1.00 32.97           C  
ATOM    854  N   GLY A 113      17.645  -2.143   6.991  1.00 13.38           N  
ATOM    855  CA  GLY A 113      17.382  -3.345   6.242  1.00 13.85           C  
ATOM    856  C   GLY A 113      17.808  -3.292   4.774  1.00 16.81           C  
ATOM    857  O   GLY A 113      17.410  -4.213   4.074  1.00 15.55           O  
ATOM    858  N   GLU A 114      18.545  -2.293   4.403  1.00 12.74           N  
ATOM    859  CA  GLU A 114      19.055  -2.096   3.031  1.00 20.68           C  
ATOM    860  C   GLU A 114      20.568  -2.255   3.002  1.00 16.21           C  
ATOM    861  O   GLU A 114      21.318  -1.394   3.467  1.00 16.36           O  
ATOM    862  CB  GLU A 114      18.749  -0.706   2.486  1.00 23.41           C  
ATOM    863  CG  GLU A 114      17.321  -0.427   2.053  1.00 28.79           C  
ATOM    864  CD  GLU A 114      16.762  -1.417   1.073  1.00 30.38           C  
ATOM    865  OE1 GLU A 114      17.447  -1.993   0.249  1.00 33.28           O  
ATOM    866  OE2 GLU A 114      15.536  -1.575   1.207  1.00 33.01           O  
ATOM    867  N   LYS A 115      20.988  -3.354   2.402  1.00 17.64           N  
ATOM    868  CA  LYS A 115      22.396  -3.713   2.225  1.00 16.35           C  
ATOM    869  C   LYS A 115      22.814  -3.172   0.849  1.00 13.69           C  
ATOM    870  O   LYS A 115      22.499  -3.789  -0.177  1.00 19.70           O  
ATOM    871  CB  LYS A 115      22.588  -5.215   2.345  1.00 22.75           C  
ATOM    872  CG  LYS A 115      22.512  -5.680   3.791  1.00 22.22           C  
ATOM    873  CD  LYS A 115      22.410  -7.205   3.920  1.00 30.21           C  
ATOM    874  CE  LYS A 115      23.004  -7.667   5.244  1.00 32.56           C  
ATOM    875  NZ  LYS A 115      24.265  -6.921   5.490  1.00 34.87           N  
ATOM    876  N   LEU A 116      23.479  -2.055   0.898  1.00 12.64           N  
ATOM    877  CA  LEU A 116      23.950  -1.332  -0.301  1.00 11.47           C  
ATOM    878  C   LEU A 116      25.439  -1.555  -0.505  1.00  8.92           C  
ATOM    879  O   LEU A 116      26.210  -1.765   0.455  1.00  9.78           O  
ATOM    880  CB  LEU A 116      23.631   0.143   0.022  1.00 18.42           C  
ATOM    881  CG  LEU A 116      22.364   0.815  -0.443  1.00 22.89           C  
ATOM    882  CD1 LEU A 116      21.265  -0.159  -0.806  1.00 19.53           C  
ATOM    883  CD2 LEU A 116      21.929   1.798   0.645  1.00 24.21           C  
ATOM    884  N   THR A 117      25.857  -1.493  -1.765  1.00 11.57           N  
ATOM    885  CA  THR A 117      27.296  -1.646  -2.068  1.00 10.45           C  
ATOM    886  C   THR A 117      27.863  -0.246  -1.906  1.00 12.44           C  
ATOM    887  O   THR A 117      27.065   0.709  -1.760  1.00 15.68           O  
ATOM    888  CB  THR A 117      27.507  -2.160  -3.544  1.00  6.20           C  
ATOM    889  OG1 THR A 117      27.009  -1.130  -4.423  1.00 14.05           O  
ATOM    890  CG2 THR A 117      26.816  -3.486  -3.858  1.00  9.07           C  
ATOM    891  N   ASP A 118      29.174  -0.150  -1.906  1.00 10.98           N  
ATOM    892  CA  ASP A 118      29.839   1.168  -1.812  1.00 10.40           C  
ATOM    893  C   ASP A 118      29.437   2.041  -3.014  1.00 13.14           C  
ATOM    894  O   ASP A 118      29.249   3.263  -2.842  1.00 16.62           O  
ATOM    895  CB  ASP A 118      31.348   1.000  -1.697  1.00 16.46           C  
ATOM    896  CG AASP A 118      32.107   2.291  -1.516  0.50 13.30           C  
ATOM    897  CG BASP A 118      31.758   0.438  -0.326  0.50 22.66           C  
ATOM    898  OD1AASP A 118      31.940   2.877  -0.421  0.50 16.97           O  
ATOM    899  OD1BASP A 118      30.962   0.421   0.650  0.50 22.97           O  
ATOM    900  OD2AASP A 118      32.863   2.737  -2.402  0.50 16.23           O  
ATOM    901  OD2BASP A 118      32.886  -0.103  -0.173  0.50 22.16           O  
ATOM    902  N   GLU A 119      29.352   1.460  -4.189  1.00 14.88           N  
ATOM    903  CA  GLU A 119      28.982   2.220  -5.391  1.00 15.46           C  
ATOM    904  C   GLU A 119      27.573   2.800  -5.229  1.00 15.37           C  
ATOM    905  O   GLU A 119      27.378   3.966  -5.625  1.00 12.27           O  
ATOM    906  CB  GLU A 119      29.080   1.382  -6.653  1.00 21.90           C  
ATOM    907  CG  GLU A 119      28.234   1.799  -7.850  1.00 31.31           C  
ATOM    908  CD  GLU A 119      28.533   1.058  -9.119  1.00 35.39           C  
ATOM    909  OE1 GLU A 119      29.696   1.312  -9.507  1.00 37.83           O  
ATOM    910  OE2 GLU A 119      27.759   0.316  -9.692  1.00 42.50           O  
ATOM    911  N   GLU A 120      26.664   2.022  -4.691  1.00 12.34           N  
