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***  E.COLI DHFR 1RX2  ***

elNémo ID: 20111006513994635

Job options:

ID        	=	 20111006513994635
JOBID     	=	 E.COLI DHFR 1RX2
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 E.COLI DHFR 1RX2

HEADER    OXIDOREDUCTASE                          19-SEP-96   1RX2              
TITLE     DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH WITH             
TITLE    2 FOLATE AND NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE               
TITLE    3 (OXIDIZED FORM)                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROFOLATE REDUCTASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: DHFR;                                                       
COMPND   5 EC: 1.5.1.3;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 STRAIN: RT500;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PRWA-1                                    
KEYWDS    OXIDOREDUCTASE, NADP, TRIMETHOPRIM RESISTANCE, METHOTREXATE           
KEYWDS   2 RESISTANCE, ONE-CARBON METABOLISM                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.R.SAWAYA                                                            
REVDAT   2   24-FEB-09 1RX2    1       VERSN                                    
REVDAT   1   11-JAN-97 1RX2    0                                                
JRNL        AUTH   M.R.SAWAYA,J.KRAUT                                           
JRNL        TITL   LOOP AND SUBDOMAIN MOVEMENTS IN THE MECHANISM OF             
JRNL        TITL 2 ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE:                    
JRNL        TITL 3 CRYSTALLOGRAPHIC EVIDENCE.                                   
JRNL        REF    BIOCHEMISTRY                  V.  36   586 1997              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   9012674                                                      
JRNL        DOI    10.1021/BI962337C                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   V.M.REYES,M.R.SAWAYA,K.A.BROWN,J.KRAUT                       
REMARK   1  TITL   ISOMORPHOUS CRYSTAL STRUCTURES OF ESCHERICHIA COLI           
REMARK   1  TITL 2 DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE,               
REMARK   1  TITL 3 5-DEAZAFOLATE, AND 5,10-DIDEAZATETRAHYDROFOLATE:             
REMARK   1  TITL 4 MECHANISTIC IMPLICATIONS                                     
REMARK   1  REF    BIOCHEMISTRY                  V.  34  2710 1995              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.BYSTROFF,J.KRAUT                                           
REMARK   1  TITL   CRYSTAL STRUCTURE OF UNLIGANDED ESCHERICHIA COLI             
REMARK   1  TITL 2 DIHYDROFOLATE REDUCTASE. LIGAND-INDUCED                      
REMARK   1  TITL 3 CONFORMATIONAL CHANGES AND COOPERATIVITY IN BINDING          
REMARK   1  REF    BIOCHEMISTRY                  V.  30  2227 1991              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   C.BYSTROFF,S.J.OATLEY,J.KRAUT                                
REMARK   1  TITL   CRYSTAL STRUCTURES OF ESCHERICHIA COLI                       
REMARK   1  TITL 2 DIHYDROFOLATE REDUCTASE: THE NADP+ HOLOENZYME AND            
REMARK   1  TITL 3 THE FOLATE.NADP+ TERNARY COMPLEX. SUBSTRATE                  
REMARK   1  TITL 4 BINDING AND A MODEL FOR THE TRANSITION STATE                 
REMARK   1  REF    BIOCHEMISTRY                  V.  29  3263 1990              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT V. 5-D                                           
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 14178                          
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
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  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.1710                 
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            : 1268                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 82                                      
REMARK   3   SOLVENT ATOMS            : 153                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.022 ; 0.020 ; 1401            
REMARK   3   BOND ANGLES            (DEGREES) : 3.000 ; 3.000 ; 1905            
REMARK   3   TORSION ANGLES         (DEGREES) : 24.300; NULL  ; 781             
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : 0.018 ; 0.020 ; 41              
REMARK   3   GENERAL PLANES               (A) : 0.008 ; 0.020 ; 194             
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : 6.000 ; NULL  ; 1401            
REMARK   3   NON-BONDED CONTACTS          (A) : 0.022 ; 0.100 ; 32              
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : MOEWS AND KRETSINGER                                 
REMARK   3   KSOL        : 0.78                                                 
REMARK   3   BSOL        : 242.30                                               
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : TNT                                              
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : TNT                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1RX2 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        : 1996                               
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : XUONG-HAMLIN MULTIWIRE             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : UCSD                               
REMARK 200  DATA SCALING SOFTWARE          : UCSD                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14178                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09100                            
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: DIFFERENCE FOURIER           
REMARK 200 SOFTWARE USED: TNT                                                   
REMARK 200 STARTING MODEL: DHFR-FOLATE COMPLEX                                  
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-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   SMTRY1   2 -1.000000  0.000000  0.000000       17.16050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.45600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.75400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.45600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       17.16050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       22.75400            
REMARK 290   SMTRY3   4  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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  48   CD    GLU A  48   OE2     0.070                       
REMARK 500    GLU A  90   CD    GLU A  90   OE2     0.069                       
REMARK 500    GLU A 101   CD    GLU A 101   OE1     0.095                       
REMARK 500    GLU A 118   CD    GLU A 118   OE2     0.075                       
REMARK 500    GLU A 120   CD    GLU A 120   OE2     0.081                       
REMARK 500    GLU A 129   CD    GLU A 129   OE2     0.081                       
REMARK 500    GLU A 154   CD    GLU A 154   OE1     0.093                       
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    LEU A   8   CB  -  CA  -  C   ANGL. DEV. = -13.0 DEGREES          
REMARK 500    ARG A  12   CD  -  NE  -  CZ  ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ARG A  12   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG A  12   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG A  33   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ASP A  37   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    TRP A  47   CB  -  CG  -  CD2 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    TRP A  47   CB  -  CG  -  CD1 ANGL. DEV. = -10.4 DEGREES          
REMARK 500    THR A  68   N   -  CA  -  CB  ANGL. DEV. = -11.7 DEGREES          
REMARK 500    ASP A  69   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A  69   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ASP A  70   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ASP A  70   CB  -  CG  -  OD2 ANGL. DEV. =  -8.3 DEGREES          
REMARK 500    ARG A  71   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ASP A  87   CB  -  CG  -  OD1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP A 116   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A 116   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ASP A 122   CB  -  CG  -  OD1 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ASP A 127   CB  -  CG  -  OD1 ANGL. DEV. =   7.8 DEGREES          
REMARK 500    ASP A 127   CB  -  CG  -  OD2 ANGL. DEV. =  -9.4 DEGREES          
REMARK 500    ASP A 132   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP A 132   CB  -  CG  -  OD2 ANGL. DEV. =  -8.3 DEGREES          
REMARK 500    ASP A 144   CB  -  CG  -  OD1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ASP A 144   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG A 159   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A 159   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  68       24.33   -144.85                                   
REMARK 500    ASP A  69      120.89   -172.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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     BME A  162                                                       
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                              MN A 300  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG A 159   O                                                      
REMARK 620 2 HOH A 383   O   169.1                                              
REMARK 620 3 HOH A 425   O    92.9  77.9                                        
REMARK 620 4 HIS A 149   ND1  94.2  95.3 172.2                                  
REMARK 620 5 ASP A 116   O   100.4  86.9  98.0  77.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 300                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOL A 161                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 162                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 164                 
DBREF  1RX2 A    1   159  UNP    P0ABQ4   DYR_ECOLI        1    159             
SEQADV 1RX2 ASP A   37  UNP  P0ABQ4    ASN    37 CONFLICT                       
SEQRES   1 A  159  MET ILE SER LEU ILE ALA ALA LEU ALA VAL ASP ARG VAL          
SEQRES   2 A  159  ILE GLY MET GLU ASN ALA MET PRO TRP ASN LEU PRO ALA          
SEQRES   3 A  159  ASP LEU ALA TRP PHE LYS ARG ASN THR LEU ASP LYS PRO          
SEQRES   4 A  159  VAL ILE MET GLY ARG HIS THR TRP GLU SER ILE GLY ARG          
SEQRES   5 A  159  PRO LEU PRO GLY ARG LYS ASN ILE ILE LEU SER SER GLN          
SEQRES   6 A  159  PRO GLY THR ASP ASP ARG VAL THR TRP VAL LYS SER VAL          
SEQRES   7 A  159  ASP GLU ALA ILE ALA ALA CYS GLY ASP VAL PRO GLU ILE          
SEQRES   8 A  159  MET VAL ILE GLY GLY GLY ARG VAL TYR GLU GLN PHE LEU          
SEQRES   9 A  159  PRO LYS ALA GLN LYS LEU TYR LEU THR HIS ILE ASP ALA          
SEQRES  10 A  159  GLU VAL GLU GLY ASP THR HIS PHE PRO ASP TYR GLU PRO          
SEQRES  11 A  159  ASP ASP TRP GLU SER VAL PHE SER GLU PHE HIS ASP ALA          
SEQRES  12 A  159  ASP ALA GLN ASN SER HIS SER TYR CYS PHE GLU ILE LEU          
SEQRES  13 A  159  GLU ARG ARG                                                  
HET     MN  A 300       1                                                       
HET    FOL  A 161      32                                                       
HET    BME  A 162       1                                                       
HET    NAP  A 164      48                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     FOL FOLIC ACID                                                       
HETNAM     BME BETA-MERCAPTOETHANOL                                             
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
FORMUL   2   MN    MN 2+                                                        
FORMUL   3  FOL    C19 H19 N7 O6                                                
FORMUL   4  BME    C2 H6 O S                                                    
FORMUL   5  NAP    C21 H28 N7 O17 P3                                            
FORMUL   6  HOH   *153(H2 O)                                                    
HELIX    1   2 PRO A   25  THR A   35  1                                  11    
HELIX    2   3 ARG A   44  ILE A   50  1                                   7    
HELIX    3   4 VAL A   78  CYS A   85  1                                   8    
HELIX    4   5 GLY A   97  LYS A  106  1                                  10    
SHEET    1   A 8 TRP A 133  SER A 135  0                                        
SHEET    2   A 8 TYR A 151  ARG A 158 -1  N  GLU A 157   O  GLU A 134           
SHEET    3   A 8 ALA A 107  ILE A 115 -1  N  HIS A 114   O  CYS A 152           
SHEET    4   A 8 ILE A   2  ILE A   5  1  N  ILE A   2   O  GLN A 108           
SHEET    5   A 8 ILE A  91  GLY A  95  1  N  ILE A  91   O  SER A   3           
SHEET    6   A 8 PRO A  39  GLY A  43  1  N  PRO A  39   O  MET A  92           
SHEET    7   A 8 LYS A  58  LEU A  62  1  N  LYS A  58   O  VAL A  40           
SHEET    8   A 8 THR A  73  VAL A  75  1  N  THR A  73   O  ILE A  61           
LINK         S2  BME A 162                 SG  CYS A 152     1555   1555  1.96  
LINK        MN    MN A 300                 O   ARG A 159     1555   1555  2.36  
LINK        MN    MN A 300                 O   HOH A 383     1555   1555  2.45  
LINK        MN    MN A 300                 O   HOH A 425     1555   1555  2.39  
LINK        MN    MN A 300                 ND1 HIS A 149     1555   1455  2.32  
LINK        MN    MN A 300                 O  AASP A 116     1555   1455  2.46  
CISPEP   1 GLY A   95    GLY A   96          0         0.67                     
SITE     1 AC1  6 ASP A 116  HIS A 149  ARG A 159  HOH A 383                    
SITE     2 AC1  6 HOH A 424  HOH A 425                                          
SITE     1 AC2 17 ILE A   5  ALA A   6  ALA A   7  MET A  20                    
SITE     2 AC2 17 ASP A  27  LEU A  28  PHE A  31  LYS A  32                    
SITE     3 AC2 17 ARG A  52  ARG A  57  ILE A  94  THR A 113                    
SITE     4 AC2 17 NAP A 164  HOH A 302  HOH A 324  HOH A 362                    
SITE     5 AC2 17 HOH A 441                                                     
SITE     1 AC3  3 SER A 138  CYS A 152  GLU A 154                               
SITE     1 AC4 34 ALA A   6  ALA A   7  ILE A  14  GLY A  15                    
SITE     2 AC4 34 MET A  16  ASN A  18  ALA A  19  MET A  20                    
SITE     3 AC4 34 GLY A  43  ARG A  44  HIS A  45  THR A  46                    
SITE     4 AC4 34 LEU A  62  SER A  63  SER A  64  LYS A  76                    
SITE     5 AC4 34 ILE A  94  GLY A  95  GLY A  96  GLY A  97                    
SITE     6 AC4 34 ARG A  98  VAL A  99  TYR A 100  GLN A 102                    
SITE     7 AC4 34 ASP A 131  FOL A 161  HOH A 324  HOH A 328                    
SITE     8 AC4 34 HOH A 335  HOH A 342  HOH A 343  HOH A 354                    
SITE     9 AC4 34 HOH A 361  HOH A 400                                          
CRYST1   34.321   45.508   98.912  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.029137  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.021974  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010110        0.00000                         
ATOM      1  N   MET A   1      12.325  42.425   9.642  1.00 25.18           N  
ATOM      2  CA  MET A   1      12.776  42.435  11.024  1.00 21.41           C  
ATOM      3  C   MET A   1      14.204  42.974  11.105  1.00  9.22           C  
ATOM      4  O   MET A   1      14.922  43.039  10.121  1.00 18.46           O  
ATOM      5  CB  MET A   1      12.667  41.006  11.557  1.00 37.55           C  
ATOM      6  CG  MET A   1      13.868  40.607  12.372  1.00 54.99           C  
ATOM      7  SD  MET A   1      14.115  38.836  12.333  1.00 57.40           S  
ATOM      8  CE  MET A   1      14.172  38.499  10.567  1.00 40.66           C  
ATOM      9  N   ILE A   2      14.628  43.343  12.317  1.00  4.19           N  
ATOM     10  CA  ILE A   2      15.975  43.905  12.515  1.00  6.08           C  
ATOM     11  C   ILE A   2      16.837  42.918  13.254  1.00 11.90           C  
ATOM     12  O   ILE A   2      16.367  42.291  14.216  1.00 10.06           O  
ATOM     13  CB  ILE A   2      15.840  45.103  13.417  1.00 10.47           C  
ATOM     14  CG1 ILE A   2      15.114  46.180  12.599  1.00 17.50           C  
ATOM     15  CG2 ILE A   2      17.245  45.600  13.744  1.00  3.85           C  
ATOM     16  CD1 ILE A   2      14.600  47.255  13.550  1.00 17.37           C  
ATOM     17  N   SER A   3      18.098  42.841  12.788  1.00  8.56           N  
ATOM     18  CA  SER A   3      19.045  41.934  13.361  1.00  4.87           C  
ATOM     19  C   SER A   3      20.359  42.608  13.549  1.00  6.86           C  
ATOM     20  O   SER A   3      20.704  43.447  12.749  1.00  6.05           O  
ATOM     21  CB  SER A   3      19.346  40.783  12.363  1.00  9.38           C  
ATOM     22  OG  SER A   3      18.181  40.063  11.963  1.00 10.13           O  
ATOM     23  N   LEU A   4      21.045  42.195  14.603  1.00  3.54           N  
ATOM     24  CA  LEU A   4      22.413  42.724  14.852  1.00  8.53           C  
ATOM     25  C   LEU A   4      23.494  41.658  14.463  1.00 14.03           C  
ATOM     26  O   LEU A   4      23.302  40.490  14.686  1.00  8.78           O  
ATOM     27  CB  LEU A   4      22.627  43.188  16.305  1.00 12.43           C  
ATOM     28  CG  LEU A   4      22.158  44.641  16.572  1.00  9.27           C  
ATOM     29  CD1 LEU A   4      20.691  44.833  16.243  1.00  8.73           C  
ATOM     30  CD2 LEU A   4      22.362  44.899  18.024  1.00 10.07           C  
ATOM     31  N   ILE A   5      24.631  42.018  13.840  1.00  6.00           N  
ATOM     32  CA  ILE A   5      25.620  41.013  13.520  1.00  5.07           C  
