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***  HYDROLASE 17-SEP-08 3EIY  ***

elNémo ID: 220307235056119413

Job options:

ID        	=	 220307235056119413
JOBID     	=	 HYDROLASE 17-SEP-08 3EIY
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    HYDROLASE                               17-SEP-08   3EIY              
TITLE     CRYSTAL STRUCTURE OF INORGANIC PYROPHOSPHATASE FROM BURKHOLDERIA      
TITLE    2 PSEUDOMALLEI WITH BOUND PYROPHOSPHATE                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INORGANIC PYROPHOSPHATASE;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.6.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI 1710B;                
SOURCE   3 ORGANISM_TAXID: 320372;                                              
SOURCE   4 GENE: PPA, BURPS1710B_1237;                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: AVA0421                                   
KEYWDS    STRUCTURAL GENOMICS, SSGCID, PYROPHOSPHATASE, HYDROLASE,              
KEYWDS   2 BUPSA.00023.A, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS     
KEYWDS   3 DISEASE'                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   4   23-OCT-13 3EIY    1       REMARK                                   
REVDAT   3   05-OCT-11 3EIY    1       JRNL   VERSN                             
REVDAT   2   24-FEB-09 3EIY    1       VERSN                                    
REVDAT   1   30-SEP-08 3EIY    0                                                
JRNL        AUTH   W.C.VAN VOORHIS,W.G.HOL,P.J.MYLER,L.J.STEWART                
JRNL        TITL   THE ROLE OF MEDICAL STRUCTURAL GENOMICS IN DISCOVERING NEW   
JRNL        TITL 2 DRUGS FOR INFECTIOUS DISEASES.                               
JRNL        REF    PLOS COMPUT BIOL              V.   5 00530 2009              
JRNL        REFN                                                                
JRNL        PMID   19855826                                                     
JRNL        DOI    10.1371/JOURNAL.PCBI.1000530                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   L.BAUGH,L.A.GALLAGHER,R.PATRAPUVICH,M.C.CLIFTON,             
REMARK   1  AUTH 2 A.S.GARDBERG,T.E.EDWARDS,B.ARMOUR,D.W.BEGLEY,S.H.DIETERICH,  
REMARK   1  AUTH 3 D.M.DRANOW,J.ABENDROTH,J.W.FAIRMAN,D.FOX,B.L.STAKER,I.PHAN,  
REMARK   1  AUTH 4 A.GILLESPIE,R.CHOI,S.NAKAZAWA-HEWITT,M.T.NGUYEN,A.NAPULI,    
REMARK   1  AUTH 5 L.BARRETT,G.W.BUCHKO,R.STACY,P.J.MYLER,L.J.STEWART,C.MANOIL, 
REMARK   1  AUTH 6 W.C.VAN VOORHIS                                              
REMARK   1  TITL   COMBINING FUNCTIONAL AND STRUCTURAL GENOMICS TO SAMPLE THE   
REMARK   1  TITL 2 ESSENTIAL BURKHOLDERIA STRUCTOME.                            
REMARK   1  REF    PLOS ONE                      V.   8 53851 2013              
REMARK   1  REFN                   ESSN 1932-6203                               
REMARK   1  PMID   23382856                                                     
REMARK   1  DOI    10.1371/JOURNAL.PONE.0053851                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0067                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 19547                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 991                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1250                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.60                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 71                           
REMARK   3   BIN FREE R VALUE                    : 0.4070                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1330                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 112                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.80000                                              
REMARK   3    B22 (A**2) : 0.80000                                              
REMARK   3    B33 (A**2) : -1.21000                                             
REMARK   3    B12 (A**2) : 0.40000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.156         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.152         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.110         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.164         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1393 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1886 ; 1.460 ; 1.994       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   173 ; 5.857 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    56 ;32.570 ;25.357       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   222 ;15.203 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     4 ;18.890 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   209 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1034 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   870 ; 0.890 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1408 ; 1.604 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   523 ; 2.198 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   478 ; 3.551 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3EIY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB049380.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-SEP-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.30                               
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 MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19792                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.10300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NA/K PHOSPHATE, PH 6.3, 49.5%     
REMARK 280  PEG 200. CRYSTAL 3 MONTHS OLD., PH 6.30, VAPOR DIFFUSION, SITTING   
REMARK 280  DROP, TEMPERATURE 289K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       55.61650            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       55.61650            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       55.61650            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       55.61650            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       55.61650            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       55.61650            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 20130 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -208.0 KCAL/MOL                       
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 350   BIOMT1   2 -0.500000 -0.866025  0.000000       50.47600            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000       87.42700            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000      -50.47600            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000       87.42700            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.500000 -0.866025  0.000000       50.47600            
REMARK 350   BIOMT2   4 -0.866025 -0.500000  0.000000       87.42700            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000       55.61650            
REMARK 350   BIOMT1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000       55.61650            
REMARK 350   BIOMT1   6  0.500000  0.866025  0.000000      -50.47600            
REMARK 350   BIOMT2   6  0.866025 -0.500000  0.000000       87.42700            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000       55.61650            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.0 KCAL/MOL                        
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 350   BIOMT1   2 -0.500000 -0.866025  0.000000       50.47600            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000       87.42700            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000      -50.47600            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000       87.42700            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 K      K A 176  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -20                                                      
REMARK 465     ALA A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     MET A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     THR A   -10                                                      
REMARK 465     LEU A    -9                                                      
REMARK 465     GLU A    -8                                                      
REMARK 465     ALA A    -7                                                      
REMARK 465     GLN A    -6                                                      
REMARK 465     THR A    -5                                                      
REMARK 465     GLN A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 113    CG   CD   CE   NZ                                   
REMARK 470     LYS A 147    CG   CD   CE   NZ                                   
REMARK 470     LYS A 152    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   238     O    HOH A   281              2.06            
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    ASP A  11       81.33   -159.79                                   
REMARK 500    ASP A  98     -168.63   -122.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 176   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  11   OD1                                                    
REMARK 620 2 LEU A  12   O    92.8                                              
REMARK 620 3 GLN A  14   OE1 100.9  87.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 178  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  71   OD2                                                    
REMARK 620 2 ASP A 103   OD1  94.9                                              
REMARK 620 3 ALA A 104   O   102.5  85.4                                        
REMARK 620 4 HOH A 247   O   169.6  95.4  79.9                                  
REMARK 620 5 HOH A 245   O    72.2 146.6 127.0  98.2                            
REMARK 620 6 HOH A 263   O    85.2 155.0  70.3  86.0  56.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 177  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  98   OD2                                                    
REMARK 620 2 ASP A 103   OD2  91.4                                              
REMARK 620 3 POP A 179   O6   93.1 172.2                                        
REMARK 620 4 HOH A 257   O    78.3  74.9 112.2                                  
REMARK 620 5 POP A 179   O3  165.9 100.0  76.6  96.5                            
REMARK 620 6 HOH A 201   O    89.4  88.0  85.7 158.6  99.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 176                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 177                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 178                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POP A 179                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 180                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 181                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 182                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: BUPSA.00023.A   RELATED DB: TARGETDB                     
REMARK 900 RELATED ID: 3D63   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN, "OPEN" CONFORMATION, APO FORM, IN SPACE            
REMARK 900 GROUP P21212                                                         
REMARK 900 RELATED ID: 3EIZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EJ0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EJ2   RELATED DB: PDB                                   
DBREF  3EIY A    1   175  UNP    Q3JUV5   Q3JUV5_BURP1     1    175             
SEQADV 3EIY MET A  -20  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY ALA A  -19  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY HIS A  -18  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY HIS A  -17  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY HIS A  -16  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY HIS A  -15  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY HIS A  -14  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY HIS A  -13  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY MET A  -12  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY GLY A  -11  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY THR A  -10  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY LEU A   -9  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY GLU A   -8  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY ALA A   -7  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY GLN A   -6  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY THR A   -5  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY GLN A   -4  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY GLY A   -3  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY PRO A   -2  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY GLY A   -1  UNP  Q3JUV5              EXPRESSION TAG                 
SEQADV 3EIY SER A    0  UNP  Q3JUV5              EXPRESSION TAG                 
SEQRES   1 A  196  MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU          
SEQRES   2 A  196  ALA GLN THR GLN GLY PRO GLY SER MET SER PHE SER ASN          
SEQRES   3 A  196  VAL PRO ALA GLY LYS ASP LEU PRO GLN ASP PHE ASN VAL          
SEQRES   4 A  196  ILE ILE GLU ILE PRO ALA GLN SER GLU PRO VAL LYS TYR          
SEQRES   5 A  196  GLU ALA ASP LYS ALA LEU GLY LEU LEU VAL VAL ASP ARG          
SEQRES   6 A  196  PHE ILE GLY THR GLY MET ARG TYR PRO VAL ASN TYR GLY          
SEQRES   7 A  196  PHE ILE PRO GLN THR LEU SER GLY ASP GLY ASP PRO VAL          
SEQRES   8 A  196  ASP VAL LEU VAL ILE THR PRO PHE PRO LEU LEU ALA GLY          
SEQRES   9 A  196  SER VAL VAL ARG ALA ARG ALA LEU GLY MET LEU LYS MET          
SEQRES  10 A  196  THR ASP GLU SER GLY VAL ASP ALA LYS LEU VAL ALA VAL          
SEQRES  11 A  196  PRO HIS ASP LYS VAL CYS PRO MET THR ALA ASN LEU LYS          
SEQRES  12 A  196  SER ILE ASP ASP VAL PRO ALA TYR LEU LYS ASP GLN ILE          
SEQRES  13 A  196  LYS HIS PHE PHE GLU GLN TYR LYS ALA LEU GLU LYS GLY          
SEQRES  14 A  196  LYS TRP VAL LYS VAL GLU GLY TRP ASP GLY ILE ASP ALA          
SEQRES  15 A  196  ALA HIS LYS GLU ILE THR ASP GLY VAL ALA ASN PHE LYS          
SEQRES  16 A  196  LYS                                                          
HET      K  A 176       1                                                       
HET     NA  A 177       1                                                       
HET     NA  A 178       1                                                       
HET    POP  A 179       9                                                       
HET    PG4  A 180      13                                                       
HET    PEG  A 181       7                                                       
HET    PEG  A 182       7                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM      NA SODIUM ION                                                       
HETNAM     POP PYROPHOSPHATE 2-                                                 
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
FORMUL   2    K    K 1+                                                         
FORMUL   3   NA    2(NA 1+)                                                     
FORMUL   5  POP    H2 O7 P2 2-                                                  
FORMUL   6  PG4    C8 H18 O5                                                    
FORMUL   7  PEG    2(C4 H10 O3)                                                 
FORMUL   9  HOH   *112(H2 O)                                                    
HELIX    1   1 SER A    2  VAL A    6  5                                   5    
HELIX    2   2 CYS A  115  ALA A  119  5                                   5    
HELIX    3   3 SER A  123  VAL A  127  5                                   5    
HELIX    4   4 PRO A  128  TYR A  142  1                                  15    
HELIX    5   5 GLY A  158  LYS A  175  1                                  18    
SHEET    1   A 7 VAL A 151  ASP A 157  0                                        
SHEET    2   A 7 VAL A  85  ASP A  98 -1  N  LYS A  95   O  GLY A 155           
SHEET    3   A 7 GLY A 101  PRO A 110 -1  O  LYS A 105   N  LEU A  94           
SHEET    4   A 7 VAL A  70  VAL A  74  1  N  LEU A  73   O  ALA A 108           
SHEET    5   A 7 ASN A  55  ILE A  59 -1  N  GLY A  57   O  VAL A  72           
SHEET    6   A 7 PHE A  16  ILE A  22 -1  N  ILE A  19   O  PHE A  58           
SHEET    7   A 7 VAL A  85  ASP A  98 -1  O  ALA A  88   N  PHE A  16           
SHEET    1   B 2 VAL A  29  ASP A  34  0                                        
SHEET    2   B 2 LEU A  39  PHE A  45 -1  O  LEU A  39   N  ASP A  34           
LINK         OD1 ASP A  11                 K     K A 176     1555   1555  2.73  
LINK         O   LEU A  12                 K     K A 176     1555   1555  2.65  
LINK         OE1 GLN A  14                 K     K A 176     1555   1555  2.92  
LINK         OD2 ASP A  71                NA    NA A 178     1555   1555  2.81  
LINK         OD2 ASP A  98                NA    NA A 177     1555   1555  2.65  
LINK         OD1 ASP A 103                NA    NA A 178     1555   1555  2.53  
LINK         OD2 ASP A 103                NA    NA A 177     1555   1555  2.58  
LINK         O   ALA A 104                NA    NA A 178     1555   1555  2.92  
LINK        NA    NA A 177                 O6  POP A 179     1555   1555  2.56  
LINK        NA    NA A 177                 O   HOH A 257     1555   1555  2.65  
LINK        NA    NA A 177                 O3  POP A 179     1555   1555  2.20  
LINK        NA    NA A 177                 O   HOH A 201     1555   1555  2.50  
LINK        NA    NA A 178                 O   HOH A 247     1555   1555  2.86  
LINK        NA    NA A 178                 O   HOH A 245     1555   1555  2.66  
LINK        NA    NA A 178                 O   HOH A 263     1555   1555  2.50  
