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***  OXIDOREDUCTASE 26-AUG-10 2XPE  ***

elNémo ID: 20012116271243251

Job options:

ID        	=	 20012116271243251
JOBID     	=	 OXIDOREDUCTASE 26-AUG-10 2XPE
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    OXIDOREDUCTASE                          26-AUG-10   2XPE              
TITLE     OXIDISED THIOL PEROXIDASE (TPX) FROM YERSINIA PSEUDOTUBERCULOSIS      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THIOL PEROXIDASE;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.11.1.-;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: YERSINIA PSEUDOTUBERCULOSIS;                    
SOURCE   3 ORGANISM_TAXID: 502800;                                              
SOURCE   4 STRAIN: YPIII;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-151                                   
KEYWDS    OXIDOREDUCTASE, PEROXIREDOXIN, THIOREDOXIN-FOLD, ROS PROTECTION       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.GABRIELSEN,C.E.ZETTERSTROM,D.WANG,M.ELOFSSON,A.J.ROE                
REVDAT   3   10-OCT-12 2XPE    1       JRNL                                     
REVDAT   2   31-AUG-11 2XPE    1       REMARK                                   
REVDAT   1   10-AUG-11 2XPE    0                                                
JRNL        AUTH   M.GABRIELSEN,K.S.BECKHAM,V.A.FEHER,C.E.ZETTERSTROM,D.WANG,   
JRNL        AUTH 2 S.MULLER,M.ELOFSSON,R.E.AMARO,O.BYRON,A.J.ROE                
JRNL        TITL   STRUCTURAL CHARACTERISATION OF TPX FROM YERSINIA             
JRNL        TITL 2 PSEUDOTUBERCULOSIS REVEALS INSIGHTS INTO THE BINDING OF      
JRNL        TITL 3 SALICYLIDENE ACYLHYDRAZIDE COMPOUNDS.                        
JRNL        REF    PLOS ONE                      V.   7 32217 2012              
JRNL        REFN                   ISSN 1932-6203                               
JRNL        PMID   22384182                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0032217                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   D.WANG,C.E.ZETTERSTROM,M.GABRIELSEN,K.S.H.BECKHAM,           
REMARK   1  AUTH 2 J.J.TREE,S.E.MACDONALD,O.BYRON,T.J.MITCHELL,                 
REMARK   1  AUTH 3 D.L.GALLY,P.HERZYK,A.MAHAJAN,H.UVELL,R.BURCHMORE,            
REMARK   1  AUTH 4 B.O.SMITH,M.ELOFSSON,A.J.ROE                                 
REMARK   1  TITL   IDENTIFICATION OF BACTERIAL TARGET PROTEINS FOR              
REMARK   1  TITL 2 THE SALICYLIDENE ACYLHYDRAZIDE CLASS OF VIRULENCE-           
REMARK   1  TITL 3 BLOCKING COMPOUNDS.                                          
REMARK   1  REF    J.BIOL.CHEM.                  V. 286 29922 2011              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   21724850                                                     
REMARK   1  DOI    10.1074/JBC.M111.233858                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 52.118                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.5                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.738                         
REMARK   3   NUMBER OF REFLECTIONS             : 11814                          
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) : 0.301                           
REMARK   3   R VALUE            (WORKING SET) : 0.2989                          
REMARK   3   FREE R VALUE                     : 0.3358                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.73                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 558                             
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) : 2.5                          
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.565                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 814                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.369                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 50                           
REMARK   3   BIN FREE R VALUE                    : 0.525                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2362                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 27                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.4                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.880                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.948                                               
REMARK   3    B22 (A**2) : 4.954                                                
REMARK   3    B33 (A**2) : 2.994                                                
REMARK   3    B12 (A**2) : -0.000                                               
REMARK   3    B13 (A**2) : 0.000                                                
REMARK   3    B23 (A**2) : 0.000                                                
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.901         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.393         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0             
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0             
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.902                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.886                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2397 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3271 ; 0.920 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   328 ; 4.420 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    88 ;39.070 ;25.682       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   354 ;16.981 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;13.647 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   405 ; 0.054 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1795 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1021 ; 0.175 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1664 ; 0.294 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    99 ; 0.092 ; 0.200       
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):    25 ; 0.147 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.055 ; 0.200       
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):  1630 ; 0.229 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2598 ; 0.420 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   767 ; 0.309 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   673 ; 0.544 ; 4.500       
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 BULK SOLVENT                                    
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.400                                         
REMARK   3   ION PROBE RADIUS   : 0.800                                         
REMARK   3   SHRINKAGE RADIUS   : 0.8                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2XPE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-AUG-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-45175.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : SI (111) DOUBLE CRYSTAL            
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11830                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.50                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.27                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 13.54                              
REMARK 200  R MERGE                    (I) : 0.14                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.60                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.25                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.47                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.00                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1QXH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M TRI-POTASSIUM CITRATE, 20% PEG     
REMARK 280  3350, PH 7.5                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       28.18550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.69700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.72200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.69700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.18550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.72200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.2 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -32                                                      
REMARK 465     HIS A   -31                                                      
REMARK 465     HIS A   -30                                                      
REMARK 465     HIS A   -29                                                      
REMARK 465     HIS A   -28                                                      
REMARK 465     HIS A   -27                                                      
REMARK 465     HIS A   -26                                                      
REMARK 465     GLY A   -25                                                      
REMARK 465     LYS A   -24                                                      
REMARK 465     PRO A   -23                                                      
REMARK 465     ILE A   -22                                                      
REMARK 465     PRO A   -21                                                      
REMARK 465     ASN A   -20                                                      
REMARK 465     PRO A   -19                                                      
REMARK 465     LEU A   -18                                                      
REMARK 465     LEU A   -17                                                      
REMARK 465     GLY A   -16                                                      
REMARK 465     LEU A   -15                                                      
REMARK 465     ASP A   -14                                                      
REMARK 465     SER A   -13                                                      
REMARK 465     THR A   -12                                                      
REMARK 465     GLU A   -11                                                      
REMARK 465     ASN A   -10                                                      
REMARK 465     LEU A    -9                                                      
REMARK 465     TYR A    -8                                                      
REMARK 465     PHE A    -7                                                      
REMARK 465     GLN A    -6                                                      
REMARK 465     GLY A    -5                                                      
REMARK 465     ILE A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     PHE A    -1                                                      
REMARK 465     THR A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     MET B   -32                                                      
REMARK 465     HIS B   -31                                                      
REMARK 465     HIS B   -30                                                      
REMARK 465     HIS B   -29                                                      
REMARK 465     HIS B   -28                                                      
REMARK 465     HIS B   -27                                                      
REMARK 465     HIS B   -26                                                      
REMARK 465     GLY B   -25                                                      
REMARK 465     LYS B   -24                                                      
REMARK 465     PRO B   -23                                                      
REMARK 465     ILE B   -22                                                      
REMARK 465     PRO B   -21                                                      
REMARK 465     ASN B   -20                                                      
REMARK 465     PRO B   -19                                                      
REMARK 465     LEU B   -18                                                      
REMARK 465     LEU B   -17                                                      
REMARK 465     GLY B   -16                                                      
REMARK 465     LEU B   -15                                                      
REMARK 465     ASP B   -14                                                      
REMARK 465     SER B   -13                                                      
REMARK 465     THR B   -12                                                      
REMARK 465     GLU B   -11                                                      
REMARK 465     ASN B   -10                                                      
REMARK 465     LEU B    -9                                                      
REMARK 465     TYR B    -8                                                      
REMARK 465     PHE B    -7                                                      
REMARK 465     GLN B    -6                                                      
REMARK 465     GLY B    -5                                                      
REMARK 465     ILE B    -4                                                      
REMARK 465     ASP B    -3                                                      
REMARK 465     PRO B    -2                                                      
REMARK 465     PHE B    -1                                                      
REMARK 465     THR B     0                                                      
REMARK 465     MET B     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     GLN A   8    CG   CD   OE1  NE2                                  
REMARK 470     ILE A  21    CG1  CG2  CD1                                       
REMARK 470     LYS A  24    CG   CD   CE   NZ                                   
REMARK 470     ARG A  66    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  67    CB   CG   CD   CE   NZ                              
REMARK 470     GLU A  76    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 141    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 167    CG   CD   CE   NZ                                   
REMARK 470     LYS B  17    CD   CE   NZ                                        
REMARK 470     LYS B  26    CD   CE   NZ                                        
REMARK 470     LYS B  33    CG   CD   CE   NZ                                   
REMARK 470     ARG B  66    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  67    CG   CD   CE   NZ                                   
REMARK 470     GLN B  70    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  76    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  93    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     GLU B  98    CB   CG   CD   OE1  OE2                             
REMARK 470     LEU B 100    CB   CG   CD1  CD2                                  
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    GLN A   8      100.10    -35.45                                   
REMARK 500    ASN A  10      153.79    100.88                                   
REMARK 500    LYS A  26      108.79     82.78                                   
REMARK 500    ALA A  63      -29.82     65.93                                   
REMARK 500    LEU A 109      -66.32    -21.21                                   
REMARK 500    ASP B 142       -3.74     76.68                                   
REMARK 500    ASN B 158       94.96    -69.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2XPD   RELATED DB: PDB                                   
REMARK 900 REDUCED THIOL PEROXIDASE (TPX) FROM YERSINIA                         
REMARK 900 PSEUDOTUBERCULOSIS                                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE INCLUDES THE NON-CLEAVED HIS6-TAG AND THE TEV           
REMARK 999 PROTEASE RECOGNITION SITE.                                           
DBREF  2XPE A    1   167  UNP    Q66A71   Q66A71_YERPS     1    167             
DBREF  2XPE B    1   167  UNP    Q66A71   Q66A71_YERPS     1    167             
SEQADV 2XPE MET A  -32  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE HIS A  -31  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE HIS A  -30  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE HIS A  -29  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE HIS A  -28  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE HIS A  -27  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE HIS A  -26  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE GLY A  -25  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE LYS A  -24  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE PRO A  -23  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE ILE A  -22  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE PRO A  -21  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE ASN A  -20  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE PRO A  -19  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE LEU A  -18  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE LEU A  -17  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE GLY A  -16  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE LEU A  -15  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE ASP A  -14  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE SER A  -13  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE THR A  -12  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE GLU A  -11  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE ASN A  -10  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE LEU A   -9  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE TYR A   -8  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE PHE A   -7  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE GLN A   -6  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE GLY A   -5  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE ILE A   -4  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE ASP A   -3  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE PRO A   -2  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE PHE A   -1  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE THR A    0  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE MET B  -32  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE HIS B  -31  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE HIS B  -30  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE HIS B  -29  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE HIS B  -28  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE HIS B  -27  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE HIS B  -26  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE GLY B  -25  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE LYS B  -24  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE PRO B  -23  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE ILE B  -22  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE PRO B  -21  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE ASN B  -20  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE PRO B  -19  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE LEU B  -18  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE LEU B  -17  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE GLY B  -16  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE LEU B  -15  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE ASP B  -14  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE SER B  -13  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE THR B  -12  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE GLU B  -11  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE ASN B  -10  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE LEU B   -9  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE TYR B   -8  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE PHE B   -7  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE GLN B   -6  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE GLY B   -5  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE ILE B   -4  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE ASP B   -3  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE PRO B   -2  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE PHE B   -1  UNP  Q66A71              EXPRESSION TAG                 
SEQADV 2XPE THR B    0  UNP  Q66A71              EXPRESSION TAG                 
SEQRES   1 A  200  MET HIS HIS HIS HIS HIS HIS GLY LYS PRO ILE PRO ASN          
SEQRES   2 A  200  PRO LEU LEU GLY LEU ASP SER THR GLU ASN LEU TYR PHE          
SEQRES   3 A  200  GLN GLY ILE ASP PRO PHE THR MET THR GLN THR VAL HIS          
SEQRES   4 A  200  PHE GLN GLY ASN PRO VAL SER VAL ALA GLY LYS LEU PRO          
SEQRES   5 A  200  GLN ILE GLY ASP LYS ALA LYS ASP PHE THR LEU VAL ALA          
SEQRES   6 A  200  LYS ASP LEU SER ASP VAL ALA LEU SER SER PHE ALA GLY          
SEQRES   7 A  200  LYS ARG LYS VAL LEU ASN ILE PHE PRO SER ILE ASP THR          
SEQRES   8 A  200  GLY VAL CYS ALA ALA SER VAL ARG LYS PHE ASN GLN LEU          
SEQRES   9 A  200  ALA GLY GLU LEU GLU ASN THR VAL VAL LEU CYS ILE SER          
SEQRES  10 A  200  SER ASP LEU PRO PHE ALA GLN SER ARG PHE CYS GLY ALA          
SEQRES  11 A  200  GLU GLY LEU SER ASN VAL ILE THR LEU SER THR LEU ARG          
SEQRES  12 A  200  GLY ALA ASP PHE LYS GLN ALA TYR GLY VAL ALA ILE THR          
SEQRES  13 A  200  GLU GLY PRO LEU ALA GLY LEU THR ALA ARG ALA VAL VAL          
SEQRES  14 A  200  VAL LEU ASP GLY GLN ASP ASN VAL ILE TYR SER GLU LEU          
SEQRES  15 A  200  VAL ASN GLU ILE THR THR GLU PRO ASN TYR ASP ALA ALA          
SEQRES  16 A  200  LEU ALA ALA LEU LYS                                          
SEQRES   1 B  200  MET HIS HIS HIS HIS HIS HIS GLY LYS PRO ILE PRO ASN          
SEQRES   2 B  200  PRO LEU LEU GLY LEU ASP SER THR GLU ASN LEU TYR PHE          
SEQRES   3 B  200  GLN GLY ILE ASP PRO PHE THR MET THR GLN THR VAL HIS          
SEQRES   4 B  200  PHE GLN GLY ASN PRO VAL SER VAL ALA GLY LYS LEU PRO          
SEQRES   5 B  200  GLN ILE GLY ASP LYS ALA LYS ASP PHE THR LEU VAL ALA          
SEQRES   6 B  200  LYS ASP LEU SER ASP VAL ALA LEU SER SER PHE ALA GLY          
SEQRES   7 B  200  LYS ARG LYS VAL LEU ASN ILE PHE PRO SER ILE ASP THR          
SEQRES   8 B  200  GLY VAL CYS ALA ALA SER VAL ARG LYS PHE ASN GLN LEU          
SEQRES   9 B  200  ALA GLY GLU LEU GLU ASN THR VAL VAL LEU CYS ILE SER          
SEQRES  10 B  200  SER ASP LEU PRO PHE ALA GLN SER ARG PHE CYS GLY ALA          
SEQRES  11 B  200  GLU GLY LEU SER ASN VAL ILE THR LEU SER THR LEU ARG          
SEQRES  12 B  200  GLY ALA ASP PHE LYS GLN ALA TYR GLY VAL ALA ILE THR          
SEQRES  13 B  200  GLU GLY PRO LEU ALA GLY LEU THR ALA ARG ALA VAL VAL          
SEQRES  14 B  200  VAL LEU ASP GLY GLN ASP ASN VAL ILE TYR SER GLU LEU          
SEQRES  15 B  200  VAL ASN GLU ILE THR THR GLU PRO ASN TYR ASP ALA ALA          
SEQRES  16 B  200  LEU ALA ALA LEU LYS                                          
FORMUL   3  HOH   *27(H2 O)                                                     
HELIX    1   1 SER A   41  ALA A   44  5                                   4    
HELIX    2   2 ALA A   63  LEU A   75  1                                  13    
HELIX    3   3 GLY A  111  TYR A  118  1                                   8    
HELIX    4   4 GLU A  124  ALA A  128  5                                   5    
HELIX    5   5 ASN A  158  ALA A  165  1                                   8    
HELIX    6   6 SER B   41  ALA B   44  5                                   4    
HELIX    7   7 ALA B   62  LEU B   75  1                                  14    
HELIX    8   8 LEU B   87  SER B   92  1                                   6    
HELIX    9   9 ASP B  113  TYR B  118  1                                   6    
HELIX   10  10 GLU B  124  ALA B  128  5                                   5    
HELIX   11  11 ASN B  158  ALA B  165  1                                   8    
SHEET    1  AA 2 VAL A   5  HIS A   6  0                                        
SHEET    2  AA 2 PRO A  11  VAL A  12 -1  O  VAL A  12   N  VAL A   5           
SHEET    1  AB 2 VAL A  14  ALA A  15  0                                        
SHEET    2  AB 2 ALA A 121  ILE A 122 -1  O  ALA A 121   N  ALA A  15           
SHEET    1  AC 2 THR A  29  VAL A  31  0                                        
SHEET    2  AC 2 ASP A  37  ALA A  39 -1  O  VAL A  38   N  LEU A  30           
SHEET    1  AD 5 VAL A 103  SER A 107  0                                        
SHEET    2  AD 5 THR A  78  SER A  84  1  O  VAL A  80   N  ILE A 104           
SHEET    3  AD 5 ARG A  47  ILE A  52  1  O  ARG A  47   N  VAL A  79           
SHEET    4  AD 5 ALA A 134  LEU A 138 -1  O  ALA A 134   N  ILE A  52           
SHEET    5  AD 5 VAL A 144  LEU A 149 -1  N  ILE A 145   O  VAL A 137           
SHEET    1  BA 3 GLN B   3  PHE B   7  0                                        
SHEET    2  BA 3 ASN B  10  ALA B  15 -1  O  ASN B  10   N  PHE B   7           
SHEET    3  BA 3 ALA B 121  ILE B 122 -1  O  ALA B 121   N  ALA B  15           
SHEET    1  BB 2 THR B  29  VAL B  31  0                                        
SHEET    2  BB 2 ASP B  37  ALA B  39 -1  O  VAL B  38   N  LEU B  30           
SHEET    1  BC 5 VAL B 103  SER B 107  0                                        
SHEET    2  BC 5 THR B  78  SER B  84  1  O  VAL B  80   N  ILE B 104           
SHEET    3  BC 5 ARG B  47  ILE B  52  1  O  ARG B  47   N  VAL B  79           
SHEET    4  BC 5 ALA B 134  LEU B 138 -1  O  ALA B 134   N  ILE B  52           
SHEET    5  BC 5 VAL B 144  LEU B 149 -1  N  ILE B 145   O  VAL B 137           
SSBOND   1 CYS B   61    CYS B   95                          1555   1555  2.03  
CISPEP   1 GLN A    8    GLY A    9          0        -3.65                     
CISPEP   2 LEU B  166    LYS B  167          0         4.74                     
CRYST1   56.371   63.444   91.394  90.00  90.00  90.00 P 21 21 21    8          
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      0.017740  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015762  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010942        0.00000                         
ATOM      1  N   THR A   4     -10.241  -7.617  15.432  1.00 72.12           N  
ATOM      2  CA  THR A   4      -9.635  -8.042  14.137  1.00 72.11           C  
ATOM      3  C   THR A   4      -9.982  -7.064  13.012  1.00 72.12           C  
ATOM      4  O   THR A   4     -11.149  -6.910  12.644  1.00 72.22           O  
ATOM      5  CB  THR A   4     -10.064  -9.485  13.758  1.00 72.10           C  
ATOM      6  OG1 THR A   4      -9.586 -10.400  14.752  1.00 72.11           O  
ATOM      7  CG2 THR A   4      -9.502  -9.889  12.400  1.00 71.92           C  
ATOM      8  N   VAL A   5      -8.956  -6.406  12.480  1.00 72.10           N  
ATOM      9  CA  VAL A   5      -9.111  -5.477  11.358  1.00 72.12           C  
ATOM     10  C   VAL A   5      -8.790  -6.168  10.031  1.00 72.18           C  
ATOM     11  O   VAL A   5      -8.514  -7.369  10.003  1.00 72.17           O  
ATOM     12  CB  VAL A   5      -8.230  -4.207  11.522  1.00 72.04           C  
ATOM     13  CG1 VAL A   5      -8.694  -3.382  12.709  1.00 72.00           C  
ATOM     14  CG2 VAL A   5      -6.755  -4.575  11.659  1.00 72.09           C  
ATOM     15  N   HIS A   6      -8.837  -5.407   8.939  1.00 72.27           N  
ATOM     16  CA  HIS A   6      -8.538  -5.933   7.610  1.00 72.43           C  
ATOM     17  C   HIS A   6      -7.724  -4.934   6.791  1.00 72.49           C  
ATOM     18  O   HIS A   6      -8.027  -3.738   6.772  1.00 72.53           O  
ATOM     19  CB  HIS A   6      -9.828  -6.286   6.859  1.00 72.50           C  
ATOM     20  CG  HIS A   6     -10.722  -7.232   7.600  1.00 72.75           C  
ATOM     21  ND1 HIS A   6     -11.614  -6.813   8.564  1.00 72.98           N  
ATOM     22  CD2 HIS A   6     -10.861  -8.576   7.518  1.00 72.99           C  
ATOM     23  CE1 HIS A   6     -12.261  -7.859   9.046  1.00 73.09           C  
ATOM     24  NE2 HIS A   6     -11.824  -8.941   8.428  1.00 73.07           N  
ATOM     25  N   PHE A   7      -6.686  -5.436   6.125  1.00 72.56           N  
ATOM     26  CA  PHE A   7      -5.904  -4.645   5.176  1.00 72.59           C  
ATOM     27  C   PHE A   7      -5.847  -5.375   3.840  1.00 72.57           C  
ATOM     28  O   PHE A   7      -5.348  -6.500   3.766  1.00 72.53           O  
ATOM     29  CB  PHE A   7      -4.491  -4.371   5.710  1.00 72.62           C  
ATOM     30  CG  PHE A   7      -3.617  -3.596   4.755  1.00 72.68           C  
ATOM     31  CD1 PHE A   7      -3.789  -2.222   4.587  1.00 72.70           C  
ATOM     32  CD2 PHE A   7      -2.616  -4.239   4.030  1.00 72.72           C  
ATOM     33  CE1 PHE A   7      -2.982  -1.503   3.707  1.00 72.63           C  
ATOM     34  CE2 PHE A   7      -1.804  -3.529   3.147  1.00 72.73           C  
ATOM     35  CZ  PHE A   7      -1.988  -2.158   2.986  1.00 72.69           C  
ATOM     36  N   GLN A   8      -6.352  -4.712   2.800  1.00 72.56           N  
ATOM     37  CA  GLN A   8      -6.515  -5.284   1.458  1.00 72.50           C  
ATOM     38  C   GLN A   8      -5.409  -6.264   1.040  1.00 72.47           C  
ATOM     39  O   GLN A   8      -4.319  -5.844   0.645  1.00 72.57           O  
ATOM     40  CB  GLN A   8      -6.646  -4.162   0.421  1.00 72.51           C  
ATOM     41  N   GLY A   9      -5.676  -7.567   1.142  1.00 72.35           N  
ATOM     42  CA  GLY A   9      -6.922  -8.101   1.697  1.00 72.17           C  
ATOM     43  C   GLY A   9      -6.636  -9.128   2.781  1.00 72.06           C  