ATOM    912  CA  GLU A 120      25.278   2.502  -4.482  1.00 13.81           C  
ATOM    913  C   GLU A 120      25.279   3.634  -3.464  1.00 17.51           C  
ATOM    914  O   GLU A 120      24.531   4.617  -3.684  1.00 20.47           O  
ATOM    915  CB  GLU A 120      24.275   1.438  -4.102  1.00 11.80           C  
ATOM    916  CG  GLU A 120      24.131   0.193  -4.933  1.00 19.49           C  
ATOM    917  CD  GLU A 120      23.297  -0.974  -4.607  1.00 19.71           C  
ATOM    918  OE1 GLU A 120      23.591  -1.576  -3.547  1.00 23.54           O  
ATOM    919  OE2 GLU A 120      22.385  -1.363  -5.331  1.00 26.94           O  
ATOM    920  N   VAL A 121      26.048   3.563  -2.404  1.00 14.00           N  
ATOM    921  CA  VAL A 121      26.113   4.619  -1.379  1.00 20.56           C  
ATOM    922  C   VAL A 121      26.760   5.882  -1.951  1.00 18.88           C  
ATOM    923  O   VAL A 121      26.317   7.023  -1.682  1.00 15.07           O  
ATOM    924  CB  VAL A 121      26.812   4.159  -0.092  1.00 20.95           C  
ATOM    925  CG1 VAL A 121      27.103   5.328   0.854  1.00 21.82           C  
ATOM    926  CG2 VAL A 121      26.052   3.073   0.657  1.00 27.91           C  
ATOM    927  N   ASP A 122      27.794   5.712  -2.748  1.00 16.45           N  
ATOM    928  CA  ASP A 122      28.518   6.833  -3.372  1.00 18.15           C  
ATOM    929  C   ASP A 122      27.550   7.623  -4.263  1.00 17.09           C  
ATOM    930  O   ASP A 122      27.649   8.855  -4.258  1.00 18.60           O  
ATOM    931  CB  ASP A 122      29.775   6.375  -4.104  1.00 20.93           C  
ATOM    932  CG  ASP A 122      30.974   6.132  -3.223  1.00 26.20           C  
ATOM    933  OD1 ASP A 122      31.122   6.680  -2.118  1.00 30.64           O  
ATOM    934  OD2 ASP A 122      31.830   5.341  -3.686  1.00 32.60           O  
ATOM    935  N   GLU A 123      26.676   6.947  -4.958  1.00 17.41           N  
ATOM    936  CA  GLU A 123      25.689   7.582  -5.856  1.00 17.64           C  
ATOM    937  C   GLU A 123      24.688   8.388  -5.035  1.00 17.66           C  
ATOM    938  O   GLU A 123      24.236   9.460  -5.458  1.00 15.21           O  
ATOM    939  CB  GLU A 123      24.930   6.530  -6.620  1.00 24.75           C  
ATOM    940  CG  GLU A 123      24.268   6.843  -7.949  1.00 31.70           C  
ATOM    941  CD  GLU A 123      23.512   5.685  -8.539  1.00 36.02           C  
ATOM    942  OE1 GLU A 123      24.068   4.589  -8.248  1.00 41.52           O  
ATOM    943  OE2 GLU A 123      22.490   5.801  -9.201  1.00 37.82           O  
ATOM    944  N   MET A 124      24.335   7.867  -3.883  1.00 18.88           N  
ATOM    945  CA  MET A 124      23.383   8.529  -2.972  1.00 19.52           C  
ATOM    946  C   MET A 124      24.019   9.826  -2.459  1.00 18.78           C  
ATOM    947  O   MET A 124      23.299  10.839  -2.377  1.00 21.59           O  
ATOM    948  CB  MET A 124      22.938   7.658  -1.804  1.00 22.22           C  
ATOM    949  CG  MET A 124      22.070   6.484  -2.155  1.00 27.24           C  
ATOM    950  SD  MET A 124      21.539   5.654  -0.595  1.00 33.21           S  
ATOM    951  CE  MET A 124      21.621   7.041   0.533  1.00 28.08           C  
ATOM    952  N   ILE A 125      25.282   9.782  -2.101  1.00 15.76           N  
ATOM    953  CA  ILE A 125      26.016  10.923  -1.558  1.00 18.72           C  
ATOM    954  C   ILE A 125      26.114  12.003  -2.648  1.00 22.84           C  
ATOM    955  O   ILE A 125      25.806  13.161  -2.399  1.00 24.22           O  
ATOM    956  CB  ILE A 125      27.428  10.567  -1.003  1.00 21.27           C  
ATOM    957  CG1 ILE A 125      27.331   9.576   0.187  1.00 19.99           C  
ATOM    958  CG2 ILE A 125      28.300  11.783  -0.560  1.00 14.28           C  
ATOM    959  CD1 ILE A 125      26.725  10.085   1.496  1.00 23.70           C  
ATOM    960  N   ARG A 126      26.563  11.550  -3.808  1.00 24.18           N  
ATOM    961  CA  ARG A 126      26.755  12.441  -4.958  1.00 24.45           C  
ATOM    962  C   ARG A 126      25.526  13.269  -5.256  1.00 25.57           C  
ATOM    963  O   ARG A 126      25.674  14.473  -5.500  1.00 25.35           O  
ATOM    964  CB  ARG A 126      27.177  11.672  -6.225  1.00 21.84           C  
ATOM    965  CG  ARG A 126      28.661  11.326  -6.167  1.00 24.22           C  
ATOM    966  CD  ARG A 126      29.237  11.012  -7.504  1.00 28.33           C  
ATOM    967  NE  ARG A 126      28.865   9.668  -7.957  1.00 32.06           N  
ATOM    968  CZ  ARG A 126      27.901   9.520  -8.860  1.00 31.98           C  
ATOM    969  NH1 ARG A 126      27.295  10.614  -9.306  1.00 37.36           N  
ATOM    970  NH2 ARG A 126      27.577   8.328  -9.338  1.00 29.43           N  