CISPEP   1 LEU A   12    PRO A   13          0        -0.44                     
SITE     1 AC1  3 ASP A  11  LEU A  12  GLN A  14                               
SITE     1 AC2  6 ASP A  98  ASP A 103  LYS A 143  POP A 179                    
SITE     2 AC2  6 HOH A 201  HOH A 257                                          
SITE     1 AC3  7 ASP A  66  ASP A  71  ASP A 103  ALA A 104                    
SITE     2 AC3  7 HOH A 245  HOH A 247  HOH A 263                               
SITE     1 AC4 14 LYS A  30  ARG A  44  TYR A  56  ASP A 103                    
SITE     2 AC4 14 LYS A 105  TYR A 142  LYS A 143   NA A 177                    
SITE     3 AC4 14 HOH A 200  HOH A 221  HOH A 238  HOH A 239                    
SITE     4 AC4 14 HOH A 260  HOH A 267                                          
SITE     1 AC5  7 GLY A   9  LYS A  10  ASP A  11  LEU A  12                    
SITE     2 AC5  7 GLN A  14  ASP A 160  HIS A 163                               
SITE     1 AC6  4 LYS A 136  VAL A 153  GLU A 154  TRP A 156                    
SITE     1 AC7  3 ARG A  87  LYS A 113  VAL A 114                               
CRYST1  100.952  100.952  111.233  90.00  90.00 120.00 P 63 2 2     12          
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      0.009906  0.005719  0.000000        0.00000                         
SCALE2      0.000000  0.011438  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008990        0.00000                         
ATOM      1  N   SER A   2       2.527  54.656  -1.667  1.00 52.73           N  
ATOM      2  CA  SER A   2       3.259  54.783  -0.368  1.00 52.54           C  
ATOM      3  C   SER A   2       4.127  53.553  -0.105  1.00 52.03           C  
ATOM      4  O   SER A   2       5.274  53.451  -0.594  1.00 52.45           O  
ATOM      5  CB  SER A   2       2.273  54.944   0.792  1.00 52.69           C  
ATOM      6  OG  SER A   2       2.066  56.306   1.121  1.00 54.37           O  
ATOM      7  N   PHE A   3       3.563  52.626   0.674  1.00 50.61           N  
ATOM      8  CA  PHE A   3       4.261  51.413   1.102  1.00 48.73           C  
ATOM      9  C   PHE A   3       4.881  50.670  -0.064  1.00 48.17           C  
ATOM     10  O   PHE A   3       6.035  50.257   0.019  1.00 47.56           O  
ATOM     11  CB  PHE A   3       3.342  50.479   1.896  1.00 47.95           C  
ATOM     12  CG  PHE A   3       2.747  51.112   3.120  1.00 46.23           C  
ATOM     13  CD1 PHE A   3       3.425  52.100   3.804  1.00 43.75           C  
ATOM     14  CD2 PHE A   3       1.509  50.701   3.594  1.00 45.77           C  
ATOM     15  CE1 PHE A   3       2.893  52.679   4.942  1.00 44.62           C  
ATOM     16  CE2 PHE A   3       0.955  51.280   4.728  1.00 45.65           C  
ATOM     17  CZ  PHE A   3       1.655  52.273   5.409  1.00 45.91           C  
ATOM     18  N   SER A   4       4.122  50.518  -1.151  1.00 47.69           N  
ATOM     19  CA  SER A   4       4.593  49.745  -2.323  1.00 47.00           C  
ATOM     20  C   SER A   4       5.896  50.254  -2.977  1.00 45.29           C  
ATOM     21  O   SER A   4       6.627  49.479  -3.592  1.00 45.34           O  
ATOM     22  CB  SER A   4       3.489  49.633  -3.387  1.00 47.47           C  
ATOM     23  OG  SER A   4       3.169  50.916  -3.908  1.00 49.92           O  
ATOM     24  N   ASN A   5       6.184  51.544  -2.832  1.00 43.32           N  
ATOM     25  CA  ASN A   5       7.351  52.145  -3.480  1.00 41.42           C  
ATOM     26  C   ASN A   5       8.584  52.307  -2.574  1.00 39.00           C  
ATOM     27  O   ASN A   5       9.629  52.802  -3.000  1.00 38.69           O  
ATOM     28  CB  ASN A   5       6.958  53.491  -4.094  1.00 42.02           C  
ATOM     29  CG  ASN A   5       6.108  53.321  -5.366  1.00 45.67           C  
ATOM     30  OD1 ASN A   5       4.862  53.286  -5.312  1.00 48.48           O  
ATOM     31  ND2 ASN A   5       6.784  53.176  -6.513  1.00 47.35           N  
ATOM     32  N   VAL A   6       8.466  51.922  -1.312  1.00 35.70           N  
ATOM     33  CA  VAL A   6       9.636  51.959  -0.457  1.00 32.41           C  
ATOM     34  C   VAL A   6      10.595  50.807  -0.862  1.00 30.30           C  
ATOM     35  O   VAL A   6      10.176  49.658  -0.964  1.00 29.28           O  
ATOM     36  CB  VAL A   6       9.242  51.846   1.038  1.00 32.26           C  
ATOM     37  CG1 VAL A   6      10.476  51.902   1.905  1.00 30.72           C  
ATOM     38  CG2 VAL A   6       8.257  52.934   1.415  1.00 30.80           C  
ATOM     39  N   PRO A   7      11.890  51.109  -1.064  1.00 28.73           N  
ATOM     40  CA  PRO A   7      12.827  50.031  -1.447  1.00 27.85           C  
ATOM     41  C   PRO A   7      12.952  49.030  -0.321  1.00 26.92           C  
ATOM     42  O   PRO A   7      12.827  49.397   0.859  1.00 26.32           O  
ATOM     43  CB  PRO A   7      14.159  50.763  -1.644  1.00 27.56           C  
ATOM     44  CG  PRO A   7      13.784  52.193  -1.869  1.00 28.99           C  
ATOM     45  CD  PRO A   7      12.550  52.421  -1.016  1.00 28.59           C  
ATOM     46  N   ALA A   8      13.208  47.777  -0.660  1.00 26.04           N  
ATOM     47  CA  ALA A   8      13.463  46.785   0.378  1.00 25.67           C  
ATOM     48  C   ALA A   8      14.702  47.145   1.205  1.00 25.55           C  
ATOM     49  O   ALA A   8      14.786  46.804   2.395  1.00 25.75           O  
ATOM     50  CB  ALA A   8      13.588  45.395  -0.224  1.00 25.25           C  
ATOM     51  N   GLY A   9      15.668  47.834   0.598  1.00 25.34           N  
ATOM     52  CA  GLY A   9      16.864  48.237   1.344  1.00 25.46           C  
ATOM     53  C   GLY A   9      17.905  48.951   0.506  1.00 26.30           C  
ATOM     54  O   GLY A   9      17.865  48.854  -0.717  1.00 26.99           O  
ATOM     55  N   LYS A  10      18.834  49.654   1.159  1.00 26.15           N  
ATOM     56  CA  LYS A  10      19.941  50.322   0.477  1.00 27.63           C  
ATOM     57  C   LYS A  10      21.104  49.348   0.102  1.00 27.17           C  
ATOM     58  O   LYS A  10      21.920  49.640  -0.769  1.00 28.04           O  
ATOM     59  CB  LYS A  10      20.522  51.442   1.352  1.00 27.27           C  
ATOM     60  CG  LYS A  10      19.619  52.654   1.569  1.00 32.65           C  
ATOM     61  CD  LYS A  10      20.334  53.690   2.451  1.00 38.46           C  
ATOM     62  CE  LYS A  10      19.720  55.094   2.319  1.00 42.10           C  
ATOM     63  NZ  LYS A  10      18.235  55.016   2.421  1.00 42.82           N  
ATOM     64  N   ASP A  11      21.204  48.221   0.782  1.00 26.40           N  
ATOM     65  CA  ASP A  11      22.265  47.261   0.452  1.00 25.76           C  
ATOM     66  C   ASP A  11      21.901  45.893   0.979  1.00 24.71           C  
ATOM     67  O   ASP A  11      22.369  45.488   2.037  1.00 25.14           O  
ATOM     68  CB  ASP A  11      23.639  47.723   0.995  1.00 25.24           C  
ATOM     69  CG  ASP A  11      24.809  47.007   0.321  1.00 26.43           C  
ATOM     70  OD1 ASP A  11      24.583  45.956  -0.326  1.00 25.79           O  
ATOM     71  OD2 ASP A  11      25.973  47.447   0.460  1.00 27.48           O  
ATOM     72  N   LEU A  12      21.065  45.188   0.225  1.00 24.00           N  
ATOM     73  CA  LEU A  12      20.522  43.892   0.629  1.00 24.17           C  
ATOM     74  C   LEU A  12      21.527  42.731   0.574  1.00 24.26           C  
ATOM     75  O   LEU A  12      22.415  42.717  -0.279  1.00 23.90           O  
ATOM     76  CB  LEU A  12      19.327  43.549  -0.255  1.00 23.47           C  
ATOM     77  CG  LEU A  12      18.183  44.559  -0.124  1.00 24.51           C  
ATOM     78  CD1 LEU A  12      17.245  44.405  -1.303  1.00 24.49           C  
ATOM     79  CD2 LEU A  12      17.457  44.315   1.204  1.00 21.79           C  
ATOM     80  N   PRO A  13      21.386  41.743   1.476  1.00 24.36           N  
ATOM     81  CA  PRO A  13      20.351  41.670   2.533  1.00 24.17           C  
ATOM     82  C   PRO A  13      20.685  42.375   3.838  1.00 24.39           C  
ATOM     83  O   PRO A  13      19.834  42.426   4.711  1.00 25.43           O  
ATOM     84  CB  PRO A  13      20.288  40.158   2.827  1.00 23.15           C  
ATOM     85  CG  PRO A  13      21.729  39.721   2.577  1.00 24.50           C  
ATOM     86  CD  PRO A  13      22.089  40.451   1.320  1.00 23.40           C  
ATOM     87  N   GLN A  14      21.914  42.858   4.024  1.00 24.55           N  
ATOM     88  CA  GLN A  14      22.326  43.248   5.367  1.00 24.52           C  
ATOM     89  C   GLN A  14      21.819  44.648   5.828  1.00 24.75           C  
ATOM     90  O   GLN A  14      21.677  44.894   7.030  1.00 24.93           O  
ATOM     91  CB  GLN A  14      23.855  43.075   5.569  1.00 24.43           C  
ATOM     92  CG  GLN A  14      24.713  44.188   5.026  1.00 23.98           C  
ATOM     93  CD  GLN A  14      25.043  43.985   3.535  1.00 28.20           C  
ATOM     94  OE1 GLN A  14      24.581  43.009   2.886  1.00 24.90           O  
ATOM     95  NE2 GLN A  14      25.852  44.905   2.978  1.00 26.11           N  
ATOM     96  N   ASP A  15      21.564  45.534   4.870  1.00 23.84           N  
ATOM     97  CA  ASP A  15      21.118  46.909   5.116  1.00 24.38           C  
ATOM     98  C   ASP A  15      19.713  47.043   4.478  1.00 23.69           C  
ATOM     99  O   ASP A  15      19.595  47.207   3.252  1.00 24.21           O  
ATOM    100  CB  ASP A  15      22.139  47.858   4.480  1.00 23.38           C  
ATOM    101  CG  ASP A  15      21.822  49.319   4.698  1.00 26.33           C  
ATOM    102  OD1 ASP A  15      20.881  49.684   5.451  1.00 27.50           O  
ATOM    103  OD2 ASP A  15      22.525  50.140   4.100  1.00 26.80           O  
ATOM    104  N   PHE A  16      18.663  46.860   5.294  1.00 23.31           N  
ATOM    105  CA  PHE A  16      17.273  46.837   4.816  1.00 23.19           C  
ATOM    106  C   PHE A  16      16.304  47.845   5.526  1.00 23.35           C  
ATOM    107  O   PHE A  16      16.611  48.396   6.589  1.00 23.52           O  
ATOM    108  CB  PHE A  16      16.708  45.420   4.913  1.00 22.15           C  
ATOM    109  CG  PHE A  16      16.755  44.850   6.304  1.00 23.52           C  
ATOM    110  CD1 PHE A  16      15.651  44.981   7.178  1.00 21.74           C  
ATOM    111  CD2 PHE A  16      17.894  44.177   6.749  1.00 21.69           C  
ATOM    112  CE1 PHE A  16      15.692  44.448   8.458  1.00 23.07           C  
ATOM    113  CE2 PHE A  16      17.962  43.648   8.041  1.00 21.56           C  
ATOM    114  CZ  PHE A  16      16.870  43.770   8.903  1.00 22.24           C  
ATOM    115  N   ASN A  17      15.127  48.049   4.936  1.00 23.34           N  
ATOM    116  CA  ASN A  17      14.124  48.961   5.479  1.00 22.99           C  
ATOM    117  C   ASN A  17      12.974  48.168   6.088  1.00 22.52           C  
ATOM    118  O   ASN A  17      12.615  47.109   5.587  1.00 21.94           O  
ATOM    119  CB  ASN A  17      13.567  49.872   4.354  1.00 24.37           C  
ATOM    120  CG  ASN A  17      14.635  50.818   3.792  1.00 24.52           C  
ATOM    121  OD1 ASN A  17      15.483  51.296   4.541  1.00 26.24           O  
ATOM    122  ND2 ASN A  17      14.609  51.063   2.469  1.00 22.96           N  
ATOM    123  N   VAL A  18      12.406  48.688   7.175  1.00 22.23           N  
ATOM    124  CA  VAL A  18      11.233  48.079   7.822  1.00 20.84           C  
ATOM    125  C   VAL A  18      10.145  49.150   7.953  1.00 20.77           C  
ATOM    126  O   VAL A  18      10.375  50.259   8.466  1.00 20.23           O  
ATOM    127  CB  VAL A  18      11.556  47.505   9.264  1.00 21.36           C  
ATOM    128  CG1 VAL A  18      10.350  46.768   9.827  1.00 19.07           C  
ATOM    129  CG2 VAL A  18      12.803  46.559   9.236  1.00 19.34           C  
ATOM    130  N   ILE A  19       8.968  48.830   7.446  1.00 20.63           N  
ATOM    131  CA  ILE A  19       7.808  49.672   7.712  1.00 21.06           C  
ATOM    132  C   ILE A  19       7.109  49.163   8.967  1.00 20.14           C  
ATOM    133  O   ILE A  19       6.763  47.954   9.057  1.00 19.42           O  
ATOM    134  CB  ILE A  19       6.841  49.673   6.498  1.00 22.11           C  
ATOM    135  CG1 ILE A  19       7.500  50.469   5.349  1.00 22.28           C  
ATOM    136  CG2 ILE A  19       5.467  50.272   6.876  1.00 19.98           C  
ATOM    137  CD1 ILE A  19       6.887  50.180   3.973  1.00 24.13           C  
ATOM    138  N   ILE A  20       6.914  50.062   9.937  1.00 19.07           N  
ATOM    139  CA  ILE A  20       6.335  49.641  11.228  1.00 18.73           C  
ATOM    140  C   ILE A  20       4.808  49.541  11.151  1.00 19.01           C  
ATOM    141  O   ILE A  20       4.148  50.500  10.726  1.00 20.15           O  
ATOM    142  CB  ILE A  20       6.767  50.609  12.367  1.00 18.68           C  
ATOM    143  CG1 ILE A  20       8.310  50.664  12.407  1.00 18.52           C  
ATOM    144  CG2 ILE A  20       6.131  50.202  13.761  1.00 17.94           C  
ATOM    145  CD1 ILE A  20       8.972  49.240  12.614  1.00 16.95           C  
ATOM    146  N   GLU A  21       4.251  48.404  11.563  1.00 18.77           N  
ATOM    147  CA  GLU A  21       2.788  48.243  11.677  1.00 19.87           C  
ATOM    148  C   GLU A  21       2.290  48.373  13.130  1.00 19.89           C  
ATOM    149  O   GLU A  21       1.226  48.954  13.377  1.00 20.64           O  
ATOM    150  CB  GLU A  21       2.343  46.896  11.092  1.00 19.24           C  
ATOM    151  CG  GLU A  21       2.620  46.756   9.582  1.00 21.01           C  
ATOM    152  CD  GLU A  21       2.500  45.327   9.118  1.00 22.65           C  
ATOM    153  OE1 GLU A  21       3.120  44.447   9.729  1.00 26.58           O  
ATOM    154  OE2 GLU A  21       1.771  45.072   8.153  1.00 23.20           O  
ATOM    155  N   ILE A  22       3.076  47.870  14.079  1.00 19.73           N  
ATOM    156  CA  ILE A  22       2.667  47.809  15.505  1.00 19.94           C  
ATOM    157  C   ILE A  22       3.788  48.237  16.456  1.00 19.81           C  
ATOM    158  O   ILE A  22       4.767  47.517  16.605  1.00 21.37           O  
ATOM    159  CB  ILE A  22       2.182  46.370  15.899  1.00 20.44           C  
ATOM    160  CG1 ILE A  22       1.021  45.935  15.009  1.00 19.03           C  
ATOM    161  CG2 ILE A  22       1.789  46.307  17.367  1.00 19.40           C  
ATOM    162  CD1 ILE A  22       0.659  44.455  15.118  1.00 19.72           C  
ATOM    163  N   PRO A  23       3.672  49.434  17.073  1.00 19.24           N  
ATOM    164  CA  PRO A  23       4.714  49.919  18.016  1.00 18.94           C  
ATOM    165  C   PRO A  23       4.816  48.987  19.246  1.00 19.28           C  
ATOM    166  O   PRO A  23       3.819  48.398  19.666  1.00 19.56           O  
ATOM    167  CB  PRO A  23       4.201  51.308  18.436  1.00 18.92           C  
ATOM    168  CG  PRO A  23       3.286  51.728  17.295  1.00 17.76           C  
ATOM    169  CD  PRO A  23       2.608  50.421  16.861  1.00 17.40           C  
ATOM    170  N   ALA A  24       6.026  48.803  19.761  1.00 18.68           N  
ATOM    171  CA  ALA A  24       6.227  48.079  21.006  1.00 18.54           C  
ATOM    172  C   ALA A  24       5.270  48.569  22.090  1.00 18.10           C  
ATOM    173  O   ALA A  24       5.137  49.785  22.277  1.00 18.29           O  
ATOM    174  CB  ALA A  24       7.660  48.250  21.486  1.00 17.41           C  
ATOM    175  N   GLN A  25       4.623  47.639  22.805  1.00 17.44           N  
ATOM    176  CA  GLN A  25       3.743  48.001  23.972  1.00 18.87           C  
ATOM    177  C   GLN A  25       2.476  48.811  23.642  1.00 18.88           C  
ATOM    178  O   GLN A  25       1.787  49.325  24.541  1.00 19.08           O  
ATOM    179  CB  GLN A  25       4.570  48.733  25.062  1.00 18.70           C  
ATOM    180  CG  GLN A  25       5.715  47.839  25.644  1.00 19.85           C  
ATOM    181  CD  GLN A  25       5.192  46.588  26.346  1.00 22.15           C  
ATOM    182  OE1 GLN A  25       4.040  46.540  26.806  1.00 25.01           O  
ATOM    183  NE2 GLN A  25       6.035  45.573  26.446  1.00 22.42           N  
ATOM    184  N   SER A  26       2.145  48.938  22.364  1.00 19.33           N  
ATOM    185  CA  SER A  26       0.912  49.648  21.988  1.00 19.59           C  
ATOM    186  C   SER A  26      -0.320  48.844  22.464  1.00 20.50           C  
ATOM    187  O   SER A  26      -0.237  47.623  22.727  1.00 20.29           O  
ATOM    188  CB  SER A  26       0.884  49.925  20.458  1.00 19.67           C  
ATOM    189  OG  SER A  26       1.003  48.706  19.704  1.00 19.08           O  
ATOM    190  N   GLU A  27      -1.464  49.514  22.603  1.00 20.38           N  
ATOM    191  CA  GLU A  27      -2.696  48.815  22.968  1.00 21.73           C  
ATOM    192  C   GLU A  27      -2.899  47.630  22.013  1.00 21.32           C  
ATOM    193  O   GLU A  27      -2.468  47.677  20.875  1.00 21.54           O  
ATOM    194  CB  GLU A  27      -3.896  49.808  23.027  1.00 21.74           C  
ATOM    195  CG  GLU A  27      -3.758  50.649  24.300  1.00 23.24           C  
ATOM    196  CD  GLU A  27      -4.826  51.710  24.535  1.00 25.87           C  
ATOM    197  OE1 GLU A  27      -5.477  52.149  23.596  1.00 25.51           O  
ATOM    198  OE2 GLU A  27      -5.000  52.130  25.698  1.00 25.72           O  
ATOM    199  N   PRO A  28      -3.555  46.560  22.480  1.00 21.62           N  
ATOM    200  CA  PRO A  28      -3.561  45.259  21.771  1.00 21.72           C  
ATOM    201  C   PRO A  28      -4.457  45.171  20.496  1.00 22.43           C  
ATOM    202  O   PRO A  28      -5.421  44.391  20.437  1.00 22.00           O  
ATOM    203  CB  PRO A  28      -4.038  44.271  22.855  1.00 21.26           C  
ATOM    204  CG  PRO A  28      -4.768  45.110  23.839  1.00 21.70           C  