ATOM     44  O   GLY A   9      -5.503  -9.602   2.902  1.00 71.98           O  
ATOM     45  N   ASN A  10      -7.662  -9.450   3.572  1.00 71.96           N  
ATOM     46  CA  ASN A  10      -7.613 -10.494   4.620  1.00 71.84           C  
ATOM     47  C   ASN A  10      -7.433  -9.996   6.066  1.00 71.62           C  
ATOM     48  O   ASN A  10      -6.877  -8.916   6.284  1.00 71.57           O  
ATOM     49  CB  ASN A  10      -6.597 -11.603   4.286  1.00 71.91           C  
ATOM     50  CG  ASN A  10      -7.148 -12.621   3.302  1.00 72.15           C  
ATOM     51  OD1 ASN A  10      -7.594 -13.699   3.697  1.00 72.37           O  
ATOM     52  ND2 ASN A  10      -7.133 -12.279   2.016  1.00 72.27           N  
ATOM     53  N   PRO A  11      -7.911 -10.786   7.055  1.00 71.42           N  
ATOM     54  CA  PRO A  11      -7.947 -10.384   8.468  1.00 71.24           C  
ATOM     55  C   PRO A  11      -6.578 -10.190   9.117  1.00 71.01           C  
ATOM     56  O   PRO A  11      -5.616 -10.879   8.771  1.00 71.00           O  
ATOM     57  CB  PRO A  11      -8.686 -11.547   9.145  1.00 71.30           C  
ATOM     58  CG  PRO A  11      -9.421 -12.233   8.048  1.00 71.42           C  
ATOM     59  CD  PRO A  11      -8.523 -12.114   6.867  1.00 71.41           C  
ATOM     60  N   VAL A  12      -6.518  -9.250  10.060  1.00 70.73           N  
ATOM     61  CA  VAL A  12      -5.289  -8.899  10.773  1.00 70.41           C  
ATOM     62  C   VAL A  12      -5.575  -8.787  12.274  1.00 70.18           C  
ATOM     63  O   VAL A  12      -6.546  -8.146  12.680  1.00 70.15           O  
ATOM     64  CB  VAL A  12      -4.694  -7.553  10.267  1.00 70.45           C  
ATOM     65  CG1 VAL A  12      -3.330  -7.314  10.875  1.00 70.41           C  
ATOM     66  CG2 VAL A  12      -4.596  -7.521   8.740  1.00 70.42           C  
ATOM     67  N   SER A  13      -4.726  -9.407  13.092  1.00 69.89           N  
ATOM     68  CA  SER A  13      -4.883  -9.369  14.548  1.00 69.57           C  
ATOM     69  C   SER A  13      -4.379  -8.063  15.150  1.00 69.33           C  
ATOM     70  O   SER A  13      -3.393  -7.493  14.681  1.00 69.27           O  
ATOM     71  CB  SER A  13      -4.166 -10.552  15.200  1.00 69.54           C  
ATOM     72  OG  SER A  13      -4.790 -11.776  14.855  1.00 69.65           O  
ATOM     73  N   VAL A  14      -5.075  -7.594  16.185  1.00 69.08           N  
ATOM     74  CA  VAL A  14      -4.671  -6.407  16.941  1.00 68.82           C  
ATOM     75  C   VAL A  14      -4.627  -6.746  18.433  1.00 68.74           C  
ATOM     76  O   VAL A  14      -5.622  -7.203  19.000  1.00 68.73           O  
ATOM     77  CB  VAL A  14      -5.621  -5.200  16.700  1.00 68.79           C  
ATOM     78  CG1 VAL A  14      -5.134  -3.964  17.453  1.00 68.64           C  
ATOM     79  CG2 VAL A  14      -5.744  -4.891  15.218  1.00 68.68           C  
ATOM     80  N   ALA A  15      -3.471  -6.517  19.056  1.00 68.62           N  
ATOM     81  CA  ALA A  15      -3.250  -6.845  20.467  1.00 68.51           C  
ATOM     82  C   ALA A  15      -4.081  -5.978  21.413  1.00 68.46           C  
ATOM     83  O   ALA A  15      -4.138  -4.754  21.262  1.00 68.43           O  
ATOM     84  CB  ALA A  15      -1.773  -6.745  20.808  1.00 68.47           C  
ATOM     85  N   GLY A  16      -4.715  -6.627  22.389  1.00 68.38           N  
ATOM     86  CA  GLY A  16      -5.611  -5.955  23.328  1.00 68.29           C  
ATOM     87  C   GLY A  16      -6.932  -5.602  22.671  1.00 68.23           C  
ATOM     88  O   GLY A  16      -7.401  -6.323  21.786  1.00 68.25           O  
ATOM     89  N   LYS A  17      -7.536  -4.500  23.115  1.00 68.13           N  
ATOM     90  CA  LYS A  17      -8.737  -3.952  22.476  1.00 68.08           C  
ATOM     91  C   LYS A  17      -8.988  -2.497  22.887  1.00 67.88           C  
ATOM     92  O   LYS A  17      -8.550  -2.057  23.955  1.00 67.72           O  
ATOM     93  CB  LYS A  17      -9.972  -4.824  22.757  1.00 68.18           C  
ATOM     94  CG  LYS A  17     -11.038  -4.809  21.644  1.00 68.57           C  
ATOM     95  CD  LYS A  17     -10.707  -5.765  20.482  1.00 68.91           C  
ATOM     96  CE  LYS A  17      -9.947  -5.071  19.346  1.00 68.95           C  
ATOM     97  NZ  LYS A  17      -9.547  -6.027  18.272  1.00 69.03           N  
ATOM     98  N   LEU A  18      -9.696  -1.768  22.026  1.00 67.65           N  
ATOM     99  CA  LEU A  18      -9.927  -0.334  22.190  1.00 67.48           C  
ATOM    100  C   LEU A  18     -10.817  -0.022  23.397  1.00 67.37           C  
ATOM    101  O   LEU A  18     -11.842  -0.680  23.594  1.00 67.36           O  
ATOM    102  CB  LEU A  18     -10.548   0.244  20.913  1.00 67.47           C  
ATOM    103  CG  LEU A  18     -10.310   1.715  20.565  1.00 67.44           C  
ATOM    104  CD1 LEU A  18      -8.923   1.926  19.978  1.00 67.60           C  
ATOM    105  CD2 LEU A  18     -11.363   2.188  19.585  1.00 67.65           C  
ATOM    106  N   PRO A  19     -10.417   0.977  24.213  1.00 67.24           N  
ATOM    107  CA  PRO A  19     -11.201   1.424  25.367  1.00 67.16           C  
ATOM    108  C   PRO A  19     -12.571   1.958  24.958  1.00 67.07           C  
ATOM    109  O   PRO A  19     -12.664   2.822  24.084  1.00 67.04           O  
ATOM    110  CB  PRO A  19     -10.348   2.553  25.957  1.00 67.15           C  
ATOM    111  CG  PRO A  19      -8.969   2.253  25.513  1.00 67.22           C  
ATOM    112  CD  PRO A  19      -9.119   1.672  24.142  1.00 67.24           C  
ATOM    113  N   GLN A  20     -13.617   1.431  25.591  1.00 66.92           N  
ATOM    114  CA  GLN A  20     -14.996   1.798  25.277  1.00 66.73           C  
ATOM    115  C   GLN A  20     -15.423   3.063  26.017  1.00 66.56           C  
ATOM    116  O   GLN A  20     -14.748   3.499  26.954  1.00 66.52           O  
ATOM    117  CB  GLN A  20     -15.939   0.638  25.614  1.00 66.77           C  
ATOM    118  CG  GLN A  20     -15.883  -0.531  24.633  1.00 67.01           C  
ATOM    119  CD  GLN A  20     -16.755  -0.320  23.403  1.00 67.42           C  
ATOM    120  OE1 GLN A  20     -16.532   0.600  22.613  1.00 67.57           O  
ATOM    121  NE2 GLN A  20     -17.752  -1.182  23.232  1.00 67.46           N  
ATOM    122  N   ILE A  21     -16.541   3.648  25.584  1.00 66.33           N  
ATOM    123  CA  ILE A  21     -17.111   4.833  26.226  1.00 66.14           C  
ATOM    124  C   ILE A  21     -17.475   4.546  27.684  1.00 65.99           C  
ATOM    125  O   ILE A  21     -18.094   3.522  27.986  1.00 65.96           O  
ATOM    126  CB  ILE A  21     -18.356   5.343  25.473  1.00 66.15           C  
ATOM    127  N   GLY A  22     -17.073   5.447  28.580  1.00 65.74           N  
ATOM    128  CA  GLY A  22     -17.293   5.275  30.016  1.00 65.52           C  
ATOM    129  C   GLY A  22     -16.026   4.962  30.793  1.00 65.39           C  
ATOM    130  O   GLY A  22     -15.887   5.363  31.950  1.00 65.33           O  
ATOM    131  N   ASP A  23     -15.104   4.244  30.151  1.00 65.31           N  
ATOM    132  CA  ASP A  23     -13.826   3.857  30.755  1.00 65.16           C  
ATOM    133  C   ASP A  23     -12.882   5.046  30.957  1.00 65.09           C  
ATOM    134  O   ASP A  23     -13.073   6.116  30.368  1.00 65.09           O  
ATOM    135  CB  ASP A  23     -13.126   2.793  29.896  1.00 65.13           C  
ATOM    136  CG  ASP A  23     -13.939   1.512  29.753  1.00 65.24           C  
ATOM    137  OD1 ASP A  23     -14.680   1.149  30.694  1.00 65.32           O  
ATOM    138  OD2 ASP A  23     -13.824   0.857  28.694  1.00 65.02           O  
ATOM    139  N   LYS A  24     -11.871   4.847  31.801  1.00 64.91           N  
ATOM    140  CA  LYS A  24     -10.788   5.814  31.968  1.00 64.81           C  
ATOM    141  C   LYS A  24      -9.669   5.509  30.974  1.00 64.68           C  
ATOM    142  O   LYS A  24      -9.373   4.342  30.699  1.00 64.70           O  
ATOM    143  CB  LYS A  24     -10.251   5.793  33.401  1.00 64.83           C  
ATOM    144  N   ALA A  25      -9.053   6.567  30.450  1.00 64.52           N  
ATOM    145  CA  ALA A  25      -8.065   6.473  29.369  1.00 64.32           C  
ATOM    146  C   ALA A  25      -6.835   5.621  29.702  1.00 64.19           C  
ATOM    147  O   ALA A  25      -6.468   4.730  28.931  1.00 64.10           O  
ATOM    148  CB  ALA A  25      -7.639   7.870  28.926  1.00 64.28           C  
ATOM    149  N   LYS A  26      -6.221   5.906  30.853  1.00 64.03           N  
ATOM    150  CA  LYS A  26      -4.951   5.305  31.295  1.00 63.88           C  
ATOM    151  C   LYS A  26      -3.749   6.022  30.672  1.00 63.69           C  
ATOM    152  O   LYS A  26      -3.488   5.895  29.473  1.00 63.63           O  
ATOM    153  CB  LYS A  26      -4.892   3.789  31.033  1.00 63.92           C  
ATOM    154  CG  LYS A  26      -4.150   3.010  32.106  1.00 64.05           C  
ATOM    155  CD  LYS A  26      -5.072   2.672  33.278  1.00 64.27           C  
ATOM    156  CE  LYS A  26      -4.516   3.181  34.603  1.00 64.43           C  
ATOM    157  NZ  LYS A  26      -3.113   2.753  34.864  1.00 64.45           N  
ATOM    158  N   ASP A  27      -3.026   6.768  31.511  1.00 63.44           N  
ATOM    159  CA  ASP A  27      -1.933   7.652  31.082  1.00 63.14           C  
ATOM    160  C   ASP A  27      -0.900   6.981  30.179  1.00 62.88           C  
ATOM    161  O   ASP A  27      -0.557   5.811  30.363  1.00 62.81           O  
ATOM    162  CB  ASP A  27      -1.233   8.270  32.300  1.00 63.16           C  
ATOM    163  CG  ASP A  27      -0.356   9.461  31.934  1.00 63.25           C  
ATOM    164  OD1 ASP A  27      -0.896  10.489  31.471  1.00 63.13           O  
ATOM    165  OD2 ASP A  27       0.876   9.371  32.123  1.00 63.25           O  
ATOM    166  N   PHE A  28      -0.420   7.745  29.201  1.00 62.60           N  
ATOM    167  CA  PHE A  28       0.619   7.296  28.281  1.00 62.30           C  
ATOM    168  C   PHE A  28       1.667   8.389  28.074  1.00 62.04           C  
ATOM    169  O   PHE A  28       1.449   9.548  28.433  1.00 61.93           O  
ATOM    170  CB  PHE A  28       0.008   6.878  26.934  1.00 62.33           C  
ATOM    171  CG  PHE A  28      -0.688   7.998  26.197  1.00 62.45           C  
ATOM    172  CD1 PHE A  28       0.026   8.861  25.368  1.00 62.57           C  
ATOM    173  CD2 PHE A  28      -2.062   8.179  26.318  1.00 62.67           C  
ATOM    174  CE1 PHE A  28      -0.616   9.894  24.684  1.00 62.57           C  
ATOM    175  CE2 PHE A  28      -2.714   9.205  25.635  1.00 62.55           C  
ATOM    176  CZ  PHE A  28      -1.989  10.064  24.818  1.00 62.54           C  
ATOM    177  N   THR A  29       2.801   8.008  27.493  1.00 61.74           N  
ATOM    178  CA  THR A  29       3.847   8.955  27.128  1.00 61.43           C  
ATOM    179  C   THR A  29       4.412   8.593  25.754  1.00 61.13           C  
ATOM    180  O   THR A  29       4.837   7.456  25.527  1.00 61.13           O  
ATOM    181  CB  THR A  29       4.973   9.004  28.191  1.00 61.52           C  
ATOM    182  OG1 THR A  29       4.404   9.253  29.484  1.00 61.63           O  
ATOM    183  CG2 THR A  29       5.987  10.103  27.871  1.00 61.50           C  
ATOM    184  N   LEU A  30       4.389   9.563  24.843  1.00 60.67           N  
ATOM    185  CA  LEU A  30       4.925   9.392  23.493  1.00 60.25           C  
ATOM    186  C   LEU A  30       5.906  10.518  23.150  1.00 60.03           C  
ATOM    187  O   LEU A  30       6.166  11.393  23.978  1.00 59.99           O  
ATOM    188  CB  LEU A  30       3.791   9.315  22.460  1.00 60.21           C  
ATOM    189  CG  LEU A  30       2.823   8.126  22.522  1.00 60.01           C  
ATOM    190  CD1 LEU A  30       1.604   8.383  21.651  1.00 59.85           C  
ATOM    191  CD2 LEU A  30       3.496   6.814  22.132  1.00 59.64           C  
ATOM    192  N   VAL A  31       6.440  10.490  21.930  1.00 59.70           N  
ATOM    193  CA  VAL A  31       7.515  11.399  21.528  1.00 59.42           C  
ATOM    194  C   VAL A  31       7.028  12.469  20.546  1.00 59.28           C  
ATOM    195  O   VAL A  31       6.394  12.155  19.539  1.00 59.24           O  
ATOM    196  CB  VAL A  31       8.709  10.619  20.908  1.00 59.44           C  
ATOM    197  CG1 VAL A  31       9.924  11.518  20.758  1.00 59.37           C  
ATOM    198  CG2 VAL A  31       9.061   9.405  21.755  1.00 59.22           C  
ATOM    199  N   ALA A  32       7.336  13.729  20.848  1.00 59.16           N  
ATOM    200  CA  ALA A  32       6.983  14.856  19.983  1.00 59.05           C  
ATOM    201  C   ALA A  32       8.011  15.063  18.865  1.00 59.06           C  
ATOM    202  O   ALA A  32       9.022  14.358  18.805  1.00 59.02           O  
ATOM    203  CB  ALA A  32       6.824  16.123  20.809  1.00 59.03           C  
ATOM    204  N   LYS A  33       7.749  16.033  17.986  1.00 59.07           N  
ATOM    205  CA  LYS A  33       8.613  16.302  16.829  1.00 59.06           C  
ATOM    206  C   LYS A  33      10.021  16.784  17.198  1.00 58.98           C  
ATOM    207  O   LYS A  33      10.969  16.587  16.435  1.00 58.98           O  
ATOM    208  CB  LYS A  33       7.941  17.269  15.842  1.00 59.10           C  
ATOM    209  CG  LYS A  33       7.754  18.697  16.347  1.00 59.48           C  
ATOM    210  CD  LYS A  33       7.454  19.646  15.194  1.00 59.88           C  
ATOM    211  CE  LYS A  33       7.336  21.089  15.669  1.00 60.08           C  
ATOM    212  NZ  LYS A  33       6.088  21.333  16.445  1.00 60.00           N  
ATOM    213  N   ASP A  34      10.147  17.412  18.367  1.00 58.89           N  
ATOM    214  CA  ASP A  34      11.439  17.879  18.869  1.00 58.76           C  
ATOM    215  C   ASP A  34      12.177  16.772  19.631  1.00 58.67           C  
ATOM    216  O   ASP A  34      13.213  17.021  20.256  1.00 58.64           O  
ATOM    217  CB  ASP A  34      11.250  19.115  19.759  1.00 58.73           C  
ATOM    218  CG  ASP A  34      10.544  18.796  21.068  1.00 58.72           C  
ATOM    219  OD1 ASP A  34       9.731  17.848  21.104  1.00 58.84           O  
ATOM    220  OD2 ASP A  34      10.803  19.500  22.066  1.00 58.75           O  
ATOM    221  N   LEU A  35      11.619  15.561  19.575  1.00 58.53           N  
ATOM    222  CA  LEU A  35      12.178  14.357  20.211  1.00 58.38           C  
ATOM    223  C   LEU A  35      12.053  14.333  21.740  1.00 58.24           C  
ATOM    224  O   LEU A  35      12.695  13.521  22.411  1.00 58.30           O  
ATOM    225  CB  LEU A  35      13.630  14.107  19.771  1.00 58.45           C  
ATOM    226  CG  LEU A  35      13.894  13.816  18.290  1.00 58.51           C  
ATOM    227  CD1 LEU A  35      15.323  14.185  17.926  1.00 58.68           C  
ATOM    228  CD2 LEU A  35      13.602  12.360  17.943  1.00 58.62           C  
ATOM    229  N   SER A  36      11.215  15.214  22.282  1.00 58.07           N  
ATOM    230  CA  SER A  36      10.975  15.271  23.724  1.00 57.85           C  
ATOM    231  C   SER A  36       9.833  14.337  24.123  1.00 57.70           C  
ATOM    232  O   SER A  36       9.071  13.877  23.269  1.00 57.67           O  
ATOM    233  CB  SER A  36      10.674  16.706  24.165  1.00 57.84           C  
ATOM    234  OG  SER A  36       9.445  17.161  23.626  1.00 57.63           O  
ATOM    235  N   ASP A  37       9.724  14.061  25.422  1.00 57.48           N  
ATOM    236  CA  ASP A  37       8.665  13.201  25.951  1.00 57.25           C  
ATOM    237  C   ASP A  37       7.417  14.000  26.306  1.00 56.97           C  
ATOM    238  O   ASP A  37       7.488  14.978  27.057  1.00 56.96           O  
ATOM    239  CB  ASP A  37       9.157  12.422  27.177  1.00 57.33           C  
ATOM    240  CG  ASP A  37      10.062  11.257  26.812  1.00 57.58           C  
ATOM    241  OD1 ASP A  37      10.487  11.158  25.640  1.00 57.98           O  
ATOM    242  OD2 ASP A  37      10.350  10.434  27.705  1.00 58.03           O  
ATOM    243  N   VAL A  38       6.280  13.575  25.758  1.00 56.59           N  
ATOM    244  CA  VAL A  38       4.990  14.214  26.023  1.00 56.27           C  
ATOM    245  C   VAL A  38       4.004  13.209  26.630  1.00 56.06           C  
ATOM    246  O   VAL A  38       3.654  12.203  26.003  1.00 56.08           O  
ATOM    247  CB  VAL A  38       4.395  14.876  24.744  1.00 56.27           C  
ATOM    248  CG1 VAL A  38       2.996  15.415  25.006  1.00 56.16           C  
ATOM    249  CG2 VAL A  38       5.300  15.998  24.244  1.00 56.29           C  
ATOM    250  N   ALA A  39       3.570  13.491  27.856  1.00 55.76           N  
ATOM    251  CA  ALA A  39       2.618  12.641  28.568  1.00 55.46           C  
ATOM    252  C   ALA A  39       1.191  13.166  28.420  1.00 55.24           C  
ATOM    253  O   ALA A  39       0.984  14.354  28.176  1.00 55.26           O  
ATOM    254  CB  ALA A  39       3.001  12.533  30.040  1.00 55.41           C  
ATOM    255  N   LEU A  40       0.213  12.274  28.567  1.00 54.98           N  
ATOM    256  CA  LEU A  40      -1.203  12.642  28.469  1.00 54.79           C  
ATOM    257  C   LEU A  40      -1.604  13.680  29.526  1.00 54.68           C  
ATOM    258  O   LEU A  40      -2.366  14.608  29.237  1.00 54.62           O  
ATOM    259  CB  LEU A  40      -2.091  11.393  28.564  1.00 54.71           C  
ATOM    260  CG  LEU A  40      -3.620  11.527  28.544  1.00 54.63           C  
ATOM    261  CD1 LEU A  40      -4.128  12.135  27.240  1.00 54.49           C  
ATOM    262  CD2 LEU A  40      -4.277  10.173  28.799  1.00 54.50           C  
ATOM    263  N   SER A  41      -1.067  13.522  30.735  1.00 54.47           N  
ATOM    264  CA  SER A  41      -1.350  14.418  31.856  1.00 54.29           C  
ATOM    265  C   SER A  41      -0.858  15.856  31.646  1.00 54.18           C  
ATOM    266  O   SER A  41      -1.200  16.747  32.427  1.00 54.26           O  
ATOM    267  CB  SER A  41      -0.759  13.849  33.148  1.00 54.26           C  
ATOM    268  OG  SER A  41       0.653  13.769  33.066  1.00 54.33           O  
ATOM    269  N   SER A  42      -0.063  16.080  30.600  1.00 53.97           N  
ATOM    270  CA  SER A  42       0.444  17.420  30.286  1.00 53.82           C  
ATOM    271  C   SER A  42      -0.618  18.318  29.638  1.00 53.70           C  
ATOM    272  O   SER A  42      -0.401  19.520  29.460  1.00 53.68           O  
ATOM    273  CB  SER A  42       1.692  17.341  29.400  1.00 53.80           C  
ATOM    274  OG  SER A  42       1.361  16.978  28.072  1.00 53.62           O  
ATOM    275  N   PHE A  43      -1.756  17.726  29.284  1.00 53.60           N  
ATOM    276  CA  PHE A  43      -2.873  18.466  28.694  1.00 53.43           C  
ATOM    277  C   PHE A  43      -4.069  18.512  29.647  1.00 53.34           C  
ATOM    278  O   PHE A  43      -5.225  18.454  29.218  1.00 53.45           O  
ATOM    279  CB  PHE A  43      -3.275  17.851  27.347  1.00 53.35           C  
ATOM    280  CG  PHE A  43      -2.164  17.822  26.333  1.00 53.27           C  
ATOM    281  CD1 PHE A  43      -1.798  18.978  25.644  1.00 53.02           C  
ATOM    282  CD2 PHE A  43      -1.489  16.636  26.058  1.00 53.20           C  
ATOM    283  CE1 PHE A  43      -0.770  18.954  24.703  1.00 52.96           C  
ATOM    284  CE2 PHE A  43      -0.462  16.600  25.116  1.00 52.99           C  
ATOM    285  CZ  PHE A  43      -0.101  17.762  24.439  1.00 52.94           C  
ATOM    286  N   ALA A  44      -3.773  18.630  30.942  1.00 53.16           N  
ATOM    287  CA  ALA A  44      -4.783  18.621  32.001  1.00 52.87           C  
ATOM    288  C   ALA A  44      -5.939  19.593  31.746  1.00 52.64           C  
ATOM    289  O   ALA A  44      -5.722  20.784  31.501  1.00 52.68           O  
ATOM    290  CB  ALA A  44      -4.130  18.906  33.353  1.00 52.89           C  
ATOM    291  N   GLY A  45      -7.161  19.066  31.792  1.00 52.29           N  
ATOM    292  CA  GLY A  45      -8.369  19.881  31.666  1.00 51.86           C  
ATOM    293  C   GLY A  45      -8.934  19.975  30.262  1.00 51.63           C  
ATOM    294  O   GLY A  45     -10.124  20.234  30.085  1.00 51.70           O  
ATOM    295  N   LYS A  46      -8.075  19.772  29.266  1.00 51.40           N  
ATOM    296  CA  LYS A  46      -8.473  19.827  27.861  1.00 51.07           C  
ATOM    297  C   LYS A  46      -9.161  18.536  27.424  1.00 50.88           C  
ATOM    298  O   LYS A  46      -8.987  17.488  28.050  1.00 50.89           O  
ATOM    299  CB  LYS A  46      -7.249  20.078  26.976  1.00 51.08           C  
ATOM    300  CG  LYS A  46      -6.615  21.449  27.140  1.00 51.20           C  
ATOM    301  CD  LYS A  46      -5.261  21.515  26.449  1.00 51.20           C  
ATOM    302  CE  LYS A  46      -4.742  22.945  26.373  1.00 51.30           C  
ATOM    303  NZ  LYS A  46      -5.486  23.765  25.373  1.00 51.20           N  
ATOM    304  N   ARG A  47      -9.953  18.624  26.358  1.00 50.55           N  
ATOM    305  CA  ARG A  47     -10.454  17.436  25.674  1.00 50.24           C  
ATOM    306  C   ARG A  47      -9.373  16.943  24.727  1.00 50.02           C  
ATOM    307  O   ARG A  47      -8.619  17.745  24.164  1.00 50.05           O  
ATOM    308  CB  ARG A  47     -11.731  17.739  24.886  1.00 50.28           C  
ATOM    309  CG  ARG A  47     -13.002  17.850  25.724  1.00 50.51           C  
ATOM    310  CD  ARG A  47     -13.350  19.297  26.079  1.00 50.93           C  
ATOM    311  NE  ARG A  47     -13.630  20.115  24.895  1.00 51.28           N  
ATOM    312  CZ  ARG A  47     -14.796  20.154  24.252  1.00 51.55           C  
ATOM    313  NH1 ARG A  47     -15.824  19.418  24.661  1.00 51.37           N  
ATOM    314  NH2 ARG A  47     -14.936  20.937  23.189  1.00 51.82           N  
ATOM    315  N   LYS A  48      -9.301  15.625  24.553  1.00 49.61           N  
ATOM    316  CA  LYS A  48      -8.272  15.014  23.717  1.00 49.26           C  
ATOM    317  C   LYS A  48      -8.861  14.141  22.612  1.00 48.97           C  
ATOM    318  O   LYS A  48      -9.521  13.135  22.884  1.00 48.97           O  
ATOM    319  CB  LYS A  48      -7.297  14.184  24.564  1.00 49.33           C  
ATOM    320  CG  LYS A  48      -6.462  14.972  25.570  1.00 49.58           C  
ATOM    321  CD  LYS A  48      -7.120  15.002  26.942  1.00 49.94           C  
ATOM    322  CE  LYS A  48      -6.220  15.667  27.965  1.00 50.21           C  
ATOM    323  NZ  LYS A  48      -6.969  16.059  29.194  1.00 50.23           N  
ATOM    324  N   VAL A  49      -8.619  14.539  21.367  1.00 48.49           N  
ATOM    325  CA  VAL A  49      -8.924  13.698  20.218  1.00 48.06           C  
ATOM    326  C   VAL A  49      -7.658  12.926  19.855  1.00 47.78           C  
ATOM    327  O   VAL A  49      -6.640  13.520  19.488  1.00 47.74           O  
ATOM    328  CB  VAL A  49      -9.427  14.521  19.003  1.00 48.13           C  
ATOM    329  CG1 VAL A  49      -9.633  13.620  17.787  1.00 48.08           C  
ATOM    330  CG2 VAL A  49     -10.719  15.253  19.345  1.00 47.99           C  
ATOM    331  N   LEU A  50      -7.726  11.603  19.984  1.00 47.28           N  
ATOM    332  CA  LEU A  50      -6.603  10.735  19.663  1.00 46.79           C  
ATOM    333  C   LEU A  50      -6.807  10.111  18.285  1.00 46.58           C  
ATOM    334  O   LEU A  50      -7.405   9.041  18.151  1.00 46.46           O  
ATOM    335  CB  LEU A  50      -6.413   9.661  20.743  1.00 46.75           C  
ATOM    336  CG  LEU A  50      -6.272  10.103  22.207  1.00 46.82           C  
ATOM    337  CD1 LEU A  50      -6.172   8.897  23.126  1.00 46.79           C  
ATOM    338  CD2 LEU A  50      -5.079  11.024  22.421  1.00 46.80           C  
ATOM    339  N   ASN A  51      -6.322  10.810  17.263  1.00 46.34           N  
ATOM    340  CA  ASN A  51      -6.434  10.356  15.883  1.00 46.19           C  
ATOM    341  C   ASN A  51      -5.261   9.438  15.550  1.00 46.12           C  
ATOM    342  O   ASN A  51      -4.137   9.894  15.322  1.00 46.10           O  
ATOM    343  CB  ASN A  51      -6.504  11.553  14.925  1.00 46.07           C  
ATOM    344  CG  ASN A  51      -7.317  11.261  13.675  1.00 45.96           C  
ATOM    345  OD1 ASN A  51      -7.818  10.153  13.488  1.00 46.14           O  
ATOM    346  ND2 ASN A  51      -7.450  12.260  12.808  1.00 45.48           N  
ATOM    347  N   ILE A  52      -5.538   8.137  15.536  1.00 46.02           N  
ATOM    348  CA  ILE A  52      -4.502   7.111  15.468  1.00 45.87           C  
ATOM    349  C   ILE A  52      -4.399   6.506  14.060  1.00 45.90           C  
ATOM    350  O   ILE A  52      -5.380   5.987  13.525  1.00 45.83           O  
ATOM    351  CB  ILE A  52      -4.741   6.019  16.548  1.00 45.83           C  
ATOM    352  CG1 ILE A  52      -4.982   6.668  17.919  1.00 45.74           C  
ATOM    353  CG2 ILE A  52      -3.565   5.079  16.634  1.00 45.76           C  
ATOM    354  CD1 ILE A  52      -5.642   5.760  18.944  1.00 45.54           C  
ATOM    355  N   PHE A  53      -3.203   6.588  13.476  1.00 45.93           N  
ATOM    356  CA  PHE A  53      -2.955   6.187  12.086  1.00 46.09           C  
ATOM    357  C   PHE A  53      -1.894   5.096  11.984  1.00 46.36           C  
ATOM    358  O   PHE A  53      -0.966   5.066  12.796  1.00 46.37           O  
ATOM    359  CB  PHE A  53      -2.451   7.382  11.264  1.00 45.95           C  
ATOM    360  CG  PHE A  53      -3.448   8.492  11.099  1.00 45.49           C  
ATOM    361  CD1 PHE A  53      -3.574   9.484  12.071  1.00 45.07           C  
ATOM    362  CD2 PHE A  53      -4.226   8.577   9.949  1.00 44.91           C  
ATOM    363  CE1 PHE A  53      -4.480  10.526  11.911  1.00 44.96           C  
ATOM    364  CE2 PHE A  53      -5.135   9.618   9.779  1.00 44.72           C  
ATOM    365  CZ  PHE A  53      -5.264  10.593  10.763  1.00 44.61           C  
ATOM    366  N   PRO A  54      -2.014   4.207  10.975  1.00 46.71           N  
ATOM    367  CA  PRO A  54      -0.922   3.298  10.609  1.00 47.07           C  
ATOM    368  C   PRO A  54       0.338   4.061  10.193  1.00 47.55           C  
ATOM    369  O   PRO A  54       1.434   3.734  10.653  1.00 47.65           O  
ATOM    370  CB  PRO A  54      -1.495   2.524   9.416  1.00 46.97           C  
ATOM    371  CG  PRO A  54      -2.955   2.566   9.610  1.00 46.72           C  
ATOM    372  CD  PRO A  54      -3.247   3.902  10.226  1.00 46.78           C  
ATOM    373  N   SER A  55       0.168   5.062   9.328  1.00 47.97           N  
ATOM    374  CA  SER A  55       1.248   5.964   8.936  1.00 48.42           C  
ATOM    375  C   SER A  55       0.703   7.268   8.369  1.00 48.89           C  
ATOM    376  O   SER A  55      -0.253   7.271   7.589  1.00 48.98           O  
ATOM    377  CB  SER A  55       2.178   5.312   7.912  1.00 48.37           C  
ATOM    378  OG  SER A  55       3.329   6.113   7.697  1.00 48.03           O  
ATOM    379  N   ILE A  56       1.322   8.373   8.767  1.00 49.44           N  
ATOM    380  CA  ILE A  56       0.966   9.693   8.250  1.00 50.06           C  
ATOM    381  C   ILE A  56       2.011  10.209   7.257  1.00 50.54           C  
ATOM    382  O   ILE A  56       1.873  11.303   6.705  1.00 50.58           O  
ATOM    383  CB  ILE A  56       0.739  10.719   9.389  1.00 49.99           C  
ATOM    384  CG1 ILE A  56       1.914  10.730  10.376  1.00 50.08           C  
ATOM    385  CG2 ILE A  56      -0.586  10.447  10.088  1.00 49.93           C  
ATOM    386  CD1 ILE A  56       1.942  11.939  11.305  1.00 50.44           C  
ATOM    387  N   ASP A  57       3.044   9.402   7.028  1.00 51.17           N  
ATOM    388  CA  ASP A  57       4.131   9.755   6.122  1.00 51.85           C  
ATOM    389  C   ASP A  57       3.701   9.633   4.657  1.00 52.27           C  
ATOM    390  O   ASP A  57       3.920   8.600   4.012  1.00 52.31           O  
ATOM    391  CB  ASP A  57       5.364   8.889   6.407  1.00 51.82           C  
ATOM    392  CG  ASP A  57       6.632   9.429   5.757  1.00 52.12           C  
ATOM    393  OD1 ASP A  57       6.629  10.583   5.273  1.00 51.93           O  
ATOM    394  OD2 ASP A  57       7.644   8.695   5.741  1.00 52.70           O  
ATOM    395  N   THR A  58       3.081  10.698   4.149  1.00 52.79           N  
ATOM    396  CA  THR A  58       2.651  10.773   2.748  1.00 53.34           C  
ATOM    397  C   THR A  58       2.657  12.213   2.222  1.00 53.71           C  
ATOM    398  O   THR A  58       2.502  13.166   2.991  1.00 53.81           O  
ATOM    399  CB  THR A  58       1.256  10.117   2.523  1.00 53.33           C  
ATOM    400  OG1 THR A  58       0.919  10.160   1.130  1.00 53.29           O  
ATOM    401  CG2 THR A  58       0.164  10.819   3.338  1.00 53.36           C  
ATOM    402  N   GLY A  59       2.842  12.356   0.912  1.00 54.18           N  
ATOM    403  CA  GLY A  59       2.867  13.666   0.263  1.00 54.80           C  
ATOM    404  C   GLY A  59       1.507  14.131  -0.224  1.00 55.28           C  
ATOM    405  O   GLY A  59       1.367  15.260  -0.696  1.00 55.38           O  
ATOM    406  N   VAL A  60       0.506  13.260  -0.111  1.00 55.76           N  
ATOM    407  CA  VAL A  60      -0.857  13.564  -0.555  1.00 56.23           C  
ATOM    408  C   VAL A  60      -1.900  12.798   0.269  1.00 56.53           C  
ATOM    409  O   VAL A  60      -1.902  11.563   0.301  1.00 56.60           O  
ATOM    410  CB  VAL A  60      -1.044  13.324  -2.095  1.00 56.22           C  
ATOM    411  CG1 VAL A  60      -0.622  11.909  -2.504  1.00 56.35           C  