ATOM    971  N   GLU A 127      24.390  12.629  -5.224  1.00 24.18           N  
ATOM    972  CA  GLU A 127      23.122  13.312  -5.518  1.00 26.34           C  
ATOM    973  C   GLU A 127      22.833  14.487  -4.602  1.00 27.12           C  
ATOM    974  O   GLU A 127      22.190  15.478  -5.013  1.00 26.79           O  
ATOM    975  CB  GLU A 127      22.013  12.274  -5.386  1.00 29.28           C  
ATOM    976  CG  GLU A 127      20.822  12.359  -6.327  1.00 39.60           C  
ATOM    977  CD  GLU A 127      20.027  11.088  -6.386  1.00 42.87           C  
ATOM    978  OE1 GLU A 127      20.744  10.133  -6.727  1.00 46.47           O  
ATOM    979  OE2 GLU A 127      18.846  11.002  -6.125  1.00 49.38           O  
ATOM    980  N   ALA A 128      23.292  14.421  -3.362  1.00 24.46           N  
ATOM    981  CA  ALA A 128      23.050  15.486  -2.379  1.00 23.77           C  
ATOM    982  C   ALA A 128      24.225  16.373  -2.083  1.00 23.91           C  
ATOM    983  O   ALA A 128      24.025  17.409  -1.411  1.00 29.10           O  
ATOM    984  CB  ALA A 128      22.580  14.790  -1.093  1.00 25.84           C  
ATOM    985  N   ASP A 129      25.404  16.021  -2.541  1.00 25.22           N  
ATOM    986  CA  ASP A 129      26.669  16.705  -2.327  1.00 26.68           C  
ATOM    987  C   ASP A 129      26.828  17.969  -3.176  1.00 29.48           C  
ATOM    988  O   ASP A 129      27.341  17.834  -4.298  1.00 28.32           O  
ATOM    989  CB  ASP A 129      27.812  15.714  -2.601  1.00 25.33           C  
ATOM    990  CG  ASP A 129      29.132  16.286  -2.148  1.00 26.32           C  
ATOM    991  OD1 ASP A 129      29.127  17.280  -1.406  1.00 28.49           O  
ATOM    992  OD2 ASP A 129      30.167  15.723  -2.566  1.00 28.27           O  
ATOM    993  N   ILE A 130      26.440  19.103  -2.626  1.00 32.93           N  
ATOM    994  CA  ILE A 130      26.497  20.404  -3.305  1.00 32.17           C  
ATOM    995  C   ILE A 130      27.853  21.092  -3.333  1.00 34.02           C  
ATOM    996  O   ILE A 130      28.127  21.801  -4.316  1.00 34.80           O  
ATOM    997  CB  ILE A 130      25.450  21.406  -2.695  1.00 31.49           C  
ATOM    998  CG1 ILE A 130      24.014  20.836  -2.738  1.00 28.74           C  
ATOM    999  CG2 ILE A 130      25.497  22.795  -3.397  1.00 28.12           C  
ATOM   1000  CD1 ILE A 130      23.101  21.543  -1.695  1.00 30.45           C  
ATOM   1001  N   ASP A 131      28.645  20.910  -2.302  1.00 35.99           N  
ATOM   1002  CA  ASP A 131      29.977  21.525  -2.190  1.00 36.40           C  
ATOM   1003  C   ASP A 131      31.067  20.539  -2.618  1.00 37.81           C  
ATOM   1004  O   ASP A 131      32.271  20.784  -2.429  1.00 39.78           O  
ATOM   1005  CB  ASP A 131      30.180  22.103  -0.789  1.00 35.20           C  
ATOM   1006  CG  ASP A 131      30.282  21.040   0.281  1.00 37.29           C  
ATOM   1007  OD1 ASP A 131      30.424  19.858  -0.114  1.00 35.06           O  
ATOM   1008  OD2 ASP A 131      30.250  21.330   1.488  1.00 39.90           O  
ATOM   1009  N   GLY A 132      30.638  19.438  -3.191  1.00 37.47           N  
ATOM   1010  CA  GLY A 132      31.471  18.349  -3.693  1.00 34.52           C  
ATOM   1011  C   GLY A 132      32.682  18.039  -2.837  1.00 35.62           C  
ATOM   1012  O   GLY A 132      33.821  18.092  -3.345  1.00 39.10           O  
ATOM   1013  N   ASP A 133      32.462  17.709  -1.575  1.00 34.75           N  
ATOM   1014  CA  ASP A 133      33.548  17.362  -0.645  1.00 28.46           C  
ATOM   1015  C   ASP A 133      33.453  15.859  -0.353  1.00 28.01           C  
ATOM   1016  O   ASP A 133      34.275  15.315   0.376  1.00 26.53           O  
ATOM   1017  CB  ASP A 133      33.597  18.222   0.605  1.00 31.74           C  
ATOM   1018  CG  ASP A 133      32.466  17.941   1.590  1.00 32.07           C  
ATOM   1019  OD1 ASP A 133      31.410  17.478   1.113  1.00 32.00           O  
ATOM   1020  OD2 ASP A 133      32.636  18.199   2.795  1.00 31.53           O  
ATOM   1021  N   GLY A 134      32.473  15.226  -0.951  1.00 27.96           N  
ATOM   1022  CA  GLY A 134      32.203  13.799  -0.846  1.00 29.38           C  
ATOM   1023  C   GLY A 134      31.418  13.385   0.396  1.00 29.34           C  
ATOM   1024  O   GLY A 134      31.260  12.176   0.617  1.00 31.75           O  
ATOM   1025  N   GLN A 135      30.955  14.351   1.155  1.00 29.92           N  
ATOM   1026  CA  GLN A 135      30.185  14.092   2.384  1.00 28.61           C  
ATOM   1027  C   GLN A 135      28.912  14.918   2.382  1.00 26.53           C  
ATOM   1028  O   GLN A 135      28.816  15.812   1.536  1.00 25.59           O  