ATOM    205  CD  PRO A  28      -4.153  46.479  23.829  1.00 21.25           C  
ATOM    206  N   VAL A  29      -4.098  45.952  19.485  1.00 23.11           N  
ATOM    207  CA  VAL A  29      -4.811  46.024  18.207  1.00 23.26           C  
ATOM    208  C   VAL A  29      -3.804  45.704  17.111  1.00 23.88           C  
ATOM    209  O   VAL A  29      -2.754  46.345  17.004  1.00 23.18           O  
ATOM    210  CB  VAL A  29      -5.430  47.448  17.974  1.00 23.27           C  
ATOM    211  CG1 VAL A  29      -6.368  47.470  16.769  1.00 21.69           C  
ATOM    212  CG2 VAL A  29      -6.114  47.970  19.256  1.00 22.25           C  
ATOM    213  N   LYS A  30      -4.115  44.681  16.315  1.00 24.89           N  
ATOM    214  CA  LYS A  30      -3.209  44.200  15.259  1.00 26.06           C  
ATOM    215  C   LYS A  30      -3.450  44.954  13.937  1.00 26.00           C  
ATOM    216  O   LYS A  30      -4.425  44.686  13.244  1.00 26.59           O  
ATOM    217  CB  LYS A  30      -3.467  42.692  15.077  1.00 26.61           C  
ATOM    218  CG  LYS A  30      -2.248  41.822  14.884  1.00 28.45           C  
ATOM    219  CD  LYS A  30      -1.999  41.562  13.421  1.00 28.74           C  
ATOM    220  CE  LYS A  30      -0.999  40.442  13.240  1.00 30.16           C  
ATOM    221  NZ  LYS A  30      -0.274  40.696  11.977  1.00 28.79           N  
ATOM    222  N   TYR A  31      -2.613  45.936  13.595  1.00 25.80           N  
ATOM    223  CA  TYR A  31      -2.729  46.580  12.294  1.00 25.22           C  
ATOM    224  C   TYR A  31      -1.864  45.867  11.261  1.00 27.00           C  
ATOM    225  O   TYR A  31      -0.798  45.336  11.598  1.00 26.61           O  
ATOM    226  CB  TYR A  31      -2.308  48.046  12.361  1.00 25.12           C  
ATOM    227  CG  TYR A  31      -3.212  48.892  13.226  1.00 23.08           C  
ATOM    228  CD1 TYR A  31      -4.287  49.571  12.673  1.00 19.20           C  
ATOM    229  CD2 TYR A  31      -3.015  48.958  14.603  1.00 18.39           C  
ATOM    230  CE1 TYR A  31      -5.114  50.341  13.448  1.00 19.06           C  
ATOM    231  CE2 TYR A  31      -3.845  49.730  15.405  1.00 20.45           C  
ATOM    232  CZ  TYR A  31      -4.898  50.419  14.815  1.00 18.45           C  
ATOM    233  OH  TYR A  31      -5.738  51.188  15.591  1.00 21.38           O  
ATOM    234  N   GLU A  32      -2.333  45.871  10.016  1.00 27.55           N  
ATOM    235  CA  GLU A  32      -1.576  45.372   8.868  1.00 30.56           C  
ATOM    236  C   GLU A  32      -1.594  46.427   7.779  1.00 30.42           C  
ATOM    237  O   GLU A  32      -2.638  46.991   7.484  1.00 30.34           O  
ATOM    238  CB  GLU A  32      -2.173  44.050   8.322  1.00 31.34           C  
ATOM    239  CG  GLU A  32      -2.005  42.866   9.281  1.00 36.06           C  
ATOM    240  CD  GLU A  32      -2.344  41.526   8.649  1.00 43.47           C  
ATOM    241  OE1 GLU A  32      -2.926  41.513   7.531  1.00 44.52           O  
ATOM    242  OE2 GLU A  32      -2.042  40.483   9.294  1.00 47.61           O  
ATOM    243  N   ALA A  33      -0.434  46.703   7.200  1.00 31.88           N  
ATOM    244  CA  ALA A  33      -0.345  47.623   6.073  1.00 33.76           C  
ATOM    245  C   ALA A  33      -1.055  47.022   4.860  1.00 35.50           C  
ATOM    246  O   ALA A  33      -0.894  45.835   4.550  1.00 36.09           O  
ATOM    247  CB  ALA A  33       1.091  47.937   5.747  1.00 33.39           C  
ATOM    248  N   ASP A  34      -1.890  47.820   4.207  1.00 36.96           N  
ATOM    249  CA  ASP A  34      -2.438  47.426   2.914  1.00 38.49           C  
ATOM    250  C   ASP A  34      -1.577  48.087   1.835  1.00 39.63           C  
ATOM    251  O   ASP A  34      -1.554  49.309   1.686  1.00 38.98           O  
ATOM    252  CB  ASP A  34      -3.896  47.845   2.800  1.00 38.53           C  
ATOM    253  CG  ASP A  34      -4.540  47.355   1.528  1.00 39.38           C  
ATOM    254  OD1 ASP A  34      -4.180  47.841   0.442  1.00 37.36           O  
ATOM    255  OD2 ASP A  34      -5.405  46.469   1.619  1.00 42.57           O  
ATOM    256  N   LYS A  35      -0.810  47.282   1.120  1.00 41.54           N  
ATOM    257  CA  LYS A  35       0.108  47.856   0.134  1.00 44.05           C  
ATOM    258  C   LYS A  35      -0.633  48.369  -1.124  1.00 44.94           C  
ATOM    259  O   LYS A  35      -0.100  49.187  -1.886  1.00 45.87           O  
ATOM    260  CB  LYS A  35       1.242  46.868  -0.197  1.00 44.78           C  
ATOM    261  CG  LYS A  35       2.517  47.072   0.672  1.00 44.98           C  
ATOM    262  CD  LYS A  35       2.936  45.792   1.403  1.00 45.99           C  
ATOM    263  CE  LYS A  35       1.747  45.213   2.158  1.00 47.71           C  
ATOM    264  NZ  LYS A  35       2.070  44.230   3.257  1.00 48.24           N  
ATOM    265  N   ALA A  36      -1.873  47.914  -1.313  1.00 44.65           N  
ATOM    266  CA  ALA A  36      -2.707  48.405  -2.391  1.00 44.81           C  
ATOM    267  C   ALA A  36      -3.519  49.652  -2.006  1.00 44.91           C  
ATOM    268  O   ALA A  36      -4.046  50.317  -2.886  1.00 45.28           O  
ATOM    269  CB  ALA A  36      -3.656  47.309  -2.864  1.00 44.78           C  
ATOM    270  N   LEU A  37      -3.680  49.937  -0.708  1.00 43.77           N  
ATOM    271  CA  LEU A  37      -4.397  51.142  -0.298  1.00 42.57           C  
ATOM    272  C   LEU A  37      -3.404  52.197   0.145  1.00 41.06           C  
ATOM    273  O   LEU A  37      -3.735  53.383   0.193  1.00 41.20           O  
ATOM    274  CB  LEU A  37      -5.379  50.861   0.844  1.00 42.92           C  
ATOM    275  CG  LEU A  37      -6.450  49.797   0.612  1.00 43.81           C  
ATOM    276  CD1 LEU A  37      -7.367  49.636   1.818  1.00 44.72           C  
ATOM    277  CD2 LEU A  37      -7.258  50.154  -0.608  1.00 45.97           C  
ATOM    278  N   GLY A  38      -2.183  51.759   0.469  1.00 39.85           N  
ATOM    279  CA  GLY A  38      -1.176  52.617   1.131  1.00 37.63           C  
ATOM    280  C   GLY A  38      -1.501  53.016   2.583  1.00 36.28           C  
ATOM    281  O   GLY A  38      -1.003  54.034   3.081  1.00 36.55           O  
ATOM    282  N   LEU A  39      -2.339  52.234   3.265  1.00 33.68           N  
ATOM    283  CA  LEU A  39      -2.850  52.621   4.595  1.00 31.37           C  
ATOM    284  C   LEU A  39      -2.765  51.448   5.548  1.00 29.37           C  
ATOM    285  O   LEU A  39      -2.761  50.301   5.099  1.00 28.58           O  
ATOM    286  CB  LEU A  39      -4.311  53.094   4.516  1.00 30.92           C  
ATOM    287  CG  LEU A  39      -4.593  54.380   3.727  1.00 31.84           C  
ATOM    288  CD1 LEU A  39      -6.088  54.592   3.563  1.00 31.37           C  
ATOM    289  CD2 LEU A  39      -3.950  55.577   4.413  1.00 30.83           C  
ATOM    290  N   LEU A  40      -2.685  51.738   6.854  1.00 27.18           N  
ATOM    291  CA  LEU A  40      -2.802  50.690   7.873  1.00 26.07           C  
ATOM    292  C   LEU A  40      -4.260  50.295   8.039  1.00 24.63           C  
ATOM    293  O   LEU A  40      -5.140  51.150   8.125  1.00 23.26           O  
ATOM    294  CB  LEU A  40      -2.218  51.115   9.238  1.00 25.71           C  
ATOM    295  CG  LEU A  40      -0.687  51.351   9.263  1.00 25.93           C  
ATOM    296  CD1 LEU A  40      -0.250  52.020  10.547  1.00 24.92           C  
ATOM    297  CD2 LEU A  40       0.064  50.039   9.032  1.00 24.73           C  
ATOM    298  N   VAL A  41      -4.486  48.988   8.093  1.00 24.43           N  
ATOM    299  CA  VAL A  41      -5.822  48.433   8.262  1.00 25.12           C  
ATOM    300  C   VAL A  41      -5.926  47.622   9.556  1.00 25.36           C  
ATOM    301  O   VAL A  41      -4.999  46.846   9.885  1.00 24.93           O  
ATOM    302  CB  VAL A  41      -6.155  47.533   7.039  1.00 25.41           C  
ATOM    303  CG1 VAL A  41      -7.438  46.711   7.244  1.00 26.79           C  
ATOM    304  CG2 VAL A  41      -6.270  48.406   5.797  1.00 24.02           C  
ATOM    305  N   VAL A  42      -7.038  47.774  10.285  1.00 24.79           N  
ATOM    306  CA  VAL A  42      -7.232  46.981  11.515  1.00 25.06           C  
ATOM    307  C   VAL A  42      -7.535  45.513  11.174  1.00 25.94           C  
ATOM    308  O   VAL A  42      -8.638  45.197  10.731  1.00 26.93           O  
ATOM    309  CB  VAL A  42      -8.420  47.451  12.370  1.00 24.99           C  
ATOM    310  CG1 VAL A  42      -8.436  46.718  13.688  1.00 24.48           C  
ATOM    311  CG2 VAL A  42      -8.400  48.939  12.607  1.00 24.84           C  
ATOM    312  N   ASP A  43      -6.578  44.619  11.376  1.00 25.33           N  
ATOM    313  CA  ASP A  43      -6.825  43.221  11.140  1.00 26.20           C  
ATOM    314  C   ASP A  43      -7.737  42.626  12.210  1.00 25.70           C  
ATOM    315  O   ASP A  43      -8.787  42.081  11.879  1.00 25.64           O  
ATOM    316  CB  ASP A  43      -5.524  42.401  11.040  1.00 27.86           C  
ATOM    317  CG  ASP A  43      -5.814  40.952  10.725  1.00 30.64           C  
ATOM    318  OD1 ASP A  43      -6.372  40.686   9.642  1.00 37.20           O  
ATOM    319  OD2 ASP A  43      -5.576  40.084  11.564  1.00 33.64           O  
ATOM    320  N   ARG A  44      -7.345  42.729  13.482  1.00 23.76           N  
ATOM    321  CA  ARG A  44      -8.190  42.297  14.561  1.00 24.05           C  
ATOM    322  C   ARG A  44      -7.761  42.917  15.906  1.00 24.08           C  
ATOM    323  O   ARG A  44      -6.608  43.338  16.065  1.00 24.67           O  
ATOM    324  CB  ARG A  44      -8.171  40.764  14.678  1.00 24.30           C  
ATOM    325  CG  ARG A  44      -6.835  40.203  15.246  1.00 24.56           C  
ATOM    326  CD  ARG A  44      -6.770  38.712  15.056  1.00 28.25           C  
ATOM    327  NE  ARG A  44      -5.527  38.105  15.527  1.00 30.15           N  
ATOM    328  CZ  ARG A  44      -4.436  37.938  14.774  1.00 30.95           C  
ATOM    329  NH1 ARG A  44      -4.413  38.364  13.500  1.00 29.56           N  
ATOM    330  NH2 ARG A  44      -3.363  37.358  15.299  1.00 27.85           N  
ATOM    331  N   PHE A  45      -8.708  42.999  16.839  1.00 23.14           N  
ATOM    332  CA  PHE A  45      -8.408  43.175  18.265  1.00 23.01           C  
ATOM    333  C   PHE A  45      -7.891  41.854  18.809  1.00 23.22           C  
ATOM    334  O   PHE A  45      -8.571  40.821  18.730  1.00 22.43           O  
ATOM    335  CB  PHE A  45      -9.621  43.696  19.024  1.00 23.17           C  
ATOM    336  CG  PHE A  45      -9.904  45.174  18.756  1.00 23.12           C  
ATOM    337  CD1 PHE A  45      -9.587  46.141  19.696  1.00 22.31           C  
ATOM    338  CD2 PHE A  45     -10.456  45.591  17.546  1.00 22.00           C  
ATOM    339  CE1 PHE A  45      -9.815  47.525  19.445  1.00 19.37           C  
ATOM    340  CE2 PHE A  45     -10.689  46.946  17.299  1.00 24.14           C  
ATOM    341  CZ  PHE A  45     -10.363  47.920  18.257  1.00 20.26           C  
ATOM    342  N   ILE A  46      -6.653  41.870  19.303  1.00 22.58           N  
ATOM    343  CA  ILE A  46      -6.049  40.660  19.811  1.00 22.68           C  
ATOM    344  C   ILE A  46      -6.900  40.042  20.937  1.00 22.39           C  
ATOM    345  O   ILE A  46      -7.174  40.697  21.955  1.00 22.85           O  
ATOM    346  CB  ILE A  46      -4.573  40.901  20.294  1.00 22.60           C  
ATOM    347  CG1 ILE A  46      -3.715  41.434  19.130  1.00 21.33           C  
ATOM    348  CG2 ILE A  46      -4.021  39.618  20.954  1.00 19.70           C  
ATOM    349  CD1 ILE A  46      -2.327  41.989  19.546  1.00 21.68           C  
ATOM    350  N   GLY A  47      -7.299  38.783  20.761  1.00 21.82           N  
ATOM    351  CA  GLY A  47      -8.248  38.135  21.701  1.00 20.72           C  
ATOM    352  C   GLY A  47      -7.794  38.069  23.156  1.00 20.43           C  
ATOM    353  O   GLY A  47      -8.593  38.229  24.093  1.00 19.67           O  
ATOM    354  N   THR A  48      -6.499  37.840  23.355  1.00 19.77           N  
ATOM    355  CA  THR A  48      -5.932  37.739  24.683  1.00 19.66           C  
ATOM    356  C   THR A  48      -5.613  39.106  25.314  1.00 20.30           C  
ATOM    357  O   THR A  48      -5.329  39.200  26.512  1.00 20.72           O  
ATOM    358  CB  THR A  48      -4.619  36.917  24.634  1.00 20.30           C  
ATOM    359  OG1 THR A  48      -3.768  37.491  23.644  1.00 20.44           O  
ATOM    360  CG2 THR A  48      -4.860  35.453  24.277  1.00 17.40           C  
ATOM    361  N   GLY A  49      -5.651  40.181  24.535  1.00 20.99           N  
ATOM    362  CA  GLY A  49      -5.269  41.493  25.078  1.00 20.69           C  
ATOM    363  C   GLY A  49      -3.758  41.638  25.240  1.00 20.94           C  
ATOM    364  O   GLY A  49      -3.299  42.624  25.806  1.00 21.56           O  
ATOM    365  N   MET A  50      -2.983  40.667  24.749  1.00 19.51           N  
ATOM    366  CA  MET A  50      -1.499  40.721  24.822  1.00 18.69           C  
ATOM    367  C   MET A  50      -0.883  41.715  23.837  1.00 18.94           C  
ATOM    368  O   MET A  50      -1.429  41.916  22.738  1.00 19.06           O  
ATOM    369  CB  MET A  50      -0.898  39.311  24.595  1.00 18.46           C  
ATOM    370  CG  MET A  50      -1.205  38.359  25.743  1.00 16.28           C  
ATOM    371  SD  MET A  50      -0.534  36.732  25.499  1.00 20.35           S  
ATOM    372  CE  MET A  50       1.161  36.996  26.020  1.00 15.70           C  
ATOM    373  N   ARG A  51       0.266  42.306  24.221  1.00 18.83           N  
ATOM    374  CA  ARG A  51       0.901  43.405  23.476  1.00 18.83           C  
ATOM    375  C   ARG A  51       2.255  42.953  22.927  1.00 19.23           C  
ATOM    376  O   ARG A  51       3.000  42.203  23.600  1.00 18.63           O  
ATOM    377  CB  ARG A  51       1.111  44.671  24.362  1.00 18.43           C  
ATOM    378  CG  ARG A  51      -0.162  45.289  24.984  1.00 17.94           C  
ATOM    379  CD  ARG A  51       0.141  46.584  25.739  1.00 17.07           C  
ATOM    380  NE  ARG A  51      -1.057  47.096  26.434  1.00 17.53           N  
ATOM    381  CZ  ARG A  51      -1.381  48.382  26.591  1.00 17.75           C  
ATOM    382  NH1 ARG A  51      -0.616  49.350  26.093  1.00 15.93           N  
ATOM    383  NH2 ARG A  51      -2.498  48.705  27.248  1.00 17.88           N  
ATOM    384  N   TYR A  52       2.587  43.425  21.724  1.00 18.81           N  
ATOM    385  CA  TYR A  52       3.925  43.167  21.179  1.00 20.17           C  
ATOM    386  C   TYR A  52       4.969  43.754  22.104  1.00 19.88           C  
ATOM    387  O   TYR A  52       4.909  44.924  22.419  1.00 19.46           O  
ATOM    388  CB  TYR A  52       4.063  43.715  19.744  1.00 19.61           C  
ATOM    389  CG  TYR A  52       3.327  42.878  18.720  1.00 21.97           C  
ATOM    390  CD1 TYR A  52       4.031  42.070  17.818  1.00 22.85           C  
ATOM    391  CD2 TYR A  52       1.918  42.863  18.667  1.00 21.92           C  
ATOM    392  CE1 TYR A  52       3.370  41.301  16.883  1.00 21.48           C  
ATOM    393  CE2 TYR A  52       1.241  42.079  17.734  1.00 22.65           C  
ATOM    394  CZ  TYR A  52       1.964  41.293  16.853  1.00 23.39           C  
ATOM    395  OH  TYR A  52       1.315  40.519  15.914  1.00 21.36           O  
ATOM    396  N   PRO A  53       5.919  42.920  22.572  1.00 21.29           N  
ATOM    397  CA  PRO A  53       7.017  43.398  23.428  1.00 21.87           C  
ATOM    398  C   PRO A  53       8.071  44.269  22.717  1.00 21.70           C  
ATOM    399  O   PRO A  53       8.819  44.986  23.394  1.00 21.93           O  
ATOM    400  CB  PRO A  53       7.642  42.106  23.998  1.00 21.72           C  
ATOM    401  CG  PRO A  53       7.174  40.998  23.100  1.00 22.80           C  
ATOM    402  CD  PRO A  53       5.885  41.443  22.446  1.00 22.07           C  
ATOM    403  N   VAL A  54       8.100  44.236  21.382  1.00 20.85           N  
ATOM    404  CA  VAL A  54       9.007  45.057  20.582  1.00 21.55           C  
ATOM    405  C   VAL A  54       8.232  45.490  19.356  1.00 20.83           C  
ATOM    406  O   VAL A  54       7.140  44.972  19.117  1.00 20.05           O  
ATOM    407  CB  VAL A  54      10.281  44.275  20.107  1.00 22.98           C  
ATOM    408  CG1 VAL A  54      11.079  43.719  21.297  1.00 23.11           C  
ATOM    409  CG2 VAL A  54       9.884  43.163  19.151  1.00 24.55           C  
ATOM    410  N   ASN A  55       8.770  46.452  18.602  1.00 19.90           N  
ATOM    411  CA  ASN A  55       8.127  46.907  17.367  1.00 21.21           C  
ATOM    412  C   ASN A  55       7.999  45.819  16.329  1.00 20.69           C  
ATOM    413  O   ASN A  55       8.869  44.984  16.187  1.00 21.68           O  
ATOM    414  CB  ASN A  55       8.838  48.129  16.748  1.00 20.69           C  
ATOM    415  CG  ASN A  55       9.109  49.224  17.771  1.00 20.45           C  
ATOM    416  OD1 ASN A  55       8.221  50.008  18.123  1.00 17.26           O  
ATOM    417  ND2 ASN A  55      10.351  49.292  18.238  1.00 18.77           N  
ATOM    418  N   TYR A  56       6.903  45.849  15.596  1.00 20.79           N  
ATOM    419  CA  TYR A  56       6.622  44.831  14.583  1.00 20.61           C  
ATOM    420  C   TYR A  56       6.243  45.465  13.238  1.00 20.45           C  
ATOM    421  O   TYR A  56       5.457  46.410  13.177  1.00 19.77           O  
ATOM    422  CB  TYR A  56       5.479  43.957  15.068  1.00 20.53           C  
ATOM    423  CG  TYR A  56       5.162  42.754  14.189  1.00 22.99           C  
ATOM    424  CD1 TYR A  56       6.112  41.762  13.982  1.00 23.35           C  
ATOM    425  CD2 TYR A  56       3.898  42.608  13.593  1.00 22.26           C  
ATOM    426  CE1 TYR A  56       5.834  40.653  13.201  1.00 24.86           C  