ATOM    412  CG2 VAL A  60      -2.478  13.628  -2.536  1.00 56.27           C  
ATOM    413  N   CYS A  61      -2.774  13.547   0.940  1.00 56.84           N  
ATOM    414  CA  CYS A  61      -3.845  12.960   1.745  1.00 57.14           C  
ATOM    415  C   CYS A  61      -5.231  13.366   1.236  1.00 57.08           C  
ATOM    416  O   CYS A  61      -5.360  14.265   0.396  1.00 57.17           O  
ATOM    417  CB  CYS A  61      -3.681  13.333   3.222  1.00 57.25           C  
ATOM    418  SG  CYS A  61      -4.183  15.021   3.628  1.00 58.35           S  
ATOM    419  N   ALA A  62      -6.260  12.706   1.769  1.00 56.96           N  
ATOM    420  CA  ALA A  62      -7.643  12.882   1.317  1.00 56.85           C  
ATOM    421  C   ALA A  62      -8.295  14.218   1.709  1.00 56.76           C  
ATOM    422  O   ALA A  62      -9.466  14.447   1.393  1.00 56.83           O  
ATOM    423  CB  ALA A  62      -8.499  11.709   1.791  1.00 56.91           C  
ATOM    424  N   ALA A  63      -7.540  15.080   2.395  1.00 56.58           N  
ATOM    425  CA  ALA A  63      -7.992  16.419   2.831  1.00 56.37           C  
ATOM    426  C   ALA A  63      -9.115  16.419   3.870  1.00 56.16           C  
ATOM    427  O   ALA A  63      -9.213  17.343   4.683  1.00 56.19           O  
ATOM    428  CB  ALA A  63      -8.366  17.299   1.640  1.00 56.39           C  
ATOM    429  N   SER A  64      -9.959  15.390   3.829  1.00 55.84           N  
ATOM    430  CA  SER A  64     -10.997  15.182   4.833  1.00 55.49           C  
ATOM    431  C   SER A  64     -10.365  14.861   6.185  1.00 55.22           C  
ATOM    432  O   SER A  64     -10.936  15.168   7.234  1.00 55.18           O  
ATOM    433  CB  SER A  64     -11.936  14.053   4.405  1.00 55.51           C  
ATOM    434  OG  SER A  64     -13.017  13.924   5.311  1.00 55.53           O  
ATOM    435  N   VAL A  65      -9.184  14.245   6.145  1.00 54.89           N  
ATOM    436  CA  VAL A  65      -8.396  13.983   7.350  1.00 54.68           C  
ATOM    437  C   VAL A  65      -7.864  15.288   7.947  1.00 54.44           C  
ATOM    438  O   VAL A  65      -7.821  15.443   9.170  1.00 54.36           O  
ATOM    439  CB  VAL A  65      -7.233  12.971   7.100  1.00 54.72           C  
ATOM    440  CG1 VAL A  65      -7.778  11.616   6.675  1.00 54.82           C  
ATOM    441  CG2 VAL A  65      -6.253  13.486   6.057  1.00 54.84           C  
ATOM    442  N   ARG A  66      -7.477  16.219   7.072  1.00 54.13           N  
ATOM    443  CA  ARG A  66      -7.013  17.545   7.477  1.00 53.81           C  
ATOM    444  C   ARG A  66      -8.173  18.398   7.984  1.00 53.59           C  
ATOM    445  O   ARG A  66      -8.021  19.141   8.955  1.00 53.61           O  
ATOM    446  CB  ARG A  66      -6.313  18.253   6.313  1.00 53.85           C  
ATOM    447  N   LYS A  67      -9.325  18.275   7.323  1.00 53.32           N  
ATOM    448  CA  LYS A  67     -10.538  19.009   7.695  1.00 52.94           C  
ATOM    449  C   LYS A  67     -10.993  18.689   9.118  1.00 52.64           C  
ATOM    450  O   LYS A  67     -11.278  19.597   9.902  1.00 52.64           O  
ATOM    451  N   PHE A  68     -11.045  17.398   9.440  1.00 52.35           N  
ATOM    452  CA  PHE A  68     -11.459  16.927  10.764  1.00 52.06           C  
ATOM    453  C   PHE A  68     -10.552  17.410  11.897  1.00 51.96           C  
ATOM    454  O   PHE A  68     -11.042  17.841  12.943  1.00 51.90           O  
ATOM    455  CB  PHE A  68     -11.555  15.397  10.778  1.00 51.98           C  
ATOM    456  CG  PHE A  68     -11.644  14.804  12.159  1.00 51.86           C  
ATOM    457  CD1 PHE A  68     -12.813  14.915  12.907  1.00 51.74           C  
ATOM    458  CD2 PHE A  68     -10.559  14.128  12.708  1.00 51.65           C  
ATOM    459  CE1 PHE A  68     -12.899  14.365  14.182  1.00 51.86           C  
ATOM    460  CE2 PHE A  68     -10.635  13.573  13.982  1.00 51.81           C  
ATOM    461  CZ  PHE A  68     -11.807  13.692  14.721  1.00 52.04           C  
ATOM    462  N   ASN A  69      -9.240  17.320  11.687  1.00 51.88           N  
ATOM    463  CA  ASN A  69      -8.258  17.779  12.668  1.00 51.89           C  
ATOM    464  C   ASN A  69      -8.309  19.293  12.875  1.00 51.98           C  
ATOM    465  O   ASN A  69      -8.116  19.781  13.994  1.00 51.91           O  
ATOM    466  CB  ASN A  69      -6.843  17.340  12.271  1.00 51.78           C  
ATOM    467  CG  ASN A  69      -6.645  15.833  12.365  1.00 51.81           C  
ATOM    468  OD1 ASN A  69      -7.263  15.158  13.192  1.00 51.74           O  
ATOM    469  ND2 ASN A  69      -5.774  15.300  11.516  1.00 51.61           N  
ATOM    470  N   GLN A  70      -8.573  20.021  11.791  1.00 52.07           N  
ATOM    471  CA  GLN A  70      -8.740  21.470  11.838  1.00 52.23           C  
ATOM    472  C   GLN A  70      -9.965  21.851  12.666  1.00 52.20           C  
ATOM    473  O   GLN A  70      -9.866  22.684  13.569  1.00 52.20           O  
ATOM    474  CB  GLN A  70      -8.846  22.049  10.422  1.00 52.32           C  
ATOM    475  CG  GLN A  70      -8.864  23.573  10.366  1.00 52.78           C  
ATOM    476  CD  GLN A  70      -8.740  24.116   8.952  1.00 53.68           C  
ATOM    477  OE1 GLN A  70      -9.543  23.795   8.070  1.00 54.03           O  
ATOM    478  NE2 GLN A  70      -7.732  24.954   8.731  1.00 53.71           N  
ATOM    479  N   LEU A  71     -11.105  21.229  12.357  1.00 52.17           N  
ATOM    480  CA  LEU A  71     -12.367  21.493  13.058  1.00 52.18           C  
ATOM    481  C   LEU A  71     -12.282  21.181  14.552  1.00 52.16           C  
ATOM    482  O   LEU A  71     -12.730  21.977  15.381  1.00 52.18           O  
ATOM    483  CB  LEU A  71     -13.525  20.714  12.421  1.00 52.14           C  
ATOM    484  CG  LEU A  71     -14.065  21.186  11.067  1.00 52.35           C  
ATOM    485  CD1 LEU A  71     -14.916  20.095  10.425  1.00 52.47           C  
ATOM    486  CD2 LEU A  71     -14.855  22.489  11.189  1.00 52.31           C  
ATOM    487  N   ALA A  72     -11.702  20.028  14.883  1.00 52.07           N  
ATOM    488  CA  ALA A  72     -11.502  19.632  16.275  1.00 52.13           C  
ATOM    489  C   ALA A  72     -10.458  20.515  16.964  1.00 52.16           C  
ATOM    490  O   ALA A  72     -10.550  20.770  18.164  1.00 52.09           O  
ATOM    491  CB  ALA A  72     -11.116  18.165  16.365  1.00 52.04           C  
ATOM    492  N   GLY A  73      -9.478  20.984  16.194  1.00 52.23           N  
ATOM    493  CA  GLY A  73      -8.470  21.916  16.694  1.00 52.36           C  
ATOM    494  C   GLY A  73      -9.034  23.291  17.013  1.00 52.41           C  
ATOM    495  O   GLY A  73      -8.594  23.943  17.962  1.00 52.36           O  
ATOM    496  N   GLU A  74     -10.010  23.724  16.215  1.00 52.46           N  
ATOM    497  CA  GLU A  74     -10.676  25.019  16.390  1.00 52.56           C  
ATOM    498  C   GLU A  74     -11.509  25.094  17.668  1.00 52.42           C  
ATOM    499  O   GLU A  74     -11.556  26.139  18.323  1.00 52.45           O  
ATOM    500  CB  GLU A  74     -11.576  25.325  15.191  1.00 52.65           C  
ATOM    501  CG  GLU A  74     -10.849  25.843  13.960  1.00 53.24           C  
ATOM    502  CD  GLU A  74     -11.801  26.212  12.831  1.00 54.17           C  
ATOM    503  OE1 GLU A  74     -11.392  26.110  11.654  1.00 54.48           O  
ATOM    504  OE2 GLU A  74     -12.958  26.601  13.117  1.00 54.48           O  
ATOM    505  N   LEU A  75     -12.160  23.982  18.008  1.00 52.20           N  
ATOM    506  CA  LEU A  75     -13.055  23.904  19.163  1.00 51.90           C  
ATOM    507  C   LEU A  75     -12.360  24.281  20.468  1.00 51.69           C  
ATOM    508  O   LEU A  75     -11.175  23.999  20.653  1.00 51.69           O  
ATOM    509  CB  LEU A  75     -13.671  22.506  19.271  1.00 51.96           C  
ATOM    510  CG  LEU A  75     -14.688  22.098  18.199  1.00 51.97           C  
ATOM    511  CD1 LEU A  75     -14.757  20.585  18.074  1.00 52.49           C  
ATOM    512  CD2 LEU A  75     -16.071  22.677  18.482  1.00 51.98           C  
ATOM    513  N   GLU A  76     -13.116  24.925  21.357  1.00 51.47           N  
ATOM    514  CA  GLU A  76     -12.597  25.447  22.621  1.00 51.19           C  
ATOM    515  C   GLU A  76     -12.193  24.339  23.586  1.00 51.02           C  
ATOM    516  O   GLU A  76     -12.905  23.340  23.727  1.00 51.08           O  
ATOM    517  CB  GLU A  76     -13.631  26.360  23.285  1.00 51.16           C  
ATOM    518  N   ASN A  77     -11.050  24.535  24.245  1.00 50.76           N  
ATOM    519  CA  ASN A  77     -10.515  23.590  25.230  1.00 50.48           C  
ATOM    520  C   ASN A  77     -10.298  22.192  24.629  1.00 50.38           C  
ATOM    521  O   ASN A  77     -10.720  21.180  25.197  1.00 50.26           O  
ATOM    522  CB  ASN A  77     -11.418  23.548  26.474  1.00 50.44           C  
ATOM    523  CG  ASN A  77     -10.751  22.900  27.671  1.00 50.13           C  
ATOM    524  OD1 ASN A  77      -9.554  23.068  27.905  1.00 50.48           O  
ATOM    525  ND2 ASN A  77     -11.534  22.164  28.449  1.00 49.49           N  
ATOM    526  N   THR A  78      -9.633  22.159  23.474  1.00 50.24           N  
ATOM    527  CA  THR A  78      -9.407  20.918  22.729  1.00 50.17           C  
ATOM    528  C   THR A  78      -7.971  20.793  22.215  1.00 50.08           C  
ATOM    529  O   THR A  78      -7.369  21.774  21.769  1.00 50.10           O  
ATOM    530  CB  THR A  78     -10.371  20.795  21.525  1.00 50.12           C  
ATOM    531  OG1 THR A  78     -11.674  21.268  21.890  1.00 50.14           O  
ATOM    532  CG2 THR A  78     -10.469  19.345  21.057  1.00 50.18           C  
ATOM    533  N   VAL A  79      -7.432  19.578  22.283  1.00 49.93           N  
ATOM    534  CA  VAL A  79      -6.141  19.271  21.673  1.00 49.75           C  
ATOM    535  C   VAL A  79      -6.217  17.980  20.845  1.00 49.62           C  
ATOM    536  O   VAL A  79      -6.665  16.938  21.331  1.00 49.49           O  
ATOM    537  CB  VAL A  79      -4.979  19.255  22.721  1.00 49.75           C  
ATOM    538  CG1 VAL A  79      -5.174  18.157  23.774  1.00 49.75           C  
ATOM    539  CG2 VAL A  79      -3.622  19.132  22.031  1.00 49.65           C  
ATOM    540  N   VAL A  80      -5.804  18.078  19.583  1.00 49.51           N  
ATOM    541  CA  VAL A  80      -5.806  16.942  18.661  1.00 49.34           C  
ATOM    542  C   VAL A  80      -4.430  16.288  18.660  1.00 49.27           C  
ATOM    543  O   VAL A  80      -3.428  16.925  18.321  1.00 49.28           O  
ATOM    544  CB  VAL A  80      -6.178  17.367  17.216  1.00 49.35           C  
ATOM    545  CG1 VAL A  80      -6.244  16.156  16.291  1.00 49.51           C  
ATOM    546  CG2 VAL A  80      -7.501  18.116  17.193  1.00 49.27           C  
ATOM    547  N   LEU A  81      -4.389  15.017  19.047  1.00 49.16           N  
ATOM    548  CA  LEU A  81      -3.139  14.270  19.085  1.00 49.09           C  
ATOM    549  C   LEU A  81      -3.113  13.199  18.000  1.00 49.17           C  
ATOM    550  O   LEU A  81      -3.784  12.170  18.111  1.00 49.10           O  
ATOM    551  CB  LEU A  81      -2.905  13.666  20.476  1.00 49.05           C  
ATOM    552  CG  LEU A  81      -2.841  14.635  21.667  1.00 48.87           C  
ATOM    553  CD1 LEU A  81      -2.763  13.874  22.983  1.00 48.43           C  
ATOM    554  CD2 LEU A  81      -1.677  15.622  21.548  1.00 48.57           C  
ATOM    555  N   CYS A  82      -2.346  13.465  16.945  1.00 49.32           N  
ATOM    556  CA  CYS A  82      -2.204  12.540  15.823  1.00 49.50           C  
ATOM    557  C   CYS A  82      -1.070  11.559  16.068  1.00 49.64           C  
ATOM    558  O   CYS A  82       0.101  11.943  16.123  1.00 49.69           O  
ATOM    559  CB  CYS A  82      -1.982  13.297  14.514  1.00 49.38           C  
ATOM    560  SG  CYS A  82      -3.485  14.003  13.838  1.00 49.35           S  
ATOM    561  N   ILE A  83      -1.431  10.287  16.204  1.00 49.80           N  
ATOM    562  CA  ILE A  83      -0.492   9.255  16.625  1.00 49.85           C  
ATOM    563  C   ILE A  83      -0.250   8.219  15.524  1.00 50.02           C  
ATOM    564  O   ILE A  83      -1.191   7.647  14.974  1.00 50.00           O  
ATOM    565  CB  ILE A  83      -0.969   8.588  17.944  1.00 49.84           C  
ATOM    566  CG1 ILE A  83      -1.018   9.631  19.069  1.00 49.53           C  
ATOM    567  CG2 ILE A  83      -0.061   7.419  18.333  1.00 49.84           C  
ATOM    568  CD1 ILE A  83      -2.070   9.370  20.127  1.00 49.40           C  
ATOM    569  N   SER A  84       1.023   8.005  15.201  1.00 50.34           N  
ATOM    570  CA  SER A  84       1.439   6.971  14.257  1.00 50.65           C  
ATOM    571  C   SER A  84       2.738   6.313  14.725  1.00 50.90           C  
ATOM    572  O   SER A  84       3.330   6.732  15.723  1.00 50.89           O  
ATOM    573  CB  SER A  84       1.615   7.562  12.854  1.00 50.67           C  
ATOM    574  OG  SER A  84       2.685   8.491  12.816  1.00 50.67           O  
ATOM    575  N   SER A  85       3.172   5.281  14.004  1.00 51.25           N  
ATOM    576  CA  SER A  85       4.454   4.635  14.285  1.00 51.51           C  
ATOM    577  C   SER A  85       5.638   5.321  13.594  1.00 51.62           C  
ATOM    578  O   SER A  85       6.791   4.962  13.840  1.00 51.70           O  
ATOM    579  CB  SER A  85       4.406   3.141  13.947  1.00 51.58           C  
ATOM    580  OG  SER A  85       4.041   2.378  15.088  1.00 51.83           O  
ATOM    581  N   ASP A  86       5.347   6.311  12.747  1.00 51.84           N  
ATOM    582  CA  ASP A  86       6.377   7.123  12.092  1.00 52.12           C  
ATOM    583  C   ASP A  86       7.258   7.844  13.115  1.00 52.40           C  
ATOM    584  O   ASP A  86       6.792   8.220  14.193  1.00 52.31           O  
ATOM    585  CB  ASP A  86       5.741   8.167  11.162  1.00 52.08           C  
ATOM    586  CG  ASP A  86       4.923   7.548  10.037  1.00 51.99           C  
ATOM    587  OD1 ASP A  86       5.445   6.681   9.304  1.00 52.08           O  
ATOM    588  OD2 ASP A  86       3.754   7.954   9.871  1.00 51.21           O  
ATOM    589  N   LEU A  87       8.530   8.031  12.772  1.00 52.79           N  
ATOM    590  CA  LEU A  87       9.450   8.796  13.608  1.00 53.23           C  
ATOM    591  C   LEU A  87       9.197  10.294  13.433  1.00 53.74           C  
ATOM    592  O   LEU A  87       8.686  10.711  12.389  1.00 53.80           O  
ATOM    593  CB  LEU A  87      10.905   8.463  13.258  1.00 53.13           C  
ATOM    594  CG  LEU A  87      11.417   7.031  13.434  1.00 53.06           C  
ATOM    595  CD1 LEU A  87      12.929   7.015  13.319  1.00 52.90           C  
ATOM    596  CD2 LEU A  87      10.981   6.424  14.760  1.00 52.89           C  
ATOM    597  N   PRO A  88       9.557  11.111  14.446  1.00 54.19           N  
ATOM    598  CA  PRO A  88       9.364  12.566  14.383  1.00 54.68           C  
ATOM    599  C   PRO A  88       9.995  13.233  13.155  1.00 55.24           C  
ATOM    600  O   PRO A  88       9.709  14.398  12.874  1.00 55.46           O  
ATOM    601  CB  PRO A  88      10.046  13.061  15.660  1.00 54.62           C  
ATOM    602  CG  PRO A  88       9.935  11.920  16.599  1.00 54.46           C  
ATOM    603  CD  PRO A  88      10.092  10.693  15.756  1.00 54.19           C  
ATOM    604  N   PHE A  89      10.842  12.498  12.439  1.00 55.83           N  
ATOM    605  CA  PHE A  89      11.460  12.992  11.210  1.00 56.43           C  
ATOM    606  C   PHE A  89      10.501  12.898  10.021  1.00 56.89           C  
ATOM    607  O   PHE A  89      10.568  13.711   9.098  1.00 57.03           O  
ATOM    608  CB  PHE A  89      12.748  12.215  10.901  1.00 56.33           C  
ATOM    609  CG  PHE A  89      13.629  11.986  12.101  1.00 56.17           C  
ATOM    610  CD1 PHE A  89      13.762  10.711  12.645  1.00 56.12           C  
ATOM    611  CD2 PHE A  89      14.322  13.042  12.691  1.00 56.04           C  
ATOM    612  CE1 PHE A  89      14.573  10.487  13.758  1.00 55.90           C  
ATOM    613  CE2 PHE A  89      15.136  12.830  13.806  1.00 55.93           C  
ATOM    614  CZ  PHE A  89      15.262  11.551  14.339  1.00 55.78           C  
ATOM    615  N   ALA A  90       9.615  11.903  10.057  1.00 57.41           N  
ATOM    616  CA  ALA A  90       8.689  11.623   8.957  1.00 57.91           C  
ATOM    617  C   ALA A  90       7.300  12.228   9.171  1.00 58.31           C  
ATOM    618  O   ALA A  90       6.563  12.463   8.209  1.00 58.44           O  
ATOM    619  CB  ALA A  90       8.580  10.121   8.736  1.00 57.89           C  
ATOM    620  N   GLN A  91       6.953  12.471  10.433  1.00 58.78           N  
ATOM    621  CA  GLN A  91       5.646  13.014  10.812  1.00 59.18           C  
ATOM    622  C   GLN A  91       5.460  14.464  10.360  1.00 59.56           C  
ATOM    623  O   GLN A  91       4.329  14.937  10.213  1.00 59.61           O  
ATOM    624  CB  GLN A  91       5.445  12.903  12.326  1.00 59.08           C  
ATOM    625  CG  GLN A  91       5.446  11.468  12.843  1.00 59.08           C  
ATOM    626  CD  GLN A  91       5.133  11.363  14.323  1.00 58.59           C  
ATOM    627  OE1 GLN A  91       5.818  11.948  15.161  1.00 58.71           O  
ATOM    628  NE2 GLN A  91       4.097  10.602  14.652  1.00 58.56           N  
ATOM    629  N   SER A  92       6.579  15.151  10.133  1.00 60.03           N  
ATOM    630  CA  SER A  92       6.593  16.551   9.709  1.00 60.43           C  
ATOM    631  C   SER A  92       5.999  16.772   8.317  1.00 60.65           C  
ATOM    632  O   SER A  92       5.441  17.836   8.043  1.00 60.70           O  
ATOM    633  CB  SER A  92       8.021  17.100   9.757  1.00 60.49           C  
ATOM    634  OG  SER A  92       8.894  16.317   8.959  1.00 60.71           O  
ATOM    635  N   ARG A  93       6.122  15.770   7.446  1.00 60.96           N  
ATOM    636  CA  ARG A  93       5.598  15.855   6.078  1.00 61.12           C  
ATOM    637  C   ARG A  93       4.067  15.881   6.028  1.00 61.25           C  
ATOM    638  O   ARG A  93       3.486  16.541   5.162  1.00 61.35           O  
ATOM    639  CB  ARG A  93       6.093  14.692   5.207  1.00 61.18           C  
ATOM    640  CG  ARG A  93       7.521  14.222   5.443  1.00 61.40           C  
ATOM    641  CD  ARG A  93       8.118  13.682   4.148  1.00 62.01           C  
ATOM    642  NE  ARG A  93       8.605  12.305   4.268  1.00 62.47           N  
ATOM    643  CZ  ARG A  93       9.808  11.951   4.716  1.00 62.38           C  
ATOM    644  NH1 ARG A  93      10.683  12.868   5.114  1.00 62.45           N  
ATOM    645  NH2 ARG A  93      10.135  10.667   4.772  1.00 62.18           N  
ATOM    646  N   PHE A  94       3.431  15.171   6.964  1.00 61.33           N  
ATOM    647  CA  PHE A  94       1.991  14.869   6.913  1.00 61.40           C  
ATOM    648  C   PHE A  94       1.094  16.007   6.431  1.00 61.54           C  
ATOM    649  O   PHE A  94       1.130  17.121   6.956  1.00 61.63           O  
ATOM    650  CB  PHE A  94       1.489  14.306   8.252  1.00 61.35           C  
ATOM    651  CG  PHE A  94       0.055  13.811   8.218  1.00 61.09           C  
ATOM    652  CD1 PHE A  94      -0.804  14.071   9.281  1.00 60.75           C  
ATOM    653  CD2 PHE A  94      -0.434  13.086   7.128  1.00 60.72           C  
ATOM    654  CE1 PHE A  94      -2.122  13.618   9.264  1.00 60.56           C  
ATOM    655  CE2 PHE A  94      -1.748  12.633   7.100  1.00 60.54           C  
ATOM    656  CZ  PHE A  94      -2.594  12.898   8.170  1.00 60.62           C  
ATOM    657  N   CYS A  95       0.284  15.680   5.429  1.00 61.73           N  
ATOM    658  CA  CYS A  95      -0.588  16.624   4.739  1.00 62.00           C  
ATOM    659  C   CYS A  95      -1.893  16.892   5.501  1.00 61.89           C  
ATOM    660  O   CYS A  95      -2.727  17.690   5.058  1.00 61.82           O  
ATOM    661  CB  CYS A  95      -0.881  16.090   3.329  1.00 62.03           C  
ATOM    662  SG  CYS A  95      -1.707  17.236   2.199  1.00 63.23           S  
ATOM    663  N   GLY A  96      -2.061  16.233   6.647  1.00 61.82           N  
ATOM    664  CA  GLY A  96      -3.281  16.365   7.444  1.00 61.75           C  
ATOM    665  C   GLY A  96      -3.094  16.940   8.838  1.00 61.72           C  
ATOM    666  O   GLY A  96      -4.044  16.998   9.619  1.00 61.68           O  
ATOM    667  N   ALA A  97      -1.870  17.362   9.150  1.00 61.77           N  
ATOM    668  CA  ALA A  97      -1.551  17.970  10.446  1.00 61.77           C  
ATOM    669  C   ALA A  97      -0.638  19.188  10.290  1.00 61.76           C  
ATOM    670  O   ALA A  97      -0.325  19.872  11.266  1.00 61.72           O  
ATOM    671  CB  ALA A  97      -0.920  16.938  11.376  1.00 61.84           C  
ATOM    672  N   GLU A  98      -0.230  19.443   9.048  1.00 61.84           N  
ATOM    673  CA  GLU A  98       0.664  20.544   8.678  1.00 61.88           C  
ATOM    674  C   GLU A  98       0.220  21.926   9.187  1.00 61.72           C  
ATOM    675  O   GLU A  98      -0.884  22.387   8.892  1.00 61.73           O  
ATOM    676  CB  GLU A  98       0.871  20.553   7.148  1.00 62.03           C  
ATOM    677  CG  GLU A  98      -0.258  21.175   6.273  1.00 62.44           C  
ATOM    678  CD  GLU A  98      -1.684  20.762   6.664  1.00 62.86           C  
ATOM    679  OE1 GLU A  98      -2.575  21.640   6.655  1.00 62.82           O  
ATOM    680  OE2 GLU A  98      -1.919  19.577   6.987  1.00 62.93           O  
ATOM    681  N   GLY A  99       1.084  22.565   9.971  1.00 61.59           N  
ATOM    682  CA  GLY A  99       0.865  23.938  10.439  1.00 61.38           C  
ATOM    683  C   GLY A  99      -0.487  24.237  11.065  1.00 61.20           C  
ATOM    684  O   GLY A  99      -0.911  25.393  11.109  1.00 61.24           O  
ATOM    685  N   LEU A 100      -1.165  23.196  11.544  1.00 60.98           N  
ATOM    686  CA  LEU A 100      -2.452  23.346  12.219  1.00 60.74           C  
ATOM    687  C   LEU A 100      -2.274  23.884  13.640  1.00 60.55           C  
ATOM    688  O   LEU A 100      -1.225  23.687  14.261  1.00 60.61           O  
ATOM    689  CB  LEU A 100      -3.214  22.016  12.217  1.00 60.77           C  
ATOM    690  CG  LEU A 100      -4.332  21.772  11.188  1.00 60.82           C  
ATOM    691  CD1 LEU A 100      -4.084  22.446   9.840  1.00 60.74           C  
ATOM    692  CD2 LEU A 100      -4.542  20.275  10.991  1.00 60.61           C  
ATOM    693  N   SER A 101      -3.303  24.567  14.141  1.00 60.23           N  
ATOM    694  CA  SER A 101      -3.231  25.281  15.419  1.00 59.90           C  
ATOM    695  C   SER A 101      -3.049  24.369  16.636  1.00 59.63           C  
ATOM    696  O   SER A 101      -2.003  24.403  17.289  1.00 59.70           O  
ATOM    697  CB  SER A 101      -4.455  26.185  15.606  1.00 59.90           C  
ATOM    698  OG  SER A 101      -4.520  27.168  14.589  1.00 60.01           O  
ATOM    699  N   ASN A 102      -4.061  23.557  16.930  1.00 59.16           N  
ATOM    700  CA  ASN A 102      -4.032  22.690  18.108  1.00 58.76           C  
ATOM    701  C   ASN A 102      -3.868  21.207  17.772  1.00 58.48           C  
ATOM    702  O   ASN A 102      -4.379  20.334  18.483  1.00 58.40           O  
ATOM    703  CB  ASN A 102      -5.272  22.932  18.977  1.00 58.77           C  
ATOM    704  CG  ASN A 102      -5.275  24.308  19.617  1.00 58.50           C  
ATOM    705  OD1 ASN A 102      -4.434  24.617  20.462  1.00 58.26           O  
ATOM    706  ND2 ASN A 102      -6.228  25.142  19.221  1.00 58.00           N  
ATOM    707  N   VAL A 103      -3.142  20.932  16.690  1.00 58.09           N  
ATOM    708  CA  VAL A 103      -2.865  19.561  16.268  1.00 57.69           C  
ATOM    709  C   VAL A 103      -1.383  19.228  16.452  1.00 57.48           C  
ATOM    710  O   VAL A 103      -0.512  19.836  15.822  1.00 57.29           O  
ATOM    711  CB  VAL A 103      -3.309  19.298  14.808  1.00 57.68           C  
ATOM    712  CG1 VAL A 103      -3.046  17.846  14.416  1.00 57.57           C  
ATOM    713  CG2 VAL A 103      -4.783  19.630  14.631  1.00 57.65           C  
ATOM    714  N   ILE A 104      -1.118  18.261  17.327  1.00 57.30           N  
ATOM    715  CA  ILE A 104       0.243  17.834  17.649  1.00 57.08           C  
ATOM    716  C   ILE A 104       0.452  16.375  17.234  1.00 56.96           C  
ATOM    717  O   ILE A 104      -0.383  15.513  17.520  1.00 56.92           O  
ATOM    718  CB  ILE A 104       0.554  18.009  19.161  1.00 57.07           C  
ATOM    719  CG1 ILE A 104       0.155  19.415  19.637  1.00 57.15           C  
ATOM    720  CG2 ILE A 104       2.035  17.746  19.447  1.00 57.09           C  
ATOM    721  CD1 ILE A 104       0.015  19.561  21.145  1.00 56.83           C  
ATOM    722  N   THR A 105       1.564  16.112  16.550  1.00 56.82           N  
ATOM    723  CA  THR A 105       1.917  14.751  16.136  1.00 56.66           C  
ATOM    724  C   THR A 105       2.776  14.062  17.190  1.00 56.49           C  
ATOM    725  O   THR A 105       3.709  14.659  17.728  1.00 56.49           O  
ATOM    726  CB  THR A 105       2.652  14.723  14.776  1.00 56.61           C  
ATOM    727  OG1 THR A 105       3.785  15.601  14.818  1.00 56.74           O  
ATOM    728  CG2 THR A 105       1.722  15.153  13.653  1.00 56.42           C  
ATOM    729  N   LEU A 106       2.446  12.807  17.484  1.00 56.33           N  
ATOM    730  CA  LEU A 106       3.183  12.019  18.469  1.00 56.24           C  
ATOM    731  C   LEU A 106       3.627  10.681  17.884  1.00 56.25           C  
ATOM    732  O   LEU A 106       2.899  10.068  17.097  1.00 56.16           O  
ATOM    733  CB  LEU A 106       2.346  11.806  19.735  1.00 56.26           C  
ATOM    734  CG  LEU A 106       1.938  13.029  20.567  1.00 56.06           C  
ATOM    735  CD1 LEU A 106       0.972  12.623  21.669  1.00 55.81           C  
ATOM    736  CD2 LEU A 106       3.148  13.752  21.157  1.00 56.06           C  
ATOM    737  N   SER A 107       4.821  10.241  18.278  1.00 56.29           N  
ATOM    738  CA  SER A 107       5.456   9.045  17.717  1.00 56.33           C  
ATOM    739  C   SER A 107       5.475   7.855  18.678  1.00 56.41           C  
ATOM    740  O   SER A 107       5.590   8.023  19.892  1.00 56.32           O  
ATOM    741  CB  SER A 107       6.885   9.366  17.273  1.00 56.32           C  
ATOM    742  OG  SER A 107       7.537   8.218  16.752  1.00 56.25           O  
ATOM    743  N   THR A 108       5.384   6.658  18.103  1.00 56.59           N  
ATOM    744  CA  THR A 108       5.411   5.391  18.836  1.00 56.77           C  
ATOM    745  C   THR A 108       6.822   4.988  19.285  1.00 56.88           C  
ATOM    746  O   THR A 108       6.980   4.119  20.147  1.00 56.99           O  
ATOM    747  CB  THR A 108       4.753   4.266  17.985  1.00 56.79           C  
ATOM    748  OG1 THR A 108       3.360   4.175  18.308  1.00 57.00           O  
ATOM    749  CG2 THR A 108       5.413   2.902  18.207  1.00 56.96           C  
ATOM    750  N   LEU A 109       7.833   5.638  18.709  1.00 56.95           N  
ATOM    751  CA  LEU A 109       9.253   5.313  18.926  1.00 57.06           C  
ATOM    752  C   LEU A 109       9.573   4.533  20.211  1.00 57.13           C  
ATOM    753  O   LEU A 109      10.005   3.381  20.146  1.00 57.11           O  
ATOM    754  CB  LEU A 109      10.118   6.581  18.830  1.00 57.02           C  
ATOM    755  CG  LEU A 109      11.637   6.443  18.990  1.00 56.97           C  
ATOM    756  CD1 LEU A 109      12.218   5.445  17.994  1.00 56.83           C  
ATOM    757  CD2 LEU A 109      12.322   7.795  18.860  1.00 56.90           C  
ATOM    758  N   ARG A 110       9.367   5.167  21.365  1.00 57.23           N  
ATOM    759  CA  ARG A 110       9.629   4.529  22.657  1.00 57.24           C  
ATOM    760  C   ARG A 110       8.376   4.465  23.536  1.00 57.43           C  
ATOM    761  O   ARG A 110       8.456   4.493  24.768  1.00 57.50           O  
ATOM    762  CB  ARG A 110      10.793   5.214  23.386  1.00 57.17           C  
ATOM    763  CG  ARG A 110      10.648   6.717  23.578  1.00 56.69           C  
ATOM    764  CD  ARG A 110      11.870   7.289  24.275  1.00 55.82           C  
ATOM    765  NE  ARG A 110      11.851   8.748  24.337  1.00 55.17           N  
ATOM    766  CZ  ARG A 110      12.312   9.551  23.382  1.00 54.73           C  
ATOM    767  NH1 ARG A 110      12.829   9.046  22.270  1.00 54.57           N  
ATOM    768  NH2 ARG A 110      12.250  10.867  23.537  1.00 54.45           N  
ATOM    769  N   GLY A 111       7.222   4.368  22.883  1.00 57.56           N  
ATOM    770  CA  GLY A 111       5.943   4.253  23.568  1.00 57.68           C  
ATOM    771  C   GLY A 111       5.108   3.115  23.019  1.00 57.83           C  
ATOM    772  O   GLY A 111       3.927   3.296  22.713  1.00 57.93           O  
ATOM    773  N   ALA A 112       5.726   1.940  22.891  1.00 57.89           N  
ATOM    774  CA  ALA A 112       5.022   0.718  22.495  1.00 57.86           C  
ATOM    775  C   ALA A 112       4.056   0.261  23.593  1.00 57.86           C  
ATOM    776  O   ALA A 112       3.229  -0.632  23.382  1.00 57.89           O  
ATOM    777  CB  ALA A 112       6.021  -0.386  22.161  1.00 57.91           C  
ATOM    778  N   ASP A 113       4.174   0.894  24.760  1.00 57.75           N  
ATOM    779  CA  ASP A 113       3.315   0.635  25.915  1.00 57.65           C  