ATOM   1029  CB  GLN A 135      30.980  14.519   3.624  1.00 29.34           C  
ATOM   1030  CG  GLN A 135      32.233  13.695   3.786  1.00 35.92           C  
ATOM   1031  CD  GLN A 135      33.166  14.341   4.781  1.00 40.73           C  
ATOM   1032  OE1 GLN A 135      33.369  15.549   4.744  1.00 43.44           O  
ATOM   1033  NE2 GLN A 135      33.703  13.493   5.652  1.00 38.16           N  
ATOM   1034  N   VAL A 136      27.995  14.620   3.290  1.00 27.00           N  
ATOM   1035  CA  VAL A 136      26.768  15.445   3.308  1.00 26.02           C  
ATOM   1036  C   VAL A 136      26.772  16.226   4.622  1.00 27.90           C  
ATOM   1037  O   VAL A 136      26.897  15.634   5.704  1.00 25.44           O  
ATOM   1038  CB  VAL A 136      25.479  14.693   2.989  1.00 27.97           C  
ATOM   1039  CG1 VAL A 136      25.705  13.495   2.076  1.00 30.03           C  
ATOM   1040  CG2 VAL A 136      24.669  14.349   4.216  1.00 32.46           C  
ATOM   1041  N   ASN A 137      26.663  17.529   4.443  1.00 25.75           N  
ATOM   1042  CA  ASN A 137      26.632  18.420   5.637  1.00 26.18           C  
ATOM   1043  C   ASN A 137      25.155  18.560   5.973  1.00 22.55           C  
ATOM   1044  O   ASN A 137      24.331  18.016   5.227  1.00 19.93           O  
ATOM   1045  CB  ASN A 137      27.409  19.699   5.411  1.00 28.53           C  
ATOM   1046  CG  ASN A 137      26.779  20.659   4.433  1.00 26.88           C  
ATOM   1047  OD1 ASN A 137      27.400  21.702   4.129  1.00 35.85           O  
ATOM   1048  ND2 ASN A 137      25.584  20.378   3.952  1.00 26.83           N  
ATOM   1049  N   TYR A 138      24.850  19.270   7.048  1.00 24.78           N  
ATOM   1050  CA  TYR A 138      23.454  19.448   7.469  1.00 23.50           C  
ATOM   1051  C   TYR A 138      22.606  20.150   6.436  1.00 20.23           C  
ATOM   1052  O   TYR A 138      21.456  19.754   6.155  1.00 20.32           O  
ATOM   1053  CB  TYR A 138      23.390  20.117   8.873  1.00 28.35           C  
ATOM   1054  CG  TYR A 138      21.944  20.343   9.283  1.00 27.38           C  
ATOM   1055  CD1 TYR A 138      21.108  19.250   9.542  1.00 26.39           C  
ATOM   1056  CD2 TYR A 138      21.414  21.628   9.398  1.00 27.44           C  
ATOM   1057  CE1 TYR A 138      19.776  19.426   9.906  1.00 31.51           C  
ATOM   1058  CE2 TYR A 138      20.077  21.809   9.751  1.00 28.63           C  
ATOM   1059  CZ  TYR A 138      19.268  20.721  10.010  1.00 28.67           C  
ATOM   1060  OH  TYR A 138      17.971  20.946  10.369  1.00 32.79           O  
ATOM   1061  N   GLU A 139      23.178  21.224   5.879  1.00 22.97           N  
ATOM   1062  CA  GLU A 139      22.463  21.984   4.853  1.00 24.26           C  
ATOM   1063  C   GLU A 139      22.033  21.063   3.718  1.00 22.58           C  
ATOM   1064  O   GLU A 139      20.863  21.061   3.315  1.00 22.14           O  
ATOM   1065  CB  GLU A 139      23.281  23.145   4.276  1.00 27.79           C  
ATOM   1066  CG  GLU A 139      22.625  23.737   3.029  1.00 35.74           C  
ATOM   1067  CD  GLU A 139      23.085  25.080   2.549  1.00 38.18           C  
ATOM   1068  OE1 GLU A 139      24.243  25.347   2.914  1.00 38.14           O  
ATOM   1069  OE2 GLU A 139      22.347  25.771   1.862  1.00 38.80           O  
ATOM   1070  N   GLU A 140      22.977  20.280   3.211  1.00 24.44           N  
ATOM   1071  CA  GLU A 140      22.708  19.329   2.111  1.00 21.16           C  
ATOM   1072  C   GLU A 140      21.702  18.264   2.524  1.00 22.90           C  
ATOM   1073  O   GLU A 140      20.886  17.783   1.722  1.00 21.73           O  
ATOM   1074  CB  GLU A 140      24.006  18.672   1.650  1.00 25.54           C  
ATOM   1075  CG  GLU A 140      25.053  19.500   0.918  1.00 27.23           C  
ATOM   1076  CD  GLU A 140      26.457  19.013   0.996  1.00 27.89           C  
ATOM   1077  OE1 GLU A 140      26.825  18.170   1.799  1.00 26.44           O  
ATOM   1078  OE2 GLU A 140      27.259  19.519   0.179  1.00 24.17           O  
ATOM   1079  N   PHE A 141      21.754  17.901   3.800  1.00 24.94           N  
ATOM   1080  CA  PHE A 141      20.845  16.890   4.380  1.00 23.65           C  
ATOM   1081  C   PHE A 141      19.413  17.413   4.405  1.00 25.48           C  
ATOM   1082  O   PHE A 141      18.481  16.674   4.057  1.00 26.26           O  
ATOM   1083  CB  PHE A 141      21.309  16.408   5.752  1.00 25.31           C  
ATOM   1084  CG  PHE A 141      20.487  15.368   6.444  1.00 24.55           C  
ATOM   1085  CD1 PHE A 141      20.674  14.013   6.172  1.00 26.37           C  
ATOM   1086  CD2 PHE A 141      19.532  15.738   7.399  1.00 27.96           C  
ATOM   1087  CE1 PHE A 141      19.910  13.040   6.824  1.00 25.57           C  