ATOM     33  C   ILE A   5      26.888  41.640  14.081  1.00  8.19           C  
ATOM     34  O   ILE A   5      27.149  42.857  13.891  1.00  7.83           O  
ATOM     35  CB  ILE A   5      25.823  40.702  12.105  1.00  6.56           C  
ATOM     36  CG1 ILE A   5      27.060  39.745  11.904  1.00  8.05           C  
ATOM     37  CG2 ILE A   5      26.064  42.058  11.400  1.00  4.85           C  
ATOM     38  CD1 ILE A   5      26.985  38.896  10.635  1.00  5.95           C  
ATOM     39  N   ALA A   6      27.705  40.830  14.787  1.00  6.51           N  
ATOM     40  CA  ALA A   6      28.946  41.368  15.355  1.00  5.93           C  
ATOM     41  C   ALA A   6      29.882  40.272  15.803  1.00 10.21           C  
ATOM     42  O   ALA A   6      29.369  39.176  16.029  1.00 10.51           O  
ATOM     43  CB  ALA A   6      28.608  42.179  16.603  1.00  1.44           C  
ATOM     44  N   ALA A   7      31.178  40.606  15.920  1.00  5.36           N  
ATOM     45  CA  ALA A   7      32.212  39.690  16.372  1.00  8.75           C  
ATOM     46  C   ALA A   7      32.717  40.211  17.745  1.00 10.37           C  
ATOM     47  O   ALA A   7      33.167  41.353  17.893  1.00 12.41           O  
ATOM     48  CB  ALA A   7      33.347  39.654  15.340  1.00 10.71           C  
ATOM     49  N   LEU A   8      32.681  39.408  18.795  1.00  8.32           N  
ATOM     50  CA  LEU A   8      33.145  39.877  20.062  1.00  7.12           C  
ATOM     51  C   LEU A   8      34.237  38.990  20.596  1.00 16.16           C  
ATOM     52  O   LEU A   8      34.136  37.776  20.521  1.00 13.04           O  
ATOM     53  CB  LEU A   8      32.114  39.632  21.212  1.00 12.36           C  
ATOM     54  CG  LEU A   8      30.752  40.338  21.260  1.00 16.96           C  
ATOM     55  CD1 LEU A   8      30.093  40.533  19.851  1.00 12.89           C  
ATOM     56  CD2 LEU A   8      29.854  39.424  22.107  1.00 15.83           C  
ATOM     57  N   ALA A   9      35.244  39.639  21.187  1.00 11.92           N  
ATOM     58  CA  ALA A   9      36.305  38.945  21.807  1.00 14.03           C  
ATOM     59  C   ALA A   9      35.928  38.953  23.258  1.00 11.06           C  
ATOM     60  O   ALA A   9      34.785  39.326  23.670  1.00  8.76           O  
ATOM     61  CB  ALA A   9      37.562  39.739  21.696  1.00 14.53           C  
ATOM     62  N   VAL A  10      36.905  38.538  24.038  1.00 12.09           N  
ATOM     63  CA  VAL A  10      36.750  38.464  25.477  1.00 17.92           C  
ATOM     64  C   VAL A  10      36.197  39.780  26.060  1.00 17.06           C  
ATOM     65  O   VAL A  10      36.520  40.901  25.670  1.00 13.41           O  
ATOM     66  CB  VAL A  10      38.093  38.046  26.150  1.00 14.97           C  
ATOM     67  CG1 VAL A  10      37.924  38.196  27.657  1.00 17.15           C  
ATOM     68  CG2 VAL A  10      38.435  36.560  25.814  1.00 13.79           C  
ATOM     69  N   ASP A  11      35.314  39.642  27.014  1.00 14.26           N  
ATOM     70  CA  ASP A  11      34.763  40.812  27.612  1.00 19.66           C  
ATOM     71  C   ASP A  11      33.876  41.656  26.711  1.00 14.03           C  
ATOM     72  O   ASP A  11      33.662  42.799  27.047  1.00 16.72           O  
ATOM     73  CB  ASP A  11      35.856  41.663  28.252  1.00 31.74           C  
ATOM     74  CG  ASP A  11      36.179  41.026  29.576  1.00 48.82           C  
ATOM     75  OD1 ASP A  11      35.471  40.116  30.017  1.00 50.04           O  
ATOM     76  OD2 ASP A  11      37.262  41.528  30.192  1.00 49.82           O  
ATOM     77  N   ARG A  12      33.362  41.108  25.629  1.00 13.97           N  
ATOM     78  CA  ARG A  12      32.496  41.869  24.711  1.00  6.03           C  
ATOM     79  C   ARG A  12      33.223  42.951  23.957  1.00 14.82           C  
ATOM     80  O   ARG A  12      32.577  43.812  23.411  1.00 19.58           O  
ATOM     81  CB  ARG A  12      31.263  42.465  25.448  1.00 13.90           C  
ATOM     82  CG  ARG A  12      30.370  41.476  26.193  1.00 13.77           C  
ATOM     83  CD  ARG A  12      29.005  42.050  26.588  1.00 15.44           C  
ATOM     84  NE  ARG A  12      29.025  43.519  26.771  1.00 23.78           N  
ATOM     85  CZ  ARG A  12      29.169  44.299  27.869  1.00 27.01           C  
ATOM     86  NH1 ARG A  12      29.330  43.868  29.135  1.00 29.08           N  
ATOM     87  NH2 ARG A  12      29.132  45.619  27.660  1.00 20.36           N  
ATOM     88  N   VAL A  13      34.547  42.919  23.913  1.00 15.85           N  
ATOM     89  CA  VAL A  13      35.283  43.911  23.208  1.00  6.33           C  
ATOM     90  C   VAL A  13      35.020  43.833  21.763  1.00 14.57           C  
ATOM     91  O   VAL A  13      35.133  42.713  21.279  1.00  8.47           O  
ATOM     92  CB  VAL A  13      36.783  43.666  23.397  1.00  4.74           C  
ATOM     93  CG1 VAL A  13      37.584  44.608  22.489  1.00 13.56           C  
ATOM     94  CG2 VAL A  13      37.016  44.128  24.804  1.00  6.39           C  
ATOM     95  N   ILE A  14      34.715  44.984  21.084  1.00 10.29           N  
ATOM     96  CA  ILE A  14      34.466  44.913  19.691  1.00 11.69           C  
ATOM     97  C   ILE A  14      35.384  45.747  18.841  1.00 12.80           C  
ATOM     98  O   ILE A  14      35.375  45.622  17.609  1.00  9.07           O  
ATOM     99  CB  ILE A  14      33.019  45.232  19.335  1.00 16.17           C  
ATOM    100  CG1 ILE A  14      32.641  46.606  19.855  1.00 14.84           C  
ATOM    101  CG2 ILE A  14      32.121  44.210  20.031  1.00 11.51           C  
ATOM    102  CD1 ILE A  14      31.403  47.131  19.076  1.00 19.97           C  
ATOM    103  N   GLY A  15      36.173  46.589  19.481  1.00 16.45           N  
ATOM    104  CA  GLY A  15      37.076  47.362  18.632  1.00 15.49           C  
ATOM    105  C   GLY A  15      38.115  48.072  19.480  1.00 19.94           C  
ATOM    106  O   GLY A  15      38.058  48.144  20.728  1.00 15.89           O  
ATOM    107  N   MET A  16      39.081  48.609  18.798  1.00 15.00           N  
ATOM    108  CA  MET A  16      40.104  49.326  19.523  1.00 21.83           C  
ATOM    109  C   MET A  16      40.603  50.390  18.578  1.00 18.40           C  
ATOM    110  O   MET A  16      41.005  50.048  17.435  1.00 12.28           O  
ATOM    111  CB  MET A  16      41.292  48.452  20.043  1.00 27.10           C  
ATOM    112  CG  MET A  16      42.387  49.357  20.667  1.00 35.23           C  
ATOM    113  SD  MET A  16      41.766  50.334  22.099  1.00 46.30           S  
ATOM    114  CE  MET A  16      43.099  51.460  22.589  1.00 51.59           C  
ATOM    115  N   GLU A  17      40.567  51.637  19.027  1.00 16.62           N  
ATOM    116  CA  GLU A  17      41.065  52.668  18.104  1.00 33.18           C  
ATOM    117  C   GLU A  17      40.525  52.635  16.679  1.00 37.15           C  
ATOM    118  O   GLU A  17      41.318  52.801  15.748  1.00 33.65           O  
ATOM    119  CB  GLU A  17      42.587  52.717  18.079  1.00 29.31           C  
ATOM    120  CG  GLU A  17      42.917  53.112  19.509  1.00 49.59           C  
ATOM    121  CD  GLU A  17      44.357  53.067  19.874  1.00 67.50           C  
ATOM    122  OE1 GLU A  17      45.216  52.445  19.272  1.00 67.59           O  
ATOM    123  OE2 GLU A  17      44.553  53.711  20.991  1.00 80.28           O  
ATOM    124  N   ASN A  18      39.198  52.383  16.549  1.00 30.83           N  
ATOM    125  CA  ASN A  18      38.505  52.320  15.276  1.00 31.37           C  
ATOM    126  C   ASN A  18      38.934  51.201  14.330  1.00 32.62           C  
ATOM    127  O   ASN A  18      38.890  51.361  13.092  1.00 36.84           O  
ATOM    128  CB  ASN A  18      38.428  53.683  14.561  1.00 35.53           C  
ATOM    129  CG  ASN A  18      37.245  53.925  13.651  1.00 32.53           C  
ATOM    130  OD1 ASN A  18      37.410  54.339  12.483  1.00 31.48           O  
ATOM    131  ND2 ASN A  18      36.058  53.847  14.244  1.00 32.33           N  
ATOM    132  N   ALA A  19      39.318  50.079  14.905  1.00 24.58           N  
ATOM    133  CA  ALA A  19      39.717  48.947  14.097  1.00 25.52           C  
ATOM    134  C   ALA A  19      39.507  47.649  14.892  1.00 28.29           C  
ATOM    135  O   ALA A  19      39.262  47.690  16.094  1.00 35.60           O  
ATOM    136  CB  ALA A  19      41.181  49.076  13.726  1.00 28.25           C  
ATOM    137  N   MET A  20      39.610  46.499  14.223  1.00 26.45           N  
ATOM    138  CA  MET A  20      39.432  45.222  14.902  1.00 27.94           C  
ATOM    139  C   MET A  20      40.788  44.601  14.909  1.00 27.18           C  
ATOM    140  O   MET A  20      41.266  44.299  13.834  1.00 39.67           O  
ATOM    141  CB  MET A  20      38.395  44.363  14.162  1.00 37.49           C  
ATOM    142  CG  MET A  20      37.070  45.125  14.106  1.00 39.52           C  
ATOM    143  SD  MET A  20      35.698  44.221  13.383  1.00 33.42           S  
ATOM    144  CE  MET A  20      36.482  43.890  11.765  1.00 30.79           C  
ATOM    145  N   PRO A  21      41.408  44.426  16.092  1.00 28.14           N  
ATOM    146  CA  PRO A  21      42.751  43.856  16.182  1.00 38.06           C  
ATOM    147  C   PRO A  21      43.011  42.502  15.521  1.00 44.25           C  
ATOM    148  O   PRO A  21      44.088  42.283  14.919  1.00 48.82           O  
ATOM    149  CB  PRO A  21      43.132  43.843  17.653  1.00 33.26           C  
ATOM    150  CG  PRO A  21      41.959  44.429  18.413  1.00 31.85           C  
ATOM    151  CD  PRO A  21      40.830  44.627  17.436  1.00 24.02           C  
ATOM    152  N   TRP A  22      42.035  41.587  15.614  1.00 34.95           N  
ATOM    153  CA  TRP A  22      42.209  40.264  15.025  1.00 30.20           C  
ATOM    154  C   TRP A  22      41.945  40.181  13.543  1.00 39.45           C  
ATOM    155  O   TRP A  22      41.479  41.123  12.893  1.00 40.58           O  
ATOM    156  CB  TRP A  22      41.278  39.291  15.702  1.00 21.28           C  
ATOM    157  CG  TRP A  22      39.878  39.740  15.472  1.00 22.13           C  
ATOM    158  CD1 TRP A  22      39.139  39.473  14.368  1.00 20.98           C  
ATOM    159  CD2 TRP A  22      39.025  40.542  16.348  1.00 20.83           C  
ATOM    160  NE1 TRP A  22      37.884  40.017  14.507  1.00 13.86           N  
ATOM    161  CE2 TRP A  22      37.791  40.688  15.706  1.00 14.89           C  
ATOM    162  CE3 TRP A  22      39.184  41.126  17.612  1.00 16.14           C  
ATOM    163  CZ2 TRP A  22      36.715  41.390  16.282  1.00 18.28           C  
ATOM    164  CZ3 TRP A  22      38.124  41.813  18.193  1.00 20.97           C  
ATOM    165  CH2 TRP A  22      36.899  41.934  17.534  1.00 26.64           C  
ATOM    166  N   ASN A  23      42.249  38.990  13.024  1.00 40.56           N  
ATOM    167  CA  ASN A  23      42.052  38.688  11.628  1.00 37.41           C  
ATOM    168  C   ASN A  23      41.544  37.264  11.546  1.00 32.29           C  
ATOM    169  O   ASN A  23      42.207  36.275  11.864  1.00 27.79           O  
ATOM    170  CB  ASN A  23      43.290  39.023  10.775  1.00 43.34           C  
ATOM    171  CG  ASN A  23      43.360  38.321   9.454  1.00 47.69           C  
ATOM    172  OD1 ASN A  23      42.763  38.740   8.457  1.00 57.53           O  
ATOM    173  ND2 ASN A  23      44.233  37.331   9.402  1.00 48.04           N  
ATOM    174  N   LEU A  24      40.296  37.145  11.143  1.00 18.29           N  
ATOM    175  CA  LEU A  24      39.713  35.818  11.062  1.00 14.31           C  
ATOM    176  C   LEU A  24      38.894  35.747   9.834  1.00 13.70           C  
ATOM    177  O   LEU A  24      37.696  36.147   9.861  1.00 18.92           O  
ATOM    178  CB  LEU A  24      38.695  35.579  12.182  1.00 16.23           C  
ATOM    179  CG  LEU A  24      39.260  35.518  13.560  1.00 21.63           C  
ATOM    180  CD1 LEU A  24      38.053  35.061  14.351  1.00 30.27           C  
ATOM    181  CD2 LEU A  24      40.357  34.444  13.767  1.00 12.11           C  
ATOM    182  N   PRO A  25      39.577  35.249   8.810  1.00 10.24           N  
ATOM    183  CA  PRO A  25      39.034  35.051   7.504  1.00 13.93           C  
ATOM    184  C   PRO A  25      37.703  34.289   7.514  1.00 15.29           C  
ATOM    185  O   PRO A  25      36.741  34.605   6.738  1.00 15.58           O  
ATOM    186  CB  PRO A  25      40.136  34.333   6.661  1.00 13.43           C  
ATOM    187  CG  PRO A  25      41.434  34.560   7.428  1.00 14.76           C  
ATOM    188  CD  PRO A  25      41.016  34.930   8.874  1.00 15.37           C  
ATOM    189  N   ALA A  26      37.590  33.275   8.391  1.00  9.06           N  
ATOM    190  CA  ALA A  26      36.304  32.571   8.385  1.00  3.58           C  
ATOM    191  C   ALA A  26      35.122  33.432   8.880  1.00 11.61           C  
ATOM    192  O   ALA A  26      33.997  33.262   8.477  1.00 15.55           O  
ATOM    193  CB  ALA A  26      36.338  31.437   9.410  1.00  8.95           C  
ATOM    194  N   ASP A  27      35.379  34.328   9.820  1.00 10.50           N  
ATOM    195  CA  ASP A  27      34.362  35.188  10.421  1.00  5.47           C  
ATOM    196  C   ASP A  27      33.901  36.196   9.382  1.00 12.02           C  
ATOM    197  O   ASP A  27      32.728  36.508   9.278  1.00 13.60           O  
ATOM    198  CB  ASP A  27      34.845  35.811  11.705  1.00 10.39           C  
ATOM    199  CG  ASP A  27      33.755  36.765  12.201  1.00 16.13           C  
ATOM    200  OD1 ASP A  27      32.582  36.468  12.240  1.00 13.17           O  
ATOM    201  OD2 ASP A  27      34.159  38.006  12.403  1.00 17.53           O  
ATOM    202  N   LEU A  28      34.857  36.717   8.576  1.00  6.85           N  
ATOM    203  CA  LEU A  28      34.482  37.619   7.557  1.00 16.12           C  
ATOM    204  C   LEU A  28      33.712  36.884   6.464  1.00 22.22           C  
ATOM    205  O   LEU A  28      32.908  37.504   5.739  1.00 17.15           O  
ATOM    206  CB  LEU A  28      35.655  38.346   6.954  1.00 23.60           C  
ATOM    207  CG  LEU A  28      36.010  39.512   7.845  1.00 36.88           C  
ATOM    208  CD1 LEU A  28      36.996  40.325   7.088  1.00 42.32           C  
ATOM    209  CD2 LEU A  28      34.780  40.375   8.122  1.00 44.55           C  
ATOM    210  N   ALA A  29      33.928  35.566   6.337  1.00 13.51           N  
ATOM    211  CA  ALA A  29      33.147  34.981   5.298  1.00 15.89           C  
ATOM    212  C   ALA A  29      31.689  34.855   5.771  1.00 11.26           C  
ATOM    213  O   ALA A  29      30.672  34.954   5.031  1.00 18.73           O  
ATOM    214  CB  ALA A  29      33.737  33.596   5.070  1.00 17.41           C  
ATOM    215  N   TRP A  30      31.589  34.606   7.063  1.00  7.64           N  
ATOM    216  CA  TRP A  30      30.304  34.444   7.650  1.00  7.04           C  
ATOM    217  C   TRP A  30      29.555  35.742   7.628  1.00  8.59           C  
ATOM    218  O   TRP A  30      28.375  35.713   7.362  1.00 11.33           O  
ATOM    219  CB  TRP A  30      30.449  33.879   9.072  1.00  8.21           C  
ATOM    220  CG  TRP A  30      29.400  34.171  10.088  1.00  9.12           C  
ATOM    221  CD1 TRP A  30      29.385  35.248  10.889  1.00  8.16           C  
ATOM    222  CD2 TRP A  30      28.334  33.340  10.523  1.00  8.07           C  
ATOM    223  NE1 TRP A  30      28.344  35.185  11.796  1.00 10.23           N  
ATOM    224  CE2 TRP A  30      27.676  33.997  11.583  1.00  9.49           C  
ATOM    225  CE3 TRP A  30      27.856  32.077  10.094  1.00 17.34           C  
ATOM    226  CZ2 TRP A  30      26.530  33.468  12.227  1.00 14.98           C  
ATOM    227  CZ3 TRP A  30      26.734  31.548  10.740  1.00 13.37           C  
ATOM    228  CH2 TRP A  30      26.067  32.221  11.808  1.00 15.97           C  
ATOM    229  N   PHE A  31      30.247  36.837   7.915  1.00  8.65           N  
ATOM    230  CA  PHE A  31      29.632  38.186   7.894  1.00  8.22           C  
ATOM    231  C   PHE A  31      29.036  38.499   6.489  1.00  9.24           C  
ATOM    232  O   PHE A  31      27.884  38.862   6.349  1.00 11.89           O  
ATOM    233  CB  PHE A  31      30.728  39.258   8.192  1.00 13.09           C  
ATOM    234  CG  PHE A  31      30.250  40.676   7.964  1.00 12.75           C  
ATOM    235  CD1 PHE A  31      29.558  41.362   8.972  1.00 10.96           C  
ATOM    236  CD2 PHE A  31      30.456  41.311   6.723  1.00 10.66           C  
ATOM    237  CE1 PHE A  31      29.118  42.664   8.722  1.00 11.74           C  
ATOM    238  CE2 PHE A  31      30.032  42.613   6.449  1.00  8.97           C  
ATOM    239  CZ  PHE A  31      29.343  43.269   7.481  1.00  5.52           C  
ATOM    240  N   LYS A  32      29.846  38.325   5.441  1.00 10.16           N  
ATOM    241  CA  LYS A  32      29.408  38.568   4.064  1.00  8.48           C  
ATOM    242  C   LYS A  32      28.199  37.724   3.705  1.00 14.49           C  
ATOM    243  O   LYS A  32      27.241  38.188   3.082  1.00 17.12           O  
ATOM    244  CB  LYS A  32      30.553  38.088   3.200  1.00 18.29           C  
ATOM    245  CG  LYS A  32      30.386  38.456   1.732  1.00 30.57           C  
ATOM    246  CD  LYS A  32      31.297  37.630   0.842  1.00 34.62           C  
ATOM    247  CE  LYS A  32      31.409  38.245  -0.523  1.00 49.69           C  
ATOM    248  NZ  LYS A  32      30.092  38.773  -0.892  1.00 58.04           N  
ATOM    249  N   ARG A  33      28.275  36.431   4.083  1.00 18.00           N  
ATOM    250  CA  ARG A  33      27.213  35.473   3.805  1.00 16.06           C  
ATOM    251  C   ARG A  33      25.853  35.853   4.386  1.00 19.86           C  
ATOM    252  O   ARG A  33      24.784  35.662   3.764  1.00 17.30           O  
ATOM    253  CB  ARG A  33      27.627  34.091   4.235  1.00 30.16           C  
ATOM    254  CG  ARG A  33      26.551  33.021   4.206  1.00 45.40           C  
ATOM    255  CD  ARG A  33      26.986  31.832   5.063  1.00 58.57           C  