ATOM    780  C   ASP A 113       1.940   1.280  25.744  1.00 57.32           C  
ATOM    781  O   ASP A 113       0.956   0.835  26.340  1.00 57.23           O  
ATOM    782  CB  ASP A 113       3.987   1.166  27.184  1.00 57.83           C  
ATOM    783  CG  ASP A 113       5.461   0.806  27.257  1.00 58.37           C  
ATOM    784  OD1 ASP A 113       5.774  -0.396  27.413  1.00 59.05           O  
ATOM    785  OD2 ASP A 113       6.304   1.726  27.156  1.00 58.82           O  
ATOM    786  N   PHE A 114       1.891   2.338  24.938  1.00 56.98           N  
ATOM    787  CA  PHE A 114       0.646   3.004  24.564  1.00 56.54           C  
ATOM    788  C   PHE A 114      -0.180   2.123  23.625  1.00 56.35           C  
ATOM    789  O   PHE A 114      -1.412   2.116  23.688  1.00 56.33           O  
ATOM    790  CB  PHE A 114       0.954   4.355  23.901  1.00 56.48           C  
ATOM    791  CG  PHE A 114      -0.159   4.884  23.037  1.00 56.32           C  
ATOM    792  CD1 PHE A 114      -1.156   5.688  23.580  1.00 56.28           C  
ATOM    793  CD2 PHE A 114      -0.211   4.577  21.680  1.00 56.08           C  
ATOM    794  CE1 PHE A 114      -2.190   6.175  22.788  1.00 56.30           C  
ATOM    795  CE2 PHE A 114      -1.241   5.057  20.881  1.00 56.29           C  
ATOM    796  CZ  PHE A 114      -2.232   5.860  21.435  1.00 56.32           C  
ATOM    797  N   LYS A 115       0.514   1.389  22.757  1.00 56.08           N  
ATOM    798  CA  LYS A 115      -0.122   0.541  21.749  1.00 55.94           C  
ATOM    799  C   LYS A 115      -0.926  -0.604  22.356  1.00 55.90           C  
ATOM    800  O   LYS A 115      -1.909  -1.056  21.766  1.00 55.97           O  
ATOM    801  CB  LYS A 115       0.923  -0.007  20.776  1.00 55.86           C  
ATOM    802  CG  LYS A 115       1.443   1.021  19.778  1.00 55.52           C  
ATOM    803  CD  LYS A 115       2.757   0.585  19.144  1.00 55.07           C  
ATOM    804  CE  LYS A 115       2.552  -0.414  18.015  1.00 54.78           C  
ATOM    805  NZ  LYS A 115       3.845  -0.790  17.380  1.00 54.55           N  
ATOM    806  N   GLN A 116      -0.502  -1.063  23.531  1.00 55.77           N  
ATOM    807  CA  GLN A 116      -1.182  -2.146  24.240  1.00 55.65           C  
ATOM    808  C   GLN A 116      -2.348  -1.628  25.081  1.00 55.31           C  
ATOM    809  O   GLN A 116      -3.445  -2.195  25.052  1.00 55.25           O  
ATOM    810  CB  GLN A 116      -0.191  -2.918  25.121  1.00 55.78           C  
ATOM    811  CG  GLN A 116       0.882  -3.683  24.343  1.00 56.28           C  
ATOM    812  CD  GLN A 116       0.317  -4.828  23.519  1.00 56.82           C  
ATOM    813  OE1 GLN A 116       0.523  -4.894  22.306  1.00 57.09           O  
ATOM    814  NE2 GLN A 116      -0.405  -5.735  24.174  1.00 56.96           N  
ATOM    815  N   ALA A 117      -2.099  -0.544  25.815  1.00 54.90           N  
ATOM    816  CA  ALA A 117      -3.088   0.062  26.710  1.00 54.57           C  
ATOM    817  C   ALA A 117      -4.307   0.621  25.974  1.00 54.29           C  
ATOM    818  O   ALA A 117      -5.372   0.798  26.568  1.00 54.41           O  
ATOM    819  CB  ALA A 117      -2.434   1.152  27.556  1.00 54.58           C  
ATOM    820  N   TYR A 118      -4.142   0.895  24.685  1.00 53.88           N  
ATOM    821  CA  TYR A 118      -5.211   1.458  23.870  1.00 53.51           C  
ATOM    822  C   TYR A 118      -5.616   0.533  22.718  1.00 53.29           C  
ATOM    823  O   TYR A 118      -6.452   0.897  21.888  1.00 53.32           O  
ATOM    824  CB  TYR A 118      -4.807   2.844  23.356  1.00 53.54           C  
ATOM    825  CG  TYR A 118      -4.798   3.917  24.429  1.00 53.49           C  
ATOM    826  CD1 TYR A 118      -5.846   4.829  24.536  1.00 53.44           C  
ATOM    827  CD2 TYR A 118      -3.743   4.017  25.340  1.00 53.44           C  
ATOM    828  CE1 TYR A 118      -5.846   5.818  25.517  1.00 53.50           C  
ATOM    829  CE2 TYR A 118      -3.733   4.998  26.326  1.00 53.39           C  
ATOM    830  CZ  TYR A 118      -4.787   5.896  26.407  1.00 53.53           C  
ATOM    831  OH  TYR A 118      -4.786   6.871  27.377  1.00 53.44           O  
ATOM    832  N   GLY A 119      -5.021  -0.659  22.681  1.00 52.95           N  
ATOM    833  CA  GLY A 119      -5.386  -1.703  21.723  1.00 52.53           C  
ATOM    834  C   GLY A 119      -5.324  -1.309  20.259  1.00 52.23           C  
ATOM    835  O   GLY A 119      -6.313  -1.435  19.535  1.00 52.24           O  
ATOM    836  N   VAL A 120      -4.159  -0.836  19.824  1.00 51.92           N  
ATOM    837  CA  VAL A 120      -3.948  -0.442  18.426  1.00 51.63           C  
ATOM    838  C   VAL A 120      -2.764  -1.168  17.771  1.00 51.39           C  
ATOM    839  O   VAL A 120      -2.477  -0.954  16.593  1.00 51.39           O  
ATOM    840  CB  VAL A 120      -3.786   1.100  18.266  1.00 51.68           C  
ATOM    841  CG1 VAL A 120      -5.128   1.807  18.428  1.00 51.57           C  
ATOM    842  CG2 VAL A 120      -2.753   1.655  19.247  1.00 51.70           C  
ATOM    843  N   ALA A 121      -2.094  -2.028  18.536  1.00 51.19           N  
ATOM    844  CA  ALA A 121      -0.907  -2.743  18.057  1.00 50.94           C  
ATOM    845  C   ALA A 121      -1.242  -3.869  17.076  1.00 50.76           C  
ATOM    846  O   ALA A 121      -1.814  -4.893  17.460  1.00 50.61           O  
ATOM    847  CB  ALA A 121      -0.087  -3.276  19.235  1.00 50.84           C  
ATOM    848  N   ILE A 122      -0.881  -3.659  15.811  1.00 50.61           N  
ATOM    849  CA  ILE A 122      -1.025  -4.672  14.762  1.00 50.44           C  
ATOM    850  C   ILE A 122       0.105  -5.693  14.887  1.00 50.41           C  
ATOM    851  O   ILE A 122       1.280  -5.322  14.970  1.00 50.45           O  
ATOM    852  CB  ILE A 122      -0.998  -4.040  13.344  1.00 50.40           C  
ATOM    853  CG1 ILE A 122      -2.089  -2.972  13.200  1.00 50.31           C  
ATOM    854  CG2 ILE A 122      -1.145  -5.117  12.268  1.00 50.24           C  
ATOM    855  CD1 ILE A 122      -2.039  -2.192  11.893  1.00 49.72           C  
ATOM    856  N   THR A 123      -0.253  -6.976  14.893  1.00 50.29           N  
ATOM    857  CA  THR A 123       0.724  -8.042  15.108  1.00 50.28           C  
ATOM    858  C   THR A 123       0.758  -9.070  13.970  1.00 50.05           C  
ATOM    859  O   THR A 123       1.387 -10.122  14.098  1.00 50.09           O  
ATOM    860  CB  THR A 123       0.487  -8.765  16.461  1.00 50.34           C  
ATOM    861  OG1 THR A 123      -0.187  -7.889  17.372  1.00 50.67           O  
ATOM    862  CG2 THR A 123       1.810  -9.204  17.076  1.00 50.48           C  
ATOM    863  N   GLU A 124       0.091  -8.763  12.859  1.00 49.81           N  
ATOM    864  CA  GLU A 124       0.042  -9.685  11.718  1.00 49.57           C  
ATOM    865  C   GLU A 124       0.198  -9.002  10.364  1.00 49.20           C  
ATOM    866  O   GLU A 124      -0.111  -7.819  10.208  1.00 49.09           O  
ATOM    867  CB  GLU A 124      -1.249 -10.507  11.734  1.00 49.70           C  
ATOM    868  CG  GLU A 124      -1.234 -11.673  12.709  1.00 50.18           C  
ATOM    869  CD  GLU A 124      -2.244 -12.742  12.352  1.00 50.72           C  
ATOM    870  OE1 GLU A 124      -3.098 -13.056  13.205  1.00 51.07           O  
ATOM    871  OE2 GLU A 124      -2.185 -13.267  11.218  1.00 50.84           O  
ATOM    872  N   GLY A 125       0.679  -9.770   9.388  1.00 48.82           N  
ATOM    873  CA  GLY A 125       0.842  -9.287   8.022  1.00 48.20           C  
ATOM    874  C   GLY A 125       2.026  -8.354   7.856  1.00 47.83           C  
ATOM    875  O   GLY A 125       2.842  -8.212   8.771  1.00 47.73           O  
ATOM    876  N   PRO A 126       2.124  -7.703   6.682  1.00 47.56           N  
ATOM    877  CA  PRO A 126       3.211  -6.772   6.382  1.00 47.28           C  
ATOM    878  C   PRO A 126       3.178  -5.527   7.270  1.00 46.97           C  
ATOM    879  O   PRO A 126       4.158  -4.781   7.322  1.00 46.90           O  
ATOM    880  CB  PRO A 126       2.948  -6.383   4.922  1.00 47.30           C  
ATOM    881  CG  PRO A 126       2.060  -7.452   4.387  1.00 47.43           C  
ATOM    882  CD  PRO A 126       1.203  -7.840   5.541  1.00 47.49           C  
ATOM    883  N   LEU A 127       2.062  -5.324   7.966  1.00 46.63           N  
ATOM    884  CA  LEU A 127       1.865  -4.146   8.805  1.00 46.35           C  
ATOM    885  C   LEU A 127       2.206  -4.379  10.275  1.00 46.22           C  
ATOM    886  O   LEU A 127       2.132  -3.450  11.083  1.00 46.22           O  
ATOM    887  CB  LEU A 127       0.429  -3.628   8.667  1.00 46.41           C  
ATOM    888  CG  LEU A 127       0.096  -2.654   7.527  1.00 46.21           C  
ATOM    889  CD1 LEU A 127       0.404  -3.218   6.144  1.00 46.14           C  
ATOM    890  CD2 LEU A 127      -1.362  -2.247   7.617  1.00 45.90           C  
ATOM    891  N   ALA A 128       2.585  -5.610  10.619  1.00 45.91           N  
ATOM    892  CA  ALA A 128       2.962  -5.947  11.993  1.00 45.65           C  
ATOM    893  C   ALA A 128       4.007  -4.972  12.541  1.00 45.43           C  
ATOM    894  O   ALA A 128       4.977  -4.640  11.860  1.00 45.27           O  
ATOM    895  CB  ALA A 128       3.466  -7.380  12.076  1.00 45.66           C  
ATOM    896  N   GLY A 129       3.787  -4.507  13.769  1.00 45.25           N  
ATOM    897  CA  GLY A 129       4.649  -3.497  14.377  1.00 45.13           C  
ATOM    898  C   GLY A 129       4.153  -2.080  14.137  1.00 45.09           C  
ATOM    899  O   GLY A 129       4.620  -1.133  14.778  1.00 45.07           O  
ATOM    900  N   LEU A 130       3.216  -1.932  13.199  1.00 44.96           N  
ATOM    901  CA  LEU A 130       2.548  -0.654  12.973  1.00 44.85           C  
ATOM    902  C   LEU A 130       1.310  -0.520  13.854  1.00 44.80           C  
ATOM    903  O   LEU A 130       0.965  -1.434  14.610  1.00 44.83           O  
ATOM    904  CB  LEU A 130       2.158  -0.481  11.500  1.00 44.74           C  
ATOM    905  CG  LEU A 130       3.244  -0.249  10.449  1.00 44.54           C  
ATOM    906  CD1 LEU A 130       2.607  -0.201   9.069  1.00 44.59           C  
ATOM    907  CD2 LEU A 130       4.023   1.029  10.722  1.00 44.31           C  
ATOM    908  N   THR A 131       0.645   0.623  13.728  1.00 44.67           N  
ATOM    909  CA  THR A 131      -0.536   0.955  14.514  1.00 44.60           C  
ATOM    910  C   THR A 131      -1.800   0.879  13.649  1.00 44.60           C  
ATOM    911  O   THR A 131      -1.748   1.146  12.449  1.00 44.65           O  
ATOM    912  CB  THR A 131      -0.351   2.354  15.168  1.00 44.62           C  
ATOM    913  OG1 THR A 131       0.080   2.194  16.526  1.00 44.65           O  
ATOM    914  CG2 THR A 131      -1.619   3.160  15.150  1.00 44.32           C  
ATOM    915  N   ALA A 132      -2.922   0.486  14.253  1.00 44.58           N  
ATOM    916  CA  ALA A 132      -4.213   0.425  13.552  1.00 44.58           C  
ATOM    917  C   ALA A 132      -4.897   1.795  13.443  1.00 44.57           C  
ATOM    918  O   ALA A 132      -4.562   2.726  14.177  1.00 44.57           O  
ATOM    919  CB  ALA A 132      -5.136  -0.581  14.234  1.00 44.54           C  
ATOM    920  N   ARG A 133      -5.853   1.913  12.521  1.00 44.63           N  
ATOM    921  CA  ARG A 133      -6.641   3.138  12.384  1.00 44.58           C  
ATOM    922  C   ARG A 133      -7.754   3.171  13.429  1.00 44.83           C  
ATOM    923  O   ARG A 133      -8.600   2.273  13.479  1.00 44.81           O  
ATOM    924  CB  ARG A 133      -7.224   3.272  10.973  1.00 44.48           C  
ATOM    925  CG  ARG A 133      -7.879   4.623  10.684  1.00 43.74           C  
ATOM    926  CD  ARG A 133      -6.835   5.705  10.446  1.00 42.99           C  
ATOM    927  NE  ARG A 133      -7.419   7.033  10.282  1.00 41.86           N  
ATOM    928  CZ  ARG A 133      -7.674   7.879  11.279  1.00 41.57           C  
ATOM    929  NH1 ARG A 133      -7.410   7.546  12.537  1.00 40.77           N  
ATOM    930  NH2 ARG A 133      -8.202   9.066  11.015  1.00 41.39           N  
ATOM    931  N   ALA A 134      -7.740   4.214  14.257  1.00 45.02           N  
ATOM    932  CA  ALA A 134      -8.698   4.367  15.348  1.00 45.26           C  
ATOM    933  C   ALA A 134      -8.840   5.821  15.797  1.00 45.45           C  
ATOM    934  O   ALA A 134      -7.892   6.604  15.723  1.00 45.44           O  
ATOM    935  CB  ALA A 134      -8.300   3.484  16.534  1.00 45.20           C  
ATOM    936  N   VAL A 135     -10.037   6.171  16.258  1.00 45.73           N  
ATOM    937  CA  VAL A 135     -10.288   7.474  16.857  1.00 46.05           C  
ATOM    938  C   VAL A 135     -10.858   7.283  18.256  1.00 46.34           C  
ATOM    939  O   VAL A 135     -11.871   6.604  18.434  1.00 46.35           O  
ATOM    940  CB  VAL A 135     -11.253   8.340  16.006  1.00 46.09           C  
ATOM    941  CG1 VAL A 135     -11.601   9.643  16.734  1.00 45.92           C  
ATOM    942  CG2 VAL A 135     -10.644   8.646  14.644  1.00 45.93           C  
ATOM    943  N   VAL A 136     -10.186   7.872  19.242  1.00 46.71           N  
ATOM    944  CA  VAL A 136     -10.662   7.855  20.622  1.00 47.10           C  
ATOM    945  C   VAL A 136     -10.749   9.285  21.145  1.00 47.44           C  
ATOM    946  O   VAL A 136      -9.771  10.036  21.108  1.00 47.33           O  
ATOM    947  CB  VAL A 136      -9.762   6.989  21.546  1.00 47.11           C  
ATOM    948  CG1 VAL A 136     -10.252   7.049  22.993  1.00 47.06           C  
ATOM    949  CG2 VAL A 136      -9.721   5.543  21.064  1.00 46.96           C  
ATOM    950  N   VAL A 137     -11.933   9.655  21.622  1.00 47.97           N  
ATOM    951  CA  VAL A 137     -12.169  10.999  22.134  1.00 48.55           C  
ATOM    952  C   VAL A 137     -12.282  10.977  23.657  1.00 49.06           C  
ATOM    953  O   VAL A 137     -13.016  10.165  24.225  1.00 49.31           O  
ATOM    954  CB  VAL A 137     -13.426  11.640  21.500  1.00 48.47           C  
ATOM    955  CG1 VAL A 137     -13.523  13.108  21.872  1.00 48.46           C  
ATOM    956  CG2 VAL A 137     -13.398  11.489  19.982  1.00 48.55           C  
ATOM    957  N   LEU A 138     -11.533  11.866  24.305  1.00 49.59           N  
ATOM    958  CA  LEU A 138     -11.545  11.998  25.760  1.00 50.14           C  
ATOM    959  C   LEU A 138     -12.064  13.375  26.162  1.00 50.55           C  
ATOM    960  O   LEU A 138     -11.891  14.347  25.425  1.00 50.60           O  
ATOM    961  CB  LEU A 138     -10.135  11.803  26.330  1.00 50.08           C  
ATOM    962  CG  LEU A 138      -9.282  10.619  25.861  1.00 49.88           C  
ATOM    963  CD1 LEU A 138      -7.855  10.772  26.361  1.00 49.51           C  
ATOM    964  CD2 LEU A 138      -9.869   9.289  26.305  1.00 49.51           C  
ATOM    965  N   ASP A 139     -12.701  13.453  27.327  1.00 51.14           N  
ATOM    966  CA  ASP A 139     -13.134  14.741  27.872  1.00 51.74           C  
ATOM    967  C   ASP A 139     -12.018  15.388  28.703  1.00 52.11           C  
ATOM    968  O   ASP A 139     -10.874  14.918  28.686  1.00 52.19           O  
ATOM    969  CB  ASP A 139     -14.445  14.602  28.671  1.00 51.76           C  
ATOM    970  CG  ASP A 139     -14.330  13.649  29.858  1.00 51.92           C  
ATOM    971  OD1 ASP A 139     -15.388  13.241  30.385  1.00 51.69           O  
ATOM    972  OD2 ASP A 139     -13.201  13.312  30.275  1.00 52.36           O  
ATOM    973  N   GLY A 140     -12.353  16.461  29.419  1.00 52.50           N  
ATOM    974  CA  GLY A 140     -11.401  17.147  30.297  1.00 53.03           C  
ATOM    975  C   GLY A 140     -10.818  16.267  31.391  1.00 53.44           C  
ATOM    976  O   GLY A 140      -9.653  16.424  31.766  1.00 53.37           O  
ATOM    977  N   GLN A 141     -11.631  15.337  31.891  1.00 53.90           N  
ATOM    978  CA  GLN A 141     -11.225  14.420  32.957  1.00 54.41           C  
ATOM    979  C   GLN A 141     -10.824  13.040  32.417  1.00 54.79           C  
ATOM    980  O   GLN A 141     -10.902  12.034  33.131  1.00 54.84           O  
ATOM    981  CB  GLN A 141     -12.339  14.297  34.004  1.00 54.43           C  
ATOM    982  N   ASP A 142     -10.404  13.014  31.151  1.00 55.20           N  
ATOM    983  CA  ASP A 142      -9.871  11.816  30.480  1.00 55.58           C  
ATOM    984  C   ASP A 142     -10.808  10.600  30.474  1.00 55.70           C  
ATOM    985  O   ASP A 142     -10.361   9.447  30.547  1.00 55.63           O  
ATOM    986  CB  ASP A 142      -8.476  11.458  31.024  1.00 55.70           C  
ATOM    987  CG  ASP A 142      -7.430  12.526  30.716  1.00 56.20           C  
ATOM    988  OD1 ASP A 142      -7.713  13.445  29.913  1.00 56.42           O  
ATOM    989  OD2 ASP A 142      -6.316  12.441  31.279  1.00 56.92           O  
ATOM    990  N   ASN A 143     -12.107  10.871  30.377  1.00 55.82           N  
ATOM    991  CA  ASN A 143     -13.112   9.830  30.202  1.00 55.99           C  
ATOM    992  C   ASN A 143     -13.449   9.666  28.729  1.00 56.00           C  
ATOM    993  O   ASN A 143     -13.638  10.659  28.020  1.00 56.03           O  
ATOM    994  CB  ASN A 143     -14.377  10.157  30.998  1.00 56.03           C  
ATOM    995  CG  ASN A 143     -14.164  10.070  32.495  1.00 56.33           C  
ATOM    996  OD1 ASN A 143     -13.688   9.055  33.010  1.00 56.37           O  
ATOM    997  ND2 ASN A 143     -14.524  11.134  33.206  1.00 56.45           N  
ATOM    998  N   VAL A 144     -13.515   8.414  28.278  1.00 56.01           N  
ATOM    999  CA  VAL A 144     -13.808   8.098  26.879  1.00 56.04           C  
ATOM   1000  C   VAL A 144     -15.265   8.430  26.564  1.00 56.10           C  
ATOM   1001  O   VAL A 144     -16.182   7.932  27.221  1.00 56.14           O  
ATOM   1002  CB  VAL A 144     -13.501   6.609  26.537  1.00 56.05           C  
ATOM   1003  CG1 VAL A 144     -13.788   6.309  25.066  1.00 55.98           C  
ATOM   1004  CG2 VAL A 144     -12.056   6.264  26.868  1.00 55.98           C  
ATOM   1005  N   ILE A 145     -15.461   9.287  25.565  1.00 56.16           N  
ATOM   1006  CA  ILE A 145     -16.800   9.715  25.153  1.00 56.14           C  
ATOM   1007  C   ILE A 145     -17.135   9.273  23.724  1.00 56.07           C  
ATOM   1008  O   ILE A 145     -18.298   9.300  23.315  1.00 56.15           O  
ATOM   1009  CB  ILE A 145     -17.009  11.245  25.336  1.00 56.16           C  
ATOM   1010  CG1 ILE A 145     -15.895  12.041  24.642  1.00 56.18           C  
ATOM   1011  CG2 ILE A 145     -17.095  11.592  26.827  1.00 56.11           C  
ATOM   1012  CD1 ILE A 145     -16.153  13.539  24.554  1.00 56.02           C  
ATOM   1013  N   TYR A 146     -16.107   8.873  22.977  1.00 55.95           N  
ATOM   1014  CA  TYR A 146     -16.272   8.247  21.664  1.00 55.81           C  
ATOM   1015  C   TYR A 146     -15.053   7.394  21.336  1.00 55.83           C  
ATOM   1016  O   TYR A 146     -13.917   7.836  21.511  1.00 55.84           O  
ATOM   1017  CB  TYR A 146     -16.499   9.292  20.561  1.00 55.77           C  
ATOM   1018  CG  TYR A 146     -16.664   8.694  19.176  1.00 55.38           C  
ATOM   1019  CD1 TYR A 146     -17.889   8.168  18.762  1.00 55.18           C  
ATOM   1020  CD2 TYR A 146     -15.592   8.647  18.283  1.00 54.81           C  
ATOM   1021  CE1 TYR A 146     -18.041   7.612  17.496  1.00 54.94           C  
ATOM   1022  CE2 TYR A 146     -15.735   8.094  17.015  1.00 54.63           C  
ATOM   1023  CZ  TYR A 146     -16.960   7.580  16.629  1.00 54.65           C  
ATOM   1024  OH  TYR A 146     -17.105   7.033  15.377  1.00 54.22           O  
ATOM   1025  N   SER A 147     -15.299   6.175  20.861  1.00 55.87           N  
ATOM   1026  CA  SER A 147     -14.225   5.281  20.433  1.00 55.89           C  
ATOM   1027  C   SER A 147     -14.624   4.476  19.202  1.00 55.87           C  
ATOM   1028  O   SER A 147     -15.672   3.830  19.185  1.00 55.84           O  
ATOM   1029  CB  SER A 147     -13.810   4.340  21.567  1.00 55.94           C  
ATOM   1030  OG  SER A 147     -14.710   3.253  21.701  1.00 55.97           O  
ATOM   1031  N   GLU A 148     -13.779   4.522  18.177  1.00 55.89           N  
ATOM   1032  CA  GLU A 148     -14.007   3.752  16.963  1.00 55.92           C  
ATOM   1033  C   GLU A 148     -12.719   3.099  16.469  1.00 56.09           C  
ATOM   1034  O   GLU A 148     -11.688   3.758  16.336  1.00 55.97           O  
ATOM   1035  CB  GLU A 148     -14.618   4.629  15.867  1.00 55.78           C  
ATOM   1036  CG  GLU A 148     -15.154   3.844  14.674  1.00 55.53           C  
ATOM   1037  CD  GLU A 148     -15.426   4.712  13.457  1.00 55.36           C  
ATOM   1038  OE1 GLU A 148     -15.449   5.954  13.591  1.00 55.51           O  
ATOM   1039  OE2 GLU A 148     -15.617   4.146  12.359  1.00 55.14           O  
ATOM   1040  N   LEU A 149     -12.791   1.795  16.224  1.00 56.34           N  
ATOM   1041  CA  LEU A 149     -11.707   1.056  15.594  1.00 56.58           C  
ATOM   1042  C   LEU A 149     -12.171   0.630  14.208  1.00 56.76           C  
ATOM   1043  O   LEU A 149     -13.060  -0.215  14.070  1.00 56.78           O  
ATOM   1044  CB  LEU A 149     -11.305  -0.150  16.451  1.00 56.61           C  
ATOM   1045  CG  LEU A 149     -10.294  -1.168  15.909  1.00 56.81           C  
ATOM   1046  CD1 LEU A 149      -9.274  -1.542  16.974  1.00 57.04           C  
ATOM   1047  CD2 LEU A 149     -11.000  -2.411  15.381  1.00 57.11           C  
ATOM   1048  N   VAL A 150     -11.580   1.238  13.183  1.00 57.05           N  
ATOM   1049  CA  VAL A 150     -11.967   0.967  11.802  1.00 57.32           C  
ATOM   1050  C   VAL A 150     -11.438  -0.400  11.378  1.00 57.53           C  
ATOM   1051  O   VAL A 150     -10.239  -0.673  11.483  1.00 57.51           O  
ATOM   1052  CB  VAL A 150     -11.476   2.063  10.824  1.00 57.28           C  
ATOM   1053  CG1 VAL A 150     -12.223   1.967   9.503  1.00 57.32           C  
ATOM   1054  CG2 VAL A 150     -11.667   3.446  11.423  1.00 57.30           C  
ATOM   1055  N   ASN A 151     -12.349  -1.249  10.907  1.00 57.85           N  
ATOM   1056  CA  ASN A 151     -12.018  -2.615  10.501  1.00 58.13           C  
ATOM   1057  C   ASN A 151     -11.423  -2.717   9.092  1.00 58.28           C  
ATOM   1058  O   ASN A 151     -11.137  -3.815   8.608  1.00 58.27           O  
ATOM   1059  CB  ASN A 151     -13.241  -3.531  10.655  1.00 58.17           C  
ATOM   1060  CG  ASN A 151     -13.448  -4.006  12.092  1.00 58.38           C  
ATOM   1061  OD1 ASN A 151     -13.470  -5.209  12.359  1.00 58.37           O  
ATOM   1062  ND2 ASN A 151     -13.597  -3.064  13.021  1.00 58.27           N  
ATOM   1063  N   GLU A 152     -11.243  -1.565   8.445  1.00 58.51           N  
ATOM   1064  CA  GLU A 152     -10.541  -1.470   7.163  1.00 58.75           C  
ATOM   1065  C   GLU A 152      -9.593  -0.262   7.164  1.00 58.72           C  
ATOM   1066  O   GLU A 152     -10.033   0.884   7.260  1.00 58.77           O  
ATOM   1067  CB  GLU A 152     -11.536  -1.415   5.994  1.00 58.76           C  
ATOM   1068  CG  GLU A 152     -10.923  -1.094   4.625  1.00 59.44           C  
ATOM   1069  CD  GLU A 152      -9.744  -1.986   4.265  1.00 60.18           C  
ATOM   1070  OE1 GLU A 152      -9.960  -3.178   3.959  1.00 60.63           O  
ATOM   1071  OE2 GLU A 152      -8.600  -1.483   4.283  1.00 60.35           O  
ATOM   1072  N   ILE A 153      -8.294  -0.542   7.050  1.00 58.73           N  
ATOM   1073  CA  ILE A 153      -7.224   0.460   7.202  1.00 58.71           C  
ATOM   1074  C   ILE A 153      -7.261   1.589   6.160  1.00 58.62           C  
ATOM   1075  O   ILE A 153      -6.879   2.726   6.451  1.00 58.61           O  
ATOM   1076  CB  ILE A 153      -5.822  -0.229   7.254  1.00 58.77           C  
ATOM   1077  CG1 ILE A 153      -5.497  -0.686   8.681  1.00 58.89           C  
ATOM   1078  CG2 ILE A 153      -4.709   0.691   6.756  1.00 58.93           C  
ATOM   1079  CD1 ILE A 153      -6.156  -1.994   9.096  1.00 59.20           C  
ATOM   1080  N   THR A 154      -7.732   1.272   4.959  1.00 58.51           N  
ATOM   1081  CA  THR A 154      -7.856   2.257   3.886  1.00 58.35           C  
ATOM   1082  C   THR A 154      -9.151   3.072   3.992  1.00 58.22           C  
ATOM   1083  O   THR A 154      -9.426   3.928   3.145  1.00 58.23           O  
ATOM   1084  CB  THR A 154      -7.788   1.580   2.500  1.00 58.37           C  
ATOM   1085  OG1 THR A 154      -8.694   0.471   2.466  1.00 58.33           O  
ATOM   1086  CG2 THR A 154      -6.378   1.085   2.210  1.00 58.48           C  
ATOM   1087  N   THR A 155      -9.931   2.809   5.039  1.00 57.96           N  
ATOM   1088  CA  THR A 155     -11.242   3.432   5.222  1.00 57.82           C  
ATOM   1089  C   THR A 155     -11.250   4.505   6.320  1.00 57.56           C  
ATOM   1090  O   THR A 155     -10.587   4.364   7.351  1.00 57.49           O  
ATOM   1091  CB  THR A 155     -12.337   2.354   5.462  1.00 57.91           C  
ATOM   1092  OG1 THR A 155     -12.659   1.721   4.216  1.00 58.25           O  
ATOM   1093  CG2 THR A 155     -13.608   2.956   6.051  1.00 58.13           C  
ATOM   1094  N   GLU A 156     -12.009   5.572   6.074  1.00 57.23           N  
ATOM   1095  CA  GLU A 156     -12.129   6.710   6.988  1.00 56.92           C  
ATOM   1096  C   GLU A 156     -13.027   6.411   8.190  1.00 56.52           C  
ATOM   1097  O   GLU A 156     -14.052   5.742   8.046  1.00 56.65           O  
ATOM   1098  CB  GLU A 156     -12.682   7.930   6.243  1.00 57.01           C  
ATOM   1099  CG  GLU A 156     -11.770   8.489   5.163  1.00 57.59           C  
ATOM   1100  CD  GLU A 156     -10.735   9.455   5.707  1.00 58.81           C  
ATOM   1101  OE1 GLU A 156      -9.946   9.059   6.594  1.00 58.99           O  
ATOM   1102  OE2 GLU A 156     -10.707  10.614   5.236  1.00 59.59           O  
ATOM   1103  N   PRO A 157     -12.643   6.909   9.380  1.00 56.06           N  
ATOM   1104  CA  PRO A 157     -13.487   6.804  10.572  1.00 55.72           C  
ATOM   1105  C   PRO A 157     -14.607   7.849  10.604  1.00 55.36           C  
ATOM   1106  O   PRO A 157     -14.541   8.852   9.889  1.00 55.34           O  
ATOM   1107  CB  PRO A 157     -12.504   7.042  11.718  1.00 55.76           C  
ATOM   1108  CG  PRO A 157     -11.422   7.849  11.127  1.00 55.88           C  
ATOM   1109  CD  PRO A 157     -11.312   7.459   9.691  1.00 55.97           C  
ATOM   1110  N   ASN A 158     -15.617   7.605  11.437  1.00 54.90           N  
ATOM   1111  CA  ASN A 158     -16.777   8.487  11.555  1.00 54.51           C  
ATOM   1112  C   ASN A 158     -16.424   9.808  12.244  1.00 54.26           C  
ATOM   1113  O   ASN A 158     -16.571   9.956  13.463  1.00 54.02           O  
ATOM   1114  CB  ASN A 158     -17.921   7.769  12.284  1.00 54.50           C  
ATOM   1115  CG  ASN A 158     -19.278   8.430  12.068  1.00 54.44           C  
ATOM   1116  OD1 ASN A 158     -19.376   9.600  11.691  1.00 54.69           O  
ATOM   1117  ND2 ASN A 158     -20.340   7.673  12.323  1.00 54.11           N  
ATOM   1118  N   TYR A 159     -15.955  10.759  11.440  1.00 54.03           N  
ATOM   1119  CA  TYR A 159     -15.550  12.078  11.923  1.00 53.83           C  
ATOM   1120  C   TYR A 159     -16.720  12.855  12.517  1.00 53.65           C  
ATOM   1121  O   TYR A 159     -16.576  13.513  13.552  1.00 53.62           O  
ATOM   1122  CB  TYR A 159     -14.911  12.891  10.793  1.00 53.84           C  
ATOM   1123  CG  TYR A 159     -13.630  12.307  10.236  1.00 53.91           C  
ATOM   1124  CD1 TYR A 159     -13.448  12.170   8.860  1.00 54.09           C  
ATOM   1125  CD2 TYR A 159     -12.602  11.888  11.082  1.00 53.94           C  
ATOM   1126  CE1 TYR A 159     -12.270  11.637   8.341  1.00 54.36           C  
ATOM   1127  CE2 TYR A 159     -11.422  11.361  10.574  1.00 54.22           C  
ATOM   1128  CZ  TYR A 159     -11.264  11.235   9.205  1.00 54.51           C  
ATOM   1129  OH  TYR A 159     -10.099  10.705   8.702  1.00 55.07           O  
ATOM   1130  N   ASP A 160     -17.874  12.761  11.855  1.00 53.44           N  
ATOM   1131  CA  ASP A 160     -19.085  13.473  12.258  1.00 53.19           C  
ATOM   1132  C   ASP A 160     -19.524  13.077  13.665  1.00 52.93           C  
ATOM   1133  O   ASP A 160     -19.894  13.935  14.465  1.00 52.87           O  
ATOM   1134  CB  ASP A 160     -20.221  13.224  11.257  1.00 53.28           C  
ATOM   1135  CG  ASP A 160     -19.761  13.322   9.810  1.00 53.71           C  
ATOM   1136  OD1 ASP A 160     -20.155  14.290   9.124  1.00 53.89           O  
ATOM   1137  OD2 ASP A 160     -19.002  12.433   9.361  1.00 54.26           O  
ATOM   1138  N   ALA A 161     -19.473  11.777  13.957  1.00 52.70           N  
ATOM   1139  CA  ALA A 161     -19.833  11.257  15.278  1.00 52.45           C  
ATOM   1140  C   ALA A 161     -18.802  11.646  16.331  1.00 52.26           C  
ATOM   1141  O   ALA A 161     -19.158  11.924  17.477  1.00 52.23           O  
ATOM   1142  CB  ALA A 161     -20.005   9.746  15.232  1.00 52.38           C  
ATOM   1143  N   ALA A 162     -17.531  11.663  15.932  1.00 52.14           N  
ATOM   1144  CA  ALA A 162     -16.438  12.058  16.816  1.00 52.07           C  
ATOM   1145  C   ALA A 162     -16.571  13.521  17.234  1.00 52.17           C  
ATOM   1146  O   ALA A 162     -16.446  13.843  18.417  1.00 52.07           O  
ATOM   1147  CB  ALA A 162     -15.095  11.808  16.153  1.00 51.97           C  