ATOM    427  CE2 TYR A  56       3.606  41.493  12.825  1.00 25.04           C  
ATOM    428  CZ  TYR A  56       4.585  40.513  12.637  1.00 26.22           C  
ATOM    429  OH  TYR A  56       4.338  39.402  11.853  1.00 26.67           O  
ATOM    430  N   GLY A  57       6.814  44.934  12.167  1.00 20.57           N  
ATOM    431  CA  GLY A  57       6.543  45.425  10.820  1.00 20.64           C  
ATOM    432  C   GLY A  57       7.020  44.440   9.773  1.00 20.42           C  
ATOM    433  O   GLY A  57       7.108  43.230  10.030  1.00 20.25           O  
ATOM    434  N   PHE A  58       7.317  44.956   8.590  1.00 21.49           N  
ATOM    435  CA  PHE A  58       7.723  44.098   7.462  1.00 22.42           C  
ATOM    436  C   PHE A  58       8.739  44.803   6.557  1.00 21.95           C  
ATOM    437  O   PHE A  58       8.846  46.035   6.548  1.00 21.27           O  
ATOM    438  CB  PHE A  58       6.473  43.668   6.628  1.00 22.41           C  
ATOM    439  CG  PHE A  58       5.792  44.818   5.923  1.00 25.13           C  
ATOM    440  CD1 PHE A  58       6.084  45.105   4.587  1.00 25.77           C  
ATOM    441  CD2 PHE A  58       4.881  45.626   6.598  1.00 22.93           C  
ATOM    442  CE1 PHE A  58       5.476  46.166   3.936  1.00 24.40           C  
ATOM    443  CE2 PHE A  58       4.289  46.717   5.972  1.00 23.86           C  
ATOM    444  CZ  PHE A  58       4.575  46.987   4.632  1.00 26.77           C  
ATOM    445  N   ILE A  59       9.456  44.013   5.766  1.00 22.61           N  
ATOM    446  CA  ILE A  59      10.300  44.571   4.683  1.00 23.33           C  
ATOM    447  C   ILE A  59       9.523  44.749   3.371  1.00 23.32           C  
ATOM    448  O   ILE A  59       9.003  43.779   2.827  1.00 24.29           O  
ATOM    449  CB  ILE A  59      11.557  43.690   4.429  1.00 22.84           C  
ATOM    450  CG1 ILE A  59      12.281  43.398   5.748  1.00 22.43           C  
ATOM    451  CG2 ILE A  59      12.476  44.360   3.354  1.00 22.00           C  
ATOM    452  CD1 ILE A  59      13.474  42.443   5.622  1.00 19.09           C  
ATOM    453  N   PRO A  60       9.420  45.985   2.872  1.00 24.84           N  
ATOM    454  CA  PRO A  60       8.675  46.182   1.622  1.00 26.36           C  
ATOM    455  C   PRO A  60       9.384  45.522   0.421  1.00 27.39           C  
ATOM    456  O   PRO A  60      10.605  45.317   0.441  1.00 27.93           O  
ATOM    457  CB  PRO A  60       8.639  47.712   1.456  1.00 25.61           C  
ATOM    458  CG  PRO A  60       9.839  48.222   2.254  1.00 25.88           C  
ATOM    459  CD  PRO A  60       9.955  47.257   3.418  1.00 25.38           C  
ATOM    460  N   GLN A  61       8.609  45.181  -0.600  1.00 28.29           N  
ATOM    461  CA  GLN A  61       9.159  44.570  -1.809  1.00 29.22           C  
ATOM    462  C   GLN A  61       9.810  43.208  -1.540  1.00 29.01           C  
ATOM    463  O   GLN A  61      10.828  42.854  -2.136  1.00 28.95           O  
ATOM    464  CB  GLN A  61      10.069  45.568  -2.526  1.00 29.21           C  
ATOM    465  CG  GLN A  61       9.202  46.671  -3.102  1.00 34.78           C  
ATOM    466  CD  GLN A  61       9.957  47.810  -3.699  1.00 43.57           C  
ATOM    467  OE1 GLN A  61       9.386  48.866  -3.940  1.00 47.87           O  
ATOM    468  NE2 GLN A  61      11.245  47.619  -3.948  1.00 46.49           N  
ATOM    469  N   THR A  62       9.218  42.458  -0.616  1.00 28.00           N  
ATOM    470  CA  THR A  62       9.631  41.093  -0.365  1.00 28.25           C  
ATOM    471  C   THR A  62       8.383  40.230  -0.370  1.00 29.87           C  
ATOM    472  O   THR A  62       7.269  40.730  -0.203  1.00 29.15           O  
ATOM    473  CB  THR A  62      10.397  40.905   0.989  1.00 28.15           C  
ATOM    474  OG1 THR A  62       9.545  41.234   2.104  1.00 27.37           O  
ATOM    475  CG2 THR A  62      11.679  41.753   1.027  1.00 26.31           C  
ATOM    476  N   LEU A  63       8.566  38.932  -0.548  1.00 31.16           N  
ATOM    477  CA  LEU A  63       7.455  38.007  -0.575  1.00 33.88           C  
ATOM    478  C   LEU A  63       7.944  36.718   0.039  1.00 35.46           C  
ATOM    479  O   LEU A  63       8.786  36.019  -0.523  1.00 35.30           O  
ATOM    480  CB  LEU A  63       6.945  37.808  -2.016  1.00 33.87           C  
ATOM    481  CG  LEU A  63       5.795  36.841  -2.280  1.00 34.60           C  
ATOM    482  CD1 LEU A  63       4.662  37.180  -1.363  1.00 36.93           C  
ATOM    483  CD2 LEU A  63       5.340  36.969  -3.724  1.00 36.15           C  
ATOM    484  N   SER A  64       7.437  36.436   1.230  1.00 38.38           N  
ATOM    485  CA  SER A  64       7.886  35.307   2.023  1.00 41.11           C  
ATOM    486  C   SER A  64       7.191  34.036   1.577  1.00 43.10           C  
ATOM    487  O   SER A  64       6.349  34.064   0.671  1.00 42.92           O  
ATOM    488  CB  SER A  64       7.564  35.543   3.500  1.00 41.35           C  
ATOM    489  OG  SER A  64       8.363  34.696   4.315  1.00 42.71           O  
ATOM    490  N   GLY A  65       7.537  32.927   2.229  1.00 45.14           N  
ATOM    491  CA  GLY A  65       6.892  31.638   1.968  1.00 47.76           C  
ATOM    492  C   GLY A  65       5.362  31.636   2.005  1.00 49.24           C  
ATOM    493  O   GLY A  65       4.723  30.859   1.293  1.00 50.21           O  
ATOM    494  N   ASP A  66       4.753  32.482   2.832  1.00 50.27           N  
ATOM    495  CA  ASP A  66       3.284  32.510   2.911  1.00 50.78           C  
ATOM    496  C   ASP A  66       2.609  33.496   1.940  1.00 50.21           C  
ATOM    497  O   ASP A  66       1.385  33.600   1.897  1.00 50.77           O  
ATOM    498  CB  ASP A  66       2.820  32.798   4.342  1.00 51.29           C  
ATOM    499  CG  ASP A  66       3.509  34.005   4.947  1.00 54.17           C  
ATOM    500  OD1 ASP A  66       3.722  35.014   4.219  1.00 55.27           O  
ATOM    501  OD2 ASP A  66       3.843  33.936   6.161  1.00 57.76           O  
ATOM    502  N   GLY A  67       3.379  34.233   1.160  1.00 48.96           N  
ATOM    503  CA  GLY A  67       2.739  35.181   0.272  1.00 47.16           C  
ATOM    504  C   GLY A  67       2.604  36.550   0.903  1.00 45.61           C  
ATOM    505  O   GLY A  67       2.093  37.467   0.266  1.00 46.42           O  
ATOM    506  N   ASP A  68       3.068  36.690   2.147  1.00 44.01           N  
ATOM    507  CA  ASP A  68       3.176  37.990   2.828  1.00 41.68           C  
ATOM    508  C   ASP A  68       4.634  38.442   2.804  1.00 38.69           C  
ATOM    509  O   ASP A  68       5.530  37.609   2.702  1.00 38.18           O  
ATOM    510  CB  ASP A  68       2.772  37.862   4.299  1.00 43.06           C  
ATOM    511  CG  ASP A  68       1.260  37.693   4.501  1.00 47.11           C  
ATOM    512  OD1 ASP A  68       0.458  38.106   3.618  1.00 50.50           O  
ATOM    513  OD2 ASP A  68       0.885  37.144   5.569  1.00 51.66           O  
ATOM    514  N   PRO A  69       4.880  39.755   2.945  1.00 35.51           N  
ATOM    515  CA  PRO A  69       6.253  40.252   3.039  1.00 33.20           C  
ATOM    516  C   PRO A  69       7.007  39.648   4.217  1.00 31.00           C  
ATOM    517  O   PRO A  69       6.388  39.081   5.103  1.00 30.18           O  
ATOM    518  CB  PRO A  69       6.082  41.767   3.260  1.00 33.04           C  
ATOM    519  CG  PRO A  69       4.739  42.103   2.734  1.00 35.64           C  
ATOM    520  CD  PRO A  69       3.880  40.839   2.971  1.00 35.76           C  
ATOM    521  N   VAL A  70       8.336  39.778   4.232  1.00 29.44           N  
ATOM    522  CA  VAL A  70       9.151  39.250   5.348  1.00 27.95           C  
ATOM    523  C   VAL A  70       8.837  40.047   6.625  1.00 26.77           C  
ATOM    524  O   VAL A  70       8.915  41.270   6.619  1.00 26.46           O  
ATOM    525  CB  VAL A  70      10.703  39.275   5.026  1.00 27.88           C  
ATOM    526  CG1 VAL A  70      11.514  38.958   6.258  1.00 27.39           C  
ATOM    527  CG2 VAL A  70      11.056  38.280   3.898  1.00 27.44           C  
ATOM    528  N   ASP A  71       8.452  39.351   7.693  1.00 26.51           N  
ATOM    529  CA  ASP A  71       8.153  39.968   9.014  1.00 26.25           C  
ATOM    530  C   ASP A  71       9.381  40.260   9.866  1.00 25.56           C  
ATOM    531  O   ASP A  71      10.322  39.450   9.926  1.00 25.69           O  
ATOM    532  CB  ASP A  71       7.284  39.034   9.838  1.00 26.37           C  
ATOM    533  CG  ASP A  71       5.942  38.790   9.227  1.00 28.24           C  
ATOM    534  OD1 ASP A  71       5.331  39.745   8.677  1.00 30.97           O  
ATOM    535  OD2 ASP A  71       5.496  37.624   9.306  1.00 28.38           O  
ATOM    536  N   VAL A  72       9.362  41.410  10.542  1.00 24.69           N  
ATOM    537  CA  VAL A  72      10.480  41.870  11.382  1.00 22.19           C  
ATOM    538  C   VAL A  72      10.034  42.475  12.735  1.00 22.12           C  
ATOM    539  O   VAL A  72       9.148  43.330  12.811  1.00 21.39           O  
ATOM    540  CB  VAL A  72      11.395  42.879  10.629  1.00 22.97           C  
ATOM    541  CG1 VAL A  72      12.704  43.137  11.390  1.00 20.10           C  
ATOM    542  CG2 VAL A  72      11.667  42.402   9.171  1.00 21.68           C  
ATOM    543  N   LEU A  73      10.666  41.984  13.798  1.00 21.86           N  
ATOM    544  CA  LEU A  73      10.673  42.593  15.127  1.00 21.24           C  
ATOM    545  C   LEU A  73      11.900  43.511  15.274  1.00 21.59           C  
ATOM    546  O   LEU A  73      13.030  43.037  15.180  1.00 22.50           O  
ATOM    547  CB  LEU A  73      10.739  41.468  16.172  1.00 21.37           C  
ATOM    548  CG  LEU A  73       9.561  40.490  16.014  1.00 21.82           C  
ATOM    549  CD1 LEU A  73       9.902  39.045  16.446  1.00 23.52           C  
ATOM    550  CD2 LEU A  73       8.331  41.011  16.770  1.00 20.84           C  
ATOM    551  N   VAL A  74      11.681  44.815  15.494  1.00 20.95           N  
ATOM    552  CA  VAL A  74      12.752  45.796  15.684  1.00 19.54           C  
ATOM    553  C   VAL A  74      12.771  46.277  17.140  1.00 20.67           C  
ATOM    554  O   VAL A  74      11.768  46.843  17.646  1.00 19.81           O  
ATOM    555  CB  VAL A  74      12.558  47.027  14.796  1.00 19.11           C  
ATOM    556  CG1 VAL A  74      13.790  47.916  14.808  1.00 16.39           C  
ATOM    557  CG2 VAL A  74      12.228  46.592  13.359  1.00 19.06           C  
ATOM    558  N   ILE A  75      13.897  46.030  17.812  1.00 20.76           N  
ATOM    559  CA  ILE A  75      14.131  46.466  19.213  1.00 21.77           C  
ATOM    560  C   ILE A  75      14.639  47.928  19.210  1.00 22.17           C  
ATOM    561  O   ILE A  75      15.604  48.245  18.487  1.00 22.78           O  
ATOM    562  CB  ILE A  75      15.171  45.535  19.898  1.00 21.89           C  
ATOM    563  CG1 ILE A  75      14.703  44.087  19.786  1.00 21.31           C  
ATOM    564  CG2 ILE A  75      15.461  45.946  21.348  1.00 21.98           C  
ATOM    565  CD1 ILE A  75      15.763  43.077  20.206  1.00 21.97           C  
ATOM    566  N   THR A  76      13.967  48.806  19.964  1.00 21.05           N  
ATOM    567  CA  THR A  76      14.385  50.220  20.093  1.00 20.95           C  
ATOM    568  C   THR A  76      14.241  50.718  21.543  1.00 20.55           C  
ATOM    569  O   THR A  76      13.450  50.161  22.299  1.00 19.88           O  
ATOM    570  CB  THR A  76      13.551  51.151  19.153  1.00 20.86           C  
ATOM    571  OG1 THR A  76      12.167  51.040  19.496  1.00 19.99           O  
ATOM    572  CG2 THR A  76      13.745  50.762  17.658  1.00 18.48           C  
ATOM    573  N   PRO A  77      14.992  51.770  21.934  1.00 20.91           N  
ATOM    574  CA  PRO A  77      14.763  52.260  23.309  1.00 21.70           C  
ATOM    575  C   PRO A  77      13.382  52.961  23.583  1.00 21.66           C  
ATOM    576  O   PRO A  77      12.953  53.016  24.743  1.00 21.57           O  
ATOM    577  CB  PRO A  77      15.953  53.209  23.563  1.00 21.31           C  
ATOM    578  CG  PRO A  77      16.481  53.561  22.213  1.00 21.76           C  
ATOM    579  CD  PRO A  77      16.165  52.408  21.295  1.00 20.66           C  
ATOM    580  N   PHE A  78      12.709  53.456  22.545  1.00 20.64           N  
ATOM    581  CA  PHE A  78      11.360  54.051  22.662  1.00 21.02           C  
ATOM    582  C   PHE A  78      10.529  53.502  21.508  1.00 20.26           C  
ATOM    583  O   PHE A  78      11.074  53.303  20.404  1.00 20.09           O  
ATOM    584  CB  PHE A  78      11.409  55.603  22.539  1.00 20.99           C  
ATOM    585  CG  PHE A  78      12.129  56.296  23.695  1.00 22.97           C  
ATOM    586  CD1 PHE A  78      11.482  56.496  24.931  1.00 22.93           C  
ATOM    587  CD2 PHE A  78      13.446  56.731  23.549  1.00 20.66           C  
ATOM    588  CE1 PHE A  78      12.148  57.089  25.992  1.00 23.48           C  
ATOM    589  CE2 PHE A  78      14.113  57.329  24.597  1.00 21.65           C  
ATOM    590  CZ  PHE A  78      13.472  57.507  25.823  1.00 23.50           C  
ATOM    591  N   PRO A  79       9.201  53.295  21.718  1.00 20.67           N  
ATOM    592  CA  PRO A  79       8.431  52.730  20.586  1.00 19.72           C  
ATOM    593  C   PRO A  79       8.502  53.606  19.329  1.00 19.61           C  
ATOM    594  O   PRO A  79       8.687  54.817  19.437  1.00 18.61           O  
ATOM    595  CB  PRO A  79       6.993  52.618  21.137  1.00 20.21           C  
ATOM    596  CG  PRO A  79       7.184  52.577  22.674  1.00 21.91           C  
ATOM    597  CD  PRO A  79       8.355  53.522  22.918  1.00 19.80           C  
ATOM    598  N   LEU A  80       8.406  52.986  18.147  1.00 19.41           N  
ATOM    599  CA  LEU A  80       8.376  53.710  16.869  1.00 19.62           C  
ATOM    600  C   LEU A  80       6.920  53.965  16.446  1.00 20.50           C  
ATOM    601  O   LEU A  80       5.997  53.210  16.777  1.00 19.42           O  
ATOM    602  CB  LEU A  80       9.054  52.878  15.740  1.00 19.52           C  
ATOM    603  CG  LEU A  80      10.550  52.569  15.948  1.00 19.77           C  
ATOM    604  CD1 LEU A  80      11.033  51.619  14.875  1.00 18.38           C  
ATOM    605  CD2 LEU A  80      11.365  53.875  15.950  1.00 18.69           C  
ATOM    606  N   LEU A  81       6.753  55.018  15.663  1.00 21.45           N  
ATOM    607  CA  LEU A  81       5.481  55.415  15.076  1.00 21.99           C  
ATOM    608  C   LEU A  81       4.960  54.399  14.062  1.00 21.60           C  
ATOM    609  O   LEU A  81       5.681  54.045  13.128  1.00 21.18           O  
ATOM    610  CB  LEU A  81       5.765  56.717  14.338  1.00 22.29           C  
ATOM    611  CG  LEU A  81       4.838  57.896  14.175  1.00 28.01           C  
ATOM    612  CD1 LEU A  81       3.889  58.076  15.398  1.00 30.54           C  
ATOM    613  CD2 LEU A  81       5.729  59.117  13.976  1.00 30.14           C  
ATOM    614  N   ALA A  82       3.701  53.961  14.200  1.00 20.50           N  
ATOM    615  CA  ALA A  82       3.095  53.083  13.205  1.00 20.23           C  
ATOM    616  C   ALA A  82       3.032  53.805  11.851  1.00 20.71           C  
ATOM    617  O   ALA A  82       2.606  54.969  11.775  1.00 19.92           O  
ATOM    618  CB  ALA A  82       1.685  52.621  13.648  1.00 19.13           C  
ATOM    619  N   GLY A  83       3.473  53.115  10.797  1.00 21.09           N  
ATOM    620  CA  GLY A  83       3.454  53.652   9.450  1.00 21.60           C  
ATOM    621  C   GLY A  83       4.756  54.354   9.070  1.00 22.41           C  
ATOM    622  O   GLY A  83       4.908  54.785   7.922  1.00 22.78           O  
ATOM    623  N   SER A  84       5.675  54.500  10.026  1.00 21.49           N  
ATOM    624  CA  SER A  84       7.003  55.049   9.743  1.00 22.62           C  
ATOM    625  C   SER A  84       7.955  53.963   9.176  1.00 23.06           C  
ATOM    626  O   SER A  84       7.665  52.766   9.271  1.00 23.25           O  
ATOM    627  CB  SER A  84       7.612  55.745  10.986  1.00 21.55           C  
ATOM    628  OG  SER A  84       7.949  54.826  12.039  1.00 21.85           O  
ATOM    629  N   VAL A  85       9.091  54.414   8.626  1.00 23.53           N  
ATOM    630  CA  VAL A  85      10.136  53.570   8.060  1.00 22.93           C  
ATOM    631  C   VAL A  85      11.427  53.725   8.856  1.00 22.89           C  
ATOM    632  O   VAL A  85      11.826  54.860   9.204  1.00 23.40           O  
ATOM    633  CB  VAL A  85      10.436  53.956   6.572  1.00 23.72           C  
ATOM    634  CG1 VAL A  85      11.236  52.843   5.886  1.00 23.82           C  
ATOM    635  CG2 VAL A  85       9.154  54.114   5.810  1.00 23.40           C  
ATOM    636  N   VAL A  86      12.073  52.594   9.143  1.00 21.59           N  
ATOM    637  CA  VAL A  86      13.346  52.564   9.868  1.00 21.61           C  
ATOM    638  C   VAL A  86      14.397  51.698   9.102  1.00 22.02           C  
ATOM    639  O   VAL A  86      14.128  50.570   8.703  1.00 21.87           O  
ATOM    640  CB  VAL A  86      13.192  52.095  11.360  1.00 21.44           C  
ATOM    641  CG1 VAL A  86      12.660  50.635  11.465  1.00 20.11           C  
ATOM    642  CG2 VAL A  86      14.521  52.237  12.127  1.00 19.16           C  
ATOM    643  N   ARG A  87      15.561  52.278   8.859  1.00 21.94           N  
ATOM    644  CA  ARG A  87      16.701  51.555   8.303  1.00 22.74           C  
ATOM    645  C   ARG A  87      17.227  50.629   9.390  1.00 22.19           C  
ATOM    646  O   ARG A  87      17.477  51.113  10.489  1.00 22.02           O  
ATOM    647  CB  ARG A  87      17.783  52.582   7.935  1.00 23.60           C  
ATOM    648  CG  ARG A  87      18.974  51.991   7.197  1.00 23.36           C  