ATOM   1088  CE2 PHE A 141      18.776  14.786   8.061  1.00 27.08           C  
ATOM   1089  CZ  PHE A 141      18.944  13.427   7.770  1.00 27.38           C  
ATOM   1090  N   VAL A 142      19.253  18.663   4.828  1.00 27.54           N  
ATOM   1091  CA  VAL A 142      17.874  19.223   4.871  1.00 32.91           C  
ATOM   1092  C   VAL A 142      17.330  19.322   3.447  1.00 33.99           C  
ATOM   1093  O   VAL A 142      16.149  19.034   3.166  1.00 32.31           O  
ATOM   1094  CB  VAL A 142      17.844  20.506   5.707  1.00 35.90           C  
ATOM   1095  CG1 VAL A 142      18.725  20.418   6.951  1.00 37.48           C  
ATOM   1096  CG2 VAL A 142      18.157  21.770   4.928  1.00 37.47           C  
ATOM   1097  N   GLN A 143      18.207  19.695   2.529  1.00 39.08           N  
ATOM   1098  CA  GLN A 143      17.788  19.809   1.115  1.00 44.99           C  
ATOM   1099  C   GLN A 143      17.223  18.466   0.642  1.00 46.83           C  
ATOM   1100  O   GLN A 143      16.179  18.449  -0.027  1.00 47.28           O  
ATOM   1101  CB  GLN A 143      18.886  20.301   0.179  1.00 48.44           C  
ATOM   1102  CG  GLN A 143      19.513  21.602   0.640  1.00 53.90           C  
ATOM   1103  CD  GLN A 143      19.498  22.650  -0.448  1.00 56.61           C  
ATOM   1104  OE1 GLN A 143      18.632  22.666  -1.319  1.00 58.44           O  
ATOM   1105  NE2 GLN A 143      20.479  23.551  -0.371  1.00 60.07           N  
ATOM   1106  N   MET A 144      17.914  17.395   0.988  1.00 48.93           N  
ATOM   1107  CA  MET A 144      17.507  16.036   0.595  1.00 51.20           C  
ATOM   1108  C   MET A 144      16.268  15.586   1.366  1.00 52.52           C  
ATOM   1109  O   MET A 144      15.403  14.875   0.826  1.00 51.30           O  
ATOM   1110  CB  MET A 144      18.697  15.101   0.717  1.00 52.48           C  
ATOM   1111  CG  MET A 144      18.692  13.996  -0.294  1.00 56.97           C  
ATOM   1112  SD  MET A 144      18.478  14.621  -1.996  1.00 60.64           S  
ATOM   1113  CE  MET A 144      19.621  16.005  -2.023  1.00 58.95           C  
ATOM   1114  N   MET A 145      16.188  16.019   2.608  1.00 53.95           N  
ATOM   1115  CA  MET A 145      15.081  15.705   3.519  1.00 56.65           C  
ATOM   1116  C   MET A 145      13.765  16.338   3.076  1.00 59.15           C  
ATOM   1117  O   MET A 145      12.816  15.644   2.680  1.00 60.32           O  
ATOM   1118  CB  MET A 145      15.452  16.115   4.943  1.00 55.72           C  
ATOM   1119  CG  MET A 145      15.940  14.930   5.739  1.00 57.44           C  
ATOM   1120  SD  MET A 145      15.881  13.459   4.657  1.00 58.23           S  
ATOM   1121  CE  MET A 145      17.490  12.736   4.995  1.00 58.02           C  
ATOM   1122  N   THR A 146      13.727  17.651   3.166  1.00 62.18           N  
ATOM   1123  CA  THR A 146      12.558  18.451   2.797  1.00 65.34           C  
ATOM   1124  C   THR A 146      12.199  18.268   1.329  1.00 67.12           C  
ATOM   1125  O   THR A 146      11.073  17.854   1.003  1.00 68.37           O  
ATOM   1126  CB  THR A 146      12.781  19.972   3.163  1.00 66.92           C  
ATOM   1127  OG1 THR A 146      13.796  20.484   2.242  1.00 68.17           O  
ATOM   1128  CG2 THR A 146      13.179  20.186   4.629  1.00 67.78           C  
ATOM   1129  N   ALA A 147      13.153  18.574   0.465  1.00 68.40           N  
ATOM   1130  CA  ALA A 147      12.996  18.460  -0.991  1.00 69.08           C  
ATOM   1131  C   ALA A 147      13.200  17.008  -1.431  1.00 69.21           C  
ATOM   1132  O   ALA A 147      12.239  16.249  -1.625  1.00 70.46           O  
ATOM   1133  CB  ALA A 147      13.966  19.389  -1.705  1.00 69.58           C  
TER    1134      ALA A 147                                                      
HETATM 1135 CA    CA A 149       1.708  47.776  24.197  1.00 12.07          CA  
HETATM 1136 CA    CA A 150      -2.112  44.438  13.360  1.00 13.42          CA  
HETATM 1137 CA    CA A 151      30.463  11.962  10.473  1.00 25.88          CA  
HETATM 1138 CA    CA A 152      29.181  17.963   0.804  1.00 29.77          CA  
HETATM 1139  C1  EOH A 153       7.868  37.805  18.104  1.00 63.73           C  
HETATM 1140  C2  EOH A 153       6.465  38.277  17.751  1.00 64.50           C  
HETATM 1141  H21 EOH A 153       6.499  39.538  17.106  1.00 64.47           H  
HETATM 1142  O   HOH A 154      25.838  15.755  14.313  1.00 40.98           O  
HETATM 1143  O   HOH A 155      30.439  -0.254  13.624  1.00 43.41           O  
HETATM 1144  O   HOH A 156      14.189  22.434   7.710  1.00 44.30           O  
HETATM 1145  O   HOH A 157     -10.877  23.833  32.893  1.00 51.19           O  