ATOM   1148  N   LEU A 163     -16.839  14.392  16.261  1.00 52.22           N  
ATOM   1149  CA  LEU A 163     -17.053  15.817  16.518  1.00 52.34           C  
ATOM   1150  C   LEU A 163     -18.291  16.069  17.376  1.00 52.46           C  
ATOM   1151  O   LEU A 163     -18.274  16.935  18.254  1.00 52.50           O  
ATOM   1152  CB  LEU A 163     -17.172  16.597  15.203  1.00 52.32           C  
ATOM   1153  CG  LEU A 163     -15.943  16.783  14.309  1.00 52.32           C  
ATOM   1154  CD1 LEU A 163     -16.363  17.403  12.986  1.00 52.46           C  
ATOM   1155  CD2 LEU A 163     -14.859  17.628  14.978  1.00 52.06           C  
ATOM   1156  N   ALA A 164     -19.352  15.303  17.119  1.00 52.59           N  
ATOM   1157  CA  ALA A 164     -20.631  15.446  17.823  1.00 52.78           C  
ATOM   1158  C   ALA A 164     -20.526  15.188  19.326  1.00 52.92           C  
ATOM   1159  O   ALA A 164     -21.257  15.795  20.111  1.00 52.98           O  
ATOM   1160  CB  ALA A 164     -21.685  14.533  17.204  1.00 52.74           C  
ATOM   1161  N   ALA A 165     -19.621  14.289  19.712  1.00 53.07           N  
ATOM   1162  CA  ALA A 165     -19.405  13.943  21.117  1.00 53.28           C  
ATOM   1163  C   ALA A 165     -18.753  15.078  21.916  1.00 53.43           C  
ATOM   1164  O   ALA A 165     -18.858  15.119  23.142  1.00 53.42           O  
ATOM   1165  CB  ALA A 165     -18.584  12.661  21.229  1.00 53.20           C  
ATOM   1166  N   LEU A 166     -18.084  15.993  21.216  1.00 53.69           N  
ATOM   1167  CA  LEU A 166     -17.489  17.175  21.845  1.00 53.94           C  
ATOM   1168  C   LEU A 166     -18.524  18.259  22.137  1.00 54.07           C  
ATOM   1169  O   LEU A 166     -18.324  19.090  23.028  1.00 54.13           O  
ATOM   1170  CB  LEU A 166     -16.368  17.755  20.979  1.00 53.94           C  
ATOM   1171  CG  LEU A 166     -14.975  17.135  21.093  1.00 54.01           C  
ATOM   1172  CD1 LEU A 166     -14.782  16.028  20.076  1.00 54.03           C  
ATOM   1173  CD2 LEU A 166     -13.930  18.208  20.885  1.00 54.49           C  
ATOM   1174  N   LYS A 167     -19.619  18.245  21.376  1.00 54.22           N  
ATOM   1175  CA  LYS A 167     -20.702  19.218  21.519  1.00 54.30           C  
ATOM   1176  C   LYS A 167     -21.523  18.958  22.778  1.00 54.44           C  
ATOM   1177  O   LYS A 167     -22.189  19.857  23.294  1.00 54.60           O  
ATOM   1178  CB  LYS A 167     -21.610  19.189  20.286  1.00 54.27           C  
TER    1179      LYS A 167                                                      
ATOM   1180  N   THR B   2      28.761  -2.623  28.602  1.00 64.38           N  
ATOM   1181  CA  THR B   2      27.906  -1.548  28.018  1.00 64.42           C  
ATOM   1182  C   THR B   2      28.743  -0.324  27.643  1.00 64.30           C  
ATOM   1183  O   THR B   2      29.346   0.324  28.504  1.00 64.30           O  
ATOM   1184  CB  THR B   2      26.753  -1.161  28.977  1.00 64.49           C  
ATOM   1185  OG1 THR B   2      25.907  -2.299  29.186  1.00 64.71           O  
ATOM   1186  CG2 THR B   2      25.919  -0.018  28.407  1.00 64.60           C  
ATOM   1187  N   GLN B   3      28.771  -0.027  26.345  1.00 64.14           N  
ATOM   1188  CA  GLN B   3      29.535   1.099  25.805  1.00 63.95           C  
ATOM   1189  C   GLN B   3      28.837   2.440  26.037  1.00 63.69           C  
ATOM   1190  O   GLN B   3      27.710   2.485  26.536  1.00 63.71           O  
ATOM   1191  CB  GLN B   3      29.815   0.896  24.310  1.00 63.97           C  
ATOM   1192  CG  GLN B   3      28.583   0.562  23.467  1.00 64.20           C  
ATOM   1193  CD  GLN B   3      28.421  -0.926  23.198  1.00 64.43           C  
ATOM   1194  OE1 GLN B   3      29.384  -1.692  23.257  1.00 64.62           O  
ATOM   1195  NE2 GLN B   3      27.198  -1.338  22.885  1.00 64.40           N  
ATOM   1196  N   THR B   4      29.521   3.524  25.678  1.00 63.43           N  
ATOM   1197  CA  THR B   4      28.983   4.879  25.809  1.00 63.16           C  
ATOM   1198  C   THR B   4      29.485   5.760  24.663  1.00 62.96           C  
ATOM   1199  O   THR B   4      30.685   5.802  24.379  1.00 62.92           O  
ATOM   1200  CB  THR B   4      29.358   5.518  27.174  1.00 63.20           C  
ATOM   1201  OG1 THR B   4      29.044   4.612  28.238  1.00 63.22           O  
ATOM   1202  CG2 THR B   4      28.601   6.827  27.398  1.00 63.26           C  
ATOM   1203  N   VAL B   5      28.555   6.447  24.002  1.00 62.71           N  
ATOM   1204  CA  VAL B   5      28.891   7.375  22.918  1.00 62.53           C  
ATOM   1205  C   VAL B   5      28.391   8.792  23.229  1.00 62.50           C  
ATOM   1206  O   VAL B   5      27.883   9.050  24.323  1.00 62.45           O  
ATOM   1207  CB  VAL B   5      28.364   6.892  21.530  1.00 62.44           C  
ATOM   1208  CG1 VAL B   5      29.035   5.586  21.114  1.00 62.42           C  
ATOM   1209  CG2 VAL B   5      26.846   6.760  21.524  1.00 62.40           C  
ATOM   1210  N   HIS B   6      28.544   9.701  22.269  1.00 62.44           N  
ATOM   1211  CA  HIS B   6      28.131  11.088  22.451  1.00 62.51           C  
ATOM   1212  C   HIS B   6      27.308  11.606  21.280  1.00 62.58           C  
ATOM   1213  O   HIS B   6      27.645  11.370  20.118  1.00 62.62           O  
ATOM   1214  CB  HIS B   6      29.346  12.000  22.653  1.00 62.45           C  
ATOM   1215  CG  HIS B   6      30.225  11.597  23.794  1.00 62.47           C  
ATOM   1216  ND1 HIS B   6      29.852  11.747  25.112  1.00 62.37           N  
ATOM   1217  CD2 HIS B   6      31.466  11.055  23.815  1.00 62.49           C  
ATOM   1218  CE1 HIS B   6      30.822  11.312  25.895  1.00 62.32           C  
ATOM   1219  NE2 HIS B   6      31.813  10.887  25.133  1.00 62.50           N  
ATOM   1220  N   PHE B   7      26.225  12.308  21.598  1.00 62.62           N  
ATOM   1221  CA  PHE B   7      25.499  13.085  20.603  1.00 62.67           C  
ATOM   1222  C   PHE B   7      25.749  14.563  20.877  1.00 62.70           C  
ATOM   1223  O   PHE B   7      25.289  15.100  21.889  1.00 62.68           O  
ATOM   1224  CB  PHE B   7      24.000  12.765  20.623  1.00 62.67           C  
ATOM   1225  CG  PHE B   7      23.207  13.510  19.583  1.00 62.67           C  
ATOM   1226  CD1 PHE B   7      23.227  13.104  18.250  1.00 62.67           C  
ATOM   1227  CD2 PHE B   7      22.444  14.618  19.934  1.00 62.78           C  
ATOM   1228  CE1 PHE B   7      22.499  13.792  17.283  1.00 62.76           C  
ATOM   1229  CE2 PHE B   7      21.712  15.311  18.975  1.00 63.09           C  
ATOM   1230  CZ  PHE B   7      21.740  14.897  17.645  1.00 63.01           C  
ATOM   1231  N   GLN B   8      26.498  15.201  19.977  1.00 62.77           N  
ATOM   1232  CA  GLN B   8      26.889  16.614  20.101  1.00 62.86           C  
ATOM   1233  C   GLN B   8      27.527  16.941  21.460  1.00 62.75           C  
ATOM   1234  O   GLN B   8      27.277  18.003  22.038  1.00 62.75           O  
ATOM   1235  CB  GLN B   8      25.696  17.541  19.819  1.00 62.93           C  
ATOM   1236  CG  GLN B   8      25.212  17.530  18.375  1.00 63.31           C  
ATOM   1237  CD  GLN B   8      23.972  18.383  18.162  1.00 63.77           C  
ATOM   1238  OE1 GLN B   8      23.006  18.305  18.924  1.00 64.02           O  
ATOM   1239  NE2 GLN B   8      23.991  19.199  17.114  1.00 63.87           N  
ATOM   1240  N   GLY B   9      28.346  16.019  21.962  1.00 62.63           N  
ATOM   1241  CA  GLY B   9      29.003  16.183  23.258  1.00 62.37           C  
ATOM   1242  C   GLY B   9      28.296  15.484  24.407  1.00 62.18           C  
ATOM   1243  O   GLY B   9      28.946  15.017  25.346  1.00 62.18           O  
ATOM   1244  N   ASN B  10      26.967  15.414  24.333  1.00 61.97           N  
ATOM   1245  CA  ASN B  10      26.155  14.782  25.377  1.00 61.77           C  
ATOM   1246  C   ASN B  10      26.259  13.258  25.386  1.00 61.61           C  
ATOM   1247  O   ASN B  10      26.108  12.622  24.341  1.00 61.61           O  
ATOM   1248  CB  ASN B  10      24.687  15.217  25.267  1.00 61.75           C  
ATOM   1249  CG  ASN B  10      24.370  16.426  26.129  1.00 61.82           C  
ATOM   1250  OD1 ASN B  10      24.528  16.393  27.350  1.00 62.13           O  
ATOM   1251  ND2 ASN B  10      23.910  17.499  25.497  1.00 61.84           N  
ATOM   1252  N   PRO B  11      26.515  12.670  26.573  1.00 61.47           N  
ATOM   1253  CA  PRO B  11      26.667  11.221  26.742  1.00 61.32           C  
ATOM   1254  C   PRO B  11      25.412  10.437  26.363  1.00 61.16           C  
ATOM   1255  O   PRO B  11      24.296  10.847  26.688  1.00 61.19           O  
ATOM   1256  CB  PRO B  11      26.954  11.066  28.242  1.00 61.35           C  
ATOM   1257  CG  PRO B  11      26.443  12.322  28.868  1.00 61.43           C  
ATOM   1258  CD  PRO B  11      26.686  13.386  27.851  1.00 61.47           C  
ATOM   1259  N   VAL B  12      25.612   9.321  25.669  1.00 60.95           N  
ATOM   1260  CA  VAL B  12      24.521   8.453  25.238  1.00 60.68           C  
ATOM   1261  C   VAL B  12      24.870   7.005  25.580  1.00 60.44           C  
ATOM   1262  O   VAL B  12      25.879   6.474  25.113  1.00 60.41           O  
ATOM   1263  CB  VAL B  12      24.243   8.597  23.713  1.00 60.73           C  
ATOM   1264  CG1 VAL B  12      23.279   7.524  23.225  1.00 60.76           C  
ATOM   1265  CG2 VAL B  12      23.702   9.983  23.384  1.00 60.70           C  
ATOM   1266  N   SER B  13      24.036   6.376  26.403  1.00 60.11           N  
ATOM   1267  CA  SER B  13      24.232   4.980  26.776  1.00 59.86           C  
ATOM   1268  C   SER B  13      23.783   4.055  25.649  1.00 59.58           C  
ATOM   1269  O   SER B  13      22.664   4.179  25.146  1.00 59.59           O  
ATOM   1270  CB  SER B  13      23.478   4.658  28.069  1.00 59.90           C  
ATOM   1271  OG  SER B  13      23.652   3.301  28.443  1.00 60.25           O  
ATOM   1272  N   VAL B  14      24.666   3.143  25.247  1.00 59.25           N  
ATOM   1273  CA  VAL B  14      24.355   2.160  24.207  1.00 58.94           C  
ATOM   1274  C   VAL B  14      24.420   0.744  24.780  1.00 58.81           C  
ATOM   1275  O   VAL B  14      25.484   0.281  25.194  1.00 58.77           O  
ATOM   1276  CB  VAL B  14      25.295   2.288  22.979  1.00 58.89           C  
ATOM   1277  CG1 VAL B  14      24.962   1.233  21.932  1.00 58.79           C  
ATOM   1278  CG2 VAL B  14      25.197   3.671  22.370  1.00 58.74           C  
ATOM   1279  N   ALA B  15      23.273   0.070  24.793  1.00 58.64           N  
ATOM   1280  CA  ALA B  15      23.151  -1.266  25.380  1.00 58.47           C  
ATOM   1281  C   ALA B  15      23.731  -2.354  24.482  1.00 58.32           C  
ATOM   1282  O   ALA B  15      23.665  -2.261  23.255  1.00 58.13           O  
ATOM   1283  CB  ALA B  15      21.693  -1.571  25.711  1.00 58.41           C  
ATOM   1284  N   GLY B  16      24.288  -3.386  25.113  1.00 58.23           N  
ATOM   1285  CA  GLY B  16      24.882  -4.514  24.403  1.00 58.00           C  
ATOM   1286  C   GLY B  16      26.360  -4.322  24.126  1.00 57.86           C  
ATOM   1287  O   GLY B  16      26.995  -3.418  24.679  1.00 57.83           O  
ATOM   1288  N   LYS B  17      26.902  -5.183  23.267  1.00 57.72           N  
ATOM   1289  CA  LYS B  17      28.308  -5.137  22.872  1.00 57.61           C  
ATOM   1290  C   LYS B  17      28.430  -5.378  21.371  1.00 57.56           C  
ATOM   1291  O   LYS B  17      27.960  -6.401  20.859  1.00 57.52           O  
ATOM   1292  CB  LYS B  17      29.121  -6.182  23.649  1.00 57.63           C  
ATOM   1293  CG  LYS B  17      30.591  -6.285  23.247  1.00 57.52           C  
ATOM   1294  N   LEU B  18      29.061  -4.434  20.675  1.00 57.42           N  
ATOM   1295  CA  LEU B  18      29.258  -4.540  19.232  1.00 57.43           C  
ATOM   1296  C   LEU B  18      30.194  -5.704  18.919  1.00 57.40           C  
ATOM   1297  O   LEU B  18      31.274  -5.805  19.511  1.00 57.44           O  
ATOM   1298  CB  LEU B  18      29.815  -3.232  18.652  1.00 57.42           C  
ATOM   1299  CG  LEU B  18      29.476  -2.868  17.198  1.00 57.51           C  
ATOM   1300  CD1 LEU B  18      29.803  -1.415  16.912  1.00 57.69           C  
ATOM   1301  CD2 LEU B  18      30.186  -3.755  16.189  1.00 57.85           C  
ATOM   1302  N   PRO B  19      29.772  -6.599  18.002  1.00 57.32           N  
ATOM   1303  CA  PRO B  19      30.594  -7.725  17.568  1.00 57.32           C  
ATOM   1304  C   PRO B  19      32.013  -7.299  17.199  1.00 57.33           C  
ATOM   1305  O   PRO B  19      32.202  -6.431  16.346  1.00 57.30           O  
ATOM   1306  CB  PRO B  19      29.847  -8.260  16.334  1.00 57.27           C  
ATOM   1307  CG  PRO B  19      28.726  -7.290  16.071  1.00 57.34           C  
ATOM   1308  CD  PRO B  19      28.442  -6.640  17.376  1.00 57.28           C  
ATOM   1309  N   GLN B  20      32.990  -7.909  17.862  1.00 57.34           N  
ATOM   1310  CA  GLN B  20      34.403  -7.614  17.651  1.00 57.35           C  
ATOM   1311  C   GLN B  20      34.894  -8.332  16.394  1.00 57.26           C  
ATOM   1312  O   GLN B  20      34.216  -9.227  15.889  1.00 57.28           O  
ATOM   1313  CB  GLN B  20      35.203  -8.078  18.872  1.00 57.40           C  
ATOM   1314  CG  GLN B  20      36.255  -7.097  19.365  1.00 57.74           C  
ATOM   1315  CD  GLN B  20      35.668  -5.990  20.226  1.00 58.01           C  
ATOM   1316  OE1 GLN B  20      35.007  -5.081  19.725  1.00 58.29           O  
ATOM   1317  NE2 GLN B  20      35.916  -6.061  21.529  1.00 57.98           N  
ATOM   1318  N   ILE B  21      36.063  -7.940  15.889  1.00 57.19           N  
ATOM   1319  CA  ILE B  21      36.672  -8.626  14.745  1.00 57.10           C  
ATOM   1320  C   ILE B  21      37.022 -10.062  15.136  1.00 57.07           C  
ATOM   1321  O   ILE B  21      37.784 -10.294  16.079  1.00 57.13           O  
ATOM   1322  CB  ILE B  21      37.925  -7.884  14.206  1.00 57.12           C  
ATOM   1323  CG1 ILE B  21      37.525  -6.554  13.553  1.00 57.26           C  
ATOM   1324  CG2 ILE B  21      38.686  -8.757  13.202  1.00 57.12           C  
ATOM   1325  CD1 ILE B  21      38.694  -5.613  13.261  1.00 57.03           C  
ATOM   1326  N   GLY B  22      36.443 -11.018  14.416  1.00 56.91           N  
ATOM   1327  CA  GLY B  22      36.636 -12.433  14.713  1.00 56.68           C  
ATOM   1328  C   GLY B  22      35.417 -13.085  15.337  1.00 56.53           C  
ATOM   1329  O   GLY B  22      35.405 -14.297  15.559  1.00 56.58           O  
ATOM   1330  N   ASP B  23      34.395 -12.281  15.628  1.00 56.31           N  
ATOM   1331  CA  ASP B  23      33.131 -12.790  16.162  1.00 56.13           C  
ATOM   1332  C   ASP B  23      32.249 -13.351  15.051  1.00 56.00           C  
ATOM   1333  O   ASP B  23      32.383 -12.966  13.888  1.00 55.98           O  
ATOM   1334  CB  ASP B  23      32.366 -11.684  16.898  1.00 56.10           C  
ATOM   1335  CG  ASP B  23      33.054 -11.233  18.176  1.00 56.11           C  
ATOM   1336  OD1 ASP B  23      34.265 -11.495  18.344  1.00 56.28           O  
ATOM   1337  OD2 ASP B  23      32.375 -10.604  19.016  1.00 56.04           O  
ATOM   1338  N   LYS B  24      31.353 -14.264  15.419  1.00 55.87           N  
ATOM   1339  CA  LYS B  24      30.288 -14.705  14.523  1.00 55.76           C  
ATOM   1340  C   LYS B  24      29.056 -13.844  14.781  1.00 55.55           C  
ATOM   1341  O   LYS B  24      28.520 -13.828  15.892  1.00 55.40           O  
ATOM   1342  CB  LYS B  24      29.968 -16.191  14.734  1.00 55.87           C  
ATOM   1343  CG  LYS B  24      28.948 -16.780  13.747  1.00 55.97           C  
ATOM   1344  CD  LYS B  24      29.564 -17.093  12.381  1.00 56.43           C  
ATOM   1345  CE  LYS B  24      30.366 -18.392  12.397  1.00 56.66           C  
ATOM   1346  NZ  LYS B  24      31.108 -18.613  11.124  1.00 56.76           N  
ATOM   1347  N   ALA B  25      28.625 -13.119  13.753  1.00 55.39           N  
ATOM   1348  CA  ALA B  25      27.493 -12.204  13.866  1.00 55.20           C  
ATOM   1349  C   ALA B  25      26.168 -12.955  13.868  1.00 55.03           C  
ATOM   1350  O   ALA B  25      25.965 -13.876  13.071  1.00 55.05           O  
ATOM   1351  CB  ALA B  25      27.524 -11.175  12.746  1.00 55.30           C  
ATOM   1352  N   LYS B  26      25.274 -12.546  14.767  1.00 54.74           N  
ATOM   1353  CA  LYS B  26      23.971 -13.190  14.932  1.00 54.44           C  
ATOM   1354  C   LYS B  26      23.048 -12.943  13.740  1.00 54.15           C  
ATOM   1355  O   LYS B  26      23.029 -11.847  13.168  1.00 54.12           O  
ATOM   1356  CB  LYS B  26      23.297 -12.726  16.228  1.00 54.47           C  
ATOM   1357  CG  LYS B  26      24.003 -13.178  17.503  1.00 54.70           C  
ATOM   1358  N   ASP B  27      22.293 -13.976  13.376  1.00 53.68           N  
ATOM   1359  CA  ASP B  27      21.323 -13.909  12.283  1.00 53.23           C  
ATOM   1360  C   ASP B  27      20.142 -13.021  12.671  1.00 52.78           C  
ATOM   1361  O   ASP B  27      19.643 -13.093  13.797  1.00 52.86           O  
ATOM   1362  CB  ASP B  27      20.836 -15.321  11.934  1.00 53.26           C  
ATOM   1363  CG  ASP B  27      20.080 -15.385  10.614  1.00 53.34           C  
ATOM   1364  OD1 ASP B  27      20.171 -14.442   9.797  1.00 53.16           O  
ATOM   1365  OD2 ASP B  27      19.394 -16.406  10.390  1.00 53.51           O  
ATOM   1366  N   PHE B  28      19.704 -12.182  11.738  1.00 52.20           N  
ATOM   1367  CA  PHE B  28      18.591 -11.270  11.979  1.00 51.63           C  
ATOM   1368  C   PHE B  28      17.632 -11.233  10.793  1.00 51.44           C  
ATOM   1369  O   PHE B  28      17.980 -11.668   9.694  1.00 51.45           O  
ATOM   1370  CB  PHE B  28      19.107  -9.858  12.302  1.00 51.54           C  
ATOM   1371  CG  PHE B  28      19.941  -9.241  11.207  1.00 50.88           C  
ATOM   1372  CD1 PHE B  28      19.339  -8.648  10.099  1.00 50.54           C  
ATOM   1373  CD2 PHE B  28      21.328  -9.244  11.291  1.00 50.37           C  
ATOM   1374  CE1 PHE B  28      20.105  -8.079   9.089  1.00 50.35           C  
ATOM   1375  CE2 PHE B  28      22.105  -8.674  10.286  1.00 50.28           C  
ATOM   1376  CZ  PHE B  28      21.492  -8.090   9.183  1.00 50.29           C  
ATOM   1377  N   THR B  29      16.430 -10.709  11.028  1.00 51.21           N  
ATOM   1378  CA  THR B  29      15.433 -10.496   9.977  1.00 51.07           C  
ATOM   1379  C   THR B  29      14.815  -9.102  10.124  1.00 50.87           C  
ATOM   1380  O   THR B  29      14.304  -8.750  11.192  1.00 50.86           O  
ATOM   1381  CB  THR B  29      14.332 -11.587  10.002  1.00 51.02           C  
ATOM   1382  OG1 THR B  29      14.938 -12.882   9.910  1.00 51.18           O  
ATOM   1383  CG2 THR B  29      13.362 -11.412   8.842  1.00 51.27           C  
ATOM   1384  N   LEU B  30      14.873  -8.316   9.051  1.00 50.61           N  
ATOM   1385  CA  LEU B  30      14.403  -6.927   9.078  1.00 50.46           C  
ATOM   1386  C   LEU B  30      13.440  -6.598   7.929  1.00 50.43           C  
ATOM   1387  O   LEU B  30      13.211  -7.424   7.043  1.00 50.37           O  
ATOM   1388  CB  LEU B  30      15.593  -5.957   9.091  1.00 50.41           C  
ATOM   1389  CG  LEU B  30      16.554  -5.990  10.287  1.00 50.04           C  
ATOM   1390  CD1 LEU B  30      17.838  -5.247   9.959  1.00 49.81           C  
ATOM   1391  CD2 LEU B  30      15.915  -5.433  11.561  1.00 49.73           C  
ATOM   1392  N   VAL B  31      12.887  -5.386   7.953  1.00 50.37           N  
ATOM   1393  CA  VAL B  31      11.828  -4.995   7.016  1.00 50.40           C  
ATOM   1394  C   VAL B  31      12.362  -4.212   5.815  1.00 50.39           C  
ATOM   1395  O   VAL B  31      12.996  -3.168   5.976  1.00 50.32           O  
ATOM   1396  CB  VAL B  31      10.714  -4.171   7.718  1.00 50.36           C  
ATOM   1397  CG1 VAL B  31       9.512  -4.006   6.805  1.00 50.48           C  
ATOM   1398  CG2 VAL B  31      10.288  -4.834   9.015  1.00 50.26           C  
ATOM   1399  N   ALA B  32      12.087  -4.725   4.617  1.00 50.45           N  
ATOM   1400  CA  ALA B  32      12.462  -4.065   3.368  1.00 50.55           C  
ATOM   1401  C   ALA B  32      11.473  -2.959   2.989  1.00 50.66           C  
ATOM   1402  O   ALA B  32      10.467  -2.753   3.673  1.00 50.62           O  
ATOM   1403  CB  ALA B  32      12.585  -5.091   2.242  1.00 50.52           C  
ATOM   1404  N   LYS B  33      11.769  -2.260   1.892  1.00 50.93           N  
ATOM   1405  CA  LYS B  33      10.977  -1.123   1.414  1.00 51.21           C  
ATOM   1406  C   LYS B  33       9.533  -1.475   1.051  1.00 51.50           C  
ATOM   1407  O   LYS B  33       8.626  -0.666   1.248  1.00 51.53           O  
ATOM   1408  CB  LYS B  33      11.666  -0.470   0.213  1.00 51.19           C  
ATOM   1409  N   ASP B  34       9.333  -2.679   0.519  1.00 51.86           N  
ATOM   1410  CA  ASP B  34       8.010  -3.160   0.115  1.00 52.14           C  
ATOM   1411  C   ASP B  34       7.259  -3.850   1.262  1.00 52.25           C  
ATOM   1412  O   ASP B  34       6.219  -4.481   1.041  1.00 52.28           O  
ATOM   1413  CB  ASP B  34       8.143  -4.113  -1.080  1.00 52.23           C  
ATOM   1414  CG  ASP B  34       9.030  -5.320  -0.781  1.00 52.63           C  
ATOM   1415  OD1 ASP B  34       9.834  -5.267   0.177  1.00 53.04           O  
ATOM   1416  OD2 ASP B  34       8.927  -6.326  -1.513  1.00 53.03           O  
ATOM   1417  N   LEU B  35       7.798  -3.719   2.475  1.00 52.35           N  
ATOM   1418  CA  LEU B  35       7.268  -4.352   3.697  1.00 52.50           C  
ATOM   1419  C   LEU B  35       7.499  -5.862   3.759  1.00 52.60           C  
ATOM   1420  O   LEU B  35       7.030  -6.534   4.682  1.00 52.60           O  
ATOM   1421  CB  LEU B  35       5.788  -4.001   3.945  1.00 52.57           C  
ATOM   1422  CG  LEU B  35       5.381  -2.539   4.167  1.00 52.42           C  
ATOM   1423  CD1 LEU B  35       3.966  -2.477   4.719  1.00 52.34           C  
ATOM   1424  CD2 LEU B  35       6.342  -1.809   5.097  1.00 52.54           C  
ATOM   1425  N   SER B  36       8.230  -6.382   2.774  1.00 52.76           N  
ATOM   1426  CA  SER B  36       8.683  -7.768   2.770  1.00 52.89           C  
ATOM   1427  C   SER B  36       9.803  -7.959   3.788  1.00 52.99           C  
ATOM   1428  O   SER B  36      10.562  -7.028   4.069  1.00 52.97           O  
ATOM   1429  CB  SER B  36       9.167  -8.162   1.370  1.00 52.90           C  
ATOM   1430  OG  SER B  36      10.121  -9.210   1.416  1.00 53.00           O  
ATOM   1431  N   ASP B  37       9.900  -9.168   4.335  1.00 53.09           N  
ATOM   1432  CA  ASP B  37      10.944  -9.490   5.306  1.00 53.26           C  
ATOM   1433  C   ASP B  37      12.214 -10.000   4.621  1.00 53.22           C  
ATOM   1434  O   ASP B  37      12.150 -10.726   3.622  1.00 53.21           O  
ATOM   1435  CB  ASP B  37      10.434 -10.495   6.345  1.00 53.33           C  
ATOM   1436  CG  ASP B  37       9.290  -9.941   7.185  1.00 53.88           C  
ATOM   1437  OD1 ASP B  37       9.431  -9.891   8.426  1.00 54.52           O  
ATOM   1438  OD2 ASP B  37       8.251  -9.548   6.607  1.00 54.61           O  
ATOM   1439  N   VAL B  38      13.364  -9.597   5.160  1.00 53.12           N  
ATOM   1440  CA  VAL B  38      14.668  -9.954   4.605  1.00 53.05           C  
ATOM   1441  C   VAL B  38      15.583 -10.465   5.721  1.00 53.08           C  
ATOM   1442  O   VAL B  38      15.835  -9.762   6.704  1.00 53.01           O  
ATOM   1443  CB  VAL B  38      15.325  -8.751   3.863  1.00 53.05           C  
ATOM   1444  CG1 VAL B  38      16.763  -9.064   3.466  1.00 53.11           C  
ATOM   1445  CG2 VAL B  38      14.513  -8.359   2.634  1.00 53.00           C  
ATOM   1446  N   ALA B  39      16.067 -11.695   5.562  1.00 53.07           N  
ATOM   1447  CA  ALA B  39      16.950 -12.319   6.545  1.00 53.01           C  
ATOM   1448  C   ALA B  39      18.412 -12.217   6.119  1.00 52.98           C  
ATOM   1449  O   ALA B  39      18.713 -12.176   4.928  1.00 53.11           O  
ATOM   1450  CB  ALA B  39      16.558 -13.775   6.760  1.00 52.92           C  
ATOM   1451  N   LEU B  40      19.312 -12.168   7.098  1.00 52.98           N  
ATOM   1452  CA  LEU B  40      20.756 -12.183   6.843  1.00 52.88           C  
ATOM   1453  C   LEU B  40      21.192 -13.513   6.218  1.00 52.96           C  
ATOM   1454  O   LEU B  40      22.187 -13.570   5.491  1.00 53.04           O  
ATOM   1455  CB  LEU B  40      21.530 -11.911   8.140  1.00 52.87           C  
ATOM   1456  CG  LEU B  40      23.062 -11.972   8.158  1.00 52.66           C  
ATOM   1457  CD1 LEU B  40      23.681 -10.810   7.386  1.00 52.63           C  
ATOM   1458  CD2 LEU B  40      23.571 -11.998   9.590  1.00 52.58           C  
ATOM   1459  N   SER B  41      20.435 -14.573   6.502  1.00 52.96           N  
ATOM   1460  CA  SER B  41      20.650 -15.886   5.896  1.00 52.90           C  
ATOM   1461  C   SER B  41      20.461 -15.850   4.378  1.00 52.84           C  
ATOM   1462  O   SER B  41      21.041 -16.664   3.656  1.00 52.75           O  
ATOM   1463  CB  SER B  41      19.709 -16.921   6.518  1.00 52.95           C  
ATOM   1464  OG  SER B  41      20.001 -17.113   7.894  1.00 52.98           O  
ATOM   1465  N   SER B  42      19.658 -14.892   3.912  1.00 52.78           N  
ATOM   1466  CA  SER B  42      19.368 -14.703   2.488  1.00 52.76           C  
ATOM   1467  C   SER B  42      20.618 -14.442   1.641  1.00 52.70           C  
ATOM   1468  O   SER B  42      20.646 -14.780   0.457  1.00 52.65           O  
ATOM   1469  CB  SER B  42      18.357 -13.563   2.307  1.00 52.78           C  
ATOM   1470  OG  SER B  42      18.176 -13.218   0.943  1.00 53.15           O  
ATOM   1471  N   PHE B  43      21.643 -13.851   2.255  1.00 52.68           N  
ATOM   1472  CA  PHE B  43      22.854 -13.431   1.541  1.00 52.57           C  
ATOM   1473  C   PHE B  43      24.060 -14.349   1.770  1.00 52.49           C  
ATOM   1474  O   PHE B  43      25.208 -13.904   1.664  1.00 52.44           O  
ATOM   1475  CB  PHE B  43      23.232 -11.994   1.928  1.00 52.59           C  
ATOM   1476  CG  PHE B  43      22.123 -10.994   1.746  1.00 52.52           C  
ATOM   1477  CD1 PHE B  43      21.884 -10.417   0.502  1.00 52.42           C  
ATOM   1478  CD2 PHE B  43      21.334 -10.612   2.826  1.00 52.52           C  
ATOM   1479  CE1 PHE B  43      20.866  -9.483   0.332  1.00 52.41           C  
ATOM   1480  CE2 PHE B  43      20.314  -9.681   2.668  1.00 52.71           C  
ATOM   1481  CZ  PHE B  43      20.079  -9.114   1.416  1.00 52.57           C  
ATOM   1482  N   ALA B  44      23.800 -15.622   2.070  1.00 52.45           N  
ATOM   1483  CA  ALA B  44      24.863 -16.596   2.346  1.00 52.31           C  
ATOM   1484  C   ALA B  44      25.925 -16.615   1.246  1.00 52.22           C  
ATOM   1485  O   ALA B  44      25.605 -16.758   0.062  1.00 52.22           O  
ATOM   1486  CB  ALA B  44      24.277 -17.989   2.553  1.00 52.37           C  
ATOM   1487  N   GLY B  45      27.183 -16.449   1.649  1.00 52.03           N  
ATOM   1488  CA  GLY B  45      28.302 -16.408   0.712  1.00 51.80           C  
ATOM   1489  C   GLY B  45      28.760 -15.005   0.349  1.00 51.61           C  
ATOM   1490  O   GLY B  45      29.948 -14.777   0.113  1.00 51.66           O  
ATOM   1491  N   LYS B  46      27.821 -14.063   0.295  1.00 51.33           N  
ATOM   1492  CA  LYS B  46      28.147 -12.672  -0.018  1.00 51.09           C  
ATOM   1493  C   LYS B  46      28.811 -11.978   1.169  1.00 50.81           C  
ATOM   1494  O   LYS B  46      28.743 -12.461   2.303  1.00 50.79           O  
ATOM   1495  CB  LYS B  46      26.894 -11.896  -0.447  1.00 51.14           C  
ATOM   1496  CG  LYS B  46      26.396 -12.212  -1.852  1.00 51.26           C  
ATOM   1497  CD  LYS B  46      25.177 -11.368  -2.201  1.00 51.87           C  
ATOM   1498  CE  LYS B  46      24.513 -11.833  -3.493  1.00 52.06           C  
ATOM   1499  NZ  LYS B  46      25.327 -11.517  -4.701  1.00 52.40           N  
ATOM   1500  N   ARG B  47      29.466 -10.853   0.899  1.00 50.40           N  
ATOM   1501  CA  ARG B  47      29.988 -10.015   1.969  1.00 49.96           C  
ATOM   1502  C   ARG B  47      28.986  -8.917   2.290  1.00 49.57           C  
ATOM   1503  O   ARG B  47      28.426  -8.286   1.389  1.00 49.61           O  
ATOM   1504  CB  ARG B  47      31.360  -9.438   1.618  1.00 50.04           C  
ATOM   1505  CG  ARG B  47      32.486 -10.467   1.669  1.00 50.42           C  
ATOM   1506  CD  ARG B  47      32.866 -10.965   0.283  1.00 50.86           C  
ATOM   1507  NE  ARG B  47      34.125 -10.378  -0.180  1.00 51.48           N  
ATOM   1508  CZ  ARG B  47      34.241  -9.209  -0.807  1.00 51.52           C  
ATOM   1509  NH1 ARG B  47      33.172  -8.465  -1.059  1.00 51.70           N  
ATOM   1510  NH2 ARG B  47      35.438  -8.780  -1.180  1.00 51.64           N  
ATOM   1511  N   LYS B  48      28.760  -8.702   3.580  1.00 49.04           N  
ATOM   1512  CA  LYS B  48      27.716  -7.796   4.032  1.00 48.46           C  
ATOM   1513  C   LYS B  48      28.287  -6.586   4.758  1.00 47.88           C  
ATOM   1514  O   LYS B  48      28.814  -6.707   5.866  1.00 47.86           O  
ATOM   1515  CB  LYS B  48      26.720  -8.526   4.944  1.00 48.54           C  