ATOM    256  NE  ARG A  33      25.905  30.886   5.301  1.00 77.52           N  
ATOM    257  CZ  ARG A  33      25.948  29.761   6.045  1.00 89.33           C  
ATOM    258  NH1 ARG A  33      27.036  29.321   6.697  1.00 93.34           N  
ATOM    259  NH2 ARG A  33      24.833  29.033   6.131  1.00 92.42           N  
ATOM    260  N   ASN A  34      25.912  36.393   5.579  1.00 11.19           N  
ATOM    261  CA  ASN A  34      24.707  36.771   6.293  1.00 13.53           C  
ATOM    262  C   ASN A  34      24.187  38.117   5.963  1.00  7.86           C  
ATOM    263  O   ASN A  34      23.055  38.442   6.214  1.00  8.58           O  
ATOM    264  CB  ASN A  34      24.982  36.654   7.804  1.00 12.07           C  
ATOM    265  CG  ASN A  34      24.996  35.154   8.249  1.00 13.97           C  
ATOM    266  OD1 ASN A  34      23.977  34.449   8.122  1.00 13.68           O  
ATOM    267  ND2 ASN A  34      26.113  34.678   8.812  1.00 12.65           N  
ATOM    268  N   THR A  35      25.014  38.893   5.358  1.00  8.68           N  
ATOM    269  CA  THR A  35      24.590  40.269   5.012  1.00  7.56           C  
ATOM    270  C   THR A  35      24.398  40.567   3.547  1.00  8.15           C  
ATOM    271  O   THR A  35      23.753  41.529   3.185  1.00 10.35           O  
ATOM    272  CB  THR A  35      25.622  41.310   5.600  1.00 12.50           C  
ATOM    273  OG1 THR A  35      26.861  41.195   4.896  1.00 10.88           O  
ATOM    274  CG2 THR A  35      25.819  41.155   7.116  1.00 10.23           C  
ATOM    275  N   LEU A  36      24.947  39.753   2.700  1.00 10.71           N  
ATOM    276  CA  LEU A  36      24.803  39.969   1.269  1.00 11.53           C  
ATOM    277  C   LEU A  36      23.335  40.024   0.849  1.00  7.95           C  
ATOM    278  O   LEU A  36      22.497  39.263   1.333  1.00  9.73           O  
ATOM    279  CB  LEU A  36      25.586  38.859   0.567  1.00 18.11           C  
ATOM    280  CG  LEU A  36      26.010  39.216  -0.823  1.00 25.81           C  
ATOM    281  CD1 LEU A  36      27.307  40.010  -0.776  1.00 28.83           C  
ATOM    282  CD2 LEU A  36      26.197  37.895  -1.563  1.00 22.52           C  
ATOM    283  N   ASP A  37      23.031  40.963  -0.044  1.00 12.24           N  
ATOM    284  CA  ASP A  37      21.676  41.230  -0.608  1.00  6.99           C  
ATOM    285  C   ASP A  37      20.679  41.774   0.342  1.00 14.12           C  
ATOM    286  O   ASP A  37      19.490  41.696   0.078  1.00 16.48           O  
ATOM    287  CB  ASP A  37      21.127  40.041  -1.319  1.00 15.54           C  
ATOM    288  CG  ASP A  37      22.002  39.692  -2.506  1.00 26.66           C  
ATOM    289  OD1 ASP A  37      22.304  40.472  -3.371  1.00 25.79           O  
ATOM    290  OD2 ASP A  37      22.361  38.438  -2.560  1.00 34.74           O  
ATOM    291  N   LYS A  38      21.172  42.302   1.474  1.00 11.33           N  
ATOM    292  CA  LYS A  38      20.348  42.895   2.510  1.00  6.25           C  
ATOM    293  C   LYS A  38      20.938  44.291   2.758  1.00 14.71           C  
ATOM    294  O   LYS A  38      22.101  44.611   2.418  1.00 11.37           O  
ATOM    295  CB  LYS A  38      20.476  42.128   3.840  1.00  7.06           C  
ATOM    296  CG  LYS A  38      20.135  40.705   3.621  1.00  5.31           C  
ATOM    297  CD  LYS A  38      20.135  40.014   4.961  1.00  5.39           C  
ATOM    298  CE  LYS A  38      20.036  38.487   4.840  1.00 11.48           C  
ATOM    299  NZ  LYS A  38      20.422  37.721   6.081  1.00 10.51           N  
ATOM    300  N   PRO A  39      20.129  45.138   3.402  1.00 17.10           N  
ATOM    301  CA  PRO A  39      20.631  46.472   3.696  1.00 10.08           C  
ATOM    302  C   PRO A  39      21.448  46.410   4.949  1.00  6.36           C  
ATOM    303  O   PRO A  39      21.067  45.723   5.840  1.00  9.23           O  
ATOM    304  CB  PRO A  39      19.403  47.365   4.018  1.00  9.18           C  
ATOM    305  CG  PRO A  39      18.163  46.489   3.913  1.00 13.59           C  
ATOM    306  CD  PRO A  39      18.637  45.065   3.506  1.00 17.70           C  
ATOM    307  N   VAL A  40      22.519  47.192   5.024  1.00 10.79           N  
ATOM    308  CA  VAL A  40      23.302  47.175   6.244  1.00  6.33           C  
ATOM    309  C   VAL A  40      23.348  48.627   6.835  1.00 12.93           C  
ATOM    310  O   VAL A  40      23.610  49.633   6.112  1.00  9.36           O  
ATOM    311  CB  VAL A  40      24.752  46.746   5.970  1.00  8.52           C  
ATOM    312  CG1 VAL A  40      24.712  45.324   5.398  1.00  9.12           C  
ATOM    313  CG2 VAL A  40      25.502  47.678   4.980  1.00 11.07           C  
ATOM    314  N   ILE A  41      23.099  48.746   8.140  1.00  7.65           N  
ATOM    315  CA  ILE A  41      23.145  50.075   8.756  1.00  6.74           C  
ATOM    316  C   ILE A  41      24.363  50.153   9.602  1.00  7.79           C  
ATOM    317  O   ILE A  41      24.616  49.181  10.333  1.00 13.64           O  
ATOM    318  CB  ILE A  41      21.933  50.194   9.665  1.00  8.57           C  
ATOM    319  CG1 ILE A  41      20.705  50.270   8.717  1.00  8.11           C  
ATOM    320  CG2 ILE A  41      22.103  51.495  10.440  1.00  9.75           C  
ATOM    321  CD1 ILE A  41      19.346  50.052   9.424  1.00  7.11           C  
ATOM    322  N   MET A  42      25.085  51.273   9.522  1.00 10.18           N  
ATOM    323  CA  MET A  42      26.282  51.397  10.334  1.00  8.97           C  
ATOM    324  C   MET A  42      26.456  52.837  10.806  1.00 12.11           C  
ATOM    325  O   MET A  42      25.882  53.806  10.220  1.00  6.57           O  
ATOM    326  CB  MET A  42      27.538  50.944   9.591  1.00  5.13           C  
ATOM    327  CG  MET A  42      28.098  51.999   8.639  1.00  8.81           C  
ATOM    328  SD  MET A  42      29.156  51.275   7.372  1.00 13.71           S  
ATOM    329  CE  MET A  42      27.897  50.757   6.206  1.00 18.26           C  
ATOM    330  N   GLY A  43      27.249  52.943  11.845  1.00  5.10           N  
ATOM    331  CA  GLY A  43      27.477  54.304  12.355  1.00  6.36           C  
ATOM    332  C   GLY A  43      28.647  54.951  11.584  1.00 19.08           C  
ATOM    333  O   GLY A  43      29.433  54.260  10.867  1.00 10.29           O  
ATOM    334  N   ARG A  44      28.778  56.279  11.735  1.00 14.25           N  
ATOM    335  CA  ARG A  44      29.829  56.959  11.039  1.00 25.17           C  
ATOM    336  C   ARG A  44      31.260  56.418  11.307  1.00 13.97           C  
ATOM    337  O   ARG A  44      32.105  56.354  10.358  1.00 12.80           O  
ATOM    338  CB  ARG A  44      29.775  58.457  11.341  1.00 34.30           C  
ATOM    339  CG  ARG A  44      30.167  59.290  10.111  1.00 42.43           C  
ATOM    340  CD  ARG A  44      31.304  60.237  10.410  1.00 38.66           C  
ATOM    341  NE  ARG A  44      31.195  60.753  11.763  1.00 49.37           N  
ATOM    342  CZ  ARG A  44      32.204  61.104  12.560  1.00 60.31           C  
ATOM    343  NH1 ARG A  44      33.482  61.009  12.200  1.00 59.90           N  
ATOM    344  NH2 ARG A  44      31.903  61.566  13.774  1.00 70.11           N  
ATOM    345  N   HIS A  45      31.537  56.032  12.587  1.00 10.14           N  
ATOM    346  CA  HIS A  45      32.887  55.561  12.820  1.00 11.86           C  
ATOM    347  C   HIS A  45      33.168  54.313  12.078  1.00 15.57           C  
ATOM    348  O   HIS A  45      34.242  54.178  11.533  1.00 14.93           O  
ATOM    349  CB  HIS A  45      33.329  55.334  14.256  1.00 16.74           C  
ATOM    350  CG  HIS A  45      33.298  56.614  15.001  1.00 29.52           C  
ATOM    351  ND1 HIS A  45      32.536  56.751  16.149  1.00 37.40           N  
ATOM    352  CD2 HIS A  45      33.925  57.779  14.728  1.00 33.20           C  
ATOM    353  CE1 HIS A  45      32.702  57.984  16.554  1.00 38.06           C  
ATOM    354  NE2 HIS A  45      33.530  58.617  15.724  1.00 40.45           N  
ATOM    355  N   THR A  46      32.178  53.445  12.080  1.00 16.93           N  
ATOM    356  CA  THR A  46      32.304  52.169  11.403  1.00 13.05           C  
ATOM    357  C   THR A  46      32.508  52.367   9.929  1.00 14.56           C  
ATOM    358  O   THR A  46      33.366  51.697   9.304  1.00 14.22           O  
ATOM    359  CB  THR A  46      31.091  51.287  11.779  1.00  8.99           C  
ATOM    360  OG1 THR A  46      31.230  51.096  13.156  1.00  7.33           O  
ATOM    361  CG2 THR A  46      31.084  49.882  11.089  1.00  9.76           C  
ATOM    362  N   TRP A  47      31.723  53.295   9.355  1.00 13.70           N  
ATOM    363  CA  TRP A  47      31.868  53.576   7.918  1.00 10.72           C  
ATOM    364  C   TRP A  47      33.312  53.931   7.579  1.00 14.26           C  
ATOM    365  O   TRP A  47      33.930  53.579   6.578  1.00 17.70           O  
ATOM    366  CB  TRP A  47      30.998  54.765   7.604  1.00  5.35           C  
ATOM    367  CG  TRP A  47      31.265  55.335   6.296  1.00  6.57           C  
ATOM    368  CD1 TRP A  47      31.579  56.636   6.262  1.00 18.94           C  
ATOM    369  CD2 TRP A  47      31.293  54.859   4.930  1.00 12.89           C  
ATOM    370  NE1 TRP A  47      31.822  57.044   5.001  1.00 15.89           N  
ATOM    371  CE2 TRP A  47      31.661  55.972   4.144  1.00 14.07           C  
ATOM    372  CE3 TRP A  47      31.139  53.635   4.220  1.00 14.74           C  
ATOM    373  CZ2 TRP A  47      31.817  55.930   2.733  1.00 15.64           C  
ATOM    374  CZ3 TRP A  47      31.274  53.610   2.828  1.00 20.80           C  
ATOM    375  CH2 TRP A  47      31.625  54.742   2.055  1.00 15.30           C  
ATOM    376  N   GLU A  48      33.861  54.656   8.488  1.00 12.51           N  
ATOM    377  CA  GLU A  48      35.214  55.072   8.359  1.00 17.55           C  
ATOM    378  C   GLU A  48      36.196  53.937   8.534  1.00 21.93           C  
ATOM    379  O   GLU A  48      37.163  53.937   7.793  1.00 16.86           O  
ATOM    380  CB  GLU A  48      35.503  56.293   9.261  1.00 18.24           C  
ATOM    381  CG  GLU A  48      34.720  57.548   8.740  1.00 32.40           C  
ATOM    382  CD  GLU A  48      34.877  58.792   9.600  1.00 53.93           C  
ATOM    383  OE1 GLU A  48      35.470  58.795  10.672  1.00 61.12           O  
ATOM    384  OE2 GLU A  48      34.321  59.875   9.084  1.00 56.64           O  
ATOM    385  N   SER A  49      36.008  52.976   9.475  1.00 19.49           N  
ATOM    386  CA  SER A  49      37.010  51.966   9.543  1.00 15.35           C  
ATOM    387  C   SER A  49      36.934  51.066   8.338  1.00 26.77           C  
ATOM    388  O   SER A  49      37.911  50.519   7.898  1.00 33.42           O  
ATOM    389  CB  SER A  49      37.157  51.211  10.822  1.00 23.81           C  
ATOM    390  OG  SER A  49      35.902  50.949  11.281  1.00 30.62           O  
ATOM    391  N   ILE A  50      35.753  50.912   7.795  1.00 26.44           N  
ATOM    392  CA  ILE A  50      35.530  50.068   6.657  1.00 21.12           C  
ATOM    393  C   ILE A  50      36.120  50.603   5.401  1.00 29.49           C  
ATOM    394  O   ILE A  50      36.527  49.869   4.456  1.00 34.38           O  
ATOM    395  CB  ILE A  50      34.082  49.904   6.469  1.00 30.73           C  
ATOM    396  CG1 ILE A  50      33.613  49.089   7.664  1.00 35.46           C  
ATOM    397  CG2 ILE A  50      33.910  49.149   5.172  1.00 28.23           C  
ATOM    398  CD1 ILE A  50      32.163  48.667   7.542  1.00 36.73           C  
ATOM    399  N   GLY A  51      36.151  51.921   5.385  1.00 24.66           N  
ATOM    400  CA  GLY A  51      36.760  52.618   4.257  1.00 23.59           C  
ATOM    401  C   GLY A  51      36.206  52.562   2.872  1.00 27.42           C  
ATOM    402  O   GLY A  51      36.843  53.154   1.998  1.00 28.85           O  
ATOM    403  N   ARG A  52      35.076  51.892   2.627  1.00 22.95           N  
ATOM    404  CA  ARG A  52      34.461  51.836   1.264  1.00 18.28           C  
ATOM    405  C   ARG A  52      33.134  51.135   1.325  1.00 13.93           C  
ATOM    406  O   ARG A  52      32.829  50.487   2.360  1.00 14.86           O  
ATOM    407  CB  ARG A  52      35.263  51.256   0.102  1.00 32.88           C  
ATOM    408  CG  ARG A  52      36.213  50.191   0.583  1.00 48.51           C  
ATOM    409  CD  ARG A  52      36.333  48.984  -0.345  1.00 66.01           C  
ATOM    410  NE  ARG A  52      35.615  47.801   0.158  1.00 80.69           N  
ATOM    411  CZ  ARG A  52      36.075  46.984   1.128  1.00 87.67           C  
ATOM    412  NH1 ARG A  52      37.260  47.178   1.741  1.00 93.57           N  
ATOM    413  NH2 ARG A  52      35.326  45.936   1.494  1.00 82.19           N  
ATOM    414  N   PRO A  53      32.362  51.322   0.281  1.00 19.99           N  
ATOM    415  CA  PRO A  53      31.055  50.690   0.240  1.00 17.12           C  
ATOM    416  C   PRO A  53      31.176  49.141   0.156  1.00 19.23           C  
ATOM    417  O   PRO A  53      32.052  48.589  -0.557  1.00 17.43           O  
ATOM    418  CB  PRO A  53      30.265  51.321  -0.932  1.00 21.44           C  
ATOM    419  CG  PRO A  53      31.206  52.376  -1.546  1.00 24.90           C  
ATOM    420  CD  PRO A  53      32.577  52.231  -0.885  1.00 20.31           C  
ATOM    421  N   LEU A  54      30.302  48.463   0.903  1.00 11.64           N  
ATOM    422  CA  LEU A  54      30.254  46.996   0.925  1.00  7.84           C  
ATOM    423  C   LEU A  54      29.414  46.636  -0.284  1.00  5.95           C  
ATOM    424  O   LEU A  54      28.274  46.989  -0.416  1.00 14.63           O  
ATOM    425  CB  LEU A  54      29.500  46.375   2.165  1.00  7.43           C  
ATOM    426  CG  LEU A  54      30.242  46.549   3.473  1.00 10.40           C  
ATOM    427  CD1 LEU A  54      29.415  45.885   4.637  1.00 16.05           C  
ATOM    428  CD2 LEU A  54      31.564  45.750   3.318  1.00 18.23           C  
ATOM    429  N   PRO A  55      29.955  45.885  -1.202  1.00  9.26           N  
ATOM    430  CA  PRO A  55      29.224  45.517  -2.385  1.00 11.74           C  
ATOM    431  C   PRO A  55      28.147  44.593  -2.172  1.00 10.68           C  
ATOM    432  O   PRO A  55      28.181  43.794  -1.245  1.00 15.83           O  
ATOM    433  CB  PRO A  55      30.190  44.708  -3.209  1.00 17.79           C  
ATOM    434  CG  PRO A  55      31.529  44.684  -2.505  1.00 14.11           C  
ATOM    435  CD  PRO A  55      31.372  45.537  -1.233  1.00 11.93           C  
ATOM    436  N   GLY A  56      27.170  44.683  -3.022  1.00  9.04           N  
ATOM    437  CA  GLY A  56      25.944  43.804  -2.988  1.00 10.98           C  
ATOM    438  C   GLY A  56      24.949  44.026  -1.863  1.00 17.90           C  
ATOM    439  O   GLY A  56      24.092  43.154  -1.599  1.00 16.26           O  
ATOM    440  N   ARG A  57      25.086  45.204  -1.199  1.00 11.59           N  
ATOM    441  CA  ARG A  57      24.240  45.595  -0.072  1.00 13.74           C  
ATOM    442  C   ARG A  57      24.037  47.086  -0.139  1.00 15.28           C  
ATOM    443  O   ARG A  57      24.931  47.852  -0.594  1.00 14.87           O  
ATOM    444  CB  ARG A  57      24.974  45.316   1.264  1.00 13.55           C  
ATOM    445  CG  ARG A  57      25.131  43.820   1.521  1.00 15.23           C  
ATOM    446  CD  ARG A  57      26.331  43.402   2.372  1.00  8.44           C  
ATOM    447  NE  ARG A  57      27.456  43.320   1.469  1.00 10.24           N  
ATOM    448  CZ  ARG A  57      28.631  42.806   1.825  1.00 12.74           C  
ATOM    449  NH1 ARG A  57      28.832  42.283   3.062  1.00  7.85           N  
ATOM    450  NH2 ARG A  57      29.612  42.777   0.927  1.00  7.10           N  
ATOM    451  N   LYS A  58      22.873  47.486   0.334  1.00 10.29           N  
ATOM    452  CA  LYS A  58      22.592  48.895   0.351  1.00 13.07           C  
ATOM    453  C   LYS A  58      23.258  49.386   1.640  1.00 13.90           C  
ATOM    454  O   LYS A  58      22.939  48.939   2.697  1.00  8.22           O  
ATOM    455  CB  LYS A  58      21.096  49.014   0.396  1.00  5.74           C  
ATOM    456  CG  LYS A  58      20.651  50.433   0.132  1.00 15.68           C  
ATOM    457  CD  LYS A  58      19.145  50.569   0.281  1.00 16.95           C  
ATOM    458  CE  LYS A  58      18.652  51.970   0.570  1.00 27.63           C  
ATOM    459  NZ  LYS A  58      17.252  52.179   0.150  1.00 33.00           N  
ATOM    460  N   ASN A  59      24.217  50.246   1.589  1.00 10.48           N  
ATOM    461  CA  ASN A  59      24.890  50.731   2.764  1.00  6.62           C  
ATOM    462  C   ASN A  59      24.226  52.027   3.235  1.00  7.87           C  
ATOM    463  O   ASN A  59      24.103  53.002   2.460  1.00  8.33           O  
ATOM    464  CB  ASN A  59      26.352  51.042   2.503  1.00 10.15           C  
ATOM    465  CG  ASN A  59      27.179  49.903   1.999  1.00 11.68           C  
ATOM    466  OD1 ASN A  59      28.353  49.786   2.380  1.00 16.30           O  
ATOM    467  ND2 ASN A  59      26.601  49.096   1.081  1.00 13.76           N  
ATOM    468  N   ILE A  60      23.811  52.038   4.487  1.00 11.62           N  
ATOM    469  CA  ILE A  60      23.158  53.185   5.126  1.00  3.13           C  
ATOM    470  C   ILE A  60      24.009  53.642   6.273  1.00  9.33           C  
ATOM    471  O   ILE A  60      24.315  52.879   7.206  1.00  7.38           O  
ATOM    472  CB  ILE A  60      21.817  52.748   5.612  1.00  3.47           C  
ATOM    473  CG1 ILE A  60      21.019  52.476   4.355  1.00 10.43           C  
ATOM    474  CG2 ILE A  60      21.008  53.835   6.379  1.00  8.45           C  
ATOM    475  CD1 ILE A  60      19.778  51.606   4.618  1.00 13.37           C  
ATOM    476  N   ILE A  61      24.417  54.906   6.223  1.00 12.47           N  
ATOM    477  CA  ILE A  61      25.235  55.374   7.336  1.00  7.34           C  
ATOM    478  C   ILE A  61      24.484  56.393   8.166  1.00  9.35           C  