HETATM 1146  O   HOH A 158      18.350  24.973   5.391  1.00 85.79           O  
HETATM 1147  O   HOH A 159       9.948  31.269   8.542  1.00 48.12           O  
HETATM 1148  O   HOH A 160      17.100  18.524  17.972  1.00 52.48           O  
HETATM 1149  O   HOH A 161      17.140  17.336  21.140  1.00 54.12           O  
HETATM 1150  O   HOH A 162      -1.259  42.615  27.484  1.00 23.46           O  
HETATM 1151  O   HOH A 163       3.037  28.899   7.078  1.00 66.65           O  
HETATM 1152  O   HOH A 164       1.068  23.838  17.148  1.00 55.37           O  
HETATM 1153  O   HOH A 165      -0.540  49.569   6.152  1.00 33.40           O  
HETATM 1154  O   HOH A 166      -6.673  37.965  26.681  1.00 70.02           O  
HETATM 1155  O   HOH A 167       1.719  39.882   6.195  1.00 38.31           O  
HETATM 1156  O   HOH A 168      -5.712  37.392  12.213  1.00 47.18           O  
HETATM 1157  O   HOH A 169       2.545  20.730  11.172  1.00 61.99           O  
HETATM 1158  O   HOH A 170      -0.613  26.849  11.200  1.00 55.20           O  
HETATM 1159  O   HOH A 171       6.021  39.647  31.357  1.00 35.60           O  
HETATM 1160  O   HOH A 172      -3.592  39.187   5.555  1.00 64.79           O  
HETATM 1161  O   HOH A 173      -4.552  29.415   7.671  1.00 56.00           O  
HETATM 1162  O   HOH A 174      -0.114  37.073  12.427  1.00 22.81           O  
HETATM 1163  O   HOH A 175      16.211  53.984  16.738  1.00 40.80           O  
HETATM 1164  O   HOH A 176      -2.531  49.857  17.427  1.00 14.77           O  
HETATM 1165  O   HOH A 177      -5.900  50.515  14.162  1.00 26.76           O  
HETATM 1166  O   HOH A 178      -6.767  29.999  16.762  1.00 55.07           O  
HETATM 1167  O   HOH A 179       8.477  38.955  13.286  1.00 36.03           O  
HETATM 1168  O   HOH A 180       3.084  35.742  10.209  1.00 65.73           O  
HETATM 1169  O   HOH A 181       1.728  50.102  22.982  1.00 10.80           O  
HETATM 1170  O   HOH A 182       4.022  50.099  12.484  1.00 24.18           O  
HETATM 1171  O   HOH A 183       4.556  49.804  16.031  1.00 17.24           O  
HETATM 1172  O   HOH A 184      -1.758  50.857  19.881  1.00 16.08           O  
HETATM 1173  O   HOH A 185      31.475  -2.535   9.428  1.00 58.12           O  
HETATM 1174  O   HOH A 186      30.061   1.030   7.173  1.00 43.06           O  
HETATM 1175  O   HOH A 187      31.816   7.516  11.822  1.00 36.18           O  
HETATM 1176  O   HOH A 188      32.626  11.191   9.251  1.00 32.51           O  
HETATM 1177  O   HOH A 189      26.548  -3.074   2.904  1.00 18.67           O  
HETATM 1178  O   HOH A 190      30.289   3.039   1.735  1.00 30.72           O  
HETATM 1179  O   HOH A 191      23.975  -0.561   3.350  1.00 18.05           O  
HETATM 1180  O   HOH A 192      27.690  -1.534   6.765  1.00 53.88           O  
HETATM 1181  O   HOH A 193      15.791  -1.525  10.264  1.00 42.60           O  
HETATM 1182  O   HOH A 194      32.305   3.780  -5.650  1.00 41.73           O  
HETATM 1183  O   HOH A 195      33.477  16.775  -5.976  1.00 50.39           O  
HETATM 1184  O   HOH A 196      30.327  13.740  -3.955  1.00 39.34           O  
HETATM 1185  O   HOH A 197      11.685  18.832  19.916  1.00 59.85           O  
HETATM 1186  O   HOH A 198      30.491   3.802  10.528  1.00 28.04           O  
HETATM 1187  O   HOH A 199      21.016  11.075  -1.859  1.00 45.05           O  
HETATM 1188  O   HOH A 200      11.501  23.731   7.195  1.00 51.50           O  
HETATM 1189  O   HOH A 201      18.310  20.288  19.351  1.00 66.84           O  
HETATM 1190  O   HOH A 202      -7.913  24.003  18.462  1.00 59.15           O  
HETATM 1191  O   HOH A 203       2.176  45.574   7.230  1.00 43.35           O  
HETATM 1192  O   HOH A 204       2.602  47.066   9.271  1.00 31.42           O  
HETATM 1193  O   HOH A 205       1.683  43.686   6.650  1.00 50.69           O  
HETATM 1194  O   HOH A 206      14.042   4.695  -1.033  1.00 51.04           O  
HETATM 1195  O   HOH A 207      10.545  51.974   9.716  1.00 51.65           O  
HETATM 1196  O   HOH A 208       8.852  52.199  12.845  1.00 40.58           O  
HETATM 1197  O   HOH A 209      12.057  47.982   7.462  1.00 30.91           O  
HETATM 1198  O   HOH A 210      16.204  46.639  26.730  1.00 24.74           O  
HETATM 1199  O   HOH A 211      18.322  48.957  19.154  1.00 30.19           O  
HETATM 1200  O   HOH A 212      12.956  50.557  19.963  1.00 42.45           O  
HETATM 1201  O   HOH A 213      12.402  43.744  28.298  1.00 22.93           O  
HETATM 1202  O   HOH A 214      25.714  -5.767  -0.090  1.00 25.86           O  
HETATM 1203  O   HOH A 215      22.236  -5.568  14.279  1.00 57.18           O  
HETATM 1204  O   HOH A 216      35.618  15.412  -3.778  1.00 57.53           O  