ATOM   1516  CG  LYS B  48      26.090  -9.780   4.357  1.00 49.05           C  
ATOM   1517  CD  LYS B  48      26.845 -11.039   4.776  1.00 49.84           C  
ATOM   1518  CE  LYS B  48      26.082 -12.292   4.388  1.00 50.11           C  
ATOM   1519  NZ  LYS B  48      26.849 -13.531   4.692  1.00 50.64           N  
ATOM   1520  N   VAL B  49      28.188  -5.423   4.122  1.00 47.19           N  
ATOM   1521  CA  VAL B  49      28.477  -4.162   4.791  1.00 46.49           C  
ATOM   1522  C   VAL B  49      27.197  -3.692   5.481  1.00 46.09           C  
ATOM   1523  O   VAL B  49      26.202  -3.374   4.823  1.00 46.02           O  
ATOM   1524  CB  VAL B  49      29.006  -3.084   3.814  1.00 46.59           C  
ATOM   1525  CG1 VAL B  49      29.182  -1.739   4.524  1.00 46.45           C  
ATOM   1526  CG2 VAL B  49      30.320  -3.525   3.190  1.00 46.47           C  
ATOM   1527  N   LEU B  50      27.231  -3.675   6.809  1.00 45.45           N  
ATOM   1528  CA  LEU B  50      26.099  -3.242   7.617  1.00 44.96           C  
ATOM   1529  C   LEU B  50      26.324  -1.818   8.112  1.00 44.73           C  
ATOM   1530  O   LEU B  50      27.056  -1.589   9.076  1.00 44.60           O  
ATOM   1531  CB  LEU B  50      25.887  -4.195   8.800  1.00 44.86           C  
ATOM   1532  CG  LEU B  50      24.995  -5.435   8.659  1.00 44.94           C  
ATOM   1533  CD1 LEU B  50      25.393  -6.351   7.503  1.00 44.80           C  
ATOM   1534  CD2 LEU B  50      24.995  -6.210   9.966  1.00 45.13           C  
ATOM   1535  N   ASN B  51      25.700  -0.861   7.436  1.00 44.46           N  
ATOM   1536  CA  ASN B  51      25.843   0.542   7.796  1.00 44.22           C  
ATOM   1537  C   ASN B  51      24.676   0.999   8.675  1.00 44.01           C  
ATOM   1538  O   ASN B  51      23.552   1.170   8.195  1.00 43.99           O  
ATOM   1539  CB  ASN B  51      25.966   1.397   6.531  1.00 44.20           C  
ATOM   1540  CG  ASN B  51      26.899   2.581   6.709  1.00 44.26           C  
ATOM   1541  OD1 ASN B  51      27.129   3.055   7.822  1.00 44.11           O  
ATOM   1542  ND2 ASN B  51      27.436   3.071   5.602  1.00 44.52           N  
ATOM   1543  N   ILE B  52      24.955   1.180   9.965  1.00 43.76           N  
ATOM   1544  CA  ILE B  52      23.928   1.473  10.971  1.00 43.52           C  
ATOM   1545  C   ILE B  52      23.805   2.972  11.243  1.00 43.43           C  
ATOM   1546  O   ILE B  52      24.792   3.635  11.568  1.00 43.30           O  
ATOM   1547  CB  ILE B  52      24.207   0.730  12.314  1.00 43.51           C  
ATOM   1548  CG1 ILE B  52      24.526  -0.759  12.089  1.00 43.69           C  
ATOM   1549  CG2 ILE B  52      23.058   0.924  13.295  1.00 43.25           C  
ATOM   1550  CD1 ILE B  52      23.461  -1.552  11.345  1.00 44.01           C  
ATOM   1551  N   PHE B  53      22.584   3.488  11.122  1.00 43.39           N  
ATOM   1552  CA  PHE B  53      22.308   4.914  11.290  1.00 43.38           C  
ATOM   1553  C   PHE B  53      21.231   5.157  12.336  1.00 43.53           C  
ATOM   1554  O   PHE B  53      20.272   4.390  12.424  1.00 43.54           O  
ATOM   1555  CB  PHE B  53      21.827   5.527   9.974  1.00 43.24           C  
ATOM   1556  CG  PHE B  53      22.844   5.500   8.867  1.00 43.19           C  
ATOM   1557  CD1 PHE B  53      23.001   4.366   8.071  1.00 42.92           C  
ATOM   1558  CD2 PHE B  53      23.616   6.625   8.589  1.00 42.94           C  
ATOM   1559  CE1 PHE B  53      23.926   4.345   7.034  1.00 42.61           C  
ATOM   1560  CE2 PHE B  53      24.545   6.613   7.551  1.00 42.69           C  
ATOM   1561  CZ  PHE B  53      24.701   5.469   6.773  1.00 42.71           C  
ATOM   1562  N   PRO B  54      21.372   6.237  13.127  1.00 43.80           N  
ATOM   1563  CA  PRO B  54      20.260   6.674  13.973  1.00 44.09           C  
ATOM   1564  C   PRO B  54      19.037   7.041  13.126  1.00 44.46           C  
ATOM   1565  O   PRO B  54      17.910   6.679  13.473  1.00 44.50           O  
ATOM   1566  CB  PRO B  54      20.822   7.912  14.681  1.00 44.19           C  
ATOM   1567  CG  PRO B  54      22.301   7.728  14.651  1.00 43.84           C  
ATOM   1568  CD  PRO B  54      22.590   7.036  13.359  1.00 43.78           C  
ATOM   1569  N   SER B  55      19.272   7.744  12.020  1.00 44.83           N  
ATOM   1570  CA  SER B  55      18.220   8.067  11.065  1.00 45.34           C  
ATOM   1571  C   SER B  55      18.795   8.340   9.682  1.00 45.68           C  
ATOM   1572  O   SER B  55      19.773   9.077   9.545  1.00 45.85           O  
ATOM   1573  CB  SER B  55      17.402   9.274  11.536  1.00 45.26           C  
ATOM   1574  OG  SER B  55      16.303   9.510  10.672  1.00 45.42           O  
ATOM   1575  N   ILE B  56      18.185   7.736   8.667  1.00 46.16           N  
ATOM   1576  CA  ILE B  56      18.518   8.025   7.271  1.00 46.65           C  
ATOM   1577  C   ILE B  56      17.442   8.884   6.602  1.00 47.19           C  
ATOM   1578  O   ILE B  56      17.482   9.126   5.393  1.00 47.09           O  
ATOM   1579  CB  ILE B  56      18.778   6.740   6.437  1.00 46.58           C  
ATOM   1580  CG1 ILE B  56      17.614   5.747   6.545  1.00 46.33           C  
ATOM   1581  CG2 ILE B  56      20.096   6.104   6.843  1.00 46.51           C  
ATOM   1582  CD1 ILE B  56      17.670   4.630   5.509  1.00 46.27           C  
ATOM   1583  N   ASP B  57      16.479   9.339   7.399  1.00 47.91           N  
ATOM   1584  CA  ASP B  57      15.428  10.211   6.900  1.00 48.78           C  
ATOM   1585  C   ASP B  57      15.948  11.647   6.829  1.00 49.30           C  
ATOM   1586  O   ASP B  57      15.809  12.426   7.780  1.00 49.34           O  
ATOM   1587  CB  ASP B  57      14.178  10.116   7.781  1.00 48.74           C  
ATOM   1588  CG  ASP B  57      12.965  10.779   7.151  1.00 48.97           C  
ATOM   1589  OD1 ASP B  57      11.925  10.884   7.840  1.00 49.22           O  
ATOM   1590  OD2 ASP B  57      13.044  11.190   5.971  1.00 48.87           O  
ATOM   1591  N   THR B  58      16.558  11.978   5.695  1.00 49.92           N  
ATOM   1592  CA  THR B  58      17.143  13.299   5.488  1.00 50.64           C  
ATOM   1593  C   THR B  58      17.105  13.736   4.023  1.00 51.20           C  
ATOM   1594  O   THR B  58      17.160  12.907   3.106  1.00 51.20           O  
ATOM   1595  CB  THR B  58      18.597  13.385   6.042  1.00 50.66           C  
ATOM   1596  OG1 THR B  58      19.111  14.710   5.851  1.00 50.39           O  
ATOM   1597  CG2 THR B  58      19.521  12.368   5.360  1.00 50.54           C  
ATOM   1598  N   GLY B  59      16.994  15.047   3.824  1.00 51.84           N  
ATOM   1599  CA  GLY B  59      17.055  15.643   2.496  1.00 52.64           C  
ATOM   1600  C   GLY B  59      18.495  15.859   2.080  1.00 53.28           C  
ATOM   1601  O   GLY B  59      18.859  15.597   0.938  1.00 53.24           O  
ATOM   1602  N   VAL B  60      19.315  16.329   3.019  1.00 53.94           N  
ATOM   1603  CA  VAL B  60      20.730  16.607   2.761  1.00 54.60           C  
ATOM   1604  C   VAL B  60      21.610  15.391   3.035  1.00 55.02           C  
ATOM   1605  O   VAL B  60      21.506  14.763   4.091  1.00 55.18           O  
ATOM   1606  CB  VAL B  60      21.250  17.831   3.571  1.00 54.61           C  
ATOM   1607  CG1 VAL B  60      20.727  19.132   2.974  1.00 54.82           C  
ATOM   1608  CG2 VAL B  60      20.882  17.722   5.054  1.00 54.63           C  
ATOM   1609  N   CYS B  61      22.474  15.066   2.076  1.00 55.51           N  
ATOM   1610  CA  CYS B  61      23.394  13.943   2.223  1.00 56.01           C  
ATOM   1611  C   CYS B  61      24.842  14.352   1.985  1.00 55.95           C  
ATOM   1612  O   CYS B  61      25.135  15.142   1.082  1.00 56.02           O  
ATOM   1613  CB  CYS B  61      23.008  12.800   1.282  1.00 56.24           C  
ATOM   1614  SG  CYS B  61      23.184  13.163  -0.492  1.00 57.64           S  
ATOM   1615  N   ALA B  62      25.738  13.812   2.810  1.00 55.94           N  
ATOM   1616  CA  ALA B  62      27.175  13.991   2.633  1.00 55.86           C  
ATOM   1617  C   ALA B  62      27.685  13.073   1.521  1.00 55.87           C  
ATOM   1618  O   ALA B  62      27.258  11.917   1.412  1.00 55.78           O  
ATOM   1619  CB  ALA B  62      27.912  13.720   3.937  1.00 55.87           C  
ATOM   1620  N   ALA B  63      28.599  13.598   0.704  1.00 55.77           N  
ATOM   1621  CA  ALA B  63      29.118  12.887  -0.469  1.00 55.65           C  
ATOM   1622  C   ALA B  63      29.824  11.583  -0.117  1.00 55.52           C  
ATOM   1623  O   ALA B  63      29.713  10.597  -0.848  1.00 55.50           O  
ATOM   1624  CB  ALA B  63      30.043  13.792  -1.275  1.00 55.71           C  
ATOM   1625  N   SER B  64      30.541  11.591   1.005  1.00 55.35           N  
ATOM   1626  CA  SER B  64      31.300  10.433   1.472  1.00 55.20           C  
ATOM   1627  C   SER B  64      30.403   9.245   1.823  1.00 55.07           C  
ATOM   1628  O   SER B  64      30.801   8.093   1.650  1.00 55.11           O  
ATOM   1629  CB  SER B  64      32.165  10.817   2.675  1.00 55.17           C  
ATOM   1630  OG  SER B  64      31.370  11.334   3.725  1.00 55.12           O  
ATOM   1631  N   VAL B  65      29.199   9.539   2.314  1.00 54.92           N  
ATOM   1632  CA  VAL B  65      28.209   8.515   2.660  1.00 54.72           C  
ATOM   1633  C   VAL B  65      27.754   7.768   1.407  1.00 54.60           C  
ATOM   1634  O   VAL B  65      27.768   6.535   1.373  1.00 54.50           O  
ATOM   1635  CB  VAL B  65      26.973   9.124   3.382  1.00 54.75           C  
ATOM   1636  CG1 VAL B  65      26.031   8.026   3.869  1.00 54.68           C  
ATOM   1637  CG2 VAL B  65      27.405  10.008   4.548  1.00 54.92           C  
ATOM   1638  N   ARG B  66      27.359   8.525   0.384  1.00 54.48           N  
ATOM   1639  CA  ARG B  66      26.921   7.954  -0.888  1.00 54.41           C  
ATOM   1640  C   ARG B  66      28.090   7.344  -1.657  1.00 54.34           C  
ATOM   1641  O   ARG B  66      27.910   6.375  -2.397  1.00 54.30           O  
ATOM   1642  CB  ARG B  66      26.216   9.009  -1.745  1.00 54.42           C  
ATOM   1643  N   LYS B  67      29.279   7.918  -1.476  1.00 54.26           N  
ATOM   1644  CA  LYS B  67      30.493   7.411  -2.112  1.00 54.27           C  
ATOM   1645  C   LYS B  67      30.899   6.056  -1.538  1.00 54.25           C  
ATOM   1646  O   LYS B  67      31.219   5.133  -2.290  1.00 54.28           O  
ATOM   1647  CB  LYS B  67      31.644   8.414  -1.985  1.00 54.27           C  
ATOM   1648  N   PHE B  68      30.877   5.941  -0.211  1.00 54.20           N  
ATOM   1649  CA  PHE B  68      31.199   4.683   0.462  1.00 54.30           C  
ATOM   1650  C   PHE B  68      30.253   3.562   0.040  1.00 54.29           C  
ATOM   1651  O   PHE B  68      30.705   2.497  -0.387  1.00 54.26           O  
ATOM   1652  CB  PHE B  68      31.184   4.855   1.986  1.00 54.30           C  
ATOM   1653  CG  PHE B  68      31.292   3.559   2.752  1.00 54.60           C  
ATOM   1654  CD1 PHE B  68      32.493   2.854   2.796  1.00 54.76           C  
ATOM   1655  CD2 PHE B  68      30.193   3.049   3.441  1.00 54.68           C  
ATOM   1656  CE1 PHE B  68      32.594   1.659   3.507  1.00 54.80           C  
ATOM   1657  CE2 PHE B  68      30.286   1.855   4.155  1.00 54.63           C  
ATOM   1658  CZ  PHE B  68      31.489   1.159   4.187  1.00 54.62           C  
ATOM   1659  N   ASN B  69      28.950   3.818   0.153  1.00 54.34           N  
ATOM   1660  CA  ASN B  69      27.920   2.831  -0.169  1.00 54.48           C  
ATOM   1661  C   ASN B  69      27.995   2.316  -1.605  1.00 54.56           C  
ATOM   1662  O   ASN B  69      27.981   1.104  -1.833  1.00 54.51           O  
ATOM   1663  CB  ASN B  69      26.521   3.384   0.133  1.00 54.44           C  
ATOM   1664  CG  ASN B  69      26.190   3.377   1.621  1.00 54.47           C  
ATOM   1665  OD1 ASN B  69      26.889   2.760   2.429  1.00 54.53           O  
ATOM   1666  ND2 ASN B  69      25.113   4.063   1.988  1.00 54.02           N  
ATOM   1667  N   GLN B  70      28.088   3.240  -2.559  1.00 54.70           N  
ATOM   1668  CA  GLN B  70      28.163   2.900  -3.979  1.00 54.95           C  
ATOM   1669  C   GLN B  70      29.417   2.092  -4.323  1.00 55.07           C  
ATOM   1670  O   GLN B  70      29.330   1.096  -5.042  1.00 55.11           O  
ATOM   1671  CB  GLN B  70      28.084   4.161  -4.845  1.00 54.94           C  
ATOM   1672  N   LEU B  71      30.567   2.522  -3.800  1.00 55.25           N  
ATOM   1673  CA  LEU B  71      31.850   1.853  -4.051  1.00 55.43           C  
ATOM   1674  C   LEU B  71      31.852   0.414  -3.554  1.00 55.47           C  
ATOM   1675  O   LEU B  71      32.224  -0.503  -4.289  1.00 55.58           O  
ATOM   1676  CB  LEU B  71      33.013   2.619  -3.407  1.00 55.49           C  
ATOM   1677  CG  LEU B  71      33.644   3.809  -4.137  1.00 55.77           C  
ATOM   1678  CD1 LEU B  71      34.480   4.634  -3.163  1.00 55.86           C  
ATOM   1679  CD2 LEU B  71      34.488   3.363  -5.328  1.00 55.90           C  
ATOM   1680  N   ALA B  72      31.434   0.226  -2.304  1.00 55.43           N  
ATOM   1681  CA  ALA B  72      31.347  -1.101  -1.703  1.00 55.38           C  
ATOM   1682  C   ALA B  72      30.291  -1.960  -2.398  1.00 55.38           C  
ATOM   1683  O   ALA B  72      30.378  -3.191  -2.390  1.00 55.46           O  
ATOM   1684  CB  ALA B  72      31.055  -0.988  -0.217  1.00 55.33           C  
ATOM   1685  N   GLY B  73      29.305  -1.299  -3.003  1.00 55.31           N  
ATOM   1686  CA  GLY B  73      28.221  -1.973  -3.705  1.00 55.30           C  
ATOM   1687  C   GLY B  73      28.633  -2.601  -5.024  1.00 55.31           C  
ATOM   1688  O   GLY B  73      28.107  -3.650  -5.405  1.00 55.37           O  
ATOM   1689  N   GLU B  74      29.568  -1.961  -5.726  1.00 55.28           N  
ATOM   1690  CA  GLU B  74      30.022  -2.452  -7.033  1.00 55.18           C  
ATOM   1691  C   GLU B  74      31.211  -3.422  -6.954  1.00 54.88           C  
ATOM   1692  O   GLU B  74      31.649  -3.964  -7.972  1.00 54.98           O  
ATOM   1693  CB  GLU B  74      30.278  -1.299  -8.017  1.00 55.22           C  
ATOM   1694  CG  GLU B  74      31.127  -0.151  -7.490  1.00 55.76           C  
ATOM   1695  CD  GLU B  74      30.817   1.167  -8.191  1.00 56.34           C  
ATOM   1696  OE1 GLU B  74      29.630   1.561  -8.227  1.00 56.09           O  
ATOM   1697  OE2 GLU B  74      31.760   1.812  -8.701  1.00 56.62           O  
ATOM   1698  N   LEU B  75      31.716  -3.634  -5.741  1.00 54.58           N  
ATOM   1699  CA  LEU B  75      32.695  -4.685  -5.467  1.00 54.24           C  
ATOM   1700  C   LEU B  75      32.054  -6.058  -5.657  1.00 53.96           C  
ATOM   1701  O   LEU B  75      30.900  -6.267  -5.274  1.00 53.87           O  
ATOM   1702  CB  LEU B  75      33.244  -4.546  -4.044  1.00 54.24           C  
ATOM   1703  CG  LEU B  75      34.594  -3.856  -3.804  1.00 54.38           C  
ATOM   1704  CD1 LEU B  75      34.780  -2.579  -4.622  1.00 54.75           C  
ATOM   1705  CD2 LEU B  75      34.776  -3.569  -2.318  1.00 54.44           C  
ATOM   1706  N   GLU B  76      32.805  -6.982  -6.254  1.00 53.67           N  
ATOM   1707  CA  GLU B  76      32.298  -8.316  -6.592  1.00 53.34           C  
ATOM   1708  C   GLU B  76      31.838  -9.098  -5.363  1.00 53.10           C  
ATOM   1709  O   GLU B  76      32.539  -9.144  -4.346  1.00 53.06           O  
ATOM   1710  CB  GLU B  76      33.351  -9.119  -7.361  1.00 53.36           C  
ATOM   1711  N   ASN B  77      30.652  -9.698  -5.475  1.00 52.66           N  
ATOM   1712  CA  ASN B  77      30.048 -10.509  -4.414  1.00 52.21           C  
ATOM   1713  C   ASN B  77      29.939  -9.765  -3.078  1.00 51.83           C  
ATOM   1714  O   ASN B  77      30.428 -10.229  -2.044  1.00 51.86           O  
ATOM   1715  CB  ASN B  77      30.797 -11.839  -4.259  1.00 52.25           C  
ATOM   1716  CG  ASN B  77      29.963 -12.904  -3.578  1.00 52.59           C  
ATOM   1717  OD1 ASN B  77      30.341 -13.417  -2.525  1.00 53.04           O  
ATOM   1718  ND2 ASN B  77      28.822 -13.245  -4.176  1.00 52.99           N  
ATOM   1719  N   THR B  78      29.289  -8.604  -3.121  1.00 51.31           N  
ATOM   1720  CA  THR B  78      29.158  -7.725  -1.959  1.00 50.76           C  
ATOM   1721  C   THR B  78      27.793  -7.038  -1.946  1.00 50.23           C  
ATOM   1722  O   THR B  78      27.278  -6.644  -2.998  1.00 50.30           O  
ATOM   1723  CB  THR B  78      30.250  -6.631  -1.958  1.00 50.79           C  
ATOM   1724  OG1 THR B  78      31.447  -7.136  -2.561  1.00 50.89           O  
ATOM   1725  CG2 THR B  78      30.555  -6.166  -0.543  1.00 51.01           C  
ATOM   1726  N   VAL B  79      27.218  -6.892  -0.754  1.00 49.46           N  
ATOM   1727  CA  VAL B  79      25.947  -6.182  -0.586  1.00 48.75           C  
ATOM   1728  C   VAL B  79      25.998  -5.205   0.599  1.00 48.25           C  
ATOM   1729  O   VAL B  79      26.646  -5.472   1.616  1.00 48.24           O  
ATOM   1730  CB  VAL B  79      24.739  -7.168  -0.485  1.00 48.78           C  
ATOM   1731  CG1 VAL B  79      24.715  -7.901   0.862  1.00 48.61           C  
ATOM   1732  CG2 VAL B  79      23.420  -6.448  -0.749  1.00 48.68           C  
ATOM   1733  N   VAL B  80      25.325  -4.068   0.446  1.00 47.60           N  
ATOM   1734  CA  VAL B  80      25.304  -3.025   1.473  1.00 46.95           C  
ATOM   1735  C   VAL B  80      23.921  -2.953   2.126  1.00 46.47           C  
ATOM   1736  O   VAL B  80      22.900  -2.915   1.436  1.00 46.37           O  
ATOM   1737  CB  VAL B  80      25.706  -1.645   0.886  1.00 46.93           C  
ATOM   1738  CG1 VAL B  80      25.789  -0.582   1.978  1.00 46.97           C  
ATOM   1739  CG2 VAL B  80      27.035  -1.746   0.152  1.00 46.90           C  
ATOM   1740  N   LEU B  81      23.899  -2.951   3.456  1.00 45.89           N  
ATOM   1741  CA  LEU B  81      22.647  -2.879   4.204  1.00 45.45           C  
ATOM   1742  C   LEU B  81      22.592  -1.620   5.061  1.00 45.12           C  
ATOM   1743  O   LEU B  81      23.292  -1.512   6.072  1.00 45.07           O  
ATOM   1744  CB  LEU B  81      22.450  -4.128   5.074  1.00 45.43           C  
ATOM   1745  CG  LEU B  81      22.603  -5.534   4.472  1.00 45.67           C  
ATOM   1746  CD1 LEU B  81      22.178  -6.592   5.485  1.00 45.90           C  
ATOM   1747  CD2 LEU B  81      21.818  -5.708   3.180  1.00 45.95           C  
ATOM   1748  N   CYS B  82      21.766  -0.667   4.640  1.00 44.66           N  
ATOM   1749  CA  CYS B  82      21.548   0.560   5.403  1.00 44.30           C  
ATOM   1750  C   CYS B  82      20.390   0.398   6.376  1.00 43.90           C  
ATOM   1751  O   CYS B  82      19.224   0.435   5.983  1.00 43.89           O  
ATOM   1752  CB  CYS B  82      21.311   1.746   4.471  1.00 44.23           C  
ATOM   1753  SG  CYS B  82      22.826   2.377   3.762  1.00 44.66           S  
ATOM   1754  N   ILE B  83      20.731   0.227   7.648  1.00 43.47           N  
ATOM   1755  CA  ILE B  83      19.759  -0.096   8.682  1.00 43.16           C  
ATOM   1756  C   ILE B  83      19.546   1.083   9.639  1.00 43.13           C  
ATOM   1757  O   ILE B  83      20.506   1.715  10.086  1.00 43.01           O  
ATOM   1758  CB  ILE B  83      20.185  -1.380   9.454  1.00 43.08           C  
ATOM   1759  CG1 ILE B  83      20.359  -2.552   8.479  1.00 42.89           C  
ATOM   1760  CG2 ILE B  83      19.170  -1.738  10.538  1.00 42.86           C  
ATOM   1761  CD1 ILE B  83      21.360  -3.602   8.923  1.00 42.47           C  
ATOM   1762  N   SER B  84      18.280   1.378   9.925  1.00 43.07           N  
ATOM   1763  CA  SER B  84      17.907   2.387  10.914  1.00 43.14           C  
ATOM   1764  C   SER B  84      16.557   2.037  11.534  1.00 43.24           C  
ATOM   1765  O   SER B  84      15.900   1.082  11.108  1.00 43.08           O  
ATOM   1766  CB  SER B  84      17.863   3.788  10.279  1.00 43.15           C  
ATOM   1767  OG  SER B  84      16.749   3.937   9.417  1.00 42.89           O  
ATOM   1768  N   SER B  85      16.151   2.810  12.541  1.00 43.45           N  
ATOM   1769  CA  SER B  85      14.817   2.675  13.132  1.00 43.68           C  
ATOM   1770  C   SER B  85      13.722   3.416  12.347  1.00 43.94           C  
ATOM   1771  O   SER B  85      12.548   3.359  12.722  1.00 44.04           O  
ATOM   1772  CB  SER B  85      14.815   3.100  14.607  1.00 43.69           C  
ATOM   1773  OG  SER B  85      15.225   2.038  15.457  1.00 43.59           O  
ATOM   1774  N   ASP B  86      14.104   4.100  11.266  1.00 44.22           N  
ATOM   1775  CA  ASP B  86      13.135   4.737  10.367  1.00 44.68           C  
ATOM   1776  C   ASP B  86      12.186   3.703   9.770  1.00 45.06           C  
ATOM   1777  O   ASP B  86      12.588   2.574   9.482  1.00 45.06           O  
ATOM   1778  CB  ASP B  86      13.835   5.474   9.216  1.00 44.58           C  
ATOM   1779  CG  ASP B  86      14.664   6.655   9.680  1.00 44.56           C  
ATOM   1780  OD1 ASP B  86      14.125   7.555  10.358  1.00 44.36           O  
ATOM   1781  OD2 ASP B  86      15.862   6.694   9.337  1.00 44.37           O  
ATOM   1782  N   LEU B  87      10.932   4.101   9.585  1.00 45.56           N  
ATOM   1783  CA  LEU B  87       9.957   3.290   8.868  1.00 46.12           C  
ATOM   1784  C   LEU B  87      10.292   3.246   7.374  1.00 46.75           C  
ATOM   1785  O   LEU B  87      10.808   4.229   6.832  1.00 46.63           O  
ATOM   1786  CB  LEU B  87       8.544   3.842   9.089  1.00 46.01           C  
ATOM   1787  CG  LEU B  87       7.688   3.205  10.190  1.00 45.86           C  
ATOM   1788  CD1 LEU B  87       8.338   3.268  11.568  1.00 45.52           C  
ATOM   1789  CD2 LEU B  87       6.322   3.851  10.222  1.00 45.70           C  
ATOM   1790  N   PRO B  88      10.004   2.107   6.705  1.00 47.37           N  
ATOM   1791  CA  PRO B  88      10.309   1.914   5.279  1.00 47.99           C  
ATOM   1792  C   PRO B  88       9.782   3.016   4.353  1.00 48.71           C  
ATOM   1793  O   PRO B  88      10.262   3.151   3.224  1.00 48.94           O  
ATOM   1794  CB  PRO B  88       9.626   0.585   4.955  1.00 47.87           C  
ATOM   1795  CG  PRO B  88       9.632  -0.153   6.238  1.00 47.69           C  
ATOM   1796  CD  PRO B  88       9.418   0.890   7.299  1.00 47.33           C  
ATOM   1797  N   PHE B  89       8.810   3.793   4.824  1.00 49.48           N  
ATOM   1798  CA  PHE B  89       8.257   4.900   4.041  1.00 50.28           C  
ATOM   1799  C   PHE B  89       9.196   6.105   4.049  1.00 50.68           C  
ATOM   1800  O   PHE B  89       9.156   6.939   3.140  1.00 50.78           O  
ATOM   1801  CB  PHE B  89       6.870   5.299   4.564  1.00 50.34           C  
ATOM   1802  CG  PHE B  89       6.014   4.129   4.974  1.00 50.69           C  
ATOM   1803  CD1 PHE B  89       5.552   3.217   4.027  1.00 51.15           C  
ATOM   1804  CD2 PHE B  89       5.675   3.939   6.311  1.00 50.85           C  
ATOM   1805  CE1 PHE B  89       4.764   2.130   4.408  1.00 51.53           C  
ATOM   1806  CE2 PHE B  89       4.887   2.859   6.702  1.00 51.03           C  
ATOM   1807  CZ  PHE B  89       4.430   1.951   5.749  1.00 51.39           C  
ATOM   1808  N   ALA B  90      10.039   6.180   5.078  1.00 51.20           N  
ATOM   1809  CA  ALA B  90      11.000   7.270   5.245  1.00 51.75           C  
ATOM   1810  C   ALA B  90      12.410   6.876   4.797  1.00 52.16           C  
ATOM   1811  O   ALA B  90      13.260   7.741   4.567  1.00 52.26           O  
ATOM   1812  CB  ALA B  90      11.014   7.741   6.694  1.00 51.73           C  
ATOM   1813  N   GLN B  91      12.646   5.570   4.674  1.00 52.64           N  
ATOM   1814  CA  GLN B  91      13.945   5.038   4.258  1.00 53.10           C  
ATOM   1815  C   GLN B  91      14.185   5.192   2.754  1.00 53.60           C  
ATOM   1816  O   GLN B  91      15.327   5.119   2.290  1.00 53.74           O  
ATOM   1817  CB  GLN B  91      14.083   3.564   4.660  1.00 52.95           C  
ATOM   1818  CG  GLN B  91      14.260   3.323   6.159  1.00 52.57           C  
ATOM   1819  CD  GLN B  91      14.674   1.892   6.489  1.00 51.92           C  
ATOM   1820  OE1 GLN B  91      14.121   0.930   5.956  1.00 51.27           O  
ATOM   1821  NE2 GLN B  91      15.650   1.752   7.380  1.00 51.46           N  
ATOM   1822  N   SER B  92      13.110   5.412   2.002  1.00 54.17           N  
ATOM   1823  CA  SER B  92      13.174   5.474   0.540  1.00 54.81           C  
ATOM   1824  C   SER B  92      13.440   6.882  -0.005  1.00 55.25           C  
ATOM   1825  O   SER B  92      13.428   7.099  -1.221  1.00 55.32           O  
ATOM   1826  CB  SER B  92      11.898   4.885  -0.069  1.00 54.76           C  
ATOM   1827  OG  SER B  92      10.744   5.432   0.547  1.00 54.91           O  
ATOM   1828  N   ARG B  93      13.679   7.832   0.897  1.00 55.74           N  
ATOM   1829  CA  ARG B  93      14.062   9.190   0.516  1.00 56.31           C  
ATOM   1830  C   ARG B  93      15.525   9.451   0.870  1.00 56.75           C  
ATOM   1831  O   ARG B  93      15.955  10.605   0.961  1.00 56.87           O  
ATOM   1832  N   PHE B  94      16.280   8.370   1.062  1.00 57.02           N  
ATOM   1833  CA  PHE B  94      17.679   8.445   1.476  1.00 57.32           C  
ATOM   1834  C   PHE B  94      18.621   8.459   0.276  1.00 57.48           C  
ATOM   1835  O   PHE B  94      18.560   7.584  -0.590  1.00 57.52           O  
ATOM   1836  CB  PHE B  94      18.014   7.289   2.430  1.00 57.39           C  
ATOM   1837  CG  PHE B  94      19.431   7.304   2.952  1.00 57.67           C  
ATOM   1838  CD1 PHE B  94      20.200   6.141   2.932  1.00 58.16           C  
ATOM   1839  CD2 PHE B  94      19.998   8.470   3.469  1.00 57.93           C  
ATOM   1840  CE1 PHE B  94      21.509   6.137   3.419  1.00 58.28           C  
ATOM   1841  CE2 PHE B  94      21.306   8.478   3.956  1.00 58.08           C  
ATOM   1842  CZ  PHE B  94      22.063   7.310   3.929  1.00 58.32           C  
ATOM   1843  N   CYS B  95      19.491   9.465   0.248  1.00 57.67           N  
ATOM   1844  CA  CYS B  95      20.440   9.686  -0.844  1.00 57.80           C  
ATOM   1845  C   CYS B  95      21.558   8.641  -0.899  1.00 57.81           C  
ATOM   1846  O   CYS B  95      22.002   8.256  -1.986  1.00 57.76           O  
ATOM   1847  CB  CYS B  95      21.011  11.103  -0.731  1.00 57.91           C  
ATOM   1848  SG  CYS B  95      22.677  11.410  -1.388  1.00 58.07           S  
ATOM   1849  N   GLY B  96      22.001   8.186   0.272  1.00 57.82           N  
ATOM   1850  CA  GLY B  96      23.053   7.175   0.372  1.00 57.76           C  
ATOM   1851  C   GLY B  96      22.683   5.823  -0.216  1.00 57.77           C  
ATOM   1852  O   GLY B  96      23.563   5.028  -0.552  1.00 57.81           O  
ATOM   1853  N   ALA B  97      21.381   5.565  -0.343  1.00 57.73           N  
ATOM   1854  CA  ALA B  97      20.878   4.307  -0.898  1.00 57.68           C  
ATOM   1855  C   ALA B  97      19.946   4.513  -2.097  1.00 57.62           C  
ATOM   1856  O   ALA B  97      19.561   3.546  -2.760  1.00 57.70           O  
ATOM   1857  CB  ALA B  97      20.179   3.491   0.188  1.00 57.71           C  
ATOM   1858  N   GLU B  98      19.595   5.770  -2.370  1.00 57.49           N  
ATOM   1859  CA  GLU B  98      18.701   6.123  -3.476  1.00 57.26           C  
ATOM   1860  C   GLU B  98      19.307   5.792  -4.837  1.00 57.13           C  
ATOM   1861  O   GLU B  98      20.268   6.433  -5.273  1.00 57.14           O  
ATOM   1862  N   GLY B  99      18.743   4.779  -5.491  1.00 56.96           N  
ATOM   1863  CA  GLY B  99      19.187   4.347  -6.818  1.00 56.68           C  
ATOM   1864  C   GLY B  99      20.570   3.718  -6.865  1.00 56.48           C  
ATOM   1865  O   GLY B  99      21.167   3.606  -7.938  1.00 56.51           O  
ATOM   1866  N   LEU B 100      21.079   3.307  -5.703  1.00 56.28           N  
ATOM   1867  CA  LEU B 100      22.388   2.663  -5.607  1.00 55.94           C  
ATOM   1868  C   LEU B 100      22.234   1.153  -5.746  1.00 55.68           C  
ATOM   1869  O   LEU B 100      21.594   0.512  -4.909  1.00 55.76           O  
ATOM   1870  N   SER B 101      22.824   0.596  -6.802  1.00 55.30           N  
ATOM   1871  CA  SER B 101      22.710  -0.833  -7.102  1.00 54.95           C  
ATOM   1872  C   SER B 101      23.392  -1.700  -6.042  1.00 54.52           C  
ATOM   1873  O   SER B 101      24.477  -1.365  -5.558  1.00 54.56           O  
ATOM   1874  CB  SER B 101      23.277  -1.135  -8.491  1.00 55.06           C  
ATOM   1875  OG  SER B 101      22.694  -2.307  -9.034  1.00 55.45           O  
ATOM   1876  N   ASN B 102      22.739  -2.810  -5.696  1.00 54.02           N  
ATOM   1877  CA  ASN B 102      23.169  -3.721  -4.619  1.00 53.39           C  
ATOM   1878  C   ASN B 102      23.307  -3.057  -3.241  1.00 52.86           C  
ATOM   1879  O   ASN B 102      24.140  -3.451  -2.419  1.00 52.72           O  
ATOM   1880  CB  ASN B 102      24.437  -4.501  -5.008  1.00 53.54           C  
ATOM   1881  CG  ASN B 102      24.182  -5.545  -6.095  1.00 53.94           C  
ATOM   1882  OD1 ASN B 102      23.038  -5.805  -6.482  1.00 54.32           O  
ATOM   1883  ND2 ASN B 102      25.257  -6.150  -6.588  1.00 54.05           N  