ATOM    649  CD  ARG A  87      19.981  53.075   6.916  1.00 25.35           C  
ATOM    650  NE  ARG A  87      21.014  52.623   5.994  1.00 26.55           N  
ATOM    651  CZ  ARG A  87      22.042  53.356   5.581  1.00 30.00           C  
ATOM    652  NH1 ARG A  87      22.199  54.589   6.009  1.00 30.00           N  
ATOM    653  NH2 ARG A  87      22.922  52.846   4.730  1.00 29.59           N  
ATOM    654  N   ALA A  88      17.362  49.318   9.097  1.00 21.61           N  
ATOM    655  CA  ALA A  88      17.679  48.293  10.097  1.00 20.95           C  
ATOM    656  C   ALA A  88      18.751  47.274   9.647  1.00 21.61           C  
ATOM    657  O   ALA A  88      19.144  47.220   8.463  1.00 21.00           O  
ATOM    658  CB  ALA A  88      16.418  47.553  10.513  1.00 21.45           C  
ATOM    659  N   ARG A  89      19.239  46.501  10.616  1.00 21.20           N  
ATOM    660  CA  ARG A  89      20.154  45.376  10.373  1.00 21.57           C  
ATOM    661  C   ARG A  89      19.695  44.194  11.214  1.00 21.96           C  
ATOM    662  O   ARG A  89      19.012  44.373  12.257  1.00 21.50           O  
ATOM    663  CB  ARG A  89      21.613  45.764  10.731  1.00 20.98           C  
ATOM    664  CG  ARG A  89      21.869  45.980  12.223  1.00 19.77           C  
ATOM    665  CD  ARG A  89      23.319  46.440  12.496  1.00 21.57           C  
ATOM    666  NE  ARG A  89      23.500  46.936  13.863  1.00 20.57           N  
ATOM    667  CZ  ARG A  89      23.630  46.151  14.929  1.00 21.84           C  
ATOM    668  NH1 ARG A  89      23.633  44.840  14.798  1.00 19.04           N  
ATOM    669  NH2 ARG A  89      23.774  46.671  16.132  1.00 24.53           N  
ATOM    670  N   ALA A  90      20.093  42.985  10.816  1.00 22.44           N  
ATOM    671  CA  ALA A  90      19.509  41.774  11.382  1.00 23.02           C  
ATOM    672  C   ALA A  90      20.309  41.265  12.545  1.00 23.69           C  
ATOM    673  O   ALA A  90      21.524  41.444  12.591  1.00 24.80           O  
ATOM    674  CB  ALA A  90      19.382  40.685  10.333  1.00 23.51           C  
ATOM    675  N   LEU A  91      19.625  40.629  13.495  1.00 24.22           N  
ATOM    676  CA  LEU A  91      20.296  39.970  14.629  1.00 24.39           C  
ATOM    677  C   LEU A  91      20.118  38.460  14.517  1.00 24.55           C  
ATOM    678  O   LEU A  91      20.957  37.687  15.007  1.00 25.20           O  
ATOM    679  CB  LEU A  91      19.727  40.438  15.986  1.00 23.48           C  
ATOM    680  CG  LEU A  91      19.877  41.904  16.414  1.00 22.92           C  
ATOM    681  CD1 LEU A  91      19.353  42.033  17.849  1.00 22.77           C  
ATOM    682  CD2 LEU A  91      21.316  42.376  16.328  1.00 23.57           C  
ATOM    683  N   GLY A  92      19.021  38.032  13.890  1.00 25.11           N  
ATOM    684  CA  GLY A  92      18.676  36.607  13.886  1.00 24.76           C  
ATOM    685  C   GLY A  92      17.206  36.405  13.589  1.00 25.72           C  
ATOM    686  O   GLY A  92      16.566  37.253  12.962  1.00 24.40           O  
ATOM    687  N   MET A  93      16.646  35.283  14.026  1.00 26.58           N  
ATOM    688  CA  MET A  93      15.233  35.027  13.722  1.00 28.72           C  
ATOM    689  C   MET A  93      14.593  34.024  14.653  1.00 28.92           C  
ATOM    690  O   MET A  93      15.277  33.173  15.231  1.00 29.48           O  
ATOM    691  CB  MET A  93      15.019  34.623  12.238  1.00 29.18           C  
ATOM    692  CG  MET A  93      15.660  33.304  11.809  1.00 33.11           C  
ATOM    693  SD  MET A  93      15.636  33.076   9.990  1.00 40.50           S  
ATOM    694  CE  MET A  93      13.962  32.560   9.708  1.00 37.67           C  
ATOM    695  N   LEU A  94      13.278  34.144  14.810  1.00 29.01           N  
ATOM    696  CA  LEU A  94      12.506  33.156  15.553  1.00 30.00           C  
ATOM    697  C   LEU A  94      11.801  32.247  14.556  1.00 30.90           C  
ATOM    698  O   LEU A  94      11.070  32.735  13.699  1.00 30.26           O  
ATOM    699  CB  LEU A  94      11.484  33.838  16.460  1.00 29.19           C  
ATOM    700  CG  LEU A  94      10.751  32.998  17.514  1.00 30.25           C  
ATOM    701  CD1 LEU A  94      11.717  32.305  18.452  1.00 29.45           C  
ATOM    702  CD2 LEU A  94       9.800  33.894  18.320  1.00 28.35           C  
ATOM    703  N   LYS A  95      12.034  30.934  14.648  1.00 32.44           N  
ATOM    704  CA  LYS A  95      11.368  29.980  13.755  1.00 34.21           C  
ATOM    705  C   LYS A  95      10.137  29.384  14.420  1.00 34.50           C  
ATOM    706  O   LYS A  95      10.183  28.971  15.569  1.00 33.94           O  
ATOM    707  CB  LYS A  95      12.338  28.865  13.332  1.00 35.22           C  
ATOM    708  CG  LYS A  95      13.401  29.320  12.297  1.00 38.73           C  
ATOM    709  CD  LYS A  95      14.737  28.595  12.495  1.00 44.84           C  
ATOM    710  CE  LYS A  95      14.583  27.069  12.322  1.00 48.49           C  
ATOM    711  NZ  LYS A  95      15.502  26.237  13.209  1.00 50.26           N  
ATOM    712  N   MET A  96       9.029  29.351  13.698  1.00 35.87           N  
ATOM    713  CA  MET A  96       7.770  28.871  14.259  1.00 37.62           C  
ATOM    714  C   MET A  96       6.990  28.206  13.144  1.00 38.88           C  
ATOM    715  O   MET A  96       7.303  28.406  11.969  1.00 38.99           O  
ATOM    716  CB  MET A  96       6.915  30.046  14.783  1.00 36.87           C  
ATOM    717  CG  MET A  96       7.445  30.766  16.014  1.00 36.05           C  
ATOM    718  SD  MET A  96       6.661  32.397  16.227  1.00 32.47           S  
ATOM    719  CE  MET A  96       7.289  33.359  14.839  1.00 33.43           C  
ATOM    720  N   THR A  97       5.953  27.458  13.519  1.00 40.89           N  
ATOM    721  CA  THR A  97       4.894  27.078  12.584  1.00 43.05           C  
ATOM    722  C   THR A  97       3.560  27.461  13.229  1.00 43.77           C  
ATOM    723  O   THR A  97       3.380  27.280  14.438  1.00 44.35           O  
ATOM    724  CB  THR A  97       4.920  25.547  12.208  1.00 43.28           C  
ATOM    725  OG1 THR A  97       5.127  24.765  13.384  1.00 45.70           O  
ATOM    726  CG2 THR A  97       6.061  25.231  11.257  1.00 43.69           C  
ATOM    727  N   ASP A  98       2.644  28.028  12.446  1.00 44.41           N  
ATOM    728  CA  ASP A  98       1.321  28.342  12.967  1.00 45.30           C  
ATOM    729  C   ASP A  98       0.228  27.653  12.151  1.00 46.22           C  
ATOM    730  O   ASP A  98       0.517  26.775  11.331  1.00 46.61           O  
ATOM    731  CB  ASP A  98       1.088  29.858  13.021  1.00 45.20           C  
ATOM    732  CG  ASP A  98       0.949  30.472  11.652  1.00 45.80           C  
ATOM    733  OD1 ASP A  98       1.027  29.722  10.662  1.00 45.37           O  
ATOM    734  OD2 ASP A  98       0.764  31.704  11.562  1.00 44.84           O  
ATOM    735  N   GLU A  99      -1.028  28.042  12.377  1.00 46.47           N  
ATOM    736  CA  GLU A  99      -2.141  27.402  11.687  1.00 46.80           C  
ATOM    737  C   GLU A  99      -2.006  27.467  10.147  1.00 47.27           C  
ATOM    738  O   GLU A  99      -2.538  26.623   9.442  1.00 47.92           O  
ATOM    739  CB  GLU A  99      -3.483  27.973  12.161  1.00 45.98           C  
ATOM    740  CG  GLU A  99      -3.807  29.333  11.593  1.00 44.99           C  
ATOM    741  CD  GLU A  99      -3.196  30.497  12.389  1.00 42.89           C  
ATOM    742  OE1 GLU A  99      -3.428  31.661  11.987  1.00 42.58           O  
ATOM    743  OE2 GLU A  99      -2.503  30.248  13.405  1.00 41.44           O  
ATOM    744  N   SER A 100      -1.279  28.448   9.624  1.00 47.51           N  
ATOM    745  CA  SER A 100      -1.091  28.565   8.177  1.00 47.27           C  
ATOM    746  C   SER A 100       0.262  28.046   7.694  1.00 47.08           C  
ATOM    747  O   SER A 100       0.694  28.388   6.592  1.00 47.42           O  
ATOM    748  CB  SER A 100      -1.245  30.025   7.730  1.00 47.15           C  
ATOM    749  OG  SER A 100      -2.525  30.535   8.068  1.00 48.79           O  
ATOM    750  N   GLY A 101       0.939  27.237   8.507  1.00 46.73           N  
ATOM    751  CA  GLY A 101       2.222  26.653   8.110  1.00 45.72           C  
ATOM    752  C   GLY A 101       3.430  27.411   8.650  1.00 45.34           C  
ATOM    753  O   GLY A 101       3.320  28.159   9.633  1.00 45.08           O  
ATOM    754  N   VAL A 102       4.585  27.222   8.008  1.00 44.18           N  
ATOM    755  CA  VAL A 102       5.851  27.802   8.476  1.00 43.13           C  
ATOM    756  C   VAL A 102       5.795  29.319   8.668  1.00 42.11           C  
ATOM    757  O   VAL A 102       5.204  30.039   7.858  1.00 41.60           O  
ATOM    758  CB  VAL A 102       7.015  27.444   7.524  1.00 43.66           C  
ATOM    759  CG1 VAL A 102       8.164  28.428   7.684  1.00 43.30           C  
ATOM    760  CG2 VAL A 102       7.488  25.988   7.764  1.00 43.78           C  
ATOM    761  N   ASP A 103       6.415  29.804   9.744  1.00 41.05           N  
ATOM    762  CA  ASP A 103       6.375  31.242  10.062  1.00 39.44           C  
ATOM    763  C   ASP A 103       7.649  31.697  10.761  1.00 37.83           C  
ATOM    764  O   ASP A 103       7.784  31.562  11.973  1.00 38.58           O  
ATOM    765  CB  ASP A 103       5.182  31.541  10.962  1.00 39.54           C  
ATOM    766  CG  ASP A 103       4.926  33.029  11.126  1.00 40.16           C  
ATOM    767  OD1 ASP A 103       5.544  33.843  10.396  1.00 42.27           O  
ATOM    768  OD2 ASP A 103       4.081  33.379  11.977  1.00 38.14           O  
ATOM    769  N   ALA A 104       8.591  32.226   9.995  1.00 35.52           N  
ATOM    770  CA  ALA A 104       9.799  32.789  10.562  1.00 32.80           C  
ATOM    771  C   ALA A 104       9.611  34.300  10.727  1.00 30.91           C  
ATOM    772  O   ALA A 104       9.037  34.959   9.857  1.00 30.17           O  
ATOM    773  CB  ALA A 104      10.955  32.514   9.651  1.00 33.11           C  
ATOM    774  N   LYS A 105      10.079  34.838  11.847  1.00 29.57           N  
ATOM    775  CA  LYS A 105      10.147  36.293  12.036  1.00 28.05           C  
ATOM    776  C   LYS A 105      11.562  36.720  12.391  1.00 27.06           C  
ATOM    777  O   LYS A 105      12.174  36.150  13.289  1.00 27.14           O  
ATOM    778  CB  LYS A 105       9.142  36.750  13.090  1.00 27.30           C  
ATOM    779  CG  LYS A 105       7.712  36.235  12.749  1.00 27.03           C  
ATOM    780  CD  LYS A 105       6.645  37.016  13.447  1.00 26.83           C  
ATOM    781  CE  LYS A 105       5.287  36.300  13.367  1.00 24.94           C  
ATOM    782  NZ  LYS A 105       4.698  36.387  11.996  1.00 23.03           N  
ATOM    783  N   LEU A 106      12.058  37.734  11.691  1.00 25.68           N  
ATOM    784  CA  LEU A 106      13.374  38.275  11.962  1.00 25.87           C  
ATOM    785  C   LEU A 106      13.354  39.143  13.222  1.00 25.22           C  
ATOM    786  O   LEU A 106      12.314  39.719  13.598  1.00 24.89           O  
ATOM    787  CB  LEU A 106      13.857  39.118  10.784  1.00 25.38           C  
ATOM    788  CG  LEU A 106      14.443  38.394   9.564  1.00 27.94           C  
ATOM    789  CD1 LEU A 106      13.727  37.094   9.184  1.00 27.95           C  
ATOM    790  CD2 LEU A 106      14.567  39.332   8.388  1.00 26.61           C  
ATOM    791  N   VAL A 107      14.523  39.257  13.838  1.00 23.51           N  
ATOM    792  CA  VAL A 107      14.716  40.131  14.964  1.00 22.73           C  
ATOM    793  C   VAL A 107      15.811  41.090  14.512  1.00 22.68           C  
ATOM    794  O   VAL A 107      16.854  40.661  14.003  1.00 22.46           O  
ATOM    795  CB  VAL A 107      15.080  39.338  16.238  1.00 22.27           C  
ATOM    796  CG1 VAL A 107      15.343  40.270  17.373  1.00 22.46           C  
ATOM    797  CG2 VAL A 107      13.939  38.318  16.594  1.00 23.92           C  
ATOM    798  N   ALA A 108      15.553  42.392  14.645  1.00 21.45           N  
ATOM    799  CA  ALA A 108      16.439  43.391  14.095  1.00 20.74           C  
ATOM    800  C   ALA A 108      16.607  44.559  15.068  1.00 21.23           C  
ATOM    801  O   ALA A 108      15.871  44.634  16.070  1.00 21.11           O  
ATOM    802  CB  ALA A 108      15.903  43.883  12.721  1.00 19.22           C  
ATOM    803  N   VAL A 109      17.600  45.423  14.790  1.00 20.09           N  
ATOM    804  CA  VAL A 109      17.739  46.729  15.426  1.00 21.46           C  
ATOM    805  C   VAL A 109      17.973  47.762  14.319  1.00 21.87           C  
ATOM    806  O   VAL A 109      18.314  47.381  13.202  1.00 21.72           O  
ATOM    807  CB  VAL A 109      18.928  46.784  16.409  1.00 20.91           C  
ATOM    808  CG1 VAL A 109      18.614  46.011  17.652  1.00 20.05           C  
ATOM    809  CG2 VAL A 109      20.208  46.218  15.733  1.00 22.26           C  
ATOM    810  N   PRO A 110      17.804  49.068  14.626  1.00 22.19           N  
ATOM    811  CA  PRO A 110      18.094  50.056  13.594  1.00 22.34           C  
ATOM    812  C   PRO A 110      19.597  50.067  13.216  1.00 23.74           C  
ATOM    813  O   PRO A 110      20.435  49.546  13.963  1.00 23.41           O  
ATOM    814  CB  PRO A 110      17.717  51.405  14.280  1.00 22.83           C  
ATOM    815  CG  PRO A 110      16.791  51.058  15.399  1.00 21.11           C  
ATOM    816  CD  PRO A 110      17.289  49.695  15.870  1.00 21.07           C  
ATOM    817  N   HIS A 111      19.905  50.663  12.062  1.00 24.43           N  
ATOM    818  CA  HIS A 111      21.269  51.039  11.680  1.00 25.10           C  
ATOM    819  C   HIS A 111      21.948  51.765  12.839  1.00 25.61           C  
ATOM    820  O   HIS A 111      21.322  52.588  13.518  1.00 26.10           O  
ATOM    821  CB  HIS A 111      21.182  51.975  10.450  1.00 24.91           C  
ATOM    822  CG  HIS A 111      22.509  52.407   9.893  1.00 26.79           C  
ATOM    823  ND1 HIS A 111      23.070  51.820   8.770  1.00 29.91           N  
ATOM    824  CD2 HIS A 111      23.393  53.348  10.305  1.00 23.68           C  
ATOM    825  CE1 HIS A 111      24.235  52.393   8.514  1.00 26.42           C  
ATOM    826  NE2 HIS A 111      24.442  53.336   9.416  1.00 26.73           N  
ATOM    827  N   ASP A 112      23.234  51.504  13.051  1.00 25.54           N  
ATOM    828  CA  ASP A 112      23.979  52.129  14.147  1.00 25.57           C  
ATOM    829  C   ASP A 112      23.942  53.667  14.222  1.00 25.64           C  
ATOM    830  O   ASP A 112      24.009  54.219  15.303  1.00 25.60           O  
ATOM    831  CB  ASP A 112      25.433  51.655  14.148  1.00 26.15           C  
ATOM    832  CG  ASP A 112      25.577  50.191  14.586  1.00 25.67           C  
ATOM    833  OD1 ASP A 112      24.592  49.558  15.018  1.00 29.82           O  
ATOM    834  OD2 ASP A 112      26.687  49.675  14.528  1.00 26.95           O  
ATOM    835  N   LYS A 113      23.866  54.355  13.095  1.00 25.60           N  
ATOM    836  CA  LYS A 113      23.786  55.819  13.100  1.00 26.31           C  
ATOM    837  C   LYS A 113      22.358  56.299  13.405  1.00 26.01           C  
ATOM    838  O   LYS A 113      22.150  57.398  13.891  1.00 27.30           O  
ATOM    839  CB  LYS A 113      24.288  56.390  11.768  1.00 26.96           C  
ATOM    840  N   VAL A 114      21.370  55.453  13.158  1.00 25.69           N  
ATOM    841  CA  VAL A 114      19.998  55.764  13.562  1.00 24.61           C  
ATOM    842  C   VAL A 114      19.806  55.525  15.065  1.00 25.10           C  
ATOM    843  O   VAL A 114      19.249  56.379  15.773  1.00 24.38           O  
ATOM    844  CB  VAL A 114      19.001  54.950  12.751  1.00 25.32           C  
ATOM    845  CG1 VAL A 114      17.528  55.198  13.246  1.00 23.89           C  
ATOM    846  CG2 VAL A 114      19.202  55.234  11.260  1.00 22.62           C  
ATOM    847  N   CYS A 115      20.318  54.395  15.563  1.00 24.30           N  
ATOM    848  CA  CYS A 115      20.191  54.054  16.978  1.00 24.45           C  
ATOM    849  C   CYS A 115      21.523  53.611  17.614  1.00 25.28           C  
ATOM    850  O   CYS A 115      21.821  52.409  17.705  1.00 25.35           O  
ATOM    851  CB  CYS A 115      19.111  52.977  17.168  1.00 24.20           C  
ATOM    852  SG  CYS A 115      18.644  52.733  18.908  1.00 23.28           S  
ATOM    853  N   PRO A 116      22.343  54.583  18.036  1.00 25.64           N  
ATOM    854  CA  PRO A 116      23.601  54.246  18.715  1.00 25.83           C  
ATOM    855  C   PRO A 116      23.382  53.386  19.946  1.00 26.76           C  
ATOM    856  O   PRO A 116      24.274  52.606  20.303  1.00 27.28           O  
ATOM    857  CB  PRO A 116      24.150  55.613  19.142  1.00 25.73           C  
ATOM    858  CG  PRO A 116      23.576  56.573  18.005  1.00 26.37           C  
ATOM    859  CD  PRO A 116      22.177  56.038  17.826  1.00 24.59           C  
ATOM    860  N   MET A 117      22.213  53.510  20.569  1.00 25.92           N  
ATOM    861  CA  MET A 117      21.880  52.798  21.806  1.00 25.99           C  
ATOM    862  C   MET A 117      21.872  51.286  21.630  1.00 26.46           C  
ATOM    863  O   MET A 117      22.001  50.553  22.613  1.00 25.60           O  
ATOM    864  CB  MET A 117      20.492  53.211  22.307  1.00 25.61           C  
ATOM    865  CG  MET A 117      20.329  54.735  22.551  1.00 25.77           C  
ATOM    866  SD  MET A 117      19.862  55.666  21.073  1.00 23.51           S  
ATOM    867  CE  MET A 117      20.351  57.314  21.549  1.00 23.67           C  
ATOM    868  N   THR A 118      21.643  50.816  20.396  1.00 26.44           N  
ATOM    869  CA  THR A 118      21.572  49.368  20.159  1.00 26.45           C  
ATOM    870  C   THR A 118      22.833  48.825  19.435  1.00 26.58           C  
ATOM    871  O   THR A 118      22.882  47.643  19.071  1.00 25.87           O  