HETATM 1205  O   HOH A 217      15.285  -6.217   4.587  1.00 35.25           O  
HETATM 1206  O   HOH A 218      13.171  -3.040   4.779  1.00 56.80           O  
HETATM 1207  O   HOH A 219      11.454  -2.296   0.460  1.00 34.45           O  
HETATM 1208  O   HOH A 220      24.264  -7.193  -0.946  1.00 29.96           O  
HETATM 1209  O   HOH A 221      32.513   4.976  14.162  1.00 50.21           O  
HETATM 1210  O   HOH A 222      25.832   6.188  10.764  1.00 38.60           O  
HETATM 1211  O   HOH A 223      25.343   3.635  17.293  1.00 21.56           O  
HETATM 1212  O   HOH A 224      34.310   0.837   6.384  1.00 40.72           O  
HETATM 1213  O   HOH A 225      32.804   0.595  -5.545  1.00 26.21           O  
HETATM 1214  O   HOH A 226      17.178   6.846  -9.983  1.00 75.34           O  
HETATM 1215  O   HOH A 227      34.622  10.397  -1.981  1.00 66.78           O  
HETATM 1216  O   HOH A 228      14.508  -0.164  -0.983  1.00 48.01           O  
HETATM 1217  O   HOH A 229      27.085  20.300   8.850  1.00 33.17           O  
HETATM 1218  O   HOH A 230      26.221  13.407  15.961  1.00 31.42           O  
HETATM 1219  O   HOH A 231      33.473   1.174   9.512  1.00 66.40           O  
HETATM 1220  O   HOH A 232      33.950  12.481   7.718  1.00 53.14           O  
HETATM 1221  O   HOH A 233      29.779  18.954   3.161  1.00 28.47           O  
HETATM 1222  O   HOH A 234      25.423  25.296   4.592  1.00 36.30           O  
HETATM 1223  O   HOH A 235      12.685  16.235  20.916  1.00 70.56           O  
HETATM 1224  O   HOH A 236      -4.249  26.413  20.575  1.00 59.70           O  
HETATM 1225  O   HOH A 237       8.845  44.799   5.548  1.00 21.26           O  
HETATM 1226  O   HOH A 238       4.415  44.566   4.465  1.00 22.81           O  
HETATM 1227  O   HOH A 239      -4.674  41.835  21.733  1.00 15.22           O  
HETATM 1228  O   HOH A 240      -3.941  44.566  14.756  1.00 16.04           O  
HETATM 1229  O   HOH A 241      14.843  42.040  10.468  1.00 41.42           O  
HETATM 1230  O   HOH A 242      10.113  38.570  14.826  1.00 70.23           O  
HETATM 1231  O   HOH A 243       2.503  52.270  16.792  1.00 37.78           O  
HETATM 1232  O   HOH A 244      27.115  -2.120  -7.041  1.00 16.77           O  
HETATM 1233  O   HOH A 245      23.504  -1.418  -8.265  1.00 47.89           O  
HETATM 1234  O   HOH A 246      32.330   9.917   2.125  1.00 36.26           O  
HETATM 1235  O   HOH A 247      27.020  -5.597   3.226  1.00 27.24           O  
HETATM 1236  O   HOH A 248      -5.397  40.978  12.561  1.00 34.82           O  
HETATM 1237  O   HOH A 249      -7.732  45.028  13.445  1.00 37.46           O  
HETATM 1238  O   HOH A 250      -6.980  43.124  19.784  1.00 43.64           O  
HETATM 1239  O   HOH A 251       6.686  16.661  18.201  1.00 65.00           O  
HETATM 1240  O   HOH A 252      -3.311  45.871  16.967  1.00 26.26           O  
HETATM 1241  O   HOH A 253      -3.308  19.968  32.651  1.00 63.62           O  
HETATM 1242  O   HOH A 254      26.720  -5.430  -7.258  1.00 27.55           O  
HETATM 1243  O   HOH A 255      30.321  -0.975  -9.866  1.00 27.90           O  
HETATM 1244  O   HOH A 256      -0.975  25.719  13.696  1.00 69.68           O  
HETATM 1245  O   HOH A 257       9.462  30.774  19.119  1.00 77.16           O  
HETATM 1246  O   HOH A 258      -3.155  22.107  27.791  1.00 40.28           O  
HETATM 1247  O   HOH A 259       1.256  26.385  24.655  1.00 75.63           O  
HETATM 1248  O   HOH A 260     -12.591  30.611  33.010  1.00 40.52           O  
HETATM 1249  O   HOH A 261       0.871  25.293  19.264  1.00 52.28           O  
HETATM 1250  O   HOH A 262      10.524   6.506  16.192  1.00 57.33           O  
HETATM 1251  O   HOH A 263      -6.095  23.617  31.285  1.00 50.41           O  
HETATM 1252  O   HOH A 264      -3.071  39.677  26.546  1.00 51.20           O  
HETATM 1253  O   HOH A 265      -7.450  44.099  25.501  1.00 70.93           O  
HETATM 1254  O   HOH A 266      -4.272  41.530  24.936  1.00 34.54           O  
HETATM 1255  O   HOH A 267      22.857  44.224  17.522  1.00 29.62           O  
HETATM 1256  O   HOH A 268      24.270  44.998  20.329  1.00 28.80           O  
HETATM 1257  O   HOH A 269       9.963  49.893   7.230  1.00 47.76           O  
HETATM 1258  O   HOH A 270      -0.276  38.859   6.867  1.00 57.89           O  
HETATM 1259  O   HOH A 271       4.527  51.136   8.029  1.00 44.10           O  
HETATM 1260  O   HOH A 272      14.132  39.767  28.734  1.00 56.02           O  
HETATM 1261  O   HOH A 273       6.709  32.037  10.752  1.00 62.54           O  
HETATM 1262  O   HOH A 274      35.805   7.166   0.249  1.00 65.81           O  