ATOM   1884  N   VAL B 103      22.474  -2.043  -3.011  1.00 52.24           N  
ATOM   1885  CA  VAL B 103      22.384  -1.342  -1.731  1.00 51.57           C  
ATOM   1886  C   VAL B 103      20.907  -1.262  -1.343  1.00 51.04           C  
ATOM   1887  O   VAL B 103      20.128  -0.559  -1.996  1.00 51.05           O  
ATOM   1888  CB  VAL B 103      22.984   0.092  -1.807  1.00 51.64           C  
ATOM   1889  CG1 VAL B 103      22.865   0.802  -0.463  1.00 51.70           C  
ATOM   1890  CG2 VAL B 103      24.443   0.061  -2.265  1.00 51.55           C  
ATOM   1891  N   ILE B 104      20.523  -1.991  -0.295  1.00 50.27           N  
ATOM   1892  CA  ILE B 104      19.126  -2.009   0.161  1.00 49.50           C  
ATOM   1893  C   ILE B 104      18.948  -1.453   1.580  1.00 48.96           C  
ATOM   1894  O   ILE B 104      19.875  -1.488   2.398  1.00 48.89           O  
ATOM   1895  CB  ILE B 104      18.468  -3.425   0.041  1.00 49.60           C  
ATOM   1896  CG1 ILE B 104      19.042  -4.403   1.073  1.00 49.60           C  
ATOM   1897  CG2 ILE B 104      18.593  -3.974  -1.390  1.00 49.46           C  
ATOM   1898  CD1 ILE B 104      18.131  -5.584   1.379  1.00 49.60           C  
ATOM   1899  N   THR B 105      17.752  -0.935   1.853  1.00 48.17           N  
ATOM   1900  CA  THR B 105      17.403  -0.411   3.173  1.00 47.40           C  
ATOM   1901  C   THR B 105      16.663  -1.454   4.004  1.00 46.84           C  
ATOM   1902  O   THR B 105      15.943  -2.298   3.463  1.00 46.75           O  
ATOM   1903  CB  THR B 105      16.526   0.853   3.076  1.00 47.45           C  
ATOM   1904  OG1 THR B 105      15.360   0.569   2.291  1.00 47.42           O  
ATOM   1905  CG2 THR B 105      17.304   2.008   2.446  1.00 47.30           C  
ATOM   1906  N   LEU B 106      16.847  -1.389   5.319  1.00 46.05           N  
ATOM   1907  CA  LEU B 106      16.175  -2.294   6.244  1.00 45.27           C  
ATOM   1908  C   LEU B 106      15.741  -1.555   7.503  1.00 44.85           C  
ATOM   1909  O   LEU B 106      16.524  -0.821   8.111  1.00 44.70           O  
ATOM   1910  CB  LEU B 106      17.072  -3.487   6.603  1.00 45.27           C  
ATOM   1911  CG  LEU B 106      17.458  -4.488   5.505  1.00 45.05           C  
ATOM   1912  CD1 LEU B 106      18.528  -5.447   6.003  1.00 44.83           C  
ATOM   1913  CD2 LEU B 106      16.248  -5.254   4.987  1.00 44.77           C  
ATOM   1914  N   SER B 107      14.481  -1.753   7.877  1.00 44.34           N  
ATOM   1915  CA  SER B 107      13.905  -1.117   9.053  1.00 43.84           C  
ATOM   1916  C   SER B 107      13.854  -2.078  10.233  1.00 43.64           C  
ATOM   1917  O   SER B 107      13.764  -3.294  10.054  1.00 43.59           O  
ATOM   1918  CB  SER B 107      12.499  -0.607   8.745  1.00 43.76           C  
ATOM   1919  OG  SER B 107      11.947   0.053   9.870  1.00 43.58           O  
ATOM   1920  N   THR B 108      13.901  -1.511  11.436  1.00 43.35           N  
ATOM   1921  CA  THR B 108      13.793  -2.277  12.674  1.00 43.04           C  
ATOM   1922  C   THR B 108      12.333  -2.403  13.137  1.00 42.99           C  
ATOM   1923  O   THR B 108      12.062  -2.924  14.228  1.00 43.02           O  
ATOM   1924  CB  THR B 108      14.663  -1.665  13.804  1.00 43.06           C  
ATOM   1925  OG1 THR B 108      14.226  -0.331  14.087  1.00 42.77           O  
ATOM   1926  CG2 THR B 108      16.136  -1.637  13.408  1.00 43.00           C  
ATOM   1927  N   LEU B 109      11.403  -1.936  12.299  1.00 42.75           N  
ATOM   1928  CA  LEU B 109       9.959  -2.043  12.554  1.00 42.62           C  
ATOM   1929  C   LEU B 109       9.582  -3.420  13.102  1.00 42.58           C  
ATOM   1930  O   LEU B 109       8.729  -3.539  13.985  1.00 42.60           O  
ATOM   1931  CB  LEU B 109       9.168  -1.759  11.267  1.00 42.56           C  
ATOM   1932  CG  LEU B 109       7.638  -1.894  11.289  1.00 42.31           C  
ATOM   1933  CD1 LEU B 109       6.998  -0.757  12.073  1.00 42.29           C  
ATOM   1934  CD2 LEU B 109       7.074  -1.958   9.880  1.00 41.40           C  
ATOM   1935  N   ARG B 110      10.231  -4.445  12.554  1.00 42.46           N  
ATOM   1936  CA  ARG B 110      10.099  -5.822  12.997  1.00 42.19           C  
ATOM   1937  C   ARG B 110      11.511  -6.334  13.263  1.00 42.33           C  
ATOM   1938  O   ARG B 110      12.479  -5.827  12.682  1.00 42.25           O  
ATOM   1939  CB  ARG B 110       9.447  -6.643  11.891  1.00 42.13           C  
ATOM   1940  CG  ARG B 110       8.241  -7.462  12.307  1.00 41.43           C  
ATOM   1941  CD  ARG B 110       7.085  -7.234  11.333  1.00 39.88           C  
ATOM   1942  NE  ARG B 110       7.441  -7.476   9.933  1.00 38.39           N  
ATOM   1943  CZ  ARG B 110       6.949  -6.795   8.900  1.00 37.95           C  
ATOM   1944  NH1 ARG B 110       6.084  -5.803   9.096  1.00 37.44           N  
ATOM   1945  NH2 ARG B 110       7.331  -7.096   7.664  1.00 37.11           N  
ATOM   1946  N   GLY B 111      11.628  -7.323  14.148  1.00 42.37           N  
ATOM   1947  CA  GLY B 111      12.921  -7.905  14.511  1.00 42.39           C  
ATOM   1948  C   GLY B 111      13.859  -6.946  15.221  1.00 42.56           C  
ATOM   1949  O   GLY B 111      15.081  -7.028  15.056  1.00 42.50           O  
ATOM   1950  N   ALA B 112      13.289  -6.050  16.027  1.00 42.71           N  
ATOM   1951  CA  ALA B 112      14.048  -4.999  16.711  1.00 42.91           C  
ATOM   1952  C   ALA B 112      15.074  -5.518  17.726  1.00 43.13           C  
ATOM   1953  O   ALA B 112      15.915  -4.753  18.209  1.00 43.06           O  
ATOM   1954  CB  ALA B 112      13.096  -3.998  17.370  1.00 42.94           C  
ATOM   1955  N   ASP B 113      15.010  -6.815  18.035  1.00 43.41           N  
ATOM   1956  CA  ASP B 113      15.983  -7.460  18.925  1.00 43.70           C  
ATOM   1957  C   ASP B 113      17.410  -7.439  18.358  1.00 43.91           C  
ATOM   1958  O   ASP B 113      18.385  -7.556  19.105  1.00 44.09           O  
ATOM   1959  CB  ASP B 113      15.554  -8.894  19.258  1.00 43.76           C  
ATOM   1960  CG  ASP B 113      15.498  -9.791  18.035  1.00 43.98           C  
ATOM   1961  OD1 ASP B 113      16.307 -10.739  17.963  1.00 44.38           O  
ATOM   1962  OD2 ASP B 113      14.653  -9.551  17.146  1.00 44.18           O  
ATOM   1963  N   PHE B 114      17.516  -7.287  17.039  1.00 44.06           N  
ATOM   1964  CA  PHE B 114      18.789  -7.033  16.356  1.00 44.33           C  
ATOM   1965  C   PHE B 114      19.625  -5.936  17.036  1.00 44.51           C  
ATOM   1966  O   PHE B 114      20.849  -6.064  17.166  1.00 44.44           O  
ATOM   1967  CB  PHE B 114      18.514  -6.663  14.890  1.00 44.34           C  
ATOM   1968  CG  PHE B 114      19.621  -5.882  14.229  1.00 44.53           C  
ATOM   1969  CD1 PHE B 114      20.663  -6.538  13.580  1.00 44.50           C  
ATOM   1970  CD2 PHE B 114      19.610  -4.486  14.238  1.00 44.62           C  
ATOM   1971  CE1 PHE B 114      21.683  -5.819  12.962  1.00 44.66           C  
ATOM   1972  CE2 PHE B 114      20.629  -3.756  13.626  1.00 44.45           C  
ATOM   1973  CZ  PHE B 114      21.665  -4.423  12.985  1.00 44.82           C  
ATOM   1974  N   LYS B 115      18.955  -4.865  17.461  1.00 44.61           N  
ATOM   1975  CA  LYS B 115      19.617  -3.716  18.081  1.00 44.85           C  
ATOM   1976  C   LYS B 115      20.437  -4.107  19.315  1.00 45.05           C  
ATOM   1977  O   LYS B 115      21.597  -3.708  19.445  1.00 44.98           O  
ATOM   1978  CB  LYS B 115      18.591  -2.627  18.412  1.00 44.79           C  
ATOM   1979  CG  LYS B 115      17.935  -2.006  17.172  1.00 44.65           C  
ATOM   1980  CD  LYS B 115      16.544  -1.457  17.462  1.00 44.39           C  
ATOM   1981  CE  LYS B 115      16.596  -0.099  18.148  1.00 44.79           C  
ATOM   1982  NZ  LYS B 115      15.228   0.430  18.399  1.00 44.36           N  
ATOM   1983  N   GLN B 116      19.835  -4.903  20.198  1.00 45.45           N  
ATOM   1984  CA  GLN B 116      20.525  -5.445  21.374  1.00 45.71           C  
ATOM   1985  C   GLN B 116      21.655  -6.400  20.978  1.00 45.73           C  
ATOM   1986  O   GLN B 116      22.747  -6.351  21.551  1.00 45.82           O  
ATOM   1987  CB  GLN B 116      19.532  -6.172  22.289  1.00 45.92           C  
ATOM   1988  CG  GLN B 116      18.552  -5.259  23.034  1.00 46.34           C  
ATOM   1989  CD  GLN B 116      19.023  -4.880  24.433  1.00 46.48           C  
ATOM   1990  OE1 GLN B 116      20.224  -4.829  24.713  1.00 46.58           O  
ATOM   1991  NE2 GLN B 116      18.071  -4.613  25.320  1.00 46.51           N  
ATOM   1992  N   ALA B 117      21.384  -7.250  19.987  1.00 45.66           N  
ATOM   1993  CA  ALA B 117      22.312  -8.297  19.550  1.00 45.62           C  
ATOM   1994  C   ALA B 117      23.599  -7.758  18.917  1.00 45.70           C  
ATOM   1995  O   ALA B 117      24.645  -8.414  18.963  1.00 45.80           O  
ATOM   1996  CB  ALA B 117      21.610  -9.257  18.593  1.00 45.55           C  
ATOM   1997  N   TYR B 118      23.515  -6.571  18.323  1.00 45.63           N  
ATOM   1998  CA  TYR B 118      24.663  -5.948  17.673  1.00 45.50           C  
ATOM   1999  C   TYR B 118      25.191  -4.756  18.475  1.00 45.53           C  
ATOM   2000  O   TYR B 118      26.015  -3.980  17.984  1.00 45.40           O  
ATOM   2001  CB  TYR B 118      24.298  -5.531  16.245  1.00 45.48           C  
ATOM   2002  CG  TYR B 118      24.301  -6.667  15.240  1.00 45.38           C  
ATOM   2003  CD1 TYR B 118      25.195  -6.669  14.174  1.00 45.17           C  
ATOM   2004  CD2 TYR B 118      23.410  -7.741  15.355  1.00 45.00           C  
ATOM   2005  CE1 TYR B 118      25.206  -7.702  13.245  1.00 44.94           C  
ATOM   2006  CE2 TYR B 118      23.413  -8.780  14.428  1.00 44.71           C  
ATOM   2007  CZ  TYR B 118      24.316  -8.752  13.376  1.00 44.90           C  
ATOM   2008  OH  TYR B 118      24.338  -9.770  12.450  1.00 44.71           O  
ATOM   2009  N   GLY B 119      24.715  -4.624  19.711  1.00 45.60           N  
ATOM   2010  CA  GLY B 119      25.132  -3.546  20.606  1.00 45.70           C  
ATOM   2011  C   GLY B 119      25.015  -2.162  19.991  1.00 45.81           C  
ATOM   2012  O   GLY B 119      25.974  -1.391  20.004  1.00 45.82           O  
ATOM   2013  N   VAL B 120      23.840  -1.856  19.445  1.00 45.95           N  
ATOM   2014  CA  VAL B 120      23.576  -0.551  18.827  1.00 46.17           C  
ATOM   2015  C   VAL B 120      22.301   0.107  19.363  1.00 46.37           C  
ATOM   2016  O   VAL B 120      21.909   1.180  18.903  1.00 46.53           O  
ATOM   2017  CB  VAL B 120      23.523  -0.631  17.272  1.00 46.14           C  
ATOM   2018  CG1 VAL B 120      24.928  -0.688  16.688  1.00 45.77           C  
ATOM   2019  CG2 VAL B 120      22.683  -1.824  16.805  1.00 46.19           C  
ATOM   2020  N   ALA B 121      21.675  -0.532  20.348  1.00 46.52           N  
ATOM   2021  CA  ALA B 121      20.421  -0.052  20.922  1.00 46.69           C  
ATOM   2022  C   ALA B 121      20.627   1.103  21.902  1.00 46.89           C  
ATOM   2023  O   ALA B 121      21.034   0.886  23.048  1.00 46.83           O  
ATOM   2024  CB  ALA B 121      19.683  -1.201  21.601  1.00 46.63           C  
ATOM   2025  N   ILE B 122      20.349   2.327  21.447  1.00 47.17           N  
ATOM   2026  CA  ILE B 122      20.382   3.505  22.321  1.00 47.58           C  
ATOM   2027  C   ILE B 122      19.219   3.433  23.306  1.00 47.94           C  
ATOM   2028  O   ILE B 122      18.058   3.315  22.904  1.00 48.13           O  
ATOM   2029  CB  ILE B 122      20.322   4.837  21.533  1.00 47.52           C  
ATOM   2030  CG1 ILE B 122      21.582   5.022  20.683  1.00 47.51           C  
ATOM   2031  CG2 ILE B 122      20.137   6.022  22.488  1.00 47.28           C  
ATOM   2032  CD1 ILE B 122      21.481   6.148  19.662  1.00 47.94           C  
ATOM   2033  N   THR B 123      19.540   3.516  24.593  1.00 48.37           N  
ATOM   2034  CA  THR B 123      18.560   3.250  25.645  1.00 48.84           C  
ATOM   2035  C   THR B 123      18.299   4.422  26.604  1.00 49.09           C  
ATOM   2036  O   THR B 123      17.532   4.282  27.561  1.00 49.18           O  
ATOM   2037  CB  THR B 123      18.933   1.960  26.434  1.00 48.84           C  
ATOM   2038  OG1 THR B 123      17.896   1.651  27.373  1.00 49.25           O  
ATOM   2039  CG2 THR B 123      20.265   2.124  27.170  1.00 48.75           C  
ATOM   2040  N   GLU B 124      18.925   5.570  26.345  1.00 49.38           N  
ATOM   2041  CA  GLU B 124      18.702   6.764  27.169  1.00 49.67           C  
ATOM   2042  C   GLU B 124      18.511   8.036  26.342  1.00 49.65           C  
ATOM   2043  O   GLU B 124      18.938   8.112  25.185  1.00 49.70           O  
ATOM   2044  CB  GLU B 124      19.836   6.953  28.193  1.00 49.84           C  
ATOM   2045  CG  GLU B 124      21.111   7.608  27.644  1.00 50.34           C  
ATOM   2046  CD  GLU B 124      22.012   8.186  28.735  1.00 51.15           C  
ATOM   2047  OE1 GLU B 124      21.487   8.728  29.734  1.00 51.50           O  
ATOM   2048  OE2 GLU B 124      23.251   8.111  28.584  1.00 51.24           O  
ATOM   2049  N   GLY B 125      17.861   9.026  26.951  1.00 49.62           N  
ATOM   2050  CA  GLY B 125      17.714  10.357  26.361  1.00 49.40           C  
ATOM   2051  C   GLY B 125      16.786  10.438  25.160  1.00 49.23           C  
ATOM   2052  O   GLY B 125      16.020   9.504  24.899  1.00 49.27           O  
ATOM   2053  N   PRO B 126      16.861  11.559  24.412  1.00 49.01           N  
ATOM   2054  CA  PRO B 126      15.994  11.857  23.265  1.00 48.83           C  
ATOM   2055  C   PRO B 126      16.146  10.891  22.086  1.00 48.59           C  
ATOM   2056  O   PRO B 126      15.312  10.901  21.175  1.00 48.56           O  
ATOM   2057  CB  PRO B 126      16.438  13.266  22.846  1.00 48.87           C  
ATOM   2058  CG  PRO B 126      17.826  13.400  23.362  1.00 48.98           C  
ATOM   2059  CD  PRO B 126      17.831  12.643  24.655  1.00 49.03           C  
ATOM   2060  N   LEU B 127      17.197  10.075  22.106  1.00 48.30           N  
ATOM   2061  CA  LEU B 127      17.464   9.131  21.019  1.00 47.96           C  
ATOM   2062  C   LEU B 127      17.117   7.681  21.373  1.00 47.61           C  
ATOM   2063  O   LEU B 127      17.492   6.757  20.649  1.00 47.61           O  
ATOM   2064  CB  LEU B 127      18.920   9.243  20.545  1.00 48.01           C  
ATOM   2065  CG  LEU B 127      19.312  10.468  19.707  1.00 48.24           C  
ATOM   2066  CD1 LEU B 127      19.733  11.638  20.590  1.00 48.22           C  
ATOM   2067  CD2 LEU B 127      20.433  10.114  18.740  1.00 48.31           C  
ATOM   2068  N   ALA B 128      16.394   7.487  22.475  1.00 47.14           N  
ATOM   2069  CA  ALA B 128      15.975   6.148  22.894  1.00 46.73           C  
ATOM   2070  C   ALA B 128      15.015   5.528  21.878  1.00 46.44           C  
ATOM   2071  O   ALA B 128      14.107   6.197  21.377  1.00 46.35           O  
ATOM   2072  CB  ALA B 128      15.348   6.188  24.280  1.00 46.66           C  
ATOM   2073  N   GLY B 129      15.233   4.250  21.571  1.00 46.06           N  
ATOM   2074  CA  GLY B 129      14.473   3.554  20.532  1.00 45.42           C  
ATOM   2075  C   GLY B 129      15.115   3.666  19.159  1.00 45.06           C  
ATOM   2076  O   GLY B 129      14.619   3.097  18.185  1.00 45.00           O  
ATOM   2077  N   LEU B 130      16.217   4.409  19.083  1.00 44.66           N  
ATOM   2078  CA  LEU B 130      16.984   4.551  17.851  1.00 44.33           C  
ATOM   2079  C   LEU B 130      18.304   3.798  17.963  1.00 44.05           C  
ATOM   2080  O   LEU B 130      18.696   3.388  19.056  1.00 44.08           O  
ATOM   2081  CB  LEU B 130      17.240   6.032  17.539  1.00 44.36           C  
ATOM   2082  CG  LEU B 130      16.034   6.956  17.348  1.00 44.42           C  
ATOM   2083  CD1 LEU B 130      16.477   8.407  17.214  1.00 45.07           C  
ATOM   2084  CD2 LEU B 130      15.215   6.540  16.145  1.00 44.62           C  
ATOM   2085  N   THR B 131      18.983   3.619  16.832  1.00 43.79           N  
ATOM   2086  CA  THR B 131      20.263   2.904  16.798  1.00 43.59           C  
ATOM   2087  C   THR B 131      21.453   3.863  16.844  1.00 43.54           C  
ATOM   2088  O   THR B 131      21.347   5.015  16.419  1.00 43.56           O  
ATOM   2089  CB  THR B 131      20.391   2.004  15.544  1.00 43.55           C  
ATOM   2090  OG1 THR B 131      20.441   2.819  14.368  1.00 43.22           O  
ATOM   2091  CG2 THR B 131      19.216   1.043  15.437  1.00 43.44           C  
ATOM   2092  N   ALA B 132      22.578   3.384  17.370  1.00 43.43           N  
ATOM   2093  CA  ALA B 132      23.822   4.154  17.378  1.00 43.35           C  
ATOM   2094  C   ALA B 132      24.553   4.011  16.047  1.00 43.25           C  
ATOM   2095  O   ALA B 132      24.535   2.939  15.439  1.00 43.36           O  
ATOM   2096  CB  ALA B 132      24.717   3.711  18.523  1.00 43.29           C  
ATOM   2097  N   ARG B 133      25.194   5.093  15.605  1.00 43.05           N  
ATOM   2098  CA  ARG B 133      25.966   5.101  14.359  1.00 42.85           C  
ATOM   2099  C   ARG B 133      27.099   4.072  14.390  1.00 42.84           C  
ATOM   2100  O   ARG B 133      27.953   4.104  15.281  1.00 42.76           O  
ATOM   2101  CB  ARG B 133      26.523   6.504  14.078  1.00 42.77           C  
ATOM   2102  CG  ARG B 133      27.203   6.665  12.716  1.00 42.19           C  
ATOM   2103  CD  ARG B 133      26.190   6.736  11.579  1.00 41.52           C  
ATOM   2104  NE  ARG B 133      26.832   6.776  10.264  1.00 41.31           N  
ATOM   2105  CZ  ARG B 133      27.183   5.703   9.556  1.00 40.77           C  
ATOM   2106  NH1 ARG B 133      26.965   4.479  10.026  1.00 39.50           N  
ATOM   2107  NH2 ARG B 133      27.758   5.857   8.370  1.00 40.41           N  
ATOM   2108  N   ALA B 134      27.093   3.165  13.412  1.00 42.85           N  
ATOM   2109  CA  ALA B 134      28.042   2.051  13.370  1.00 43.07           C  
ATOM   2110  C   ALA B 134      28.185   1.431  11.979  1.00 43.39           C  
ATOM   2111  O   ALA B 134      27.253   1.455  11.174  1.00 43.28           O  
ATOM   2112  CB  ALA B 134      27.638   0.976  14.380  1.00 42.84           C  
ATOM   2113  N   VAL B 135      29.366   0.880  11.707  1.00 43.82           N  
ATOM   2114  CA  VAL B 135      29.587   0.041  10.529  1.00 44.25           C  
ATOM   2115  C   VAL B 135      30.118  -1.322  10.973  1.00 44.62           C  
ATOM   2116  O   VAL B 135      30.993  -1.406  11.837  1.00 44.60           O  
ATOM   2117  CB  VAL B 135      30.558   0.686   9.509  1.00 44.14           C  
ATOM   2118  CG1 VAL B 135      30.685  -0.180   8.263  1.00 44.02           C  
ATOM   2119  CG2 VAL B 135      30.078   2.065   9.112  1.00 44.31           C  
ATOM   2120  N   VAL B 136      29.560  -2.384  10.397  1.00 45.09           N  
ATOM   2121  CA  VAL B 136      30.021  -3.743  10.656  1.00 45.56           C  
ATOM   2122  C   VAL B 136      30.151  -4.470   9.323  1.00 45.96           C  
ATOM   2123  O   VAL B 136      29.189  -4.555   8.558  1.00 45.94           O  
ATOM   2124  CB  VAL B 136      29.065  -4.538  11.590  1.00 45.57           C  
ATOM   2125  CG1 VAL B 136      29.786  -5.745  12.183  1.00 45.58           C  
ATOM   2126  CG2 VAL B 136      28.517  -3.662  12.711  1.00 45.84           C  
ATOM   2127  N   VAL B 137      31.348  -4.978   9.043  1.00 46.44           N  
ATOM   2128  CA  VAL B 137      31.601  -5.698   7.799  1.00 47.00           C  
ATOM   2129  C   VAL B 137      31.760  -7.195   8.084  1.00 47.47           C  
ATOM   2130  O   VAL B 137      32.498  -7.598   8.990  1.00 47.46           O  
ATOM   2131  CB  VAL B 137      32.825  -5.134   7.033  1.00 47.00           C  
ATOM   2132  CG1 VAL B 137      32.843  -5.656   5.606  1.00 46.92           C  
ATOM   2133  CG2 VAL B 137      32.804  -3.603   7.025  1.00 46.96           C  
ATOM   2134  N   LEU B 138      31.041  -8.001   7.310  1.00 47.98           N  
ATOM   2135  CA  LEU B 138      30.966  -9.446   7.511  1.00 48.51           C  
ATOM   2136  C   LEU B 138      31.454 -10.183   6.273  1.00 48.80           C  
ATOM   2137  O   LEU B 138      31.182  -9.762   5.146  1.00 48.72           O  
ATOM   2138  CB  LEU B 138      29.518  -9.864   7.801  1.00 48.50           C  
ATOM   2139  CG  LEU B 138      28.911  -9.897   9.209  1.00 48.46           C  
ATOM   2140  CD1 LEU B 138      29.097  -8.600   9.976  1.00 48.75           C  
ATOM   2141  CD2 LEU B 138      27.427 -10.239   9.109  1.00 48.45           C  
ATOM   2142  N   ASP B 139      32.161 -11.291   6.486  1.00 49.23           N  
ATOM   2143  CA  ASP B 139      32.618 -12.133   5.378  1.00 49.71           C  
ATOM   2144  C   ASP B 139      31.521 -13.091   4.902  1.00 49.96           C  
ATOM   2145  O   ASP B 139      30.385 -13.032   5.380  1.00 50.02           O  
ATOM   2146  CB  ASP B 139      33.901 -12.891   5.752  1.00 49.70           C  
ATOM   2147  CG  ASP B 139      33.707 -13.862   6.912  1.00 49.84           C  
ATOM   2148  OD1 ASP B 139      34.723 -14.404   7.392  1.00 49.97           O  
ATOM   2149  OD2 ASP B 139      32.556 -14.092   7.343  1.00 50.16           O  
ATOM   2150  N   GLY B 140      31.877 -13.975   3.970  1.00 50.36           N  
ATOM   2151  CA  GLY B 140      30.944 -14.943   3.389  1.00 50.68           C  
ATOM   2152  C   GLY B 140      30.165 -15.777   4.389  1.00 51.00           C  
ATOM   2153  O   GLY B 140      29.013 -16.134   4.137  1.00 51.12           O  
ATOM   2154  N   GLN B 141      30.782 -16.078   5.529  1.00 51.32           N  
ATOM   2155  CA  GLN B 141      30.158 -16.933   6.541  1.00 51.71           C  
ATOM   2156  C   GLN B 141      29.944 -16.238   7.897  1.00 51.67           C  
ATOM   2157  O   GLN B 141      30.149 -16.838   8.961  1.00 51.66           O  
ATOM   2158  CB  GLN B 141      30.941 -18.247   6.695  1.00 51.87           C  
ATOM   2159  CG  GLN B 141      30.874 -19.170   5.469  1.00 52.73           C  
ATOM   2160  CD  GLN B 141      29.553 -19.924   5.358  1.00 53.96           C  
ATOM   2161  OE1 GLN B 141      28.728 -19.632   4.487  1.00 54.34           O  
ATOM   2162  NE2 GLN B 141      29.347 -20.897   6.243  1.00 54.06           N  
ATOM   2163  N   ASP B 142      29.536 -14.968   7.834  1.00 51.59           N  
ATOM   2164  CA  ASP B 142      29.052 -14.192   8.993  1.00 51.49           C  
ATOM   2165  C   ASP B 142      30.104 -13.660   9.976  1.00 51.24           C  
ATOM   2166  O   ASP B 142      29.752 -12.947  10.921  1.00 51.27           O  
ATOM   2167  CB  ASP B 142      27.958 -14.957   9.760  1.00 51.63           C  
ATOM   2168  CG  ASP B 142      26.580 -14.796   9.144  1.00 52.03           C  
ATOM   2169  OD1 ASP B 142      26.473 -14.282   8.006  1.00 52.02           O  
ATOM   2170  OD2 ASP B 142      25.596 -15.190   9.810  1.00 52.65           O  
ATOM   2171  N   ASN B 143      31.375 -13.996   9.763  1.00 50.95           N  
ATOM   2172  CA  ASN B 143      32.447 -13.526  10.646  1.00 50.63           C  
ATOM   2173  C   ASN B 143      32.754 -12.047  10.434  1.00 50.49           C  
ATOM   2174  O   ASN B 143      32.863 -11.579   9.295  1.00 50.35           O  
ATOM   2175  CB  ASN B 143      33.722 -14.359  10.477  1.00 50.61           C  
ATOM   2176  CG  ASN B 143      33.487 -15.845  10.674  1.00 50.65           C  
ATOM   2177  OD1 ASN B 143      33.673 -16.638   9.751  1.00 50.63           O  
ATOM   2178  ND2 ASN B 143      33.078 -16.230  11.878  1.00 50.78           N  
ATOM   2179  N   VAL B 144      32.891 -11.322  11.541  1.00 50.31           N  
ATOM   2180  CA  VAL B 144      33.157  -9.887  11.515  1.00 50.17           C  
ATOM   2181  C   VAL B 144      34.608  -9.628  11.138  1.00 50.09           C  
ATOM   2182  O   VAL B 144      35.528 -10.071  11.831  1.00 50.12           O  
ATOM   2183  CB  VAL B 144      32.835  -9.218  12.876  1.00 50.22           C  
ATOM   2184  CG1 VAL B 144      33.222  -7.732  12.872  1.00 50.23           C  
ATOM   2185  CG2 VAL B 144      31.364  -9.386  13.215  1.00 50.21           C  
ATOM   2186  N   ILE B 145      34.799  -8.911  10.033  1.00 49.96           N  
ATOM   2187  CA  ILE B 145      36.135  -8.564   9.549  1.00 49.82           C  
ATOM   2188  C   ILE B 145      36.477  -7.093   9.810  1.00 49.77           C  
ATOM   2189  O   ILE B 145      37.653  -6.723   9.848  1.00 50.02           O  
ATOM   2190  CB  ILE B 145      36.335  -8.932   8.052  1.00 49.79           C  
ATOM   2191  CG1 ILE B 145      35.222  -8.334   7.182  1.00 49.56           C  
ATOM   2192  CG2 ILE B 145      36.414 -10.449   7.888  1.00 49.75           C  
ATOM   2193  CD1 ILE B 145      35.498  -8.382   5.694  1.00 49.07           C  
ATOM   2194  N   TYR B 146      35.445  -6.268   9.983  1.00 49.53           N  
ATOM   2195  CA  TYR B 146      35.607  -4.886  10.438  1.00 49.28           C  
ATOM   2196  C   TYR B 146      34.397  -4.436  11.256  1.00 49.07           C  
ATOM   2197  O   TYR B 146      33.258  -4.757  10.915  1.00 49.04           O  
ATOM   2198  CB  TYR B 146      35.840  -3.928   9.260  1.00 49.41           C  
ATOM   2199  CG  TYR B 146      36.135  -2.500   9.684  1.00 49.51           C  
ATOM   2200  CD1 TYR B 146      37.436  -2.096   9.984  1.00 49.59           C  
ATOM   2201  CD2 TYR B 146      35.111  -1.558   9.800  1.00 49.54           C  
ATOM   2202  CE1 TYR B 146      37.711  -0.792  10.381  1.00 49.65           C  
ATOM   2203  CE2 TYR B 146      35.374  -0.253  10.199  1.00 49.72           C  
ATOM   2204  CZ  TYR B 146      36.676   0.124  10.485  1.00 49.94           C  
ATOM   2205  OH  TYR B 146      36.942   1.418  10.876  1.00 50.17           O  
ATOM   2206  N   SER B 147      34.658  -3.699  12.334  1.00 48.83           N  
ATOM   2207  CA  SER B 147      33.601  -3.128  13.169  1.00 48.67           C  
ATOM   2208  C   SER B 147      34.054  -1.832  13.841  1.00 48.65           C  
ATOM   2209  O   SER B 147      35.180  -1.741  14.340  1.00 48.58           O  
ATOM   2210  CB  SER B 147      33.140  -4.134  14.225  1.00 48.54           C  
ATOM   2211  OG  SER B 147      34.143  -4.354  15.200  1.00 48.52           O  
ATOM   2212  N   GLU B 148      33.172  -0.837  13.851  1.00 48.59           N  
ATOM   2213  CA  GLU B 148      33.473   0.451  14.466  1.00 48.69           C  
ATOM   2214  C   GLU B 148      32.232   1.104  15.065  1.00 48.86           C  
ATOM   2215  O   GLU B 148      31.219   1.283  14.386  1.00 48.77           O  
ATOM   2216  CB  GLU B 148      34.126   1.395  13.451  1.00 48.59           C  
ATOM   2217  CG  GLU B 148      34.644   2.701  14.049  1.00 48.42           C  
ATOM   2218  CD  GLU B 148      35.096   3.702  12.998  1.00 48.37           C  
ATOM   2219  OE1 GLU B 148      34.976   3.410  11.788  1.00 48.60           O  
ATOM   2220  OE2 GLU B 148      35.574   4.787  13.386  1.00 48.03           O  
ATOM   2221  N   LEU B 149      32.325   1.449  16.345  1.00 49.10           N  
ATOM   2222  CA  LEU B 149      31.303   2.239  17.011  1.00 49.39           C  
ATOM   2223  C   LEU B 149      31.826   3.660  17.186  1.00 49.64           C  
ATOM   2224  O   LEU B 149      32.649   3.925  18.065  1.00 49.62           O  
ATOM   2225  CB  LEU B 149      30.948   1.624  18.365  1.00 49.35           C  
ATOM   2226  CG  LEU B 149      29.743   2.190  19.120  1.00 49.29           C  
ATOM   2227  CD1 LEU B 149      28.423   1.708  18.525  1.00 49.20           C  
ATOM   2228  CD2 LEU B 149      29.847   1.796  20.572  1.00 49.15           C  
ATOM   2229  N   VAL B 150      31.352   4.564  16.333  1.00 50.07           N  
ATOM   2230  CA  VAL B 150      31.813   5.953  16.332  1.00 50.52           C  
ATOM   2231  C   VAL B 150      31.445   6.645  17.647  1.00 50.72           C  
ATOM   2232  O   VAL B 150      30.271   6.719  18.015  1.00 50.75           O  
ATOM   2233  CB  VAL B 150      31.245   6.753  15.135  1.00 50.49           C  
ATOM   2234  CG1 VAL B 150      32.136   7.947  14.831  1.00 50.89           C  
ATOM   2235  CG2 VAL B 150      31.124   5.873  13.900  1.00 50.72           C  
ATOM   2236  N   ASN B 151      32.463   7.141  18.347  1.00 51.02           N  
ATOM   2237  CA  ASN B 151      32.291   7.747  19.669  1.00 51.39           C  
ATOM   2238  C   ASN B 151      31.368   8.968  19.673  1.00 51.46           C  
ATOM   2239  O   ASN B 151      30.601   9.167  20.613  1.00 51.51           O  
ATOM   2240  CB  ASN B 151      33.649   8.097  20.287  1.00 51.45           C  
ATOM   2241  CG  ASN B 151      33.628   8.060  21.807  1.00 52.01           C  
ATOM   2242  OD1 ASN B 151      33.793   9.088  22.467  1.00 52.78           O  
ATOM   2243  ND2 ASN B 151      33.422   6.871  22.370  1.00 52.29           N  
ATOM   2244  N   GLU B 152      31.457   9.785  18.627  1.00 51.62           N  
ATOM   2245  CA  GLU B 152      30.518  10.881  18.420  1.00 51.70           C  
ATOM   2246  C   GLU B 152      29.581  10.501  17.279  1.00 51.78           C  
ATOM   2247  O   GLU B 152      30.031  10.155  16.186  1.00 51.89           O  
ATOM   2248  CB  GLU B 152      31.259  12.194  18.130  1.00 51.77           C  
ATOM   2249  CG  GLU B 152      30.387  13.351  17.614  1.00 51.81           C  
ATOM   2250  CD  GLU B 152      29.249  13.734  18.555  1.00 52.02           C  
ATOM   2251  OE1 GLU B 152      29.464  13.800  19.786  1.00 52.03           O  