ATOM    872  CB  THR A 118      20.255  48.931  19.388  1.00 26.23           C  
ATOM    873  OG1 THR A 118      20.061  49.752  18.255  1.00 25.67           O  
ATOM    874  CG2 THR A 118      18.975  49.004  20.277  1.00 24.93           C  
ATOM    875  N   ALA A 119      23.848  49.673  19.264  1.00 26.81           N  
ATOM    876  CA  ALA A 119      25.069  49.285  18.509  1.00 27.89           C  
ATOM    877  C   ALA A 119      25.785  48.057  19.057  1.00 28.60           C  
ATOM    878  O   ALA A 119      26.365  47.295  18.299  1.00 28.79           O  
ATOM    879  CB  ALA A 119      26.024  50.442  18.375  1.00 27.47           C  
ATOM    880  N   ASN A 120      25.712  47.837  20.364  1.00 30.19           N  
ATOM    881  CA  ASN A 120      26.394  46.697  20.978  1.00 31.83           C  
ATOM    882  C   ASN A 120      25.633  45.400  20.871  1.00 31.62           C  
ATOM    883  O   ASN A 120      26.124  44.389  21.335  1.00 30.93           O  
ATOM    884  CB  ASN A 120      26.733  46.965  22.447  1.00 33.05           C  
ATOM    885  CG  ASN A 120      27.805  48.055  22.605  1.00 38.99           C  
ATOM    886  OD1 ASN A 120      28.787  48.097  21.842  1.00 44.64           O  
ATOM    887  ND2 ASN A 120      27.610  48.953  23.578  1.00 43.69           N  
ATOM    888  N   LEU A 121      24.427  45.424  20.298  1.00 30.32           N  
ATOM    889  CA  LEU A 121      23.756  44.177  19.945  1.00 30.28           C  
ATOM    890  C   LEU A 121      24.232  43.750  18.545  1.00 30.14           C  
ATOM    891  O   LEU A 121      23.838  44.354  17.529  1.00 29.66           O  
ATOM    892  CB  LEU A 121      22.221  44.314  19.994  1.00 29.43           C  
ATOM    893  CG  LEU A 121      21.655  44.833  21.312  1.00 29.47           C  
ATOM    894  CD1 LEU A 121      20.133  45.148  21.240  1.00 28.60           C  
ATOM    895  CD2 LEU A 121      21.981  43.867  22.439  1.00 30.01           C  
ATOM    896  N   LYS A 122      25.104  42.739  18.514  1.00 30.23           N  
ATOM    897  CA  LYS A 122      25.692  42.242  17.272  1.00 30.77           C  
ATOM    898  C   LYS A 122      24.963  41.015  16.720  1.00 30.31           C  
ATOM    899  O   LYS A 122      24.994  40.748  15.520  1.00 30.97           O  
ATOM    900  CB  LYS A 122      27.150  41.856  17.492  1.00 31.10           C  
ATOM    901  CG  LYS A 122      27.932  42.857  18.270  1.00 34.55           C  
ATOM    902  CD  LYS A 122      28.254  44.068  17.435  1.00 37.21           C  
ATOM    903  CE  LYS A 122      29.578  44.637  17.921  1.00 41.85           C  
ATOM    904  NZ  LYS A 122      29.647  46.122  17.779  1.00 45.04           N  
ATOM    905  N   SER A 123      24.353  40.234  17.590  1.00 28.89           N  
ATOM    906  CA  SER A 123      23.593  39.080  17.119  1.00 29.25           C  
ATOM    907  C   SER A 123      22.504  38.756  18.130  1.00 29.01           C  
ATOM    908  O   SER A 123      22.439  39.361  19.199  1.00 29.07           O  
ATOM    909  CB  SER A 123      24.514  37.847  16.919  1.00 28.38           C  
ATOM    910  OG  SER A 123      24.909  37.328  18.187  1.00 30.05           O  
ATOM    911  N   ILE A 124      21.657  37.797  17.779  1.00 30.11           N  
ATOM    912  CA  ILE A 124      20.560  37.354  18.616  1.00 30.40           C  
ATOM    913  C   ILE A 124      21.044  36.980  20.043  1.00 31.66           C  
ATOM    914  O   ILE A 124      20.308  37.162  21.020  1.00 30.63           O  
ATOM    915  CB  ILE A 124      19.830  36.168  17.921  1.00 30.97           C  
ATOM    916  CG1 ILE A 124      18.526  35.811  18.648  1.00 31.32           C  
ATOM    917  CG2 ILE A 124      20.760  34.954  17.775  1.00 29.74           C  
ATOM    918  CD1 ILE A 124      17.435  36.836  18.440  1.00 33.00           C  
ATOM    919  N   ASP A 125      22.286  36.472  20.155  1.00 32.15           N  
ATOM    920  CA  ASP A 125      22.858  36.041  21.449  1.00 32.32           C  
ATOM    921  C   ASP A 125      23.117  37.191  22.390  1.00 31.43           C  
ATOM    922  O   ASP A 125      23.291  36.996  23.591  1.00 30.73           O  
ATOM    923  CB  ASP A 125      24.180  35.287  21.239  1.00 33.54           C  
ATOM    924  CG  ASP A 125      24.027  34.128  20.295  1.00 36.42           C  
ATOM    925  OD1 ASP A 125      23.000  33.427  20.372  1.00 38.93           O  
ATOM    926  OD2 ASP A 125      24.912  33.948  19.440  1.00 41.72           O  
ATOM    927  N   ASP A 126      23.151  38.402  21.849  1.00 30.57           N  
ATOM    928  CA  ASP A 126      23.341  39.566  22.696  1.00 29.73           C  
ATOM    929  C   ASP A 126      22.028  40.092  23.290  1.00 29.14           C  
ATOM    930  O   ASP A 126      22.059  40.903  24.202  1.00 28.18           O  
ATOM    931  CB  ASP A 126      24.023  40.693  21.927  1.00 29.86           C  
ATOM    932  CG  ASP A 126      25.409  40.308  21.440  1.00 31.45           C  
ATOM    933  OD1 ASP A 126      26.168  39.758  22.245  1.00 32.98           O  
ATOM    934  OD2 ASP A 126      25.732  40.556  20.265  1.00 29.33           O  
ATOM    935  N   VAL A 127      20.891  39.663  22.750  1.00 28.12           N  
ATOM    936  CA  VAL A 127      19.600  40.132  23.270  1.00 27.54           C  
ATOM    937  C   VAL A 127      19.398  39.543  24.680  1.00 27.24           C  
ATOM    938  O   VAL A 127      19.603  38.361  24.881  1.00 26.18           O  
ATOM    939  CB  VAL A 127      18.442  39.723  22.332  1.00 27.46           C  
ATOM    940  CG1 VAL A 127      17.094  40.157  22.913  1.00 26.88           C  
ATOM    941  CG2 VAL A 127      18.645  40.294  20.923  1.00 27.36           C  
ATOM    942  N   PRO A 128      19.011  40.375  25.658  1.00 27.18           N  
ATOM    943  CA  PRO A 128      18.809  39.845  26.999  1.00 27.22           C  
ATOM    944  C   PRO A 128      17.902  38.614  26.998  1.00 27.86           C  
ATOM    945  O   PRO A 128      16.919  38.562  26.249  1.00 27.80           O  
ATOM    946  CB  PRO A 128      18.130  41.002  27.724  1.00 26.62           C  
ATOM    947  CG  PRO A 128      18.769  42.235  27.104  1.00 28.03           C  
ATOM    948  CD  PRO A 128      18.898  41.850  25.616  1.00 27.41           C  
ATOM    949  N   ALA A 129      18.221  37.627  27.834  1.00 27.80           N  
ATOM    950  CA  ALA A 129      17.410  36.415  27.870  1.00 28.35           C  
ATOM    951  C   ALA A 129      15.934  36.714  28.217  1.00 28.08           C  
ATOM    952  O   ALA A 129      15.010  36.049  27.696  1.00 27.99           O  
ATOM    953  CB  ALA A 129      18.005  35.402  28.850  1.00 28.21           C  
ATOM    954  N   TYR A 130      15.720  37.696  29.098  1.00 27.53           N  
ATOM    955  CA  TYR A 130      14.362  38.016  29.546  1.00 27.52           C  
ATOM    956  C   TYR A 130      13.523  38.512  28.358  1.00 27.66           C  
ATOM    957  O   TYR A 130      12.357  38.146  28.241  1.00 27.90           O  
ATOM    958  CB  TYR A 130      14.350  39.024  30.720  1.00 27.57           C  
ATOM    959  CG  TYR A 130      14.359  40.464  30.262  1.00 27.15           C  
ATOM    960  CD1 TYR A 130      13.183  41.099  29.871  1.00 29.10           C  
ATOM    961  CD2 TYR A 130      15.554  41.175  30.181  1.00 27.46           C  
ATOM    962  CE1 TYR A 130      13.203  42.410  29.409  1.00 28.74           C  
ATOM    963  CE2 TYR A 130      15.584  42.465  29.730  1.00 28.56           C  
ATOM    964  CZ  TYR A 130      14.398  43.072  29.348  1.00 29.54           C  
ATOM    965  OH  TYR A 130      14.443  44.369  28.916  1.00 34.94           O  
ATOM    966  N   LEU A 131      14.121  39.315  27.477  1.00 27.44           N  
ATOM    967  CA  LEU A 131      13.440  39.796  26.273  1.00 27.71           C  
ATOM    968  C   LEU A 131      13.166  38.664  25.271  1.00 27.69           C  
ATOM    969  O   LEU A 131      12.027  38.483  24.788  1.00 27.08           O  
ATOM    970  CB  LEU A 131      14.240  40.910  25.608  1.00 27.68           C  
ATOM    971  CG  LEU A 131      13.453  41.705  24.555  1.00 29.36           C  
ATOM    972  CD1 LEU A 131      12.160  42.314  25.137  1.00 28.92           C  
ATOM    973  CD2 LEU A 131      14.328  42.790  23.943  1.00 29.57           C  
ATOM    974  N   LYS A 132      14.211  37.901  24.953  1.00 27.29           N  
ATOM    975  CA  LYS A 132      14.038  36.681  24.180  1.00 27.37           C  
ATOM    976  C   LYS A 132      12.846  35.869  24.734  1.00 26.26           C  
ATOM    977  O   LYS A 132      11.948  35.517  23.986  1.00 26.14           O  
ATOM    978  CB  LYS A 132      15.336  35.843  24.172  1.00 28.31           C  
ATOM    979  CG  LYS A 132      16.386  36.314  23.170  1.00 30.56           C  
ATOM    980  CD  LYS A 132      17.511  35.269  22.990  1.00 33.45           C  
ATOM    981  CE  LYS A 132      18.727  35.625  23.835  1.00 35.02           C  
ATOM    982  NZ  LYS A 132      19.939  34.745  23.591  1.00 37.99           N  
ATOM    983  N   ASP A 133      12.839  35.580  26.034  1.00 25.23           N  
ATOM    984  CA  ASP A 133      11.757  34.796  26.662  1.00 24.89           C  
ATOM    985  C   ASP A 133      10.358  35.406  26.531  1.00 24.44           C  
ATOM    986  O   ASP A 133       9.383  34.687  26.328  1.00 23.26           O  
ATOM    987  CB  ASP A 133      12.027  34.569  28.159  1.00 24.84           C  
ATOM    988  CG  ASP A 133      13.166  33.593  28.417  1.00 28.52           C  
ATOM    989  OD1 ASP A 133      13.562  32.849  27.490  1.00 31.06           O  
ATOM    990  OD2 ASP A 133      13.678  33.593  29.552  1.00 31.64           O  
ATOM    991  N   GLN A 134      10.272  36.724  26.710  1.00 24.07           N  
ATOM    992  CA  GLN A 134       9.018  37.455  26.504  1.00 24.53           C  
ATOM    993  C   GLN A 134       8.504  37.351  25.062  1.00 24.16           C  
ATOM    994  O   GLN A 134       7.301  37.181  24.843  1.00 23.95           O  
ATOM    995  CB  GLN A 134       9.182  38.943  26.874  1.00 24.01           C  
ATOM    996  CG  GLN A 134       9.537  39.176  28.333  1.00 25.53           C  
ATOM    997  CD  GLN A 134       9.354  40.607  28.741  1.00 25.83           C  
ATOM    998  OE1 GLN A 134       9.357  40.934  29.927  1.00 27.07           O  
ATOM    999  NE2 GLN A 134       9.165  41.470  27.766  1.00 26.58           N  
ATOM   1000  N   ILE A 135       9.399  37.479  24.086  1.00 23.99           N  
ATOM   1001  CA  ILE A 135       8.997  37.405  22.674  1.00 24.11           C  
ATOM   1002  C   ILE A 135       8.444  36.023  22.366  1.00 25.38           C  
ATOM   1003  O   ILE A 135       7.381  35.878  21.727  1.00 25.45           O  
ATOM   1004  CB  ILE A 135      10.163  37.749  21.719  1.00 24.40           C  
ATOM   1005  CG1 ILE A 135      10.565  39.216  21.892  1.00 23.65           C  
ATOM   1006  CG2 ILE A 135       9.834  37.373  20.230  1.00 20.81           C  
ATOM   1007  CD1 ILE A 135      11.932  39.561  21.290  1.00 21.20           C  
ATOM   1008  N   LYS A 136       9.138  35.006  22.859  1.00 25.73           N  
ATOM   1009  CA  LYS A 136       8.711  33.639  22.643  1.00 26.35           C  
ATOM   1010  C   LYS A 136       7.365  33.315  23.315  1.00 25.70           C  
ATOM   1011  O   LYS A 136       6.482  32.730  22.684  1.00 24.73           O  
ATOM   1012  CB  LYS A 136       9.839  32.696  23.079  1.00 27.12           C  
ATOM   1013  CG  LYS A 136       9.491  31.210  23.059  1.00 30.98           C  
ATOM   1014  CD  LYS A 136      10.754  30.398  23.454  1.00 38.08           C  
ATOM   1015  CE  LYS A 136      10.456  28.907  23.637  1.00 40.93           C  
ATOM   1016  NZ  LYS A 136       9.113  28.719  24.265  1.00 44.61           N  
ATOM   1017  N   HIS A 137       7.192  33.740  24.575  1.00 25.25           N  
ATOM   1018  CA  HIS A 137       5.900  33.625  25.278  1.00 24.60           C  
ATOM   1019  C   HIS A 137       4.757  34.338  24.511  1.00 23.92           C  
ATOM   1020  O   HIS A 137       3.645  33.784  24.345  1.00 23.75           O  
ATOM   1021  CB  HIS A 137       6.011  34.201  26.735  1.00 24.77           C  
ATOM   1022  CG  HIS A 137       4.761  34.005  27.551  1.00 25.29           C  
ATOM   1023  ND1 HIS A 137       3.872  35.028  27.824  1.00 25.11           N  
ATOM   1024  CD2 HIS A 137       4.228  32.888  28.111  1.00 22.39           C  
ATOM   1025  CE1 HIS A 137       2.856  34.556  28.526  1.00 22.79           C  
ATOM   1026  NE2 HIS A 137       3.047  33.259  28.714  1.00 26.13           N  
ATOM   1027  N   PHE A 138       5.022  35.573  24.066  1.00 23.23           N  
ATOM   1028  CA  PHE A 138       4.054  36.330  23.261  1.00 23.01           C  
ATOM   1029  C   PHE A 138       3.523  35.499  22.087  1.00 23.59           C  
ATOM   1030  O   PHE A 138       2.313  35.315  21.948  1.00 22.99           O  
ATOM   1031  CB  PHE A 138       4.588  37.688  22.737  1.00 21.76           C  
ATOM   1032  CG  PHE A 138       3.581  38.410  21.879  1.00 22.65           C  
ATOM   1033  CD1 PHE A 138       2.538  39.114  22.458  1.00 20.19           C  
ATOM   1034  CD2 PHE A 138       3.626  38.326  20.481  1.00 22.75           C  
ATOM   1035  CE1 PHE A 138       1.566  39.746  21.672  1.00 20.14           C  
ATOM   1036  CE2 PHE A 138       2.661  38.960  19.693  1.00 18.78           C  
ATOM   1037  CZ  PHE A 138       1.624  39.658  20.306  1.00 18.64           C  
ATOM   1038  N   PHE A 139       4.418  34.995  21.238  1.00 24.32           N  
ATOM   1039  CA  PHE A 139       3.966  34.206  20.091  1.00 25.35           C  
ATOM   1040  C   PHE A 139       3.302  32.873  20.431  1.00 26.07           C  
ATOM   1041  O   PHE A 139       2.369  32.435  19.751  1.00 26.11           O  
ATOM   1042  CB  PHE A 139       5.084  34.060  19.068  1.00 25.90           C  
ATOM   1043  CG  PHE A 139       5.393  35.342  18.370  1.00 27.31           C  
ATOM   1044  CD1 PHE A 139       4.535  35.827  17.393  1.00 27.14           C  
ATOM   1045  CD2 PHE A 139       6.515  36.088  18.718  1.00 26.77           C  
ATOM   1046  CE1 PHE A 139       4.796  37.021  16.763  1.00 26.81           C  
ATOM   1047  CE2 PHE A 139       6.786  37.279  18.088  1.00 27.38           C  
ATOM   1048  CZ  PHE A 139       5.915  37.750  17.096  1.00 27.03           C  
ATOM   1049  N   GLU A 140       3.747  32.247  21.508  1.00 27.11           N  
ATOM   1050  CA  GLU A 140       3.095  31.047  22.009  1.00 28.38           C  
ATOM   1051  C   GLU A 140       1.679  31.261  22.518  1.00 27.76           C  
ATOM   1052  O   GLU A 140       0.889  30.341  22.460  1.00 28.49           O  
ATOM   1053  CB  GLU A 140       3.937  30.396  23.110  1.00 28.39           C  
ATOM   1054  CG  GLU A 140       5.150  29.725  22.513  1.00 32.77           C  
ATOM   1055  CD  GLU A 140       5.926  28.953  23.534  1.00 35.86           C  
ATOM   1056  OE1 GLU A 140       5.978  29.397  24.707  1.00 36.53           O  
ATOM   1057  OE2 GLU A 140       6.491  27.914  23.149  1.00 38.06           O  
ATOM   1058  N   GLN A 141       1.358  32.463  22.996  1.00 27.27           N  
ATOM   1059  CA  GLN A 141       0.098  32.706  23.718  1.00 26.49           C  
ATOM   1060  C   GLN A 141      -0.891  33.712  23.103  1.00 26.43           C  
ATOM   1061  O   GLN A 141      -2.081  33.621  23.367  1.00 26.26           O  
ATOM   1062  CB  GLN A 141       0.390  33.129  25.170  1.00 26.70           C  
ATOM   1063  CG  GLN A 141       1.054  32.012  26.000  1.00 25.87           C  
ATOM   1064  CD  GLN A 141       0.143  30.811  26.137  1.00 27.04           C  
ATOM   1065  OE1 GLN A 141      -1.078  30.964  26.127  1.00 26.18           O  
ATOM   1066  NE2 GLN A 141       0.725  29.604  26.246  1.00 24.08           N  
ATOM   1067  N   TYR A 142      -0.431  34.650  22.283  1.00 25.24           N  
ATOM   1068  CA  TYR A 142      -1.324  35.723  21.835  1.00 25.93           C  
ATOM   1069  C   TYR A 142      -2.589  35.291  21.046  1.00 26.85           C  
ATOM   1070  O   TYR A 142      -3.600  36.023  21.036  1.00 25.86           O  
ATOM   1071  CB  TYR A 142      -0.550  36.851  21.122  1.00 24.57           C  
ATOM   1072  CG  TYR A 142      -0.237  36.657  19.645  1.00 24.88           C  
ATOM   1073  CD1 TYR A 142      -0.614  37.636  18.697  1.00 23.74           C  
ATOM   1074  CD2 TYR A 142       0.484  35.536  19.189  1.00 23.36           C  
ATOM   1075  CE1 TYR A 142      -0.311  37.485  17.323  1.00 24.35           C  
ATOM   1076  CE2 TYR A 142       0.795  35.381  17.840  1.00 23.20           C  
ATOM   1077  CZ  TYR A 142       0.408  36.350  16.908  1.00 24.71           C  
ATOM   1078  OH  TYR A 142       0.726  36.189  15.570  1.00 23.16           O  
ATOM   1079  N   LYS A 143      -2.538  34.106  20.425  1.00 27.36           N  
ATOM   1080  CA  LYS A 143      -3.656  33.620  19.616  1.00 28.59           C  
ATOM   1081  C   LYS A 143      -4.517  32.628  20.383  1.00 28.24           C  
ATOM   1082  O   LYS A 143      -5.450  32.069  19.814  1.00 28.26           O  
ATOM   1083  CB  LYS A 143      -3.179  32.956  18.314  1.00 28.24           C  
ATOM   1084  CG  LYS A 143      -2.845  33.904  17.177  1.00 30.18           C  
ATOM   1085  CD  LYS A 143      -2.035  33.123  16.136  1.00 31.30           C  
ATOM   1086  CE  LYS A 143      -2.057  33.788  14.782  1.00 32.46           C  
ATOM   1087  NZ  LYS A 143      -1.094  33.108  13.850  1.00 31.69           N  
ATOM   1088  N   ALA A 144      -4.214  32.446  21.666  1.00 28.11           N  
ATOM   1089  CA  ALA A 144      -4.911  31.489  22.514  1.00 28.53           C  
ATOM   1090  C   ALA A 144      -6.436  31.578  22.439  1.00 29.33           C  
ATOM   1091  O   ALA A 144      -7.109  30.576  22.625  1.00 29.02           O  
ATOM   1092  CB  ALA A 144      -4.446  31.610  23.979  1.00 27.54           C  
ATOM   1093  N   LEU A 145      -6.986  32.755  22.160  1.00 30.11           N  