ATOM    479  O   ILE A  61      23.866  57.297   7.571  1.00  7.69           O  
ATOM    480  CB  ILE A  61      26.391  56.200   6.796  1.00  7.48           C  
ATOM    481  CG1 ILE A  61      26.922  55.608   5.519  1.00 10.44           C  
ATOM    482  CG2 ILE A  61      27.434  56.418   7.893  1.00  7.10           C  
ATOM    483  CD1 ILE A  61      27.315  54.162   5.606  1.00 12.28           C  
ATOM    484  N   LEU A  62      24.597  56.214   9.486  1.00  6.42           N  
ATOM    485  CA  LEU A  62      23.976  57.130  10.478  1.00  7.82           C  
ATOM    486  C   LEU A  62      25.006  58.227  10.889  1.00 20.96           C  
ATOM    487  O   LEU A  62      26.122  57.905  11.377  1.00 15.90           O  
ATOM    488  CB  LEU A  62      23.488  56.472  11.805  1.00 21.33           C  
ATOM    489  CG  LEU A  62      21.986  56.145  11.844  1.00 25.74           C  
ATOM    490  CD1 LEU A  62      21.688  54.927  12.701  1.00 22.90           C  
ATOM    491  CD2 LEU A  62      21.199  57.349  12.402  1.00 26.96           C  
ATOM    492  N   SER A  63      24.625  59.541  10.694  1.00  6.80           N  
ATOM    493  CA  SER A  63      25.525  60.591  11.098  1.00  8.51           C  
ATOM    494  C   SER A  63      24.626  61.789  11.301  1.00 18.65           C  
ATOM    495  O   SER A  63      23.636  61.932  10.572  1.00 17.63           O  
ATOM    496  CB  SER A  63      26.518  60.925   9.996  1.00 15.99           C  
ATOM    497  OG  SER A  63      27.544  61.819  10.495  1.00 27.83           O  
ATOM    498  N   SER A  64      25.010  62.631  12.271  1.00 20.92           N  
ATOM    499  CA  SER A  64      24.265  63.865  12.560  1.00 19.98           C  
ATOM    500  C   SER A  64      24.709  64.940  11.507  1.00 29.44           C  
ATOM    501  O   SER A  64      24.049  65.958  11.249  1.00 28.11           O  
ATOM    502  CB  SER A  64      24.504  64.332  13.979  1.00 12.11           C  
ATOM    503  OG  SER A  64      25.878  64.666  14.170  1.00 21.92           O  
ATOM    504  N   GLN A  65      25.859  64.671  10.873  1.00 30.33           N  
ATOM    505  CA  GLN A  65      26.437  65.523   9.838  1.00 36.78           C  
ATOM    506  C   GLN A  65      25.982  65.101   8.457  1.00 38.11           C  
ATOM    507  O   GLN A  65      25.750  63.931   8.162  1.00 31.40           O  
ATOM    508  CB  GLN A  65      27.963  65.410   9.774  1.00 50.76           C  
ATOM    509  CG  GLN A  65      28.625  66.597  10.456  1.00 67.62           C  
ATOM    510  CD  GLN A  65      27.916  66.840  11.747  1.00 73.16           C  
ATOM    511  OE1 GLN A  65      27.660  65.884  12.474  1.00 77.01           O  
ATOM    512  NE2 GLN A  65      27.469  68.076  11.954  1.00 76.82           N  
ATOM    513  N   PRO A  66      25.893  66.066   7.581  1.00 40.16           N  
ATOM    514  CA  PRO A  66      25.492  65.787   6.242  1.00 39.26           C  
ATOM    515  C   PRO A  66      26.475  64.816   5.528  1.00 34.03           C  
ATOM    516  O   PRO A  66      27.664  64.781   5.866  1.00 27.36           O  
ATOM    517  CB  PRO A  66      25.469  67.173   5.572  1.00 48.36           C  
ATOM    518  CG  PRO A  66      26.034  68.196   6.546  1.00 50.40           C  
ATOM    519  CD  PRO A  66      26.470  67.426   7.759  1.00 47.37           C  
ATOM    520  N   GLY A  67      25.983  64.034   4.520  1.00 24.26           N  
ATOM    521  CA  GLY A  67      26.781  63.070   3.735  1.00 16.27           C  
ATOM    522  C   GLY A  67      27.959  63.669   2.989  1.00 20.51           C  
ATOM    523  O   GLY A  67      28.023  64.848   2.758  1.00 25.96           O  
ATOM    524  N   THR A  68      28.902  62.832   2.614  1.00 28.09           N  
ATOM    525  CA  THR A  68      30.109  63.223   1.940  1.00 25.65           C  
ATOM    526  C   THR A  68      30.586  62.204   0.920  1.00 22.17           C  
ATOM    527  O   THR A  68      31.768  62.098   0.553  1.00 26.05           O  
ATOM    528  CB  THR A  68      31.039  63.301   3.163  1.00 47.53           C  
ATOM    529  OG1 THR A  68      30.659  64.419   3.930  1.00 62.73           O  
ATOM    530  CG2 THR A  68      32.548  63.245   2.941  1.00 54.34           C  
ATOM    531  N   ASP A  69      29.649  61.434   0.454  1.00 18.35           N  
ATOM    532  CA  ASP A  69      29.930  60.403  -0.530  1.00  6.23           C  
ATOM    533  C   ASP A  69      28.601  59.895  -0.934  1.00 14.26           C  
ATOM    534  O   ASP A  69      27.802  59.417  -0.120  1.00 21.43           O  
ATOM    535  CB  ASP A  69      30.689  59.249   0.107  1.00 11.56           C  
ATOM    536  CG  ASP A  69      31.178  58.251  -0.895  1.00 10.86           C  
ATOM    537  OD1 ASP A  69      30.570  57.940  -1.895  1.00 17.17           O  
ATOM    538  OD2 ASP A  69      32.359  57.773  -0.585  1.00 14.15           O  
ATOM    539  N   ASP A  70      28.343  60.013  -2.195  1.00 16.08           N  
ATOM    540  CA  ASP A  70      27.100  59.582  -2.726  1.00 14.71           C  
ATOM    541  C   ASP A  70      27.049  58.131  -3.077  1.00 19.85           C  
ATOM    542  O   ASP A  70      26.069  57.700  -3.579  1.00 16.38           O  
ATOM    543  CB  ASP A  70      26.547  60.457  -3.847  1.00 13.31           C  
ATOM    544  CG  ASP A  70      25.908  61.675  -3.248  1.00 24.72           C  
ATOM    545  OD1 ASP A  70      25.575  61.801  -2.065  1.00 19.63           O  
ATOM    546  OD2 ASP A  70      25.719  62.580  -4.172  1.00 38.69           O  
ATOM    547  N   ARG A  71      28.089  57.398  -2.824  1.00 14.00           N  
ATOM    548  CA  ARG A  71      28.023  56.005  -3.121  1.00 14.19           C  
ATOM    549  C   ARG A  71      27.131  55.249  -2.059  1.00 16.58           C  
ATOM    550  O   ARG A  71      26.697  54.096  -2.260  1.00 19.46           O  
ATOM    551  CB  ARG A  71      29.464  55.537  -3.044  1.00  8.23           C  
ATOM    552  CG  ARG A  71      30.163  56.036  -4.275  1.00  7.92           C  
ATOM    553  CD  ARG A  71      31.573  55.461  -4.298  1.00 14.05           C  
ATOM    554  NE  ARG A  71      32.240  55.794  -3.063  1.00  9.96           N  
ATOM    555  CZ  ARG A  71      33.391  55.264  -2.702  1.00  7.80           C  
ATOM    556  NH1 ARG A  71      34.040  54.357  -3.400  1.00  8.79           N  
ATOM    557  NH2 ARG A  71      33.921  55.668  -1.570  1.00 14.05           N  
ATOM    558  N   VAL A  72      26.847  55.895  -0.901  1.00 10.21           N  
ATOM    559  CA  VAL A  72      26.027  55.320   0.182  1.00  6.33           C  
ATOM    560  C   VAL A  72      24.911  56.238   0.532  1.00  8.53           C  
ATOM    561  O   VAL A  72      24.817  57.320  -0.014  1.00 14.61           O  
ATOM    562  CB  VAL A  72      26.872  55.109   1.422  1.00  7.56           C  
ATOM    563  CG1 VAL A  72      27.991  54.161   1.010  1.00 12.68           C  
ATOM    564  CG2 VAL A  72      27.539  56.454   1.793  1.00 11.03           C  
ATOM    565  N   THR A  73      23.997  55.795   1.409  1.00  6.40           N  
ATOM    566  CA  THR A  73      22.898  56.569   1.832  1.00  5.73           C  
ATOM    567  C   THR A  73      23.138  57.147   3.206  1.00  8.33           C  
ATOM    568  O   THR A  73      23.526  56.423   4.090  1.00  8.17           O  
ATOM    569  CB  THR A  73      21.676  55.678   1.813  1.00  8.23           C  
ATOM    570  OG1 THR A  73      21.469  55.214   0.507  1.00 10.75           O  
ATOM    571  CG2 THR A  73      20.442  56.332   2.418  1.00  7.28           C  
ATOM    572  N   TRP A  74      22.912  58.450   3.425  1.00  9.41           N  
ATOM    573  CA  TRP A  74      23.141  58.991   4.765  1.00  7.92           C  
ATOM    574  C   TRP A  74      21.854  59.332   5.409  1.00 10.33           C  
ATOM    575  O   TRP A  74      21.009  59.916   4.725  1.00  8.54           O  
ATOM    576  CB  TRP A  74      23.888  60.289   4.607  1.00  3.33           C  
ATOM    577  CG  TRP A  74      25.262  60.067   4.068  1.00  7.90           C  
ATOM    578  CD1 TRP A  74      25.549  59.921   2.763  1.00 13.59           C  
ATOM    579  CD2 TRP A  74      26.487  59.910   4.783  1.00  7.85           C  
ATOM    580  NE1 TRP A  74      26.863  59.722   2.597  1.00 12.91           N  
ATOM    581  CE2 TRP A  74      27.484  59.699   3.820  1.00 15.06           C  
ATOM    582  CE3 TRP A  74      26.815  59.931   6.131  1.00  6.58           C  
ATOM    583  CZ2 TRP A  74      28.809  59.500   4.141  1.00 16.64           C  
ATOM    584  CZ3 TRP A  74      28.155  59.733   6.465  1.00 14.44           C  
ATOM    585  CH2 TRP A  74      29.154  59.519   5.484  1.00 16.54           C  
ATOM    586  N   VAL A  75      21.673  58.987   6.696  1.00 13.39           N  
ATOM    587  CA  VAL A  75      20.425  59.274   7.394  1.00 11.18           C  
ATOM    588  C   VAL A  75      20.762  59.943   8.703  1.00  8.13           C  
ATOM    589  O   VAL A  75      21.841  59.802   9.195  1.00 10.92           O  
ATOM    590  CB  VAL A  75      19.568  58.018   7.583  1.00 10.45           C  
ATOM    591  CG1 VAL A  75      19.163  57.468   6.199  1.00 12.94           C  
ATOM    592  CG2 VAL A  75      20.436  57.006   8.360  1.00  5.08           C  
ATOM    593  N   LYS A  76      19.880  60.706   9.272  1.00 11.80           N  
ATOM    594  CA  LYS A  76      20.237  61.375  10.516  1.00 10.62           C  
ATOM    595  C   LYS A  76      19.630  60.873  11.813  1.00 12.76           C  
ATOM    596  O   LYS A  76      19.879  61.497  12.866  1.00 11.47           O  
ATOM    597  CB  LYS A  76      19.920  62.881  10.439  1.00 16.03           C  
ATOM    598  CG  LYS A  76      20.554  63.639   9.309  1.00 19.24           C  
ATOM    599  CD  LYS A  76      19.747  64.911   9.039  1.00 33.52           C  
ATOM    600  CE  LYS A  76      20.145  65.615   7.751  1.00 47.60           C  
ATOM    601  NZ  LYS A  76      21.545  66.114   7.784  1.00 49.53           N  
ATOM    602  N   SER A  77      18.837  59.801  11.768  1.00 11.19           N  
ATOM    603  CA  SER A  77      18.202  59.218  12.940  1.00 12.40           C  
ATOM    604  C   SER A  77      17.860  57.774  12.684  1.00 14.33           C  
ATOM    605  O   SER A  77      17.808  57.304  11.556  1.00 13.77           O  
ATOM    606  CB  SER A  77      16.883  59.883  13.358  1.00 17.45           C  
ATOM    607  OG  SER A  77      15.906  59.556  12.390  1.00 14.41           O  
ATOM    608  N   VAL A  78      17.606  57.041  13.771  1.00 15.09           N  
ATOM    609  CA  VAL A  78      17.274  55.615  13.705  1.00  7.66           C  
ATOM    610  C   VAL A  78      16.020  55.355  12.888  1.00  8.87           C  
ATOM    611  O   VAL A  78      15.992  54.486  12.024  1.00 14.59           O  
ATOM    612  CB  VAL A  78      17.087  55.188  15.153  1.00  4.62           C  
ATOM    613  CG1 VAL A  78      16.290  53.864  15.202  1.00  8.18           C  
ATOM    614  CG2 VAL A  78      18.470  54.995  15.787  1.00  8.85           C  
ATOM    615  N   ASP A  79      14.953  56.102  13.138  1.00 11.51           N  
ATOM    616  CA  ASP A  79      13.715  55.906  12.351  1.00 10.17           C  
ATOM    617  C   ASP A  79      13.887  56.076  10.817  1.00  8.80           C  
ATOM    618  O   ASP A  79      13.292  55.330  10.031  1.00 11.12           O  
ATOM    619  CB  ASP A  79      12.611  56.832  12.822  1.00 20.29           C  
ATOM    620  CG  ASP A  79      11.881  56.156  13.968  1.00 50.12           C  
ATOM    621  OD1 ASP A  79      11.274  55.093  13.845  1.00 63.62           O  
ATOM    622  OD2 ASP A  79      12.027  56.763  15.125  1.00 55.94           O  
ATOM    623  N   GLU A  80      14.707  57.070  10.420  1.00 13.54           N  
ATOM    624  CA  GLU A  80      14.987  57.344   8.997  1.00 14.98           C  
ATOM    625  C   GLU A  80      15.893  56.227   8.429  1.00  7.74           C  
ATOM    626  O   GLU A  80      15.724  55.784   7.297  1.00 10.28           O  
ATOM    627  CB  GLU A  80      15.545  58.754   8.778  1.00 20.38           C  
ATOM    628  CG  GLU A  80      15.965  58.970   7.351  1.00 22.82           C  
ATOM    629  CD  GLU A  80      16.672  60.252   7.077  1.00 20.49           C  
ATOM    630  OE1 GLU A  80      17.095  60.885   8.142  1.00 17.45           O  
ATOM    631  OE2 GLU A  80      16.821  60.646   5.930  1.00 21.42           O  
ATOM    632  N   ALA A  81      16.832  55.771   9.272  1.00  3.56           N  
ATOM    633  CA  ALA A  81      17.658  54.706   8.835  1.00  3.80           C  
ATOM    634  C   ALA A  81      16.735  53.495   8.518  1.00 12.12           C  
ATOM    635  O   ALA A  81      16.873  52.799   7.487  1.00 13.05           O  
ATOM    636  CB  ALA A  81      18.596  54.272  10.024  1.00  4.61           C  
ATOM    637  N   ILE A  82      15.792  53.230   9.416  1.00  7.49           N  
ATOM    638  CA  ILE A  82      14.943  52.108   9.154  1.00 13.10           C  
ATOM    639  C   ILE A  82      14.037  52.366   7.975  1.00 15.42           C  
ATOM    640  O   ILE A  82      13.771  51.482   7.167  1.00  7.75           O  
ATOM    641  CB  ILE A  82      14.101  51.766  10.401  1.00 13.16           C  
ATOM    642  CG1 ILE A  82      14.909  51.202  11.572  1.00 13.68           C  
ATOM    643  CG2 ILE A  82      12.990  50.810  10.050  1.00 12.97           C  
ATOM    644  CD1 ILE A  82      14.015  51.015  12.805  1.00 15.89           C  
ATOM    645  N   ALA A  83      13.513  53.563   7.858  1.00 14.25           N  
ATOM    646  CA  ALA A  83      12.626  53.786   6.695  1.00  9.61           C  
ATOM    647  C   ALA A  83      13.407  53.703   5.394  1.00 11.49           C  
ATOM    648  O   ALA A  83      12.880  53.301   4.356  1.00 13.88           O  
ATOM    649  CB  ALA A  83      12.010  55.162   6.734  1.00 11.43           C  
ATOM    650  N   ALA A  84      14.673  54.094   5.437  1.00 10.77           N  
ATOM    651  CA  ALA A  84      15.445  54.081   4.193  1.00  6.54           C  
ATOM    652  C   ALA A  84      15.667  52.688   3.634  1.00 12.48           C  
ATOM    653  O   ALA A  84      16.027  52.454   2.466  1.00 13.71           O  
ATOM    654  CB  ALA A  84      16.754  54.885   4.423  1.00  7.49           C  
ATOM    655  N   CYS A  85      15.451  51.721   4.475  1.00 13.07           N  
ATOM    656  CA  CYS A  85      15.641  50.328   4.095  1.00 11.78           C  
ATOM    657  C   CYS A  85      14.534  49.850   3.232  1.00 22.42           C  
ATOM    658  O   CYS A  85      14.734  48.960   2.431  1.00 25.23           O  
ATOM    659  CB  CYS A  85      15.711  49.449   5.340  1.00  9.74           C  
ATOM    660  SG  CYS A  85      17.315  49.622   6.155  1.00 12.42           S  
ATOM    661  N   GLY A  86      13.362  50.433   3.385  1.00 21.03           N  
ATOM    662  CA  GLY A  86      12.240  49.972   2.564  1.00 20.41           C  
ATOM    663  C   GLY A  86      11.620  48.697   3.136  1.00 20.64           C  
ATOM    664  O   GLY A  86      11.823  48.360   4.307  1.00 21.02           O  
ATOM    665  N   ASP A  87      10.839  47.980   2.308  1.00 21.03           N  
ATOM    666  CA  ASP A  87      10.191  46.767   2.746  1.00 30.89           C  
ATOM    667  C   ASP A  87      11.049  45.604   2.387  1.00 27.53           C  
ATOM    668  O   ASP A  87      11.081  45.167   1.254  1.00 32.98           O  
ATOM    669  CB  ASP A  87       8.775  46.611   2.148  1.00 37.00           C  
ATOM    670  CG  ASP A  87       8.088  47.933   2.214  1.00 55.06           C  
ATOM    671  OD1 ASP A  87       7.790  48.285   3.450  1.00 56.13           O  
ATOM    672  OD2 ASP A  87       7.944  48.654   1.234  1.00 63.49           O  
ATOM    673  N   VAL A  88      11.761  45.130   3.372  1.00 17.28           N  
ATOM    674  CA  VAL A  88      12.611  44.017   3.158  1.00 12.51           C  
ATOM    675  C   VAL A  88      12.416  43.198   4.380  1.00 10.55           C  
ATOM    676  O   VAL A  88      12.006  43.683   5.426  1.00 17.68           O  
ATOM    677  CB  VAL A  88      14.055  44.371   2.980  1.00 15.16           C  
ATOM    678  CG1 VAL A  88      14.097  45.229   1.714  1.00 21.55           C  
ATOM    679  CG2 VAL A  88      14.541  45.178   4.231  1.00 20.20           C  
ATOM    680  N   PRO A  89      12.737  41.939   4.240  1.00 17.69           N  
ATOM    681  CA  PRO A  89      12.578  40.986   5.315  1.00 25.34           C  
ATOM    682  C   PRO A  89      13.478  41.114   6.545  1.00 19.33           C  
ATOM    683  O   PRO A  89      13.072  40.930   7.718  1.00 21.05           O  
ATOM    684  CB  PRO A  89      12.626  39.625   4.632  1.00 20.38           C  
ATOM    685  CG  PRO A  89      12.743  39.908   3.148  1.00 18.95           C  
ATOM    686  CD  PRO A  89      13.174  41.346   2.993  1.00 14.32           C  
ATOM    687  N   GLU A  90      14.719  41.449   6.250  1.00 12.64           N  
ATOM    688  CA  GLU A  90      15.671  41.580   7.333  1.00 14.98           C  
ATOM    689  C   GLU A  90      16.642  42.730   7.065  1.00 19.66           C  
ATOM    690  O   GLU A  90      17.243  42.877   5.982  1.00 10.11           O  
ATOM    691  CB  GLU A  90      16.569  40.333   7.313  1.00  4.40           C  
ATOM    692  CG  GLU A  90      17.287  40.137   8.626  1.00  6.59           C  
ATOM    693  CD  GLU A  90      18.054  38.845   8.624  1.00 18.34           C  
ATOM    694  OE1 GLU A  90      18.186  38.152   7.612  1.00 15.14           O  
ATOM    695  OE2 GLU A  90      18.398  38.447   9.836  1.00 11.85           O  
ATOM    696  N   ILE A  91      16.798  43.521   8.093  1.00 12.81           N  
ATOM    697  CA  ILE A  91      17.703  44.639   8.054  1.00  4.70           C  
ATOM    698  C   ILE A  91      18.901  44.255   8.955  1.00 10.69           C  
ATOM    699  O   ILE A  91      18.722  43.816  10.109  1.00  9.42           O  
ATOM    700  CB  ILE A  91      16.989  45.856   8.674  1.00  9.83           C  
ATOM    701  CG1 ILE A  91      15.828  46.366   7.789  1.00 13.24           C  