HETATM 1263  O   HOH A 275      -0.352  35.705   7.345  1.00 52.69           O  
HETATM 1264  O   HOH A 276      15.494  46.996   7.290  1.00 50.60           O  
HETATM 1265  O   HOH A 277      25.310  23.216   6.588  1.00 46.47           O  
HETATM 1266  O   HOH A 278       7.384  15.998   2.165  1.00 46.44           O  
HETATM 1267  O   HOH A 279       3.725  11.444   4.124  1.00 50.00           O  
HETATM 1268  O   HOH A 280       3.346   6.756   4.107  1.00 42.21           O  
HETATM 1269  O   HOH A 281       3.197   8.087   8.221  1.00 49.26           O  
HETATM 1270  O   HOH A 282       5.726   5.283   7.372  1.00 56.69           O  
HETATM 1271  O   HOH A 283       9.491   1.296   2.001  1.00 57.81           O  
HETATM 1272  O   HOH A 284       8.475  -0.612   4.263  1.00 48.44           O  
HETATM 1273  O   HOH A 285       7.231  -0.344  -2.140  1.00 39.28           O  
HETATM 1274  O   HOH A 286       7.155   8.785  10.028  1.00 49.99           O  
HETATM 1275  O   HOH A 287      15.829   7.876   7.133  1.00 55.28           O  
HETATM 1276  O   HOH A 288      18.723   9.518   2.693  1.00 47.10           O  
HETATM 1277  O   HOH A 289      21.049  11.245   2.066  1.00 51.51           O  
HETATM 1278  O   HOH A 290      17.572   8.371  -0.072  1.00 51.95           O  
HETATM 1279  O   HOH A 291      17.268   4.756   0.314  1.00 54.84           O  
HETATM 1280  O   HOH A 292      17.816   1.778  -2.310  1.00 47.29           O  
CONECT  137 1135                                                                
CONECT  154 1135                                                                
CONECT  166 1135                                                                
CONECT  175 1135                                                                
CONECT  217 1135                                                                
CONECT  218 1135                                                                
CONECT  407 1136                                                                
CONECT  420 1136                                                                
CONECT  432 1136                                                                
CONECT  441 1136                                                                
CONECT  486 1136                                                                
CONECT  487 1136                                                                
CONECT  707 1137                                                                
CONECT  724 1137                                                                
CONECT  736 1137                                                                
CONECT  745 1137                                                                
CONECT  785 1137                                                                
CONECT  786 1137                                                                
CONECT  991 1138                                                                
CONECT 1007 1138                                                                
CONECT 1019 1138                                                                
CONECT 1028 1138                                                                
CONECT 1077 1138                                                                
CONECT 1078 1138                                                                
CONECT 1135  137  154  166  175                                                 
CONECT 1135  217  218 1169                                                      
CONECT 1136  407  420  432  441                                                 
CONECT 1136  486  487 1228                                                      
CONECT 1137  707  724  736  745                                                 
CONECT 1137  785  786 1176                                                      
CONECT 1138  991 1007 1019 1028                                                 
CONECT 1138 1077 1078 1221                                                      
CONECT 1139 1140                                                                
CONECT 1140 1139 1141                                                           
CONECT 1141 1140                                                                
CONECT 1169 1135                                                                
CONECT 1176 1137                                                                
CONECT 1221 1138                                                                
CONECT 1228 1136                                                                
MASTER      389    0    5    7    4    0    8    6 1279    1   39   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.