ATOM   1094  CA  LEU A 145      -8.442  32.926  22.243  1.00 31.34           C  
ATOM   1095  C   LEU A 145      -9.115  33.091  20.884  1.00 33.19           C  
ATOM   1096  O   LEU A 145     -10.278  33.527  20.799  1.00 34.02           O  
ATOM   1097  CB  LEU A 145      -8.836  34.068  23.184  1.00 30.04           C  
ATOM   1098  CG  LEU A 145      -8.451  33.803  24.646  1.00 29.77           C  
ATOM   1099  CD1 LEU A 145      -8.766  35.020  25.539  1.00 27.97           C  
ATOM   1100  CD2 LEU A 145      -9.158  32.558  25.178  1.00 28.92           C  
ATOM   1101  N   GLU A 146      -8.404  32.722  19.826  1.00 34.54           N  
ATOM   1102  CA  GLU A 146      -9.007  32.685  18.497  1.00 36.61           C  
ATOM   1103  C   GLU A 146      -9.127  31.241  18.018  1.00 36.98           C  
ATOM   1104  O   GLU A 146      -8.131  30.520  17.940  1.00 37.28           O  
ATOM   1105  CB  GLU A 146      -8.198  33.548  17.528  1.00 36.66           C  
ATOM   1106  CG  GLU A 146      -8.473  35.038  17.752  1.00 39.16           C  
ATOM   1107  CD  GLU A 146      -7.212  35.867  17.769  1.00 41.76           C  
ATOM   1108  OE1 GLU A 146      -6.523  35.925  16.724  1.00 46.57           O  
ATOM   1109  OE2 GLU A 146      -6.907  36.480  18.809  1.00 41.40           O  
ATOM   1110  N   LYS A 147     -10.355  30.810  17.733  1.00 38.45           N  
ATOM   1111  CA  LYS A 147     -10.597  29.436  17.247  1.00 39.30           C  
ATOM   1112  C   LYS A 147      -9.881  29.202  15.918  1.00 39.80           C  
ATOM   1113  O   LYS A 147      -9.942  30.031  15.004  1.00 39.70           O  
ATOM   1114  CB  LYS A 147     -12.107  29.141  17.099  1.00 39.10           C  
ATOM   1115  N   GLY A 148      -9.196  28.069  15.813  1.00 40.78           N  
ATOM   1116  CA  GLY A 148      -8.523  27.724  14.574  1.00 41.89           C  
ATOM   1117  C   GLY A 148      -7.129  28.302  14.423  1.00 42.81           C  
ATOM   1118  O   GLY A 148      -6.505  28.152  13.366  1.00 43.25           O  
ATOM   1119  N   LYS A 149      -6.631  28.970  15.467  1.00 42.74           N  
ATOM   1120  CA  LYS A 149      -5.309  29.594  15.395  1.00 42.54           C  
ATOM   1121  C   LYS A 149      -4.401  29.040  16.468  1.00 42.14           C  
ATOM   1122  O   LYS A 149      -4.838  28.797  17.587  1.00 42.29           O  
ATOM   1123  CB  LYS A 149      -5.433  31.099  15.551  1.00 42.68           C  
ATOM   1124  CG  LYS A 149      -6.172  31.762  14.419  1.00 43.87           C  
ATOM   1125  CD  LYS A 149      -6.153  33.241  14.672  1.00 47.65           C  
ATOM   1126  CE  LYS A 149      -6.746  34.013  13.534  1.00 49.81           C  
ATOM   1127  NZ  LYS A 149      -6.712  35.448  13.904  1.00 50.78           N  
ATOM   1128  N   TRP A 150      -3.132  28.836  16.131  1.00 41.69           N  
ATOM   1129  CA  TRP A 150      -2.195  28.252  17.077  1.00 41.16           C  
ATOM   1130  C   TRP A 150      -0.741  28.515  16.617  1.00 40.09           C  
ATOM   1131  O   TRP A 150      -0.498  28.906  15.467  1.00 39.90           O  
ATOM   1132  CB  TRP A 150      -2.482  26.751  17.256  1.00 42.09           C  
ATOM   1133  CG  TRP A 150      -2.424  25.994  15.941  1.00 44.48           C  
ATOM   1134  CD1 TRP A 150      -3.473  25.731  15.085  1.00 46.23           C  
ATOM   1135  CD2 TRP A 150      -1.253  25.441  15.319  1.00 47.04           C  
ATOM   1136  NE1 TRP A 150      -3.018  25.043  13.976  1.00 47.57           N  
ATOM   1137  CE2 TRP A 150      -1.664  24.847  14.098  1.00 48.31           C  
ATOM   1138  CE3 TRP A 150       0.104  25.389  15.673  1.00 47.74           C  
ATOM   1139  CZ2 TRP A 150      -0.759  24.213  13.228  1.00 49.44           C  
ATOM   1140  CZ3 TRP A 150       1.004  24.752  14.797  1.00 48.88           C  
ATOM   1141  CH2 TRP A 150       0.565  24.178  13.597  1.00 48.25           C  
ATOM   1142  N   VAL A 151       0.209  28.336  17.527  1.00 38.25           N  
ATOM   1143  CA  VAL A 151       1.612  28.584  17.228  1.00 37.22           C  
ATOM   1144  C   VAL A 151       2.497  27.650  18.003  1.00 37.01           C  
ATOM   1145  O   VAL A 151       2.385  27.567  19.224  1.00 37.18           O  
ATOM   1146  CB  VAL A 151       2.064  29.984  17.683  1.00 36.92           C  
ATOM   1147  CG1 VAL A 151       3.609  30.090  17.614  1.00 36.17           C  
ATOM   1148  CG2 VAL A 151       1.374  31.052  16.887  1.00 37.01           C  
ATOM   1149  N   LYS A 152       3.411  26.983  17.306  1.00 37.00           N  
ATOM   1150  CA  LYS A 152       4.498  26.276  17.985  1.00 37.07           C  
ATOM   1151  C   LYS A 152       5.842  26.914  17.600  1.00 36.86           C  
ATOM   1152  O   LYS A 152       6.130  27.120  16.424  1.00 36.56           O  
ATOM   1153  CB  LYS A 152       4.462  24.764  17.671  1.00 37.12           C  
ATOM   1154  N   VAL A 153       6.626  27.265  18.610  1.00 37.55           N  
ATOM   1155  CA  VAL A 153       7.952  27.825  18.420  1.00 38.67           C  
ATOM   1156  C   VAL A 153       8.974  26.699  18.221  1.00 39.79           C  
ATOM   1157  O   VAL A 153       9.112  25.831  19.090  1.00 40.45           O  
ATOM   1158  CB  VAL A 153       8.383  28.679  19.647  1.00 38.52           C  
ATOM   1159  CG1 VAL A 153       9.857  29.052  19.544  1.00 38.07           C  
ATOM   1160  CG2 VAL A 153       7.497  29.925  19.786  1.00 37.74           C  
ATOM   1161  N   GLU A 154       9.687  26.708  17.090  1.00 40.04           N  
ATOM   1162  CA  GLU A 154      10.734  25.724  16.843  1.00 40.39           C  
ATOM   1163  C   GLU A 154      12.069  26.146  17.482  1.00 39.58           C  
ATOM   1164  O   GLU A 154      12.725  25.346  18.138  1.00 39.63           O  
ATOM   1165  CB  GLU A 154      10.906  25.461  15.339  1.00 40.95           C  
ATOM   1166  CG  GLU A 154       9.594  25.360  14.525  1.00 44.59           C  
ATOM   1167  CD  GLU A 154       8.715  24.132  14.863  1.00 51.27           C  
ATOM   1168  OE1 GLU A 154       9.167  23.234  15.624  1.00 52.36           O  
ATOM   1169  OE2 GLU A 154       7.557  24.071  14.356  1.00 52.58           O  
ATOM   1170  N   GLY A 155      12.483  27.394  17.293  1.00 38.48           N  
ATOM   1171  CA  GLY A 155      13.721  27.866  17.929  1.00 37.24           C  
ATOM   1172  C   GLY A 155      14.311  29.122  17.304  1.00 36.18           C  
ATOM   1173  O   GLY A 155      13.750  29.666  16.353  1.00 36.76           O  
ATOM   1174  N   TRP A 156      15.439  29.571  17.847  1.00 34.89           N  
ATOM   1175  CA  TRP A 156      16.155  30.742  17.367  1.00 34.38           C  
ATOM   1176  C   TRP A 156      17.174  30.356  16.302  1.00 34.36           C  
ATOM   1177  O   TRP A 156      17.674  29.239  16.305  1.00 35.16           O  
ATOM   1178  CB  TRP A 156      16.906  31.397  18.520  1.00 33.47           C  
ATOM   1179  CG  TRP A 156      16.018  31.843  19.632  1.00 33.27           C  
ATOM   1180  CD1 TRP A 156      15.803  31.203  20.822  1.00 33.92           C  
ATOM   1181  CD2 TRP A 156      15.201  33.031  19.662  1.00 30.60           C  
ATOM   1182  NE1 TRP A 156      14.910  31.924  21.596  1.00 32.30           N  
ATOM   1183  CE2 TRP A 156      14.523  33.044  20.909  1.00 31.40           C  
ATOM   1184  CE3 TRP A 156      14.973  34.070  18.760  1.00 31.26           C  
ATOM   1185  CZ2 TRP A 156      13.630  34.062  21.273  1.00 30.75           C  
ATOM   1186  CZ3 TRP A 156      14.095  35.104  19.135  1.00 32.01           C  
ATOM   1187  CH2 TRP A 156      13.444  35.090  20.380  1.00 29.67           C  
ATOM   1188  N   ASP A 157      17.469  31.272  15.386  1.00 33.86           N  
ATOM   1189  CA  ASP A 157      18.577  31.106  14.437  1.00 32.34           C  
ATOM   1190  C   ASP A 157      19.263  32.457  14.275  1.00 31.51           C  
ATOM   1191  O   ASP A 157      18.729  33.478  14.724  1.00 31.36           O  
ATOM   1192  CB  ASP A 157      18.063  30.581  13.096  1.00 32.87           C  
ATOM   1193  CG  ASP A 157      19.050  29.623  12.430  1.00 33.29           C  
ATOM   1194  OD1 ASP A 157      20.267  29.756  12.646  1.00 34.65           O  
ATOM   1195  OD2 ASP A 157      18.612  28.741  11.682  1.00 34.01           O  
ATOM   1196  N   GLY A 158      20.444  32.474  13.656  1.00 29.77           N  
ATOM   1197  CA  GLY A 158      21.324  33.641  13.683  1.00 27.83           C  
ATOM   1198  C   GLY A 158      21.263  34.514  12.449  1.00 27.09           C  
ATOM   1199  O   GLY A 158      20.326  34.406  11.659  1.00 26.51           O  
ATOM   1200  N   ILE A 159      22.272  35.374  12.288  1.00 26.02           N  
ATOM   1201  CA  ILE A 159      22.293  36.402  11.250  1.00 26.35           C  
ATOM   1202  C   ILE A 159      22.280  35.847   9.827  1.00 26.41           C  
ATOM   1203  O   ILE A 159      21.581  36.376   8.946  1.00 25.21           O  
ATOM   1204  CB  ILE A 159      23.504  37.366  11.418  1.00 26.70           C  
ATOM   1205  CG1 ILE A 159      23.361  38.233  12.685  1.00 28.08           C  
ATOM   1206  CG2 ILE A 159      23.650  38.301  10.246  1.00 26.01           C  
ATOM   1207  CD1 ILE A 159      24.668  39.003  13.012  1.00 28.81           C  
ATOM   1208  N   ASP A 160      23.038  34.772   9.597  1.00 26.15           N  
ATOM   1209  CA  ASP A 160      23.112  34.177   8.249  1.00 25.96           C  
ATOM   1210  C   ASP A 160      21.756  33.642   7.817  1.00 24.88           C  
ATOM   1211  O   ASP A 160      21.374  33.777   6.665  1.00 24.73           O  
ATOM   1212  CB  ASP A 160      24.116  33.010   8.205  1.00 26.67           C  
ATOM   1213  CG  ASP A 160      25.541  33.433   8.520  1.00 29.50           C  
ATOM   1214  OD1 ASP A 160      25.934  34.574   8.239  1.00 30.48           O  
ATOM   1215  OD2 ASP A 160      26.293  32.584   9.050  1.00 35.45           O  
ATOM   1216  N   ALA A 161      21.032  32.999   8.728  1.00 23.99           N  
ATOM   1217  CA  ALA A 161      19.680  32.532   8.392  1.00 23.50           C  
ATOM   1218  C   ALA A 161      18.751  33.702   8.082  1.00 23.21           C  
ATOM   1219  O   ALA A 161      17.935  33.606   7.165  1.00 24.21           O  
ATOM   1220  CB  ALA A 161      19.115  31.701   9.495  1.00 23.26           C  
ATOM   1221  N   ALA A 162      18.894  34.805   8.824  1.00 23.21           N  
ATOM   1222  CA  ALA A 162      18.103  36.027   8.571  1.00 23.79           C  
ATOM   1223  C   ALA A 162      18.362  36.572   7.170  1.00 23.81           C  
ATOM   1224  O   ALA A 162      17.440  36.955   6.439  1.00 23.83           O  
ATOM   1225  CB  ALA A 162      18.394  37.118   9.643  1.00 22.09           C  
ATOM   1226  N   HIS A 163      19.642  36.604   6.796  1.00 24.63           N  
ATOM   1227  CA  HIS A 163      20.029  37.073   5.475  1.00 24.48           C  
ATOM   1228  C   HIS A 163      19.483  36.211   4.326  1.00 24.40           C  
ATOM   1229  O   HIS A 163      19.062  36.754   3.319  1.00 24.93           O  
ATOM   1230  CB  HIS A 163      21.542  37.247   5.411  1.00 24.71           C  
ATOM   1231  CG  HIS A 163      22.027  38.433   6.186  1.00 24.48           C  
ATOM   1232  ND1 HIS A 163      23.346  38.602   6.556  1.00 25.05           N  
ATOM   1233  CD2 HIS A 163      21.361  39.517   6.658  1.00 24.82           C  
ATOM   1234  CE1 HIS A 163      23.478  39.748   7.207  1.00 26.44           C  
ATOM   1235  NE2 HIS A 163      22.286  40.321   7.286  1.00 25.55           N  
ATOM   1236  N   LYS A 164      19.483  34.885   4.485  1.00 24.88           N  
ATOM   1237  CA  LYS A 164      18.856  33.977   3.518  1.00 26.27           C  
ATOM   1238  C   LYS A 164      17.384  34.322   3.344  1.00 25.61           C  
ATOM   1239  O   LYS A 164      16.892  34.453   2.231  1.00 25.21           O  
ATOM   1240  CB  LYS A 164      18.864  32.524   4.009  1.00 25.32           C  
ATOM   1241  CG  LYS A 164      20.048  31.657   3.721  1.00 30.29           C  
ATOM   1242  CD  LYS A 164      19.613  30.121   3.720  1.00 34.26           C  
ATOM   1243  CE  LYS A 164      18.052  29.873   3.503  1.00 36.52           C  
ATOM   1244  NZ  LYS A 164      17.403  29.714   2.102  1.00 34.41           N  
ATOM   1245  N   GLU A 165      16.667  34.392   4.472  1.00 25.78           N  
ATOM   1246  CA  GLU A 165      15.244  34.755   4.441  1.00 25.93           C  
ATOM   1247  C   GLU A 165      15.002  36.070   3.666  1.00 25.03           C  
ATOM   1248  O   GLU A 165      14.080  36.172   2.864  1.00 25.31           O  
ATOM   1249  CB  GLU A 165      14.664  34.826   5.886  1.00 26.24           C  
ATOM   1250  CG  GLU A 165      13.251  35.378   5.967  1.00 28.43           C  
ATOM   1251  CD  GLU A 165      12.136  34.349   5.679  1.00 34.26           C  
ATOM   1252  OE1 GLU A 165      12.441  33.135   5.549  1.00 30.46           O  
ATOM   1253  OE2 GLU A 165      10.938  34.777   5.629  1.00 38.23           O  
ATOM   1254  N   ILE A 166      15.831  37.076   3.918  1.00 25.30           N  
ATOM   1255  CA  ILE A 166      15.736  38.343   3.199  1.00 25.03           C  
ATOM   1256  C   ILE A 166      16.037  38.168   1.671  1.00 26.31           C  
ATOM   1257  O   ILE A 166      15.225  38.577   0.837  1.00 25.19           O  
ATOM   1258  CB  ILE A 166      16.663  39.415   3.819  1.00 24.79           C  
ATOM   1259  CG1 ILE A 166      16.224  39.786   5.264  1.00 23.32           C  
ATOM   1260  CG2 ILE A 166      16.705  40.658   2.942  1.00 23.43           C  
ATOM   1261  CD1 ILE A 166      17.231  40.715   6.023  1.00 17.43           C  
ATOM   1262  N   THR A 167      17.178  37.556   1.314  1.00 26.73           N  
ATOM   1263  CA  THR A 167      17.499  37.327  -0.131  1.00 27.90           C  
ATOM   1264  C   THR A 167      16.388  36.528  -0.853  1.00 27.76           C  
ATOM   1265  O   THR A 167      15.948  36.919  -1.928  1.00 27.97           O  
ATOM   1266  CB  THR A 167      18.896  36.655  -0.343  1.00 27.77           C  
ATOM   1267  OG1 THR A 167      19.912  37.462   0.265  1.00 29.19           O  
ATOM   1268  CG2 THR A 167      19.220  36.514  -1.852  1.00 28.06           C  
ATOM   1269  N   ASP A 168      15.910  35.440  -0.241  1.00 28.23           N  
ATOM   1270  CA  ASP A 168      14.773  34.697  -0.801  1.00 29.21           C  
ATOM   1271  C   ASP A 168      13.567  35.601  -1.013  1.00 29.51           C  
ATOM   1272  O   ASP A 168      12.931  35.580  -2.066  1.00 29.99           O  
ATOM   1273  CB  ASP A 168      14.390  33.492   0.087  1.00 29.78           C  
ATOM   1274  CG  ASP A 168      15.502  32.434   0.167  1.00 30.95           C  
ATOM   1275  OD1 ASP A 168      16.467  32.528  -0.605  1.00 30.65           O  
ATOM   1276  OD2 ASP A 168      15.430  31.526   1.015  1.00 33.38           O  
ATOM   1277  N   GLY A 169      13.244  36.407  -0.004  1.00 29.89           N  
ATOM   1278  CA  GLY A 169      12.060  37.272  -0.081  1.00 29.50           C  
ATOM   1279  C   GLY A 169      12.136  38.287  -1.199  1.00 29.28           C  
ATOM   1280  O   GLY A 169      11.170  38.520  -1.900  1.00 27.96           O  
ATOM   1281  N   VAL A 170      13.285  38.927  -1.335  1.00 29.71           N  
ATOM   1282  CA  VAL A 170      13.504  39.857  -2.440  1.00 31.10           C  
ATOM   1283  C   VAL A 170      13.337  39.173  -3.832  1.00 33.09           C  
ATOM   1284  O   VAL A 170      12.599  39.672  -4.699  1.00 33.41           O  
ATOM   1285  CB  VAL A 170      14.887  40.574  -2.309  1.00 30.44           C  
ATOM   1286  CG1 VAL A 170      15.188  41.389  -3.551  1.00 29.32           C  
ATOM   1287  CG2 VAL A 170      14.898  41.459  -1.071  1.00 29.13           C  
ATOM   1288  N   ALA A 171      14.016  38.036  -4.018  1.00 34.61           N  
ATOM   1289  CA  ALA A 171      13.922  37.243  -5.237  1.00 36.15           C  
ATOM   1290  C   ALA A 171      12.473  36.854  -5.526  1.00 37.93           C  
ATOM   1291  O   ALA A 171      11.950  37.182  -6.592  1.00 38.85           O  
ATOM   1292  CB  ALA A 171      14.792  35.993  -5.116  1.00 35.84           C  
ATOM   1293  N   ASN A 172      11.819  36.168  -4.583  1.00 38.94           N  
ATOM   1294  CA  ASN A 172      10.408  35.776  -4.743  1.00 40.34           C  
ATOM   1295  C   ASN A 172       9.461  36.914  -5.139  1.00 40.57           C  
ATOM   1296  O   ASN A 172       8.516  36.702  -5.886  1.00 40.25           O  
ATOM   1297  CB  ASN A 172       9.869  35.131  -3.470  1.00 40.63           C  
ATOM   1298  CG  ASN A 172      10.583  33.848  -3.112  1.00 44.22           C  
ATOM   1299  OD1 ASN A 172      11.398  33.318  -3.886  1.00 46.04           O  
ATOM   1300  ND2 ASN A 172      10.284  33.332  -1.914  1.00 48.20           N  
ATOM   1301  N   PHE A 173       9.695  38.113  -4.617  1.00 41.30           N  
ATOM   1302  CA  PHE A 173       8.810  39.231  -4.915  1.00 42.45           C  
ATOM   1303  C   PHE A 173       8.895  39.652  -6.391  1.00 44.05           C  
ATOM   1304  O   PHE A 173       7.898  40.045  -6.998  1.00 43.32           O  
ATOM   1305  CB  PHE A 173       9.118  40.424  -4.012  1.00 41.78           C  
ATOM   1306  CG  PHE A 173       8.245  41.622  -4.272  1.00 39.79           C  
ATOM   1307  CD1 PHE A 173       6.955  41.682  -3.765  1.00 39.49           C  
ATOM   1308  CD2 PHE A 173       8.711  42.689  -5.021  1.00 37.99           C  
ATOM   1309  CE1 PHE A 173       6.150  42.795  -4.005  1.00 38.53           C  
ATOM   1310  CE2 PHE A 173       7.911  43.802  -5.262  1.00 36.13           C  
ATOM   1311  CZ  PHE A 173       6.631  43.850  -4.757  1.00 37.09           C  
ATOM   1312  N   LYS A 174      10.098  39.581  -6.955  1.00 46.01           N  
ATOM   1313  CA  LYS A 174      10.321  39.983  -8.344  1.00 48.08           C  
ATOM   1314  C   LYS A 174       9.802  38.906  -9.300  1.00 49.84           C  
ATOM   1315  O   LYS A 174       9.753  39.095 -10.511  1.00 50.31           O  