ATOM    702  CG2 ILE A  91      18.033  46.925   9.009  1.00  9.18           C  
ATOM    703  CD1 ILE A  91      14.827  47.268   8.545  1.00 12.13           C  
ATOM    704  N   MET A  92      20.151  44.439   8.458  1.00  7.26           N  
ATOM    705  CA  MET A  92      21.305  44.122   9.290  1.00  3.86           C  
ATOM    706  C   MET A  92      22.013  45.329   9.864  1.00 11.79           C  
ATOM    707  O   MET A  92      22.528  46.139   9.097  1.00 10.26           O  
ATOM    708  CB  MET A  92      22.398  43.456   8.393  1.00  6.41           C  
ATOM    709  CG  MET A  92      21.779  42.182   7.721  1.00 17.42           C  
ATOM    710  SD  MET A  92      21.183  40.854   8.863  1.00 15.21           S  
ATOM    711  CE  MET A  92      22.750  40.258   9.628  1.00  8.64           C  
ATOM    712  N   VAL A  93      22.100  45.406  11.185  1.00  5.11           N  
ATOM    713  CA  VAL A  93      22.785  46.465  11.822  1.00  9.18           C  
ATOM    714  C   VAL A  93      24.154  45.916  12.121  1.00 10.81           C  
ATOM    715  O   VAL A  93      24.309  44.836  12.802  1.00  8.28           O  
ATOM    716  CB  VAL A  93      22.020  46.817  13.087  1.00  7.06           C  
ATOM    717  CG1 VAL A  93      22.904  47.684  13.984  1.00  5.51           C  
ATOM    718  CG2 VAL A  93      20.696  47.483  12.698  1.00  5.89           C  
ATOM    719  N   ILE A  94      25.176  46.635  11.597  1.00  6.87           N  
ATOM    720  CA  ILE A  94      26.582  46.248  11.694  1.00  9.38           C  
ATOM    721  C   ILE A  94      27.480  47.074  12.641  1.00 10.42           C  
ATOM    722  O   ILE A  94      28.708  46.989  12.585  1.00  9.29           O  
ATOM    723  CB  ILE A  94      27.213  45.920  10.335  1.00  1.40           C  
ATOM    724  CG1 ILE A  94      27.362  47.277   9.581  1.00  7.22           C  
ATOM    725  CG2 ILE A  94      26.205  45.150   9.439  1.00  6.22           C  
ATOM    726  CD1 ILE A  94      28.141  47.137   8.276  1.00  7.49           C  
ATOM    727  N   GLY A  95      26.850  47.848  13.512  1.00  8.55           N  
ATOM    728  CA  GLY A  95      27.694  48.616  14.492  1.00  9.87           C  
ATOM    729  C   GLY A  95      27.968  50.046  14.088  1.00  8.97           C  
ATOM    730  O   GLY A  95      27.422  50.550  13.142  1.00  7.85           O  
ATOM    731  N   GLY A  96      28.824  50.705  14.785  1.00  7.36           N  
ATOM    732  CA  GLY A  96      29.561  50.148  15.940  1.00  9.60           C  
ATOM    733  C   GLY A  96      28.851  50.167  17.318  1.00  9.50           C  
ATOM    734  O   GLY A  96      27.649  50.025  17.442  1.00 10.71           O  
ATOM    735  N   GLY A  97      29.619  50.325  18.378  1.00  5.62           N  
ATOM    736  CA  GLY A  97      29.064  50.313  19.708  1.00 12.52           C  
ATOM    737  C   GLY A  97      27.791  51.113  19.985  1.00 13.37           C  
ATOM    738  O   GLY A  97      26.765  50.568  20.482  1.00 10.58           O  
ATOM    739  N   ARG A  98      27.878  52.418  19.705  1.00  9.67           N  
ATOM    740  CA  ARG A  98      26.745  53.339  19.928  1.00  9.53           C  
ATOM    741  C   ARG A  98      25.551  52.917  19.068  1.00 12.01           C  
ATOM    742  O   ARG A  98      24.410  52.910  19.520  1.00  7.50           O  
ATOM    743  CB  ARG A  98      27.133  54.791  19.552  1.00 21.93           C  
ATOM    744  CG  ARG A  98      28.160  55.467  20.488  1.00 39.37           C  
ATOM    745  CD  ARG A  98      27.722  55.479  21.952  1.00 62.96           C  
ATOM    746  NE  ARG A  98      26.630  56.402  22.268  1.00 76.03           N  
ATOM    747  CZ  ARG A  98      26.272  56.591  23.525  1.00 78.56           C  
ATOM    748  NH1 ARG A  98      26.899  55.948  24.496  1.00 78.65           N  
ATOM    749  NH2 ARG A  98      25.288  57.427  23.816  1.00 79.70           N  
ATOM    750  N   VAL A  99      25.819  52.560  17.798  1.00 12.19           N  
ATOM    751  CA  VAL A  99      24.689  52.148  16.992  1.00  3.80           C  
ATOM    752  C   VAL A  99      24.070  50.798  17.493  1.00 13.51           C  
ATOM    753  O   VAL A  99      22.879  50.580  17.444  1.00 11.30           O  
ATOM    754  CB  VAL A  99      25.204  52.004  15.563  1.00  6.35           C  
ATOM    755  CG1 VAL A  99      24.146  51.414  14.637  1.00  6.18           C  
ATOM    756  CG2 VAL A  99      25.565  53.386  15.121  1.00  7.40           C  
ATOM    757  N   TYR A 100      24.895  49.838  17.971  1.00 12.86           N  
ATOM    758  CA  TYR A 100      24.315  48.567  18.447  1.00  4.99           C  
ATOM    759  C   TYR A 100      23.412  48.818  19.607  1.00  9.19           C  
ATOM    760  O   TYR A 100      22.317  48.229  19.751  1.00  7.87           O  
ATOM    761  CB  TYR A 100      25.435  47.660  18.912  1.00  4.02           C  
ATOM    762  CG  TYR A 100      26.177  46.919  17.810  1.00  1.14           C  
ATOM    763  CD1 TYR A 100      25.533  46.313  16.747  1.00  6.31           C  
ATOM    764  CD2 TYR A 100      27.568  46.862  17.890  1.00  6.40           C  
ATOM    765  CE1 TYR A 100      26.331  45.627  15.825  1.00  8.89           C  
ATOM    766  CE2 TYR A 100      28.380  46.195  16.982  1.00  1.00           C  
ATOM    767  CZ  TYR A 100      27.725  45.558  15.947  1.00  5.45           C  
ATOM    768  OH  TYR A 100      28.498  44.930  15.030  1.00  7.95           O  
ATOM    769  N   GLU A 101      23.892  49.703  20.521  1.00  5.28           N  
ATOM    770  CA  GLU A 101      23.099  50.056  21.735  1.00  4.74           C  
ATOM    771  C   GLU A 101      21.721  50.561  21.421  1.00  7.66           C  
ATOM    772  O   GLU A 101      20.768  50.224  22.078  1.00  8.90           O  
ATOM    773  CB  GLU A 101      23.872  51.146  22.564  1.00 14.80           C  
ATOM    774  CG  GLU A 101      23.521  51.157  24.056  1.00 29.46           C  
ATOM    775  CD  GLU A 101      23.959  52.413  24.829  1.00 38.57           C  
ATOM    776  OE1 GLU A 101      25.201  52.821  24.503  1.00 39.27           O  
ATOM    777  OE2 GLU A 101      23.255  52.924  25.745  1.00 28.00           O  
ATOM    778  N   GLN A 102      21.615  51.397  20.387  1.00  6.12           N  
ATOM    779  CA  GLN A 102      20.352  51.963  19.981  1.00 15.80           C  
ATOM    780  C   GLN A 102      19.402  51.000  19.276  1.00 10.57           C  
ATOM    781  O   GLN A 102      18.193  51.174  19.335  1.00 10.48           O  
ATOM    782  CB  GLN A 102      20.549  53.171  19.028  1.00 15.28           C  
ATOM    783  CG  GLN A 102      21.234  54.400  19.678  1.00 22.22           C  
ATOM    784  CD  GLN A 102      21.572  55.450  18.633  1.00 20.33           C  
ATOM    785  OE1 GLN A 102      22.812  55.518  18.115  1.00 20.63           O  
ATOM    786  NE2 GLN A 102      20.680  56.160  18.251  1.00 25.10           N  
ATOM    787  N   PHE A 103      19.949  50.020  18.572  1.00 11.34           N  
ATOM    788  CA  PHE A 103      19.106  49.073  17.855  1.00 10.56           C  
ATOM    789  C   PHE A 103      18.756  47.784  18.596  1.00  9.81           C  
ATOM    790  O   PHE A 103      17.765  47.082  18.242  1.00  8.35           O  
ATOM    791  CB  PHE A 103      19.734  48.707  16.578  1.00  6.77           C  
ATOM    792  CG  PHE A 103      19.492  49.670  15.431  1.00 12.43           C  
ATOM    793  CD1 PHE A 103      18.361  49.595  14.630  1.00 10.61           C  
ATOM    794  CD2 PHE A 103      20.422  50.647  15.114  1.00  9.30           C  
ATOM    795  CE1 PHE A 103      18.184  50.449  13.532  1.00  7.48           C  
ATOM    796  CE2 PHE A 103      20.247  51.537  14.047  1.00 14.12           C  
ATOM    797  CZ  PHE A 103      19.110  51.444  13.251  1.00 14.35           C  
ATOM    798  N   LEU A 104      19.542  47.478  19.600  1.00  6.40           N  
ATOM    799  CA  LEU A 104      19.283  46.269  20.346  1.00  5.79           C  
ATOM    800  C   LEU A 104      17.839  45.993  20.787  1.00 12.03           C  
ATOM    801  O   LEU A 104      17.259  44.955  20.640  1.00 12.32           O  
ATOM    802  CB  LEU A 104      20.309  46.184  21.477  1.00  6.53           C  
ATOM    803  CG  LEU A 104      20.079  44.918  22.300  1.00  9.08           C  
ATOM    804  CD1 LEU A 104      20.552  43.708  21.506  1.00 10.96           C  
ATOM    805  CD2 LEU A 104      20.933  44.977  23.560  1.00 19.40           C  
ATOM    806  N   PRO A 105      17.234  46.988  21.356  1.00 12.97           N  
ATOM    807  CA  PRO A 105      15.911  46.860  21.810  1.00  8.73           C  
ATOM    808  C   PRO A 105      14.930  46.634  20.715  1.00  9.24           C  
ATOM    809  O   PRO A 105      13.824  46.106  20.860  1.00 11.49           O  
ATOM    810  CB  PRO A 105      15.589  48.215  22.478  1.00 13.93           C  
ATOM    811  CG  PRO A 105      16.843  49.078  22.521  1.00 15.13           C  
ATOM    812  CD  PRO A 105      17.925  48.225  21.872  1.00 18.21           C  
ATOM    813  N   LYS A 106      15.285  47.056  19.558  1.00  7.75           N  
ATOM    814  CA  LYS A 106      14.364  46.861  18.473  1.00 16.60           C  
ATOM    815  C   LYS A 106      14.633  45.576  17.664  1.00 13.40           C  
ATOM    816  O   LYS A 106      13.840  45.174  16.838  1.00 22.85           O  
ATOM    817  CB  LYS A 106      14.463  48.027  17.487  1.00 21.07           C  
ATOM    818  CG  LYS A 106      14.538  49.406  18.120  1.00 18.83           C  
ATOM    819  CD  LYS A 106      14.201  50.529  17.143  1.00 29.02           C  
ATOM    820  CE  LYS A 106      12.779  50.482  16.571  1.00 44.36           C  
ATOM    821  NZ  LYS A 106      11.733  50.999  17.463  1.00 52.93           N  
ATOM    822  N   ALA A 107      15.757  44.939  17.915  1.00 18.15           N  
ATOM    823  CA  ALA A 107      16.173  43.749  17.203  1.00 12.39           C  
ATOM    824  C   ALA A 107      15.454  42.413  17.600  1.00 17.43           C  
ATOM    825  O   ALA A 107      15.106  42.124  18.745  1.00 10.52           O  
ATOM    826  CB  ALA A 107      17.706  43.614  17.401  1.00  9.89           C  
ATOM    827  N   GLN A 108      15.267  41.567  16.603  1.00 11.47           N  
ATOM    828  CA  GLN A 108      14.642  40.326  16.916  1.00 13.50           C  
ATOM    829  C   GLN A 108      15.689  39.197  16.845  1.00 11.21           C  
ATOM    830  O   GLN A 108      15.440  38.066  17.315  1.00  9.96           O  
ATOM    831  CB  GLN A 108      13.555  40.033  15.842  1.00 23.75           C  
ATOM    832  CG  GLN A 108      12.195  40.675  16.142  1.00 40.21           C  
ATOM    833  CD  GLN A 108      11.454  39.840  17.186  1.00 67.77           C  
ATOM    834  OE1 GLN A 108      11.297  38.606  17.049  1.00 75.30           O  
ATOM    835  NE2 GLN A 108      11.039  40.489  18.278  1.00 78.16           N  
ATOM    836  N   LYS A 109      16.866  39.458  16.231  1.00  9.05           N  
ATOM    837  CA  LYS A 109      17.855  38.377  16.076  1.00  6.98           C  
ATOM    838  C   LYS A 109      19.241  38.860  16.143  1.00  8.83           C  
ATOM    839  O   LYS A 109      19.434  40.007  15.693  1.00 11.43           O  
ATOM    840  CB  LYS A 109      17.532  37.854  14.684  1.00 12.27           C  
ATOM    841  CG  LYS A 109      18.350  36.690  14.185  1.00 18.50           C  
ATOM    842  CD  LYS A 109      17.508  35.983  13.156  1.00 18.96           C  
ATOM    843  CE  LYS A 109      18.313  34.952  12.396  1.00 28.23           C  
ATOM    844  NZ  LYS A 109      17.500  34.195  11.412  1.00 31.50           N  
ATOM    845  N   LEU A 110      20.184  38.042  16.744  1.00  8.19           N  
ATOM    846  CA  LEU A 110      21.546  38.473  16.874  1.00  4.65           C  
ATOM    847  C   LEU A 110      22.411  37.413  16.295  1.00 10.28           C  
ATOM    848  O   LEU A 110      22.230  36.245  16.556  1.00 12.05           O  
ATOM    849  CB  LEU A 110      22.037  38.600  18.331  1.00  4.32           C  
ATOM    850  CG  LEU A 110      21.233  39.467  19.265  1.00  6.97           C  
ATOM    851  CD1 LEU A 110      21.738  39.331  20.753  1.00  8.58           C  
ATOM    852  CD2 LEU A 110      21.452  40.912  18.811  1.00 16.31           C  
ATOM    853  N   TYR A 111      23.350  37.834  15.505  1.00  8.87           N  
ATOM    854  CA  TYR A 111      24.268  36.931  14.885  1.00  2.04           C  
ATOM    855  C   TYR A 111      25.557  37.268  15.575  1.00 10.60           C  
ATOM    856  O   TYR A 111      26.189  38.261  15.217  1.00  7.54           O  
ATOM    857  CB  TYR A 111      24.509  37.172  13.373  1.00  1.90           C  
ATOM    858  CG  TYR A 111      23.307  36.941  12.497  1.00  7.07           C  
ATOM    859  CD1 TYR A 111      22.221  37.813  12.572  1.00 10.12           C  
ATOM    860  CD2 TYR A 111      23.263  35.882  11.579  1.00  9.59           C  
ATOM    861  CE1 TYR A 111      21.089  37.674  11.764  1.00  5.83           C  
ATOM    862  CE2 TYR A 111      22.141  35.712  10.768  1.00 11.91           C  
ATOM    863  CZ  TYR A 111      21.078  36.615  10.847  1.00  6.50           C  
ATOM    864  OH  TYR A 111      19.995  36.454  10.053  1.00 11.05           O  
ATOM    865  N   LEU A 112      25.979  36.474  16.525  1.00  7.82           N  
ATOM    866  CA  LEU A 112      27.276  36.767  17.202  1.00  8.27           C  
ATOM    867  C   LEU A 112      28.391  35.721  16.975  1.00 13.49           C  
ATOM    868  O   LEU A 112      28.134  34.519  16.933  1.00 12.19           O  
ATOM    869  CB  LEU A 112      27.031  36.810  18.732  1.00  3.80           C  
ATOM    870  CG  LEU A 112      25.885  37.778  19.152  1.00  5.84           C  
ATOM    871  CD1 LEU A 112      25.742  37.761  20.682  1.00 10.20           C  
ATOM    872  CD2 LEU A 112      26.291  39.150  18.720  1.00  3.67           C  
ATOM    873  N   THR A 113      29.644  36.241  16.845  1.00  8.51           N  
ATOM    874  CA  THR A 113      30.732  35.406  16.718  1.00  5.33           C  
ATOM    875  C   THR A 113      31.504  35.547  18.019  1.00 13.65           C  
ATOM    876  O   THR A 113      31.874  36.616  18.293  1.00  9.19           O  
ATOM    877  CB  THR A 113      31.685  35.807  15.604  1.00 12.08           C  
ATOM    878  OG1 THR A 113      30.887  35.697  14.409  1.00  8.71           O  
ATOM    879  CG2 THR A 113      32.977  34.917  15.679  1.00  8.06           C  
ATOM    880  N   HIS A 114      31.751  34.507  18.842  1.00  8.57           N  
ATOM    881  CA  HIS A 114      32.520  34.736  20.041  1.00  5.58           C  
ATOM    882  C   HIS A 114      33.910  34.329  19.718  1.00 10.02           C  
ATOM    883  O   HIS A 114      34.153  33.222  19.293  1.00  9.73           O  
ATOM    884  CB  HIS A 114      31.987  33.886  21.190  1.00 10.79           C  
ATOM    885  CG  HIS A 114      30.504  34.016  21.334  1.00 13.16           C  
ATOM    886  ND1 HIS A 114      29.954  35.017  22.080  1.00 14.76           N  
ATOM    887  CD2 HIS A 114      29.460  33.308  20.826  1.00 22.93           C  
ATOM    888  CE1 HIS A 114      28.623  34.903  22.070  1.00 12.36           C  
ATOM    889  NE2 HIS A 114      28.291  33.885  21.332  1.00 13.21           N  
ATOM    890  N   ILE A 115      34.842  35.206  19.946  1.00  7.85           N  
ATOM    891  CA  ILE A 115      36.190  34.888  19.613  1.00  8.93           C  
ATOM    892  C   ILE A 115      37.016  34.725  20.823  1.00  8.12           C  
ATOM    893  O   ILE A 115      36.922  35.575  21.702  1.00 10.20           O  
ATOM    894  CB  ILE A 115      36.867  36.050  18.870  1.00 14.49           C  
ATOM    895  CG1 ILE A 115      35.993  36.528  17.704  1.00 18.63           C  
ATOM    896  CG2 ILE A 115      38.301  35.724  18.406  1.00  9.73           C  
ATOM    897  CD1 ILE A 115      36.745  37.362  16.716  1.00 18.93           C  
ATOM    898  N  AASP A 116      37.840  33.666  20.772  0.50  8.62           N  
ATOM    899  CA AASP A 116      38.717  33.426  21.865  0.50 12.65           C  
ATOM    900  C  AASP A 116      39.950  34.273  21.621  0.50 18.45           C  
ATOM    901  O  AASP A 116      40.902  33.888  20.963  0.50 14.21           O  
ATOM    902  CB AASP A 116      39.072  31.946  22.112  0.50 13.84           C  
ATOM    903  CG AASP A 116      39.627  31.626  23.495  0.50 12.72           C  
ATOM    904  OD1AASP A 116      39.262  32.190  24.530  0.50 17.70           O  
ATOM    905  OD2AASP A 116      40.479  30.621  23.462  0.50 12.66           O  
ATOM    906  N   ALA A 117      39.909  35.473  22.148  1.00 17.84           N  
ATOM    907  CA  ALA A 117      41.024  36.372  22.020  1.00 15.47           C  
ATOM    908  C   ALA A 117      40.909  37.418  23.103  1.00 20.82           C  
ATOM    909  O   ALA A 117      39.819  37.917  23.454  1.00 17.95           O  
ATOM    910  CB  ALA A 117      41.003  37.000  20.665  1.00 24.53           C  
ATOM    911  N   GLU A 118      42.064  37.698  23.675  1.00 13.48           N  
ATOM    912  CA  GLU A 118      42.078  38.681  24.738  1.00 21.04           C  
ATOM    913  C   GLU A 118      42.671  39.936  24.123  1.00 23.91           C  
ATOM    914  O   GLU A 118      43.887  40.030  23.838  1.00 25.50           O  
ATOM    915  CB  GLU A 118      42.900  38.104  25.905  1.00 37.65           C  
ATOM    916  CG  GLU A 118      42.860  38.896  27.244  1.00 60.69           C  
ATOM    917  CD  GLU A 118      44.113  39.726  27.583  1.00 78.63           C  
ATOM    918  OE1 GLU A 118      45.299  39.379  27.359  1.00 81.03           O  
ATOM    919  OE2 GLU A 118      43.791  40.843  28.222  1.00 80.61           O  
ATOM    920  N   VAL A 119      41.803  40.912  23.904  1.00 17.24           N  
ATOM    921  CA  VAL A 119      42.213  42.168  23.323  1.00 20.88           C  
ATOM    922  C   VAL A 119      41.719  43.285  24.255  1.00 30.71           C  
ATOM    923  O   VAL A 119      40.596  43.222  24.783  1.00 30.14           O  
ATOM    924  CB  VAL A 119      41.572  42.322  21.890  1.00 32.48           C  
ATOM    925  CG1 VAL A 119      40.623  43.505  21.771  1.00 31.62           C  
ATOM    926  CG2 VAL A 119      42.567  42.446  20.754  1.00 42.58           C  
ATOM    927  N   GLU A 120      42.580  44.298  24.454  1.00 39.75           N  
ATOM    928  CA  GLU A 120      42.341  45.501  25.266  1.00 50.04           C  
ATOM    929  C   GLU A 120      41.689  46.519  24.277  1.00 50.17           C  
ATOM    930  O   GLU A 120      42.360  47.065  23.402  1.00 57.72           O  
ATOM    931  CB  GLU A 120      43.677  46.062  25.899  1.00 58.98           C  
ATOM    932  CG  GLU A 120      44.087  45.588  27.337  1.00 75.14           C  
ATOM    933  CD  GLU A 120      45.378  46.197  27.936  1.00 91.93           C  
ATOM    934  OE1 GLU A 120      46.124  46.980  27.341  1.00 92.40           O  
ATOM    935  OE2 GLU A 120      45.646  45.780  29.173  1.00 99.79           O  
ATOM    936  N   GLY A 121      40.381  46.793  24.363  1.00 34.67           N  
ATOM    937  CA  GLY A 121      39.790  47.726  23.415  1.00 26.35           C  
ATOM    938  C   GLY A 121      39.069  48.899  24.044  1.00 25.89           C  
ATOM    939  O   GLY A 121      39.109  49.164  25.217  1.00 32.86           O  
ATOM    940  N   ASP A 122      38.383  49.630  23.251  1.00 19.21           N  
ATOM    941  CA  ASP A 122      37.720  50.770  23.769  1.00 15.34           C  
ATOM    942  C   ASP A 122      36.253  50.830  23.443  1.00 16.57           C  
ATOM    943  O   ASP A 122      35.561  51.767  23.783  1.00 17.24           O  
ATOM    944  CB  ASP A 122      38.507  51.993  23.168  1.00 18.04           C  
ATOM    945  CG  ASP A 122      38.648  52.015  21.667  1.00 25.29           C  
ATOM    946  OD1 ASP A 122      38.092  51.283  20.902  1.00 33.09           O  
ATOM    947  OD2 ASP A 122      39.453  52.893  21.229  1.00 30.11           O  
ATOM    948  N   THR A 123      35.775  49.835  22.779  1.00 15.43           N  
ATOM    949  CA  THR A 123      34.356  49.799  22.390  1.00 19.99           C  
ATOM    950  C   THR A 123      33.838  48.415  22.771  1.00 22.79           C  
ATOM    951  O   THR A 123      34.596  47.394  22.590  1.00  8.29           O  
ATOM    952  CB  THR A 123      34.248  49.905  20.841  1.00 14.59           C  
ATOM    953  OG1 THR A 123      34.961  51.009  20.410  1.00 17.65           O  
ATOM    954  CG2 THR A 123      32.859  50.188  20.397  1.00 13.13           C  
ATOM    955  N   HIS A 124      32.595  48.383  23.268  1.00 13.39           N  
ATOM    956  CA  HIS A 124      32.037  47.106  23.655  1.00 12.70           C  
ATOM    957  C   HIS A 124      30.664  46.907  23.120  1.00 21.14           C  
ATOM    958  O   HIS A 124      29.954  47.890  22.838  1.00  9.75           O  
ATOM    959  CB  HIS A 124      31.875  46.960  25.176  1.00 11.36           C  
ATOM    960  CG  HIS A 124      33.145  47.053  25.899  1.00 13.86           C  
ATOM    961  ND1 HIS A 124      33.692  45.956  26.520  1.00 19.30           N  
ATOM    962  CD2 HIS A 124      33.981  48.126  26.072  1.00 19.40           C  
ATOM    963  CE1 HIS A 124      34.868  46.391  27.052  1.00 20.28           C  
ATOM    964  NE2 HIS A 124      35.069  47.700  26.804  1.00 20.22           N  
ATOM    965  N   PHE A 125      30.335  45.598  22.996  1.00 11.68           N  
ATOM    966  CA  PHE A 125      29.028  45.242  22.544  1.00  9.31           C  
ATOM    967  C   PHE A 125      28.132  45.482  23.764  1.00  9.50           C  
ATOM    968  O   PHE A 125      28.540  45.341  24.920  1.00 16.17           O  
ATOM    969  CB  PHE A 125      28.992  43.776  22.039  1.00  7.84           C  
ATOM    970  CG  PHE A 125      27.682  43.405  21.419  1.00  9.80           C  
ATOM    971  CD1 PHE A 125      27.402  43.764  20.096  1.00  5.75           C  
ATOM    972  CD2 PHE A 125      26.718  42.693  22.128  1.00 10.27           C  
ATOM    973  CE1 PHE A 125      26.183  43.425  19.494  1.00  7.10           C  
ATOM    974  CE2 PHE A 125      25.494  42.348  21.545  1.00  9.12           C  
ATOM    975  CZ  PHE A 125      25.228  42.727  20.226  1.00 14.18           C  
ATOM    976  N   PRO A 126      26.889  45.882  23.553  1.00 15.25           N  
ATOM    977  CA  PRO A 126      26.050  46.090  24.685  1.00 18.37           C  
ATOM    978  C   PRO A 126      25.863  44.833  25.516  1.00 18.30           C  
ATOM    979  O   PRO A 126      25.940  43.665  25.098  1.00 14.55           O  
ATOM    980  CB  PRO A 126      24.682  46.616  24.172  1.00 22.59           C  
ATOM    981  CG  PRO A 126      24.843  46.887  22.697  1.00 14.36           C  
ATOM    982  CD  PRO A 126      26.251  46.438  22.306  1.00  9.65           C  
ATOM    983  N   ASP A 127      25.594  45.086  26.758  1.00 23.05           N  
ATOM    984  CA  ASP A 127      25.391  43.962  27.653  1.00 37.99           C  
ATOM    985  C   ASP A 127      23.916  43.621  27.648  1.00 35.44           C  
ATOM    986  O   ASP A 127      23.127  44.261  28.349  1.00 36.44           O  
ATOM    987  CB  ASP A 127      25.866  44.394  29.056  1.00 37.86           C  
ATOM    988  CG  ASP A 127      25.439  43.542  30.181  1.00 41.49           C  
ATOM    989  OD1 ASP A 127      25.735  42.372  30.348  1.00 36.80           O  
ATOM    990  OD2 ASP A 127      24.784  44.262  31.024  1.00 54.55           O  
ATOM    991  N   TYR A 128      23.565  42.625  26.860  1.00 24.68           N  
ATOM    992  CA  TYR A 128      22.185  42.216  26.764  1.00 21.88           C  
ATOM    993  C   TYR A 128      21.788  41.151  27.762  1.00 29.43           C  
ATOM    994  O   TYR A 128      22.627  40.308  28.193  1.00 22.91           O  
ATOM    995  CB  TYR A 128      21.892  41.662  25.372  1.00 18.39           C  
ATOM    996  CG  TYR A 128      22.803  40.517  25.028  1.00 19.31           C  
ATOM    997  CD1 TYR A 128      24.118  40.722  24.615  1.00 24.29           C  
ATOM    998  CD2 TYR A 128      22.342  39.207  25.140  1.00 26.56           C  
ATOM    999  CE1 TYR A 128      24.956  39.650  24.299  1.00 27.82           C  
ATOM   1000  CE2 TYR A 128      23.168  38.126  24.831  1.00 24.87           C  
ATOM   1001  CZ  TYR A 128      24.482  38.336  24.403  1.00 31.15           C  
ATOM   1002  OH  TYR A 128      25.319  37.240  24.103  1.00 33.69           O  
ATOM   1003  N   GLU A 129      20.473  41.220  28.068  1.00 34.42           N  
ATOM   1004  CA  GLU A 129      19.764  40.321  28.992  1.00 30.90           C  
ATOM   1005  C   GLU A 129      19.526  38.922  28.390  1.00 26.67           C  
ATOM   1006  O   GLU A 129      18.629  38.648  27.610  1.00 32.12           O  
ATOM   1007  CB  GLU A 129      18.566  41.020  29.690  1.00 29.34           C  
ATOM   1008  CG  GLU A 129      17.638  40.139  30.601  1.00 37.05           C  
ATOM   1009  CD  GLU A 129      18.217  39.417  31.829  1.00 46.94           C  
ATOM   1010  OE1 GLU A 129      18.694  38.272  31.776  1.00 47.71           O  
ATOM   1011  OE2 GLU A 129      18.002  40.055  32.980  1.00 52.33           O  
ATOM   1012  N   PRO A 130      20.403  38.026  28.765  1.00 27.66           N  
ATOM   1013  CA  PRO A 130      20.415  36.662  28.333  1.00 31.08           C  
ATOM   1014  C   PRO A 130      19.073  35.997  28.405  1.00 28.28           C  
ATOM   1015  O   PRO A 130      18.722  35.175  27.554  1.00 28.87           O  
ATOM   1016  CB  PRO A 130      21.285  35.915  29.369  1.00 31.39           C  
ATOM   1017  CG  PRO A 130      21.310  36.823  30.573  1.00 32.06           C  
ATOM   1018  CD  PRO A 130      21.126  38.227  30.049  1.00 29.71           C  
ATOM   1019  N   ASP A 131      18.331  36.342  29.443  1.00 25.87           N  
ATOM   1020  CA  ASP A 131      17.025  35.732  29.636  1.00 21.71           C  
ATOM   1021  C   ASP A 131      16.158  35.779  28.473  1.00 25.49           C  
ATOM   1022  O   ASP A 131      15.546  34.789  28.136  1.00 32.21           O  
ATOM   1023  CB  ASP A 131      16.208  36.215  30.834  1.00 19.69           C  
ATOM   1024  CG  ASP A 131      16.816  35.645  32.118  1.00 23.56           C  
ATOM   1025  OD1 ASP A 131      17.870  34.824  31.911  1.00 23.10           O  
ATOM   1026  OD2 ASP A 131      16.355  35.904  33.239  1.00 15.36           O  
ATOM   1027  N   ASP A 132      16.145  36.930  27.910  1.00 13.83           N  
ATOM   1028  CA  ASP A 132      15.349  37.241  26.759  1.00 22.58           C  
ATOM   1029  C   ASP A 132      15.756  36.634  25.447  1.00 14.60           C  
ATOM   1030  O   ASP A 132      15.098  36.826  24.452  1.00 20.69           O  
ATOM   1031  CB  ASP A 132      15.453  38.757  26.575  1.00 41.84           C  
ATOM   1032  CG  ASP A 132      15.130  39.567  27.807  1.00 56.80           C  
ATOM   1033  OD1 ASP A 132      14.510  39.150  28.785  1.00 58.84           O  
ATOM   1034  OD2 ASP A 132      15.551  40.801  27.656  1.00 63.36           O  
ATOM   1035  N   TRP A 133      16.828  35.949  25.405  1.00 14.52           N  
ATOM   1036  CA  TRP A 133      17.193  35.435  24.120  1.00 13.94           C  
ATOM   1037  C   TRP A 133      17.309  33.966  24.103  1.00 12.71           C  
ATOM   1038  O   TRP A 133      17.699  33.424  25.118  1.00 21.00           O  
ATOM   1039  CB  TRP A 133      18.580  36.027  23.687  1.00 20.24           C  
ATOM   1040  CG  TRP A 133      18.505  37.489  23.500  1.00 20.09           C  
ATOM   1041  CD1 TRP A 133      18.721  38.418  24.489  1.00 13.14           C  
ATOM   1042  CD2 TRP A 133      18.173  38.201  22.286  1.00 16.18           C  
ATOM   1043  NE1 TRP A 133      18.557  39.699  23.991  1.00 16.92           N  
ATOM   1044  CE2 TRP A 133      18.204  39.607  22.637  1.00 15.00           C  
ATOM   1045  CE3 TRP A 133      17.878  37.839  20.948  1.00 14.81           C  
ATOM   1046  CZ2 TRP A 133      17.923  40.609  21.680  1.00  8.55           C  
ATOM   1047  CZ3 TRP A 133      17.607  38.880  19.977  1.00 10.61           C  
ATOM   1048  CH2 TRP A 133      17.612  40.242  20.331  1.00 10.99           C  
ATOM   1049  N   GLU A 134      16.980  33.364  22.951  1.00 12.61           N  
ATOM   1050  CA  GLU A 134      17.068  31.930  22.735  1.00 14.64           C  
ATOM   1051  C   GLU A 134      18.162  31.567  21.690  1.00 15.55           C  
ATOM   1052  O   GLU A 134      18.143  32.058  20.572  1.00 13.45           O  
ATOM   1053  CB  GLU A 134      15.783  31.288  22.275  1.00 22.72           C  
ATOM   1054  CG  GLU A 134      16.001  29.780  22.330  1.00 39.57           C  
ATOM   1055  CD  GLU A 134      14.737  29.086  22.006  1.00 55.59           C  
ATOM   1056  OE1 GLU A 134      13.652  29.669  22.061  1.00 69.51           O  
ATOM   1057  OE2 GLU A 134      14.941  27.845  21.616  1.00 48.64           O  
ATOM   1058  N   SER A 135      19.126  30.700  22.019  1.00 15.93           N  
ATOM   1059  CA  SER A 135      20.183  30.345  21.016  1.00 12.24           C  
ATOM   1060  C   SER A 135      19.629  29.338  20.113  1.00 15.54           C  
ATOM   1061  O   SER A 135      19.276  28.281  20.557  1.00 32.38           O  
ATOM   1062  CB  SER A 135      21.419  29.723  21.694  1.00 15.44           C  
ATOM   1063  OG  SER A 135      22.401  29.334  20.739  1.00 17.11           O  
ATOM   1064  N   VAL A 136      19.528  29.577  18.860  1.00 10.30           N  
ATOM   1065  CA  VAL A 136      18.969  28.541  18.012  1.00 17.18           C  
ATOM   1066  C   VAL A 136      19.958  27.868  17.111  1.00 20.42           C  
ATOM   1067  O   VAL A 136      19.619  26.928  16.403  1.00 20.08           O  
ATOM   1068  CB  VAL A 136      17.841  29.078  17.127  1.00 21.77           C  
ATOM   1069  CG1 VAL A 136      16.810  29.750  18.006  1.00 18.23           C  
ATOM   1070  CG2 VAL A 136      18.392  30.113  16.166  1.00 15.10           C  
ATOM   1071  N   PHE A 137      21.177  28.376  17.092  1.00 18.34           N  
ATOM   1072  CA  PHE A 137      22.242  27.852  16.247  1.00 13.89           C  
ATOM   1073  C   PHE A 137      23.578  28.155  16.931  1.00 16.48           C  
ATOM   1074  O   PHE A 137      23.772  29.245  17.502  1.00 13.07           O  
ATOM   1075  CB  PHE A 137      22.101  28.512  14.860  1.00  9.66           C  
ATOM   1076  CG  PHE A 137      23.262  28.188  13.995  1.00 16.00           C  
ATOM   1077  CD1 PHE A 137      23.240  27.032  13.210  1.00 21.20           C  
ATOM   1078  CD2 PHE A 137      24.387  29.023  13.980  1.00 17.29           C  
ATOM   1079  CE1 PHE A 137      24.325  26.704  12.391  1.00 23.42           C  
ATOM   1080  CE2 PHE A 137      25.484  28.718  13.164  1.00 27.80           C  
ATOM   1081  CZ  PHE A 137      25.444  27.552  12.381  1.00 31.81           C  
ATOM   1082  N   SER A 138      24.507  27.170  16.922  1.00 15.38           N  
ATOM   1083  CA  SER A 138      25.817  27.344  17.566  1.00 15.77           C  
ATOM   1084  C   SER A 138      26.822  26.517  16.804  1.00 22.61           C  
ATOM   1085  O   SER A 138      26.545  25.388  16.503  1.00 24.23           O  
ATOM   1086  CB  SER A 138      25.750  26.728  18.969  1.00 23.43           C  
ATOM   1087  OG  SER A 138      26.377  27.556  19.893  1.00 36.62           O  
ATOM   1088  N   GLU A 139      27.974  27.015  16.480  1.00 14.47           N  
ATOM   1089  CA  GLU A 139      28.910  26.174  15.753  1.00  8.57           C  
ATOM   1090  C   GLU A 139      30.320  26.619  16.106  1.00 13.91           C  
ATOM   1091  O   GLU A 139      30.754  27.665  15.689  1.00 13.46           O  
ATOM   1092  CB  GLU A 139      28.611  26.186  14.232  1.00 14.39           C  
ATOM   1093  CG  GLU A 139      29.663  25.576  13.253  1.00 24.92           C  
ATOM   1094  CD  GLU A 139      29.339  25.901  11.799  1.00 35.39           C  
ATOM   1095  OE1 GLU A 139      28.216  25.375  11.398  1.00 49.53           O  
ATOM   1096  OE2 GLU A 139      30.024  26.599  11.071  1.00 33.39           O  
ATOM   1097  N   PHE A 140      31.016  25.801  16.893  1.00 10.15           N  
ATOM   1098  CA  PHE A 140      32.342  26.034  17.332  1.00  6.09           C  
ATOM   1099  C   PHE A 140      33.507  25.657  16.380  1.00 21.55           C  
ATOM   1100  O   PHE A 140      33.493  24.669  15.644  1.00 14.01           O  
ATOM   1101  CB  PHE A 140      32.503  25.107  18.521  1.00 13.37           C  
ATOM   1102  CG  PHE A 140      33.857  25.308  19.107  1.00 24.94           C  
ATOM   1103  CD1 PHE A 140      34.185  26.572  19.626  1.00 22.71           C  
ATOM   1104  CD2 PHE A 140      34.796  24.265  19.146  1.00 25.96           C  
ATOM   1105  CE1 PHE A 140      35.436  26.818  20.209  1.00 19.61           C  
ATOM   1106  CE2 PHE A 140      36.056  24.526  19.715  1.00 31.48           C  
ATOM   1107  CZ  PHE A 140      36.392  25.786  20.241  1.00 19.49           C  
ATOM   1108  N   HIS A 141      34.566  26.428  16.368  1.00 15.76           N  
ATOM   1109  CA  HIS A 141      35.619  26.051  15.498  1.00  8.84           C  
ATOM   1110  C   HIS A 141      36.922  26.265  16.167  1.00 13.10           C  
ATOM   1111  O   HIS A 141      37.146  27.285  16.762  1.00 14.36           O  
ATOM   1112  CB  HIS A 141      35.589  27.046  14.338  1.00 12.83           C  
ATOM   1113  CG  HIS A 141      34.427  26.865  13.496  1.00 15.25           C  
ATOM   1114  ND1 HIS A 141      34.523  26.146  12.315  1.00 21.26           N  
ATOM   1115  CD2 HIS A 141      33.142  27.256  13.621  1.00 17.58           C  
ATOM   1116  CE1 HIS A 141      33.318  26.142  11.737  1.00 21.96           C  
ATOM   1117  NE2 HIS A 141      32.466  26.794  12.507  1.00 23.24           N  
ATOM   1118  N   ASP A 142      37.801  25.314  16.072  1.00 11.37           N  
ATOM   1119  CA  ASP A 142      39.110  25.445  16.640  1.00 15.76           C  
ATOM   1120  C   ASP A 142      39.871  26.332  15.663  1.00 16.98           C  
ATOM   1121  O   ASP A 142      39.490  26.518  14.510  1.00 21.46           O  
ATOM   1122  CB  ASP A 142      39.943  24.080  16.775  1.00 17.44           C  
ATOM   1123  CG  ASP A 142      39.647  23.310  18.042  1.00 27.55           C  
ATOM   1124  OD1 ASP A 142      39.664  23.833  19.135  1.00 29.63           O  
ATOM   1125  OD2 ASP A 142      39.185  22.095  17.865  1.00 31.02           O  
ATOM   1126  N   ALA A 143      40.974  26.878  16.130  1.00 13.85           N  
ATOM   1127  CA  ALA A 143      41.849  27.728  15.374  1.00 12.96           C  
ATOM   1128  C   ALA A 143      42.579  26.885  14.331  1.00 22.15           C  
ATOM   1129  O   ALA A 143      42.730  25.706  14.474  1.00 23.76           O  
ATOM   1130  CB  ALA A 143      42.887  28.234  16.348  1.00 15.45           C  
ATOM   1131  N   ASP A 144      43.045  27.479  13.274  1.00 18.80           N  
ATOM   1132  CA  ASP A 144      43.753  26.763  12.221  1.00 13.07           C  
ATOM   1133  C   ASP A 144      44.766  27.636  11.591  1.00 21.42           C  
ATOM   1134  O   ASP A 144      45.118  28.753  12.048  1.00 21.74           O  
ATOM   1135  CB  ASP A 144      42.849  26.199  11.142  1.00 20.77           C  
ATOM   1136  CG  ASP A 144      42.068  27.261  10.403  1.00 22.92           C  
ATOM   1137  OD1 ASP A 144      42.456  28.386  10.177  1.00 26.31           O  
ATOM   1138  OD2 ASP A 144      40.923  26.829   9.993  1.00 23.56           O  
ATOM   1139  N   ALA A 145      45.243  27.114  10.491  1.00 26.70           N  
ATOM   1140  CA  ALA A 145      46.248  27.846   9.804  1.00 31.45           C  
ATOM   1141  C   ALA A 145      45.813  29.142   9.259  1.00 25.56           C  
ATOM   1142  O   ALA A 145      46.705  29.968   9.132  1.00 26.32           O  
ATOM   1143  CB  ALA A 145      47.140  27.060   8.855  1.00 36.47           C  
ATOM   1144  N   GLN A 146      44.514  29.309   8.938  1.00 15.00           N  
ATOM   1145  CA  GLN A 146      44.124  30.586   8.415  1.00 13.48           C  
ATOM   1146  C   GLN A 146      43.494  31.407   9.497  1.00 17.23           C  