ATOM   1316  CB  LYS A 174      11.802  40.337  -8.564  1.00 47.73           C  
ATOM   1317  CG  LYS A 174      12.190  41.554  -7.729  1.00 46.64           C  
ATOM   1318  CD  LYS A 174      13.657  41.609  -7.418  1.00 45.19           C  
ATOM   1319  CE  LYS A 174      14.379  42.456  -8.444  1.00 45.69           C  
ATOM   1320  NZ  LYS A 174      15.857  42.279  -8.351  1.00 44.08           N  
ATOM   1321  N   LYS A 175       9.382  37.788  -8.715  1.00 52.11           N  
ATOM   1322  CA  LYS A 175       8.602  36.759  -9.396  1.00 54.14           C  
ATOM   1323  C   LYS A 175       9.423  35.473  -9.415  1.00 54.68           C  
ATOM   1324  O   LYS A 175       9.136  34.467  -8.751  1.00 55.07           O  
ATOM   1325  CB  LYS A 175       8.214  37.214 -10.809  1.00 54.60           C  
ATOM   1326  CG  LYS A 175       6.957  36.545 -11.369  1.00 57.59           C  
ATOM   1327  CD  LYS A 175       6.501  37.199 -12.700  1.00 61.87           C  
ATOM   1328  CE  LYS A 175       7.706  37.673 -13.531  1.00 63.51           C  
ATOM   1329  NZ  LYS A 175       8.861  36.709 -13.496  1.00 63.20           N  
ATOM   1330  OXT LYS A 175      10.451  35.432 -10.086  1.00 55.71           O  
TER    1331      LYS A 175                                                      
HETATM 1332  K     K A 176      24.990  43.276   0.005  0.50 24.45           K  
HETATM 1333 NA    NA A 177       1.633  34.181  11.897  1.00 26.73          NA  
HETATM 1334 NA    NA A 178       6.489  35.143   8.444  1.00 30.89          NA  
HETATM 1335  P1  POP A 179       1.233  37.542  11.212  1.00 32.68           P  
HETATM 1336  O1  POP A 179       1.910  38.831  11.612  1.00 32.62           O  
HETATM 1337  O2  POP A 179       1.288  37.475   9.712  1.00 33.46           O  
HETATM 1338  O3  POP A 179       1.948  36.362  11.841  1.00 30.47           O  
HETATM 1339  O   POP A 179      -0.339  37.641  11.573  1.00 33.48           O  
HETATM 1340  P2  POP A 179      -1.193  36.552  12.370  1.00 36.05           P  
HETATM 1341  O4  POP A 179      -2.611  36.792  11.954  1.00 33.39           O  
HETATM 1342  O5  POP A 179      -1.079  36.873  13.870  1.00 33.69           O  
HETATM 1343  O6  POP A 179      -0.735  35.128  12.124  1.00 33.11           O  
HETATM 1344  O1  PG4 A 180      25.225  36.156   6.596  1.00 42.63           O  
HETATM 1345  C1  PG4 A 180      25.070  35.591   5.302  1.00 44.20           C  
HETATM 1346  C2  PG4 A 180      25.728  36.597   4.386  1.00 46.03           C  
HETATM 1347  O2  PG4 A 180      24.774  36.857   3.380  1.00 48.37           O  
HETATM 1348  C3  PG4 A 180      25.201  37.981   2.614  1.00 47.94           C  
HETATM 1349  C4  PG4 A 180      25.268  39.174   3.548  1.00 46.48           C  
HETATM 1350  O3  PG4 A 180      26.617  39.507   3.811  1.00 45.59           O  
HETATM 1351  C5  PG4 A 180      26.819  40.888   3.597  1.00 45.33           C  
HETATM 1352  C6  PG4 A 180      28.266  41.161   3.954  1.00 47.26           C  
HETATM 1353  O4  PG4 A 180      28.982  41.378   2.738  1.00 48.16           O  
HETATM 1354  C7  PG4 A 180      30.163  40.616   2.604  1.00 47.41           C  
HETATM 1355  C8  PG4 A 180      31.331  41.437   3.117  1.00 51.14           C  
HETATM 1356  O5  PG4 A 180      32.081  40.607   4.011  1.00 53.41           O  
HETATM 1357  C1  PEG A 181      13.856  28.176  23.722  1.00 59.47           C  
HETATM 1358  O1  PEG A 181      14.416  29.487  23.735  1.00 59.79           O  
HETATM 1359  C2  PEG A 181      13.605  27.741  22.291  1.00 59.20           C  
HETATM 1360  O2  PEG A 181      12.908  26.499  22.379  1.00 59.79           O  
HETATM 1361  C3  PEG A 181      11.848  26.393  21.440  1.00 59.65           C  
HETATM 1362  C4  PEG A 181      10.883  25.309  21.906  1.00 59.90           C  
HETATM 1363  O4  PEG A 181      10.045  25.835  22.942  1.00 58.85           O  
HETATM 1364  C1  PEG A 182      19.721  56.811   7.363  1.00 56.17           C  
HETATM 1365  O1  PEG A 182      18.409  56.724   7.966  1.00 55.97           O  
HETATM 1366  C2  PEG A 182      20.835  56.288   8.271  1.00 54.49           C  
HETATM 1367  O2  PEG A 182      21.824  57.291   8.516  1.00 56.31           O  
HETATM 1368  C3  PEG A 182      23.176  56.838   8.332  1.00 57.82           C  
HETATM 1369  C4  PEG A 182      23.815  57.479   7.094  1.00 58.58           C  
HETATM 1370  O4  PEG A 182      24.621  56.536   6.357  1.00 59.04           O  
HETATM 1371  O   HOH A 183      -6.268  35.297  21.123  1.00 22.39           O  
HETATM 1372  O   HOH A 184      18.291  50.223   3.964  1.00 24.68           O  
HETATM 1373  O   HOH A 185      22.029  42.728   8.623  1.00 20.47           O  
HETATM 1374  O   HOH A 186      15.767  55.114   9.164  1.00 20.81           O  
HETATM 1375  O   HOH A 187       0.754  45.724  20.847  1.00 21.83           O  
HETATM 1376  O   HOH A 188      11.338  47.709  21.125  1.00 19.21           O  
HETATM 1377  O   HOH A 189      19.695  33.152  21.711  1.00 38.29           O  
HETATM 1378  O   HOH A 190      10.491  50.293  22.101  1.00 18.65           O  
HETATM 1379  O   HOH A 191       4.344  42.176   9.606  1.00 23.68           O  
HETATM 1380  O   HOH A 192      22.154  49.578  16.234  1.00 24.18           O  
HETATM 1381  O   HOH A 193      19.540  33.045   0.367  0.50 15.02           O  
HETATM 1382  O   HOH A 194      -0.281  31.958  19.977  1.00 27.04           O  
HETATM 1383  O   HOH A 195       0.714  43.186  11.724  1.00 31.86           O  
HETATM 1384  O   HOH A 196       3.567  51.947  22.586  1.00 23.51           O  
HETATM 1385  O   HOH A 197      -1.180  48.644  17.742  1.00 15.53           O  
HETATM 1386  O   HOH A 198       1.948  54.836  16.377  1.00 21.93           O  
HETATM 1387  O   HOH A 199       2.509  44.733  28.229  1.00 21.51           O  
HETATM 1388  O   HOH A 200       2.391  38.378  14.597  1.00 23.11           O  
HETATM 1389  O   HOH A 201       1.535  33.854  14.371  1.00 27.83           O  
HETATM 1390  O   HOH A 202      -6.330  29.284  19.591  1.00 32.67           O  
HETATM 1391  O   HOH A 203      -2.980  54.585   7.752  1.00 25.04           O  
HETATM 1392  O   HOH A 204      -1.529  52.313  21.859  1.00 28.95           O  
HETATM 1393  O   HOH A 205      -4.219  37.228  18.172  1.00 29.05           O  
HETATM 1394  O   HOH A 206      -9.725  38.390  17.936  1.00 25.82           O  
HETATM 1395  O   HOH A 207      -0.251  50.231  15.527  1.00 41.88           O  
HETATM 1396  O   HOH A 208      -7.548  43.260  22.219  1.00 19.57           O  
HETATM 1397  O   HOH A 209      24.427  35.212  14.096  1.00 31.41           O  
HETATM 1398  O   HOH A 210      17.913  38.657  31.156  1.00 36.76           O  
HETATM 1399  O   HOH A 211      23.606  42.865  12.451  1.00 25.35           O  
HETATM 1400  O   HOH A 212     -10.993  36.660  20.173  1.00 34.07           O  
HETATM 1401  O   HOH A 213      12.726  35.081  31.604  1.00 41.53           O  
HETATM 1402  O   HOH A 214      11.555  34.813   2.535  1.00 32.40           O  
HETATM 1403  O   HOH A 215      26.985  45.074  13.907  1.00 33.93           O  
HETATM 1404  O   HOH A 216      22.305  31.774  11.176  1.00 27.99           O  
HETATM 1405  O   HOH A 217      -5.311  51.156  18.105  1.00 23.06           O  
HETATM 1406  O   HOH A 218       4.813  38.197  26.560  1.00 30.39           O  
HETATM 1407  O   HOH A 219      16.429  31.381   6.556  1.00 31.04           O  
HETATM 1408  O   HOH A 220       2.094  31.244   8.621  1.00 39.67           O  
HETATM 1409  O   HOH A 221       3.282  37.464   7.811  1.00 36.79           O  
HETATM 1410  O   HOH A 222      12.081  42.928  -4.465  1.00 35.63           O  
HETATM 1411  O   HOH A 223      10.457  52.853  26.328  1.00 29.83           O  
HETATM 1412  O   HOH A 224     -10.834  37.817  15.537  1.00 32.13           O  
HETATM 1413  O   HOH A 225      11.844  46.500  23.826  1.00 35.48           O  
HETATM 1414  O   HOH A 226       4.136  40.856   6.472  1.00 40.41           O  
HETATM 1415  O   HOH A 227      27.046  47.404  15.617  1.00 32.79           O  
HETATM 1416  O   HOH A 228      27.357  54.793   8.601  1.00 45.22           O  
HETATM 1417  O   HOH A 229      23.653  47.745  22.742  1.00 50.33           O  
HETATM 1418  O   HOH A 230      13.464  46.940  -3.502  1.00 32.04           O  
HETATM 1419  O   HOH A 231       3.976  32.286  14.525  1.00 31.56           O  
HETATM 1420  O   HOH A 232      20.596  34.827  26.319  1.00 49.91           O  
HETATM 1421  O   HOH A 233       0.268  53.053  17.314  1.00 42.31           O  
HETATM 1422  O   HOH A 234       8.635  54.732  26.919  1.00 33.52           O  
HETATM 1423  O   HOH A 235       8.723  45.643  25.830  1.00 31.33           O  
HETATM 1424  O   HOH A 236       9.525  50.219  24.646  1.00 32.19           O  
HETATM 1425  O   HOH A 237      29.165  40.813  21.487  1.00 56.55           O  
HETATM 1426  O   HOH A 238       2.494  40.055   8.917  1.00 36.15           O  
HETATM 1427  O   HOH A 239      -0.777  34.809   9.090  1.00 37.11           O  
HETATM 1428  O   HOH A 240      23.455  48.536   9.084  1.00 28.44           O  
HETATM 1429  O   HOH A 241      24.600  49.610  11.229  1.00 23.81           O  
HETATM 1430  O   HOH A 242      21.015  49.121   7.957  1.00 22.66           O  
HETATM 1431  O   HOH A 243      24.242  43.201   9.915  1.00 27.87           O  
HETATM 1432  O   HOH A 244      26.271  42.655  13.711  1.00 28.13           O  
HETATM 1433  O   HOH A 245       5.960  36.600   6.289  1.00 41.50           O  
HETATM 1434  O   HOH A 246      18.246  32.111  23.785  1.00 56.31           O  
HETATM 1435  O   HOH A 247       7.627  32.876   7.134  1.00 33.79           O  
HETATM 1436  O   HOH A 248       1.165  51.316  -0.972  1.00 46.31           O  
HETATM 1437  O   HOH A 249       1.154  41.748  26.990  1.00 28.03           O  
HETATM 1438  O   HOH A 250       5.939  26.535  21.149  1.00 44.12           O  
HETATM 1439  O   HOH A 251      -5.540  43.055  28.186  1.00 26.47           O  
HETATM 1440  O   HOH A 252      11.949  30.493  27.231  1.00 52.78           O  
HETATM 1441  O   HOH A 253      13.331  24.495  13.440  1.00 52.00           O  
HETATM 1442  O   HOH A 254      -1.435  29.723  20.052  1.00 52.22           O  
HETATM 1443  O   HOH A 255       2.115  43.165   6.250  1.00 34.91           O  
HETATM 1444  O   HOH A 256      15.992  53.085   0.933  1.00 34.04           O  
HETATM 1445  O   HOH A 257       2.292  33.719   9.368  1.00 44.24           O  
HETATM 1446  O   HOH A 258       3.626  29.350  26.403  1.00 42.97           O  
HETATM 1447  O   HOH A 259      -3.063  50.429  19.160  1.00 33.64           O  
HETATM 1448  O   HOH A 260      -4.016  34.810  12.023  1.00 43.84           O  
HETATM 1449  O   HOH A 261      -7.025  43.005   7.425  1.00 50.38           O  
HETATM 1450  O   HOH A 262      20.664  37.966  29.449  1.00 39.40           O  
HETATM 1451  O   HOH A 263       8.219  36.489   7.242  1.00 45.22           O  
HETATM 1452  O   HOH A 264       7.603  30.314  26.808  1.00 49.95           O  
HETATM 1453  O   HOH A 265      27.192  38.462  19.035  1.00 38.71           O  
HETATM 1454  O   HOH A 266      -3.725  41.084  29.707  1.00 44.44           O  
HETATM 1455  O   HOH A 267      -3.184  38.130   9.900  1.00 31.98           O  
HETATM 1456  O   HOH A 268      -6.968  37.923  11.495  1.00 40.84           O  
HETATM 1457  O   HOH A 269      15.958  47.852  -2.923  1.00 44.94           O  
HETATM 1458  O   HOH A 270      13.106  37.129  -9.048  1.00 35.12           O  
HETATM 1459  O   HOH A 271      23.944  34.080  16.627  1.00 56.20           O  
HETATM 1460  O   HOH A 272      17.584  52.420  -1.888  1.00 38.11           O  
HETATM 1461  O   HOH A 273       5.521  45.450  -0.564  1.00 47.04           O  
HETATM 1462  O   HOH A 274      25.459  49.006   4.506  1.00 54.02           O  
HETATM 1463  O   HOH A 275      16.595  27.943  19.928  1.00 49.01           O  
HETATM 1464  O   HOH A 276      22.019  36.726  26.870  1.00 56.59           O  
HETATM 1465  O   HOH A 277      10.474  36.654   8.412  1.00 45.47           O  
HETATM 1466  O   HOH A 278      24.611  33.020  11.703  1.00 47.62           O  
HETATM 1467  O   HOH A 279      26.899  46.740   4.551  1.00 52.92           O  
HETATM 1468  O   HOH A 280       6.994  29.354  29.500  1.00 59.06           O  
HETATM 1469  O   HOH A 281       1.016  41.471   9.152  1.00 46.63           O  
HETATM 1470  O   HOH A 282      -3.738  28.411  20.723  1.00 58.68           O  
HETATM 1471  O   HOH A 283      14.325  31.639   5.778  1.00 49.26           O  
HETATM 1472  O   HOH A 284      27.777  37.727   7.983  1.00 49.01           O  
HETATM 1473  O   HOH A 285      11.301  44.913  29.125  1.00 47.44           O  
HETATM 1474  O   HOH A 286      -3.722  51.289  27.893  1.00 28.88           O  
HETATM 1475  O   HOH A 287       5.173  46.827  -3.289  1.00 59.99           O  
HETATM 1476  O   HOH A 288      -9.268  38.914  11.481  1.00 39.62           O  
HETATM 1477  O   HOH A 289       9.346  31.934  27.060  1.00 45.27           O  
HETATM 1478  O   HOH A 290      24.327  46.350   8.439  1.00 39.23           O  
HETATM 1479  O   HOH A 291      17.766  26.234  14.240  1.00 58.80           O  
HETATM 1480  O   HOH A 292      14.667  53.897  27.017  1.00 44.45           O  
HETATM 1481  O   HOH A 293      13.540  30.919   2.872  1.00 48.68           O  
HETATM 1482  O   HOH A 294      13.812  54.578  29.178  1.00 37.62           O  
CONECT   70 1332                                                                
CONECT   75 1332                                                                
CONECT   94 1332                                                                
CONECT  535 1334                                                                
CONECT  734 1333                                                                
CONECT  767 1334                                                                
CONECT  768 1333                                                                
CONECT  772 1334                                                                
CONECT 1332   70   75   94                                                      
CONECT 1333  734  768 1338 1343                                                 
CONECT 1333 1389 1445                                                           
CONECT 1334  535  767  772 1433                                                 
CONECT 1334 1435 1451                                                           
CONECT 1335 1336 1337 1338 1339                                                 
CONECT 1336 1335                                                                
CONECT 1337 1335                                                                
CONECT 1338 1333 1335                                                           
CONECT 1339 1335 1340                                                           
CONECT 1340 1339 1341 1342 1343                                                 
CONECT 1341 1340                                                                
CONECT 1342 1340                                                                
CONECT 1343 1333 1340                                                           
CONECT 1344 1345                                                                
CONECT 1345 1344 1346                                                           
CONECT 1346 1345 1347                                                           
CONECT 1347 1346 1348                                                           
CONECT 1348 1347 1349                                                           
CONECT 1349 1348 1350                                                           
CONECT 1350 1349 1351                                                           
CONECT 1351 1350 1352                                                           
CONECT 1352 1351 1353                                                           
CONECT 1353 1352 1354                                                           
CONECT 1354 1353 1355                                                           
CONECT 1355 1354 1356                                                           
CONECT 1356 1355                                                                
CONECT 1357 1358 1359                                                           
CONECT 1358 1357                                                                
CONECT 1359 1357 1360                                                           
CONECT 1360 1359 1361                                                           
CONECT 1361 1360 1362                                                           
CONECT 1362 1361 1363                                                           
CONECT 1363 1362                                                                
CONECT 1364 1365 1366                                                           
CONECT 1365 1364                                                                
CONECT 1366 1364 1367                                                           
CONECT 1367 1366 1368                                                           
CONECT 1368 1367 1369                                                           
CONECT 1369 1368 1370                                                           
CONECT 1370 1369                                                                
CONECT 1389 1333                                                                
CONECT 1433 1334                                                                
CONECT 1435 1334                                                                
CONECT 1445 1333                                                                
CONECT 1451 1334                                                                
MASTER      470    0    7    5    9    0   13    6 1481    1   54   16          
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.