ATOM   1147  O   GLN A 146      43.380  32.601   9.337  1.00 16.79           O  
ATOM   1148  CB  GLN A 146      43.070  30.595   7.278  1.00 12.36           C  
ATOM   1149  CG  GLN A 146      43.432  29.789   6.020  1.00 29.85           C  
ATOM   1150  CD  GLN A 146      42.256  29.833   5.043  1.00 35.01           C  
ATOM   1151  OE1 GLN A 146      41.805  30.915   4.638  1.00 40.11           O  
ATOM   1152  NE2 GLN A 146      41.659  28.682   4.790  1.00 40.66           N  
ATOM   1153  N   ASN A 147      43.096  30.771  10.586  1.00 12.55           N  
ATOM   1154  CA  ASN A 147      42.435  31.485  11.678  1.00 12.89           C  
ATOM   1155  C   ASN A 147      43.089  31.219  13.014  1.00 19.84           C  
ATOM   1156  O   ASN A 147      42.990  30.144  13.627  1.00 25.66           O  
ATOM   1157  CB  ASN A 147      40.955  30.998  11.750  1.00 17.87           C  
ATOM   1158  CG  ASN A 147      40.123  31.370  10.504  1.00 18.30           C  
ATOM   1159  OD1 ASN A 147      39.692  32.506  10.368  1.00 19.50           O  
ATOM   1160  ND2 ASN A 147      40.129  30.476   9.475  1.00 19.14           N  
ATOM   1161  N   SER A 148      43.719  32.284  13.433  1.00 21.40           N  
ATOM   1162  CA  SER A 148      44.506  32.469  14.636  1.00 17.50           C  
ATOM   1163  C   SER A 148      43.901  32.169  16.002  1.00 20.24           C  
ATOM   1164  O   SER A 148      44.600  32.016  16.972  1.00 26.15           O  
ATOM   1165  CB  SER A 148      45.356  33.700  14.504  1.00 17.92           C  
ATOM   1166  OG  SER A 148      45.684  34.146  15.767  1.00 29.36           O  
ATOM   1167  N   HIS A 149      42.598  32.026  16.124  1.00 21.03           N  
ATOM   1168  CA  HIS A 149      41.974  31.714  17.410  1.00 20.33           C  
ATOM   1169  C   HIS A 149      40.774  30.882  17.131  1.00 16.08           C  
ATOM   1170  O   HIS A 149      40.317  30.877  15.981  1.00 19.91           O  
ATOM   1171  CB  HIS A 149      41.346  32.994  18.059  1.00 19.20           C  
ATOM   1172  CG  HIS A 149      42.351  34.092  18.224  1.00 18.63           C  
ATOM   1173  ND1 HIS A 149      43.329  34.006  19.225  1.00 23.23           N  
ATOM   1174  CD2 HIS A 149      42.512  35.265  17.522  1.00 15.63           C  
ATOM   1175  CE1 HIS A 149      44.075  35.106  19.116  1.00 26.46           C  
ATOM   1176  NE2 HIS A 149      43.616  35.882  18.086  1.00 22.48           N  
ATOM   1177  N   SER A 150      40.253  30.245  18.174  1.00  7.97           N  
ATOM   1178  CA  SER A 150      39.060  29.502  17.944  1.00 11.28           C  
ATOM   1179  C   SER A 150      37.922  30.485  18.115  1.00 10.54           C  
ATOM   1180  O   SER A 150      38.032  31.507  18.802  1.00 12.47           O  
ATOM   1181  CB  SER A 150      38.892  28.414  18.953  1.00 21.72           C  
ATOM   1182  OG  SER A 150      39.208  29.009  20.190  1.00 18.45           O  
ATOM   1183  N   TYR A 151      36.827  30.160  17.483  1.00 12.86           N  
ATOM   1184  CA  TYR A 151      35.626  31.045  17.535  1.00 14.16           C  
ATOM   1185  C   TYR A 151      34.355  30.206  17.487  1.00 21.67           C  
ATOM   1186  O   TYR A 151      34.362  28.976  17.074  1.00 16.56           O  
ATOM   1187  CB  TYR A 151      35.631  31.980  16.276  1.00 13.84           C  
ATOM   1188  CG  TYR A 151      35.959  31.234  14.993  1.00  7.00           C  
ATOM   1189  CD1 TYR A 151      37.245  30.826  14.704  1.00 10.48           C  
ATOM   1190  CD2 TYR A 151      34.982  30.966  14.042  1.00  7.35           C  
ATOM   1191  CE1 TYR A 151      37.592  30.126  13.550  1.00 16.15           C  
ATOM   1192  CE2 TYR A 151      35.294  30.256  12.889  1.00 13.47           C  
ATOM   1193  CZ  TYR A 151      36.585  29.837  12.643  1.00 14.66           C  
ATOM   1194  OH  TYR A 151      36.849  29.163  11.515  1.00 15.80           O  
ATOM   1195  N   CYS A 152      33.272  30.886  17.917  1.00 12.76           N  
ATOM   1196  CA  CYS A 152      32.007  30.199  17.898  1.00  6.90           C  
ATOM   1197  C   CYS A 152      30.972  31.090  17.170  1.00 17.74           C  
ATOM   1198  O   CYS A 152      30.787  32.254  17.576  1.00 15.10           O  
ATOM   1199  CB  CYS A 152      31.469  29.919  19.312  1.00 10.84           C  
ATOM   1200  SG  CYS A 152      30.092  28.722  19.249  1.00 25.87           S  
ATOM   1201  N   PHE A 153      30.298  30.555  16.146  1.00  6.89           N  
ATOM   1202  CA  PHE A 153      29.254  31.317  15.484  1.00  6.25           C  
ATOM   1203  C   PHE A 153      27.919  31.038  16.167  1.00 13.52           C  
ATOM   1204  O   PHE A 153      27.536  29.878  16.355  1.00 14.88           O  
ATOM   1205  CB  PHE A 153      29.029  30.892  14.088  1.00 12.26           C  
ATOM   1206  CG  PHE A 153      30.196  31.194  13.201  1.00 11.01           C  
ATOM   1207  CD1 PHE A 153      30.829  32.439  13.215  1.00 14.11           C  
ATOM   1208  CD2 PHE A 153      30.623  30.203  12.321  1.00  9.50           C  
ATOM   1209  CE1 PHE A 153      31.924  32.654  12.363  1.00  7.95           C  
ATOM   1210  CE2 PHE A 153      31.684  30.435  11.446  1.00  7.53           C  
ATOM   1211  CZ  PHE A 153      32.354  31.661  11.489  1.00  8.41           C  
ATOM   1212  N   GLU A 154      27.153  32.064  16.536  1.00 11.75           N  
ATOM   1213  CA  GLU A 154      25.910  31.772  17.199  1.00  7.09           C  
ATOM   1214  C   GLU A 154      24.806  32.680  16.719  1.00 17.38           C  
ATOM   1215  O   GLU A 154      25.067  33.809  16.310  1.00 10.48           O  
ATOM   1216  CB  GLU A 154      26.222  32.087  18.650  1.00 10.59           C  
ATOM   1217  CG  GLU A 154      24.942  32.122  19.470  1.00 17.89           C  
ATOM   1218  CD  GLU A 154      25.194  31.859  20.945  1.00 28.41           C  
ATOM   1219  OE1 GLU A 154      25.865  32.844  21.569  1.00 20.04           O  
ATOM   1220  OE2 GLU A 154      24.612  30.952  21.543  1.00 30.85           O  
ATOM   1221  N   ILE A 155      23.588  32.175  16.746  1.00 10.22           N  
ATOM   1222  CA  ILE A 155      22.385  32.938  16.334  1.00 13.02           C  
ATOM   1223  C   ILE A 155      21.345  32.819  17.467  1.00 14.65           C  
ATOM   1224  O   ILE A 155      20.930  31.705  17.862  1.00 16.17           O  
ATOM   1225  CB  ILE A 155      21.767  32.498  15.016  1.00 12.11           C  
ATOM   1226  CG1 ILE A 155      22.819  32.681  13.992  1.00 17.03           C  
ATOM   1227  CG2 ILE A 155      20.648  33.479  14.604  1.00 18.41           C  
ATOM   1228  CD1 ILE A 155      22.379  32.228  12.626  1.00 18.81           C  
ATOM   1229  N   LEU A 156      20.938  33.992  17.974  1.00  4.43           N  
ATOM   1230  CA  LEU A 156      19.946  34.083  19.020  1.00 10.18           C  
ATOM   1231  C   LEU A 156      18.747  34.754  18.471  1.00 11.75           C  
ATOM   1232  O   LEU A 156      18.803  35.672  17.592  1.00 13.54           O  
ATOM   1233  CB  LEU A 156      20.490  35.006  20.147  1.00 11.11           C  
ATOM   1234  CG  LEU A 156      21.879  34.549  20.569  1.00 14.32           C  
ATOM   1235  CD1 LEU A 156      22.410  35.426  21.685  1.00 16.42           C  
ATOM   1236  CD2 LEU A 156      21.636  33.271  21.275  1.00 18.25           C  
ATOM   1237  N   GLU A 157      17.638  34.324  19.004  1.00 11.02           N  
ATOM   1238  CA  GLU A 157      16.340  34.887  18.633  1.00 15.99           C  
ATOM   1239  C   GLU A 157      15.646  35.357  19.887  1.00 11.61           C  
ATOM   1240  O   GLU A 157      15.608  34.649  20.917  1.00 10.48           O  
ATOM   1241  CB  GLU A 157      15.441  33.906  17.909  1.00 17.18           C  
ATOM   1242  CG  GLU A 157      16.116  33.553  16.563  1.00 25.29           C  
ATOM   1243  CD  GLU A 157      15.158  32.814  15.687  1.00 33.64           C  
ATOM   1244  OE1 GLU A 157      14.111  32.342  16.088  1.00 44.23           O  
ATOM   1245  OE2 GLU A 157      15.593  32.660  14.482  1.00 43.30           O  
ATOM   1246  N   ARG A 158      15.098  36.569  19.832  1.00  6.00           N  
ATOM   1247  CA  ARG A 158      14.434  37.070  21.011  1.00 11.93           C  
ATOM   1248  C   ARG A 158      13.210  36.158  21.388  1.00 19.19           C  
ATOM   1249  O   ARG A 158      12.331  35.801  20.609  1.00 12.90           O  
ATOM   1250  CB  ARG A 158      13.983  38.485  20.712  1.00 19.28           C  
ATOM   1251  CG  ARG A 158      13.326  39.176  21.916  1.00 23.75           C  
ATOM   1252  CD  ARG A 158      12.904  40.593  21.597  1.00 25.29           C  
ATOM   1253  NE  ARG A 158      13.997  41.557  21.254  1.00 23.06           N  
ATOM   1254  CZ  ARG A 158      14.747  42.176  22.193  1.00 23.76           C  
ATOM   1255  NH1 ARG A 158      14.567  41.927  23.510  1.00 17.07           N  
ATOM   1256  NH2 ARG A 158      15.695  43.046  21.776  1.00 25.61           N  
ATOM   1257  N   ARG A 159      13.131  35.764  22.634  1.00 15.57           N  
ATOM   1258  CA  ARG A 159      12.040  34.935  22.991  1.00 15.07           C  
ATOM   1259  C   ARG A 159      10.719  35.611  22.887  1.00 27.63           C  
ATOM   1260  O   ARG A 159       9.814  34.921  22.423  1.00 33.90           O  
ATOM   1261  CB  ARG A 159      12.223  34.620  24.435  1.00 16.65           C  
ATOM   1262  CG  ARG A 159      13.216  33.527  24.561  1.00 23.03           C  
ATOM   1263  CD  ARG A 159      13.021  32.905  25.925  1.00 30.68           C  
ATOM   1264  NE  ARG A 159      14.248  32.279  26.319  1.00 33.03           N  
ATOM   1265  CZ  ARG A 159      14.683  31.103  25.881  1.00 32.29           C  
ATOM   1266  NH1 ARG A 159      14.006  30.333  24.994  1.00 35.14           N  
ATOM   1267  NH2 ARG A 159      15.858  30.704  26.387  1.00 28.02           N  
ATOM   1268  OXT ARG A 159      10.580  36.688  23.475  1.00 22.07           O  
TER    1269      ARG A 159                                                      
HETATM 1270 MN    MN A 300       8.863  33.062  21.335  1.00 39.00          MN  
HETATM 1271  N1  FOL A 161      30.407  41.127  12.334  1.00  8.73           N  
HETATM 1272  C2  FOL A 161      31.183  39.960  12.347  1.00  9.79           C  
HETATM 1273  NA2 FOL A 161      30.747  38.763  12.656  1.00 15.94           N  
HETATM 1274  N3  FOL A 161      32.605  40.091  12.045  1.00  9.96           N  
HETATM 1275  C4  FOL A 161      33.168  41.270  11.746  1.00 13.25           C  
HETATM 1276  O4  FOL A 161      34.374  41.337  11.542  1.00 12.23           O  
HETATM 1277  C4A FOL A 161      32.264  42.476  11.702  1.00 11.59           C  
HETATM 1278  N5  FOL A 161      32.764  43.661  11.235  1.00 16.95           N  
HETATM 1279  C6  FOL A 161      31.895  44.651  11.140  1.00 12.00           C  
HETATM 1280  C7  FOL A 161      30.608  44.333  11.572  1.00 17.89           C  
HETATM 1281  N8  FOL A 161      30.128  43.253  12.021  1.00 13.00           N  
HETATM 1282  C8A FOL A 161      30.979  42.320  12.033  1.00 10.23           C  
HETATM 1283  C9  FOL A 161      32.328  46.002  10.646  1.00 12.36           C  
HETATM 1284  N10 FOL A 161      33.705  45.982  10.049  1.00  5.22           N  
HETATM 1285  C11 FOL A 161      34.306  44.202   6.323  1.00 14.57           C  
HETATM 1286  C12 FOL A 161      35.321  44.853   7.040  1.00 17.61           C  
HETATM 1287  C13 FOL A 161      35.083  45.433   8.285  1.00 18.37           C  
HETATM 1288  C14 FOL A 161      33.813  45.401   8.851  1.00  4.90           C  
HETATM 1289  C15 FOL A 161      32.788  44.778   8.245  1.00  5.27           C  
HETATM 1290  C16 FOL A 161      33.054  44.162   6.947  1.00  9.61           C  
HETATM 1291  C   FOL A 161      34.568  43.576   5.020  1.00 24.98           C  
HETATM 1292  O   FOL A 161      35.643  43.806   4.468  1.00 23.33           O  
HETATM 1293  N   FOL A 161      33.743  42.614   4.530  1.00 24.29           N  
HETATM 1294  CA  FOL A 161      33.724  41.900   3.170  1.00 27.12           C  
HETATM 1295  CB  FOL A 161      34.090  40.359   3.384  1.00 33.48           C  
HETATM 1296  CG  FOL A 161      35.338  39.693   2.575  1.00 51.31           C  
HETATM 1297  CD  FOL A 161      35.035  38.179   2.282  1.00 73.27           C  
HETATM 1298  OE1 FOL A 161      33.833  38.054   1.926  1.00 81.18           O  
HETATM 1299  OE2 FOL A 161      35.859  37.227   2.389  1.00 81.20           O  
HETATM 1300  CT  FOL A 161      32.282  41.861   2.758  1.00 19.52           C  
HETATM 1301  O1  FOL A 161      31.411  41.707   3.598  1.00 18.61           O  
HETATM 1302  O2  FOL A 161      32.016  41.926   1.554  1.00 17.81           O  
HETATM 1303  S2  BME A 162      28.634  29.703  20.113  1.00 56.39           S  
HETATM 1304  PA  NAP A 164      29.826  53.888  15.516  1.00 14.14           P  
HETATM 1305  O1A NAP A 164      28.733  53.379  16.380  1.00 14.63           O  
HETATM 1306  O2A NAP A 164      30.317  53.233  14.260  1.00 12.15           O  
HETATM 1307  O5B NAP A 164      29.561  55.380  15.016  1.00 13.75           O  
HETATM 1308  C5B NAP A 164      29.060  56.408  15.901  1.00 13.53           C  
HETATM 1309  C4B NAP A 164      28.479  57.572  15.110  1.00  9.37           C  
HETATM 1310  O4B NAP A 164      27.389  57.371  14.177  1.00 16.18           O  
HETATM 1311  C3B NAP A 164      28.040  58.800  15.909  1.00 21.68           C  
HETATM 1312  O3B NAP A 164      29.240  59.473  16.236  1.00 24.99           O  
HETATM 1313  C2B NAP A 164      27.161  59.607  14.931  1.00 21.50           C  
HETATM 1314  O2B NAP A 164      27.923  60.148  13.854  1.00 17.01           O  
HETATM 1315  C1B NAP A 164      26.449  58.422  14.273  1.00 18.46           C  
HETATM 1316  N9A NAP A 164      25.219  58.028  14.960  1.00 18.41           N  
HETATM 1317  C8A NAP A 164      24.961  56.999  15.842  1.00 16.63           C  
HETATM 1318  N7A NAP A 164      23.691  56.985  16.258  1.00 17.72           N  
HETATM 1319  C5A NAP A 164      23.107  58.100  15.602  1.00 15.17           C  
HETATM 1320  C6A NAP A 164      21.788  58.622  15.588  1.00 18.53           C  
HETATM 1321  N6A NAP A 164      20.807  58.094  16.303  1.00 18.66           N  
HETATM 1322  N1A NAP A 164      21.545  59.704  14.826  1.00 22.21           N  
HETATM 1323  C2A NAP A 164      22.579  60.199  14.121  1.00 16.72           C  
HETATM 1324  N3A NAP A 164      23.878  59.817  14.043  1.00 14.38           N  
HETATM 1325  C4A NAP A 164      24.056  58.741  14.811  1.00 12.93           C  
HETATM 1326  O3  NAP A 164      31.013  54.291  16.496  1.00 15.50           O  
HETATM 1327  PN  NAP A 164      31.810  53.473  17.660  1.00 17.41           P  
HETATM 1328  O1N NAP A 164      30.793  53.263  18.737  1.00 13.10           O  
HETATM 1329  O2N NAP A 164      33.079  54.231  17.921  1.00 23.66           O  
HETATM 1330  O5D NAP A 164      32.171  52.060  16.994  1.00 14.09           O  
HETATM 1331  C5D NAP A 164      33.277  52.099  15.983  1.00 12.52           C  
HETATM 1332  C4D NAP A 164      34.233  51.056  16.676  1.00 14.54           C  
HETATM 1333  O4D NAP A 164      33.505  49.790  16.602  1.00 19.39           O  
HETATM 1334  C3D NAP A 164      35.509  50.571  15.899  1.00 15.52           C  
HETATM 1335  O3D NAP A 164      36.583  50.172  16.654  1.00 20.14           O  
HETATM 1336  C2D NAP A 164      35.029  49.509  14.860  1.00 10.02           C  
HETATM 1337  O2D NAP A 164      36.216  48.908  14.494  1.00 13.41           O  
HETATM 1338  C1D NAP A 164      34.136  48.781  15.734  1.00 12.98           C  
HETATM 1339  N1N NAP A 164      33.147  47.709  15.215  1.00 21.64           N  
HETATM 1340  C2N NAP A 164      33.244  46.332  15.481  1.00 20.33           C  
HETATM 1341  C3N NAP A 164      32.354  45.475  14.998  1.00 16.52           C  
HETATM 1342  C7N NAP A 164      32.514  44.047  15.308  1.00 18.52           C  
HETATM 1343  O7N NAP A 164      31.638  43.198  14.971  1.00 14.57           O  
HETATM 1344  N7N NAP A 164      33.620  43.594  15.906  1.00 14.33           N  
HETATM 1345  C4N NAP A 164      31.149  45.947  14.124  1.00 16.39           C  
HETATM 1346  C5N NAP A 164      31.135  47.463  13.914  1.00 12.67           C  
HETATM 1347  C6N NAP A 164      32.083  48.137  14.444  1.00 24.21           C  
HETATM 1348  P2B NAP A 164      28.321  61.694  13.790  1.00 18.75           P  
HETATM 1349  O1X NAP A 164      28.883  61.988  12.372  1.00 18.53           O  
HETATM 1350  O2X NAP A 164      26.950  62.112  14.240  1.00 15.67           O  
HETATM 1351  O3X NAP A 164      29.448  61.927  14.775  1.00 19.14           O  
HETATM 1352  O   HOH A 301      29.739  31.324   8.203  1.00 56.74           O  
HETATM 1353  O   HOH A 302      28.553  37.263  13.896  1.00 14.50           O  
HETATM 1354  O   HOH A 304      40.401  22.955  13.756  1.00 65.83           O  
HETATM 1355  O   HOH A 307      39.152  41.278  25.212  1.00 31.18           O  
HETATM 1356  O   HOH A 309      16.559  37.396   5.863  1.00 26.16           O  
HETATM 1357  O   HOH A 311      26.323  43.528  32.912  1.00 43.65           O  
HETATM 1358  O   HOH A 312      15.969  40.981  33.472  1.00 48.34           O  
HETATM 1359  O   HOH A 314      16.502  41.643   3.760  1.00 16.91           O  
HETATM 1360  O   HOH A 315      22.515  63.840  -2.946  1.00 51.30           O  
HETATM 1361  O   HOH A 318      44.548  48.141  18.891  1.00 38.56           O  
HETATM 1362  O   HOH A 319      40.803  42.345  11.101  1.00 52.40           O  
HETATM 1363  O   HOH A 320      38.530  39.392  10.844  1.00 18.46           O  
HETATM 1364  O   HOH A 321      31.877  36.257  22.994  1.00 32.36           O  
HETATM 1365  O   HOH A 322      23.002  33.625   3.993  1.00 46.36           O  
HETATM 1366  O   HOH A 323      23.935  64.067  -5.092  1.00 33.45           O  
HETATM 1367  O   HOH A 324      35.235  47.026  12.417  1.00 40.42           O  
HETATM 1368  O   HOH A 326      20.013  24.639  14.895  1.00 59.60           O  
HETATM 1369  O   HOH A 327      12.342  37.887  24.952  1.00 20.91           O  
HETATM 1370  O   HOH A 328      19.693  60.904  15.881  1.00 27.93           O  
HETATM 1371  O   HOH A 329      39.203  30.029   6.376  1.00 46.65           O  
HETATM 1372  O   HOH A 330      36.543  53.379  26.454  1.00 44.44           O  
HETATM 1373  O   HOH A 331      33.044  50.808  25.908  1.00 71.77           O  
HETATM 1374  O   HOH A 332      17.088  42.300   1.077  1.00 27.48           O  
HETATM 1375  O   HOH A 333      24.358  48.098  27.721  1.00 48.53           O  
HETATM 1376  O   HOH A 335      26.295  62.369  17.039  1.00 48.51           O  
HETATM 1377  O   HOH A 336      11.756  49.499   6.592  1.00 20.44           O  
HETATM 1378  O   HOH A 337      26.792  62.485  -7.125  1.00 45.04           O  
HETATM 1379  O   HOH A 338      42.293  47.702  16.756  1.00 33.30           O  
HETATM 1380  O   HOH A 340      39.721  48.677  10.078  1.00 73.87           O  
HETATM 1381  O   HOH A 341      21.127  35.288   7.148  1.00 28.59           O  
HETATM 1382  O   HOH A 342      33.061  56.294  18.935  1.00 60.48           O  
HETATM 1383  O   HOH A 343      35.821  54.754  17.396  1.00 42.49           O  
HETATM 1384  O   HOH A 344      17.055  32.195  27.766  1.00 47.66           O  
HETATM 1385  O   HOH A 345      22.362  36.972   2.933  1.00 40.31           O  
HETATM 1386  O   HOH A 346      20.135  48.605  24.396  1.00 40.86           O  
HETATM 1387  O   HOH A 347      46.341  40.391  24.629  1.00 21.16           O  
HETATM 1388  O   HOH A 348      47.462  32.528  10.076  1.00 48.44           O  
HETATM 1389  O   HOH A 349      23.782  62.155  -6.334  1.00 47.23           O  
HETATM 1390  O   HOH A 350       8.046  47.404   5.981  1.00 51.20           O  
HETATM 1391  O   HOH A 351      22.765  52.766  -1.342  1.00 48.53           O  
HETATM 1392  O   HOH A 352      11.678  44.728  21.368  1.00 54.89           O  
HETATM 1393  O   HOH A 354      31.993  61.692  16.476  1.00 59.13           O  
HETATM 1394  O   HOH A 355      46.096  50.391  20.173  1.00 45.96           O  
HETATM 1395  O   HOH A 356      27.246  21.445  18.127  1.00 68.40           O  
HETATM 1396  O   HOH A 358      26.265  28.267  23.070  1.00 60.96           O  
HETATM 1397  O   HOH A 359      23.808  62.139   7.588  1.00 22.14           O  
HETATM 1398  O   HOH A 360      25.062  40.042  28.603  1.00 33.93           O  
HETATM 1399  O   HOH A 361      37.384  52.264  18.019  1.00 15.15           O  
HETATM 1400  O   HOH A 362      36.385  39.509  12.287  1.00 21.47           O  
HETATM 1401  O   HOH A 363      31.395  50.300  24.007  1.00 38.36           O  
HETATM 1402  O   HOH A 364      11.046  42.317  -0.149  1.00 55.24           O  
HETATM 1403  O   HOH A 366      32.662  44.045  29.843  1.00 61.35           O  
HETATM 1404  O   HOH A 367      41.317  28.919  22.103  1.00 44.98           O  
HETATM 1405  O   HOH A 368      41.058  25.355  21.701  1.00 55.11           O  
HETATM 1406  O   HOH A 369      32.857  30.892   7.484  1.00 18.01           O  
HETATM 1407  O   HOH A 371      46.726  35.638  17.463  1.00 27.47           O  
HETATM 1408  O   HOH A 372      44.701  28.772  14.304  1.00 51.34           O  
HETATM 1409  O   HOH A 373      28.682  23.933  18.402  1.00 56.63           O  
HETATM 1410  O   HOH A 374      22.388  62.817  16.788  1.00 45.17           O  
HETATM 1411  O   HOH A 375       8.259  43.883   2.434  1.00 80.50           O  
HETATM 1412  O   HOH A 376      22.125  60.096   1.037  1.00 19.76           O  
HETATM 1413  O   HOH A 377      18.367  42.215  25.791  1.00 25.08           O  
HETATM 1414  O   HOH A 378      19.808  35.117  34.050  1.00 18.78           O  
HETATM 1415  O   HOH A 379      16.970  44.393  24.756  1.00 47.63           O  
HETATM 1416  O   HOH A 380      10.567  54.587  10.302  1.00 40.10           O  
HETATM 1417  O   HOH A 381      24.876  51.300  -1.091  1.00 21.02           O  
HETATM 1418  O   HOH A 382      20.136  45.608  -0.048  1.00 40.81           O  
HETATM 1419  O   HOH A 383       8.059  30.885  20.553  1.00 16.56           O  
HETATM 1420  O   HOH A 384      25.723  33.390  24.529  1.00 56.02           O  
HETATM 1421  O   HOH A 385      33.057  59.552   3.796  1.00 20.55           O  
HETATM 1422  O   HOH A 386      23.554  59.598  -0.919  1.00 26.17           O  
HETATM 1423  O   HOH A 387      27.168  62.687   0.377  1.00 31.31           O  
HETATM 1424  O   HOH A 388      28.291  49.434  23.829  1.00 41.50           O  
HETATM 1425  O   HOH A 389      46.881  32.310  18.818  1.00 43.32           O  
HETATM 1426  O   HOH A 390      23.330  60.667  17.822  1.00 67.68           O  
HETATM 1427  O   HOH A 391      44.078  37.453  14.726  1.00 38.97           O  
HETATM 1428  O   HOH A 392      31.756  48.709  -3.817  1.00 35.07           O  
HETATM 1429  O   HOH A 393      32.565  59.906   6.949  1.00 49.83           O  
HETATM 1430  O   HOH A 394      24.488  58.306  -6.523  1.00 61.90           O  
HETATM 1431  O   HOH A 395      17.122  35.312   8.533  1.00 32.14           O  
HETATM 1432  O   HOH A 396      39.996  28.075   7.540  1.00 48.22           O  
HETATM 1433  O   HOH A 397      20.805  63.784  14.047  1.00 34.86           O  
HETATM 1434  O   HOH A 398      35.069  54.772   4.680  1.00 34.49           O  
HETATM 1435  O   HOH A 399      38.855  56.052   5.611  1.00 45.53           O  
HETATM 1436  O   HOH A 400      28.875  63.633  16.859  1.00 38.98           O  
HETATM 1437  O   HOH A 401      32.479  65.022   0.354  1.00 40.09           O  
HETATM 1438  O   HOH A 402      13.181  60.548  12.559  1.00 45.27           O  
HETATM 1439  O   HOH A 403      22.850  62.933   1.173  1.00 53.83           O  
HETATM 1440  O   HOH A 404      45.426  43.274  23.089  1.00 38.80           O  
HETATM 1441  O   HOH A 405      26.267  46.855  -4.835  1.00 43.41           O  
HETATM 1442  O   HOH A 406      19.829  35.503   4.612  1.00 34.39           O  
HETATM 1443  O   HOH A 407      19.152  60.124   2.784  1.00 30.16           O  
HETATM 1444  O   HOH A 408      44.324  38.330  20.915  1.00 39.01           O  
HETATM 1445  O   HOH A 409      33.632  58.942   1.302  1.00 45.24           O  
HETATM 1446  O   HOH A 410      23.376  26.961  20.928  1.00 41.65           O  
HETATM 1447  O   HOH A 411      41.852  54.269  22.733  1.00 51.75           O  
HETATM 1448  O   HOH A 412      36.013  50.136  -2.926  1.00 42.92           O  
HETATM 1449  O   HOH A 413      15.390  62.179   4.529  1.00 39.53           O  
HETATM 1450  O   HOH A 414      17.362  63.762   6.646  1.00 33.05           O  
HETATM 1451  O   HOH A 415      21.574  62.992   5.782  1.00 28.31           O  
HETATM 1452  O   HOH A 416      29.124  37.409  25.219  1.00 31.09           O  
HETATM 1453  O   HOH A 417      23.922  54.914  22.007  1.00 37.72           O  
HETATM 1454  O   HOH A 418      18.573  26.981  23.480  1.00 42.23           O  
HETATM 1455  O   HOH A 419      25.596  30.911  24.230  1.00 54.51           O  
HETATM 1456  O   HOH A 420      36.673  22.760  14.799  1.00 48.78           O  
HETATM 1457  O   HOH A 421      24.353  57.737  19.442  1.00 42.70           O  
HETATM 1458  O   HOH A 422      24.817  34.662   0.676  1.00 50.54           O  
HETATM 1459  O   HOH A 423      31.436  53.187  21.911  1.00 36.27           O  
HETATM 1460  O   HOH A 424      10.644  32.557  23.426  1.00 53.85           O  
HETATM 1461  O   HOH A 425       8.469  31.906  23.393  1.00 29.95           O  
HETATM 1462  O   HOH A 426      32.068  37.718  25.211  1.00 33.50           O  
HETATM 1463  O   HOH A 427      34.713  53.798  20.817  1.00 32.17           O  
HETATM 1464  O   HOH A 428      23.665  56.210  -3.227  1.00 45.92           O  
HETATM 1465  O   HOH A 429      27.682  25.039  20.147  1.00 58.42           O  
HETATM 1466  O   HOH A 430      40.513  39.134   8.652  1.00 37.43           O  
HETATM 1467  O   HOH A 431      38.294  49.441  27.903  1.00 46.17           O  
HETATM 1468  O   HOH A 432      22.362  60.376  -3.541  1.00 66.38           O  
HETATM 1469  O   HOH A 433      11.808  27.768  22.294  1.00 43.68           O  
HETATM 1470  O   HOH A 434      44.275  30.045  19.046  1.00 37.69           O  
HETATM 1471  O   HOH A 435      15.397  28.064  25.099  1.00 46.47           O  
HETATM 1472  O   HOH A 436      16.422  62.253  10.448  1.00 36.46           O  
HETATM 1473  O   HOH A 437      43.823  46.503  20.840  1.00 45.05           O  
HETATM 1474  O   HOH A 438      26.806  49.085  -2.139  1.00 42.99           O  
HETATM 1475  O   HOH A 439      29.276  48.261  26.005  1.00 45.48           O  
HETATM 1476  O   HOH A 440      34.738  43.629  31.575  1.00 41.56           O  
HETATM 1477  O   HOH A 441      37.100  35.717   4.364  1.00 40.43           O  
HETATM 1478  O   HOH A 442      36.032  54.926   0.528  1.00 42.09           O  
HETATM 1479  O   HOH A 443      18.823  62.507   5.104  1.00 41.12           O  
HETATM 1480  O   HOH A 444      26.161  25.448  21.812  1.00 54.41           O  
HETATM 1481  O   HOH A 445      16.920  63.815  12.322  1.00 31.37           O  
HETATM 1482  O   HOH A 446      14.513  36.192   6.411  1.00 37.32           O  
HETATM 1483  O   HOH A 447      27.849  38.509  27.695  1.00 50.53           O  
HETATM 1484  O   HOH A 448      12.848  43.248  14.705  1.00 32.66           O  
HETATM 1485  O   HOH A 449      34.266  32.704  23.490  1.00 42.99           O  
HETATM 1486  O   HOH A 450      36.230  57.298  18.616  1.00 47.13           O  
HETATM 1487  O   HOH A 451      29.040  58.367  19.300  1.00 47.39           O  
HETATM 1488  O   HOH A 452      26.300  53.121  -4.518  1.00 47.34           O  
HETATM 1489  O   HOH A 453      34.794  35.333  23.379  1.00 39.10           O  
HETATM 1490  O   HOH A 454      48.284  35.320  15.466  1.00 39.06           O  
HETATM 1491  O   HOH A 455      46.434  37.034  13.574  1.00 48.26           O  
HETATM 1492  O   HOH A 456      43.905  34.734  12.089  1.00 45.43           O  
HETATM 1493  O   HOH A 457      30.309  31.148   4.856  1.00 38.09           O  
HETATM 1494  O   HOH A 458      28.664  62.787   8.084  1.00 35.77           O  
HETATM 1495  O   HOH A 459      11.202  46.413   7.197  1.00 42.08           O  
HETATM 1496  O   HOH A 460      12.667  44.350   7.721  1.00 49.73           O  
HETATM 1497  O   HOH A 461      31.479  62.261   7.319  1.00 45.35           O  
HETATM 1498  O   HOH A 462      19.176  32.350  30.798  1.00 41.12           O  
HETATM 1499  O   HOH A 463      12.476  55.763  17.134  1.00 41.45           O  
HETATM 1500  O   HOH A 464      41.846  25.183  18.482  1.00 47.37           O  
HETATM 1501  O   HOH A 465      19.587  31.805  10.492  1.00 38.19           O  
HETATM 1502  O   HOH A 466      39.051  27.628  11.949  1.00 36.87           O  
HETATM 1503  O   HOH A 467      23.486  64.180   4.253  1.00 40.98           O  
HETATM 1504  O   HOH A 468      33.066  53.001  24.118  1.00 46.59           O  
CONECT 1200 1303                                                                
CONECT 1260 1270                                                                
CONECT 1270 1260 1419 1461                                                      
CONECT 1271 1272 1282                                                           
CONECT 1272 1271 1273 1274                                                      
CONECT 1273 1272                                                                
CONECT 1274 1272 1275                                                           
CONECT 1275 1274 1276 1277                                                      
CONECT 1276 1275                                                                
CONECT 1277 1275 1278 1282                                                      
CONECT 1278 1277 1279                                                           
CONECT 1279 1278 1280 1283                                                      
CONECT 1280 1279 1281                                                           
CONECT 1281 1280 1282                                                           
CONECT 1282 1271 1277 1281                                                      
CONECT 1283 1279 1284                                                           
CONECT 1284 1283 1288                                                           
CONECT 1285 1286 1290 1291                                                      
CONECT 1286 1285 1287                                                           
CONECT 1287 1286 1288                                                           
CONECT 1288 1284 1287 1289                                                      
CONECT 1289 1288 1290                                                           
CONECT 1290 1285 1289                                                           
CONECT 1291 1285 1292 1293                                                      
CONECT 1292 1291                                                                
CONECT 1293 1291 1294                                                           
CONECT 1294 1293 1295 1300                                                      
CONECT 1295 1294 1296                                                           
CONECT 1296 1295 1297                                                           
CONECT 1297 1296 1298 1299                                                      
CONECT 1298 1297                                                                
CONECT 1299 1297                                                                
CONECT 1300 1294 1301 1302                                                      
CONECT 1301 1300                                                                
CONECT 1302 1300                                                                
CONECT 1303 1200                                                                
CONECT 1304 1305 1306 1307 1326                                                 
CONECT 1305 1304                                                                
CONECT 1306 1304                                                                
CONECT 1307 1304 1308                                                           
CONECT 1308 1307 1309                                                           
CONECT 1309 1308 1310 1311                                                      
CONECT 1310 1309 1315                                                           
CONECT 1311 1309 1312 1313                                                      
CONECT 1312 1311                                                                
CONECT 1313 1311 1314 1315                                                      
CONECT 1314 1313 1348                                                           
CONECT 1315 1310 1313 1316                                                      
CONECT 1316 1315 1317 1325                                                      
CONECT 1317 1316 1318                                                           
CONECT 1318 1317 1319                                                           
CONECT 1319 1318 1320 1325                                                      
CONECT 1320 1319 1321 1322                                                      
CONECT 1321 1320                                                                
CONECT 1322 1320 1323                                                           
CONECT 1323 1322 1324                                                           
CONECT 1324 1323 1325                                                           
CONECT 1325 1316 1319 1324                                                      
CONECT 1326 1304 1327                                                           
CONECT 1327 1326 1328 1329 1330                                                 
CONECT 1328 1327                                                                
CONECT 1329 1327                                                                
CONECT 1330 1327 1331                                                           
CONECT 1331 1330 1332                                                           
CONECT 1332 1331 1333 1334                                                      
CONECT 1333 1332 1338                                                           
CONECT 1334 1332 1335 1336                                                      
CONECT 1335 1334                                                                
CONECT 1336 1334 1337 1338                                                      
CONECT 1337 1336                                                                
CONECT 1338 1333 1336 1339                                                      
CONECT 1339 1338 1340 1347                                                      
CONECT 1340 1339 1341                                                           
CONECT 1341 1340 1342 1345                                                      
CONECT 1342 1341 1343 1344                                                      
CONECT 1343 1342                                                                
CONECT 1344 1342                                                                
CONECT 1345 1341 1346                                                           
CONECT 1346 1345 1347                                                           
CONECT 1347 1339 1346                                                           
CONECT 1348 1314 1349 1350 1351                                                 
CONECT 1349 1348                                                                
CONECT 1350 1348                                                                
CONECT 1351 1348                                                                
CONECT 1419 1270                                                                
CONECT 1461 1270                                                                
MASTER      318    0    4    4    8    0   17    6 1503    1   86   13          
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.