ATOM   2252  OE2 GLU B 152      28.133  13.979  18.052  1.00 52.11           O  
ATOM   2253  N   ILE B 153      28.280  10.560  17.550  1.00 51.81           N  
ATOM   2254  CA  ILE B 153      27.254  10.114  16.606  1.00 51.80           C  
ATOM   2255  C   ILE B 153      27.237  10.923  15.301  1.00 51.77           C  
ATOM   2256  O   ILE B 153      27.175  10.342  14.213  1.00 51.80           O  
ATOM   2257  CB  ILE B 153      25.851  10.076  17.281  1.00 51.85           C  
ATOM   2258  CG1 ILE B 153      25.778   8.907  18.275  1.00 51.98           C  
ATOM   2259  CG2 ILE B 153      24.734   9.967  16.241  1.00 51.83           C  
ATOM   2260  CD1 ILE B 153      24.715   9.058  19.362  1.00 52.08           C  
ATOM   2261  N   THR B 154      27.318  12.249  15.416  1.00 51.71           N  
ATOM   2262  CA  THR B 154      27.235  13.151  14.255  1.00 51.68           C  
ATOM   2263  C   THR B 154      28.405  13.029  13.270  1.00 51.68           C  
ATOM   2264  O   THR B 154      28.298  13.467  12.123  1.00 51.76           O  
ATOM   2265  CB  THR B 154      27.071  14.639  14.673  1.00 51.67           C  
ATOM   2266  OG1 THR B 154      28.134  15.020  15.554  1.00 51.39           O  
ATOM   2267  CG2 THR B 154      25.728  14.867  15.362  1.00 51.65           C  
ATOM   2268  N   THR B 155      29.513  12.439  13.719  1.00 51.62           N  
ATOM   2269  CA  THR B 155      30.676  12.223  12.852  1.00 51.62           C  
ATOM   2270  C   THR B 155      30.585  10.905  12.080  1.00 51.48           C  
ATOM   2271  O   THR B 155      29.756  10.048  12.395  1.00 51.48           O  
ATOM   2272  CB  THR B 155      32.012  12.284  13.636  1.00 51.69           C  
ATOM   2273  OG1 THR B 155      31.942  11.428  14.784  1.00 51.62           O  
ATOM   2274  CG2 THR B 155      32.316  13.714  14.074  1.00 51.59           C  
ATOM   2275  N   GLU B 156      31.445  10.757  11.074  1.00 51.36           N  
ATOM   2276  CA  GLU B 156      31.440   9.588  10.192  1.00 51.22           C  
ATOM   2277  C   GLU B 156      32.510   8.556  10.564  1.00 51.12           C  
ATOM   2278  O   GLU B 156      33.602   8.924  11.002  1.00 51.09           O  
ATOM   2279  CB  GLU B 156      31.621  10.020   8.731  1.00 51.25           C  
ATOM   2280  CG  GLU B 156      30.438  10.784   8.138  1.00 51.49           C  
ATOM   2281  CD  GLU B 156      29.223   9.904   7.904  1.00 52.07           C  
ATOM   2282  OE1 GLU B 156      28.146  10.211   8.463  1.00 52.23           O  
ATOM   2283  OE2 GLU B 156      29.344   8.902   7.167  1.00 52.03           O  
ATOM   2284  N   PRO B 157      32.192   7.257  10.393  1.00 50.98           N  
ATOM   2285  CA  PRO B 157      33.130   6.146  10.583  1.00 50.83           C  
ATOM   2286  C   PRO B 157      34.244   6.102   9.537  1.00 50.63           C  
ATOM   2287  O   PRO B 157      34.136   6.732   8.484  1.00 50.64           O  
ATOM   2288  CB  PRO B 157      32.237   4.911  10.435  1.00 50.89           C  
ATOM   2289  CG  PRO B 157      31.078   5.382   9.637  1.00 50.98           C  
ATOM   2290  CD  PRO B 157      30.833   6.767  10.110  1.00 51.01           C  
ATOM   2291  N   ASN B 158      35.299   5.349   9.839  1.00 50.45           N  
ATOM   2292  CA  ASN B 158      36.442   5.190   8.945  1.00 50.34           C  
ATOM   2293  C   ASN B 158      36.078   4.384   7.694  1.00 50.42           C  
ATOM   2294  O   ASN B 158      36.107   3.150   7.699  1.00 50.37           O  
ATOM   2295  CB  ASN B 158      37.610   4.540   9.700  1.00 50.22           C  
ATOM   2296  CG  ASN B 158      38.955   4.767   9.027  1.00 49.64           C  
ATOM   2297  OD1 ASN B 158      39.067   4.759   7.802  1.00 49.15           O  
ATOM   2298  ND2 ASN B 158      39.990   4.953   9.837  1.00 49.01           N  
ATOM   2299  N   TYR B 159      35.738   5.101   6.625  1.00 50.53           N  
ATOM   2300  CA  TYR B 159      35.296   4.484   5.377  1.00 50.65           C  
ATOM   2301  C   TYR B 159      36.416   3.798   4.599  1.00 50.78           C  
ATOM   2302  O   TYR B 159      36.196   2.749   3.990  1.00 50.88           O  
ATOM   2303  CB  TYR B 159      34.571   5.500   4.488  1.00 50.58           C  
ATOM   2304  CG  TYR B 159      33.150   5.802   4.921  1.00 50.56           C  
ATOM   2305  CD1 TYR B 159      32.550   7.021   4.606  1.00 50.49           C  
ATOM   2306  CD2 TYR B 159      32.407   4.872   5.652  1.00 50.44           C  
ATOM   2307  CE1 TYR B 159      31.243   7.300   4.997  1.00 50.34           C  
ATOM   2308  CE2 TYR B 159      31.104   5.141   6.047  1.00 50.55           C  
ATOM   2309  CZ  TYR B 159      30.528   6.356   5.719  1.00 50.41           C  
ATOM   2310  OH  TYR B 159      29.238   6.622   6.118  1.00 50.23           O  
ATOM   2311  N   ASP B 160      37.605   4.399   4.619  1.00 50.94           N  
ATOM   2312  CA  ASP B 160      38.783   3.824   3.972  1.00 51.08           C  
ATOM   2313  C   ASP B 160      39.119   2.455   4.555  1.00 51.16           C  
ATOM   2314  O   ASP B 160      39.370   1.504   3.812  1.00 51.10           O  
ATOM   2315  CB  ASP B 160      39.990   4.759   4.106  1.00 51.08           C  
ATOM   2316  CG  ASP B 160      39.929   5.946   3.155  1.00 51.45           C  
ATOM   2317  OD1 ASP B 160      39.187   5.891   2.149  1.00 51.36           O  
ATOM   2318  OD2 ASP B 160      40.641   6.940   3.413  1.00 52.11           O  
ATOM   2319  N   ALA B 161      39.108   2.370   5.885  1.00 51.26           N  
ATOM   2320  CA  ALA B 161      39.419   1.139   6.606  1.00 51.47           C  
ATOM   2321  C   ALA B 161      38.382   0.040   6.371  1.00 51.70           C  
ATOM   2322  O   ALA B 161      38.737  -1.135   6.251  1.00 51.60           O  
ATOM   2323  CB  ALA B 161      39.576   1.420   8.096  1.00 51.40           C  
ATOM   2324  N   ALA B 162      37.107   0.428   6.305  1.00 51.96           N  
ATOM   2325  CA  ALA B 162      36.024  -0.510   6.016  1.00 52.16           C  
ATOM   2326  C   ALA B 162      36.181  -1.096   4.611  1.00 52.40           C  
ATOM   2327  O   ALA B 162      35.971  -2.293   4.405  1.00 52.38           O  
ATOM   2328  CB  ALA B 162      34.674   0.169   6.173  1.00 52.11           C  
ATOM   2329  N   LEU B 163      36.561  -0.240   3.663  1.00 52.63           N  
ATOM   2330  CA  LEU B 163      36.883  -0.648   2.297  1.00 52.98           C  
ATOM   2331  C   LEU B 163      38.152  -1.503   2.204  1.00 53.22           C  
ATOM   2332  O   LEU B 163      38.200  -2.465   1.434  1.00 53.27           O  
ATOM   2333  CB  LEU B 163      37.021   0.589   1.399  1.00 52.93           C  
ATOM   2334  CG  LEU B 163      36.001   0.867   0.285  1.00 53.19           C  
ATOM   2335  CD1 LEU B 163      34.551   0.602   0.695  1.00 53.10           C  
ATOM   2336  CD2 LEU B 163      36.166   2.291  -0.236  1.00 53.25           C  
ATOM   2337  N   ALA B 164      39.168  -1.149   2.992  1.00 53.49           N  
ATOM   2338  CA  ALA B 164      40.476  -1.818   2.950  1.00 53.83           C  
ATOM   2339  C   ALA B 164      40.434  -3.271   3.423  1.00 54.04           C  
ATOM   2340  O   ALA B 164      41.377  -4.030   3.193  1.00 54.13           O  
ATOM   2341  CB  ALA B 164      41.508  -1.029   3.754  1.00 53.80           C  
ATOM   2342  N   ALA B 165      39.343  -3.644   4.087  1.00 54.20           N  
ATOM   2343  CA  ALA B 165      39.146  -5.010   4.553  1.00 54.45           C  
ATOM   2344  C   ALA B 165      38.343  -5.828   3.540  1.00 54.65           C  
ATOM   2345  O   ALA B 165      37.928  -6.952   3.830  1.00 54.59           O  
ATOM   2346  CB  ALA B 165      38.457  -5.006   5.915  1.00 54.37           C  
ATOM   2347  N   LEU B 166      38.160  -5.270   2.342  1.00 54.94           N  
ATOM   2348  CA  LEU B 166      37.275  -5.856   1.332  1.00 55.28           C  
ATOM   2349  C   LEU B 166      37.854  -6.235  -0.057  1.00 55.53           C  
ATOM   2350  O   LEU B 166      37.082  -6.619  -0.937  1.00 55.55           O  
ATOM   2351  CB  LEU B 166      36.044  -4.955   1.140  1.00 55.28           C  
ATOM   2352  CG  LEU B 166      34.921  -4.992   2.180  1.00 55.16           C  
ATOM   2353  CD1 LEU B 166      33.974  -3.823   1.961  1.00 54.90           C  
ATOM   2354  CD2 LEU B 166      34.163  -6.315   2.130  1.00 55.08           C  
ATOM   2355  N   LYS B 167      39.167  -6.153  -0.293  1.00 55.82           N  
ATOM   2356  CA  LYS B 167      40.205  -5.816   0.681  1.00 56.08           C  
ATOM   2357  C   LYS B 167      41.216  -4.820   0.113  1.00 56.07           C  
ATOM   2358  O   LYS B 167      41.365  -4.687  -1.103  1.00 56.03           O  
ATOM   2359  CB  LYS B 167      40.922  -7.086   1.170  1.00 56.15           C  
ATOM   2360  CG  LYS B 167      40.839  -8.287   0.217  1.00 56.63           C  
ATOM   2361  CD  LYS B 167      41.707  -8.115  -1.030  1.00 57.26           C  
ATOM   2362  CE  LYS B 167      40.994  -8.627  -2.280  1.00 57.63           C  
ATOM   2363  NZ  LYS B 167      40.699 -10.089  -2.239  1.00 57.55           N  
TER    2364      LYS B 167                                                      
HETATM 2365  O   HOH A2001      -7.910 -12.705  14.754  1.00 46.71           O  
HETATM 2366  O   HOH A2002      -7.700 -10.717  16.827  1.00 48.93           O  
HETATM 2367  O   HOH A2003      -8.515 -10.509  -0.418  1.00 56.11           O  
HETATM 2368  O   HOH A2004     -17.174   1.836  29.822  1.00 46.94           O  
HETATM 2369  O   HOH A2005      -4.595  15.381  31.142  1.00 75.02           O  
HETATM 2370  O   HOH A2006      -2.473 -14.171   8.808  1.00 56.25           O  
HETATM 2371  O   HOH A2007       2.897 -11.621   9.127  1.00 43.45           O  
HETATM 2372  O   HOH A2008     -17.625   4.865  20.688  1.00 36.14           O  
HETATM 2373  O   HOH A2009     -15.228   0.622  17.321  1.00 48.06           O  
HETATM 2374  O   HOH A2010     -19.349  16.428  10.509  1.00 46.07           O  
HETATM 2375  O   HOH B2001      26.870  -4.718  28.273  1.00 55.90           O  
HETATM 2376  O   HOH B2002      30.671  -3.394  24.861  1.00 54.03           O  
HETATM 2377  O   HOH B2003      37.404 -11.412  19.890  1.00 44.95           O  
HETATM 2378  O   HOH B2004       5.717  -9.313   5.645  1.00 51.37           O  
HETATM 2379  O   HOH B2005      24.484 -14.628   6.231  1.00 38.75           O  
HETATM 2380  O   HOH B2006      21.075 -17.905   1.321  1.00 43.26           O  
HETATM 2381  O   HOH B2007      17.890 -10.756  -0.290  1.00 34.61           O  
HETATM 2382  O   HOH B2008      17.845   4.145  14.299  1.00 36.54           O  
HETATM 2383  O   HOH B2009      11.650   8.871   9.966  1.00 21.97           O  
HETATM 2384  O   HOH B2010      13.250  -0.134   3.720  1.00 59.91           O  
HETATM 2385  O   HOH B2011      14.964  -2.528   0.953  1.00 44.76           O  
HETATM 2386  O   HOH B2012      16.092  -0.514  -0.475  1.00 49.30           O  
HETATM 2387  O   HOH B2013      16.023  -9.554  14.311  1.00 44.26           O  
HETATM 2388  O   HOH B2014      25.248  -7.152  22.275  1.00 41.55           O  
HETATM 2389  O   HOH B2015      25.729 -10.084  16.807  1.00 44.38           O  
HETATM 2390  O   HOH B2016      39.269   7.370   7.157  1.00 39.33           O  
HETATM 2391  O   HOH B2017      37.188   7.478   5.454  1.00 38.29           O  
CONECT 1614 1848                                                                
CONECT 1848 1614                                                                
MASTER      381    0    0   11   21    0    0    6 2389    2    2   32          
END                                                                             


A second structure was input as follows:


HEADER    OXIDOREDUCTASE                          26-AUG-10   2XPD              
TITLE     REDUCED THIOL PEROXIDASE (TPX) FROM YERSINIA PSEUDOTUBERCULOSIS       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THIOL PEROXIDASE;                                          
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 EC: 1.11.1.15;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: YERSINIA PSEUDOTUBERCULOSIS;                    
SOURCE   3 ORGANISM_TAXID: 502800;                                              
SOURCE   4 STRAIN: YPIII;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET151                                     
KEYWDS    OXIDOREDUCTASE, PEROXIREDOXIN, THIOREDOXIN-FOLD, ROS PROTECTION       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.GABRIELSEN,C.E.ZETTERSTROM,D.WANG,M.ELOFSSON,A.J.ROE                
REVDAT   2   14-MAR-12 2XPD    1       JRNL   REMARK VERSN                      
REVDAT   1   29-JUN-11 2XPD    0                                                
JRNL        AUTH   M.GABRIELSEN,K.S.BECKHAM,V.A.FEHER,C.E.ZETTERSTROM,D.WANG,   
JRNL        AUTH 2 S.MULLER,M.ELOFSSON,R.E.AMARO,O.BYRON,A.J.ROE                
JRNL        TITL   STRUCTURAL CHARACTERISATION OF TPX FROM YERSINIA             
JRNL        TITL 2 PSEUDOTUBERCULOSIS REVEALS INSIGHTS INTO THE BINDING OF      
JRNL        TITL 3 SALICYLIDENE ACYLHYDRAZIDE COMPOUNDS.                        
JRNL        REF    PLOS ONE                      V.   7 32217 2012              
JRNL        REFN                   ISSN 1932-6203                               
JRNL        PMID   22384182                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0032217                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.GABRIELSEN,C.E.ZETTERSTROM,D.WANG,K.S.BECKHAM,M.ELOFSSON,  
REMARK   1  AUTH 2 N.W.ISAACS,A.J.ROE                                           
REMARK   1  TITL   EXPRESSION, PURIFICATION, CRYSTALLIZATION AND INITIAL X-RAY  
REMARK   1  TITL 2 DIFFRACTION ANALYSIS OF THIOL PEROXIDASE FROM YERSINIA       
REMARK   1  TITL 3 PSEUDOTUBERCULOSIS.                                          
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  66  1606 2010              
REMARK   1  REFN                   ISSN 1744-3091                               
REMARK   1  PMID   21139206                                                     
REMARK   1  DOI    10.1107/S1744309110039679                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.668                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2                              
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.742                         
REMARK   3   NUMBER OF REFLECTIONS             : 64411                          
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) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.2222                          
REMARK   3   FREE R VALUE                     : 0.2683                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.10                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3285                            
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) : 2.0                          
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.052                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4319                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.029                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.32                         
REMARK   3   BIN FREE R VALUE SET COUNT          : 227                          
REMARK   3   BIN FREE R VALUE                    : 0.356                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7362                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 498                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.5                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.874                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.419                                               
REMARK   3    B22 (A**2) : -0.508                                               
REMARK   3    B33 (A**2) : 0.932                                                
REMARK   3    B12 (A**2) : 0.000                                                
REMARK   3    B13 (A**2) : 0.103                                                
REMARK   3    B23 (A**2) : 0.000                                                
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0             
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.199         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.148         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.258        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.910                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.882                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7474 ; 0.022 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10167 ; 1.855 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1000 ; 6.605 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   288 ;39.817 ;25.278       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1191 ;16.933 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;21.548 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1248 ; 0.130 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5555 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3472 ; 0.219 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5207 ; 0.310 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   486 ; 0.171 ; 0.200       
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):    68 ; 0.216 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    26 ; 0.182 ; 0.200       
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):  4971 ; 1.555 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7972 ; 2.680 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2503 ; 3.161 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2195 ; 4.957 ; 4.500       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  7474 ; 2.471 ; 3.000       
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  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   167                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.1880  -6.0720  22.8390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0434 T22:   0.0610                                     
REMARK   3      T33:   0.0833 T12:   0.0027                                     
REMARK   3      T13:  -0.0072 T23:  -0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7521 L22:   0.3740                                     
REMARK   3      L33:   0.1632 L12:  -0.2525                                     
REMARK   3      L13:   0.0990 L23:  -0.0366                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0078 S12:   0.0267 S13:   0.0251                       
REMARK   3      S21:  -0.0217 S22:  -0.0231 S23:  -0.0056                       
REMARK   3      S31:  -0.0103 S32:  -0.0112 S33:   0.0153                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B   167                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0250 -17.7700  22.9740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0435 T22:   0.0573                                     
REMARK   3      T33:   0.0825 T12:   0.0018                                     
REMARK   3      T13:  -0.0091 T23:  -0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0054 L22:   0.3621                                     
REMARK   3      L33:   0.1294 L12:  -0.1818                                     
REMARK   3      L13:   0.0392 L23:  -0.0393                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0153 S12:   0.0431 S13:  -0.0605                       
REMARK   3      S21:  -0.0110 S22:  -0.0202 S23:   0.0044                       
REMARK   3      S31:   0.0043 S32:   0.0186 S33:   0.0049                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    -2        C   167                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.8540   3.0540  51.0820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0628 T22:   0.0485                                     
REMARK   3      T33:   0.0785 T12:  -0.0027                                     
REMARK   3      T13:  -0.0157 T23:   0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2775 L22:   0.7513                                     
REMARK   3      L33:   0.3786 L12:   0.0155                                     
REMARK   3      L13:  -0.0541 L23:  -0.0259                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0215 S12:  -0.0027 S13:   0.0267                       
REMARK   3      S21:   0.0140 S22:   0.0034 S23:  -0.0020                       
REMARK   3      S31:  -0.0357 S32:  -0.0008 S33:   0.0181                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   167                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.5800 -26.9720  51.3340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0594 T22:   0.0398                                     
REMARK   3      T33:   0.0951 T12:  -0.0050                                     
REMARK   3      T13:   0.0090 T23:   0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5246 L22:   0.7057                                     
REMARK   3      L33:   0.2996 L12:   0.0641                                     
REMARK   3      L13:   0.0486 L23:   0.0834                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0262 S12:   0.0052 S13:  -0.0629                       
REMARK   3      S21:  -0.0031 S22:   0.0027 S23:   0.0177                       
REMARK   3      S31:   0.0270 S32:   0.0093 S33:   0.0235                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E   167                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.2560 -19.3270  -5.5930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0555 T22:   0.0605                                     
REMARK   3      T33:   0.0751 T12:  -0.0051                                     
REMARK   3      T13:   0.0036 T23:  -0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8967 L22:   0.9128                                     
REMARK   3      L33:   0.5136 L12:   0.1249                                     
REMARK   3      L13:   0.3165 L23:  -0.1261                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0112 S12:  -0.0160 S13:   0.0026                       
REMARK   3      S21:   0.0111 S22:  -0.0034 S23:   0.1267                       
REMARK   3      S31:   0.0154 S32:  -0.0172 S33:  -0.0078                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     2        F   167                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.6350  -4.7410  -6.3410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0556 T22:   0.0664                                     
REMARK   3      T33:   0.1428 T12:  -0.0303                                     
REMARK   3      T13:  -0.0340 T23:   0.0367                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5587 L22:   2.0316                                     
REMARK   3      L33:   0.3877 L12:   0.4212                                     
REMARK   3      L13:  -0.4689 L23:  -0.4921                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1224 S12:  -0.1162 S13:  -0.0042                       
REMARK   3      S21:   0.1220 S22:  -0.1948 S23:  -0.4042                       
REMARK   3      S31:  -0.0731 S32:   0.0797 S33:   0.0724                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   501        A   501                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.6680 -24.8840  30.6550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1048 T22:   0.1145                                     
REMARK   3      T33:   0.1366 T12:   0.0199                                     
REMARK   3      T13:  -0.0105 T23:   0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3320 L22:  10.7685                                     
REMARK   3      L33:   0.1349 L12:   7.5751                                     
REMARK   3      L13:  -0.8384 L23:  -1.1893                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0368 S12:  -0.0500 S13:  -0.0675                       
REMARK   3      S21:   0.0382 S22:  -0.0640 S23:  -0.0858                       
REMARK   3      S31:  -0.0075 S32:   0.0073 S33:   0.0272                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 6                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  2001        A  2117                          
REMARK   3    RESIDUE RANGE :   B  2001        B  2101                          
REMARK   3    RESIDUE RANGE :   C  2001        C  2082                          
REMARK   3    RESIDUE RANGE :   D  2001        D  2089                          
REMARK   3    RESIDUE RANGE :   E  2001        E  2062                          
REMARK   3    RESIDUE RANGE :   F  2001        F  2047                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.1470 -12.3160  26.8060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0568 T22:   0.0573                                     
REMARK   3      T33:   0.1054 T12:  -0.0068                                     
REMARK   3      T13:  -0.0071 T23:   0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0417 L22:   0.0293                                     
REMARK   3      L33:   0.1263 L12:  -0.0312                                     
REMARK   3      L13:   0.0198 L23:  -0.0248                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0009 S12:   0.0019 S13:  -0.0072                       
REMARK   3      S21:  -0.0022 S22:  -0.0069 S23:   0.0089                       
REMARK   3      S31:  -0.0041 S32:   0.0036 S33:   0.0060                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK BULK SOLVENT                                    
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.400                                         
REMARK   3   ION PROBE RADIUS   : 0.800                                         
REMARK   3   SHRINKAGE RADIUS   : 0.800                                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 2XPD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-AUG-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-45114.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : SI (111) DOUBLE CRYSTAL            
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64433                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.00                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.67                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY                : 2.8                                
REMARK 200  R MERGE                    (I) : 0.15                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 5.30                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.8                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.64                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.70                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: MODIFIED PDB ENTRY 3HVV                              
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3 350, 0.2 M SODIUM              
REMARK 280  CITRATE TRIBASIC                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       46.03400            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.4 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.9 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.1 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -32                                                      
REMARK 465     HIS A   -31                                                      
REMARK 465     HIS A   -30                                                      
REMARK 465     HIS A   -29                                                      
REMARK 465     HIS A   -28                                                      
REMARK 465     HIS A   -27                                                      
REMARK 465     HIS A   -26                                                      
REMARK 465     GLY A   -25                                                      
REMARK 465     LYS A   -24                                                      
REMARK 465     PRO A   -23                                                      
REMARK 465     ILE A   -22                                                      
REMARK 465     PRO A   -21                                                      
REMARK 465     ASN A   -20                                                      
REMARK 465     PRO A   -19                                                      
REMARK 465     LEU A   -18                                                      
REMARK 465     LEU A   -17                                                      
REMARK 465     GLY A   -16                                                      
REMARK 465     LEU A   -15                                                      
REMARK 465     ASP A   -14                                                      
REMARK 465     SER A   -13                                                      
REMARK 465     THR A   -12                                                      
REMARK 465     GLU A   -11                                                      
REMARK 465     ASN A   -10                                                      
REMARK 465     LEU A    -9                                                      
REMARK 465     TYR A    -8                                                      
REMARK 465     PHE A    -7                                                      
REMARK 465     GLN A    -6                                                      
REMARK 465     GLY A    -5                                                      
REMARK 465     ILE A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     PHE A    -1                                                      
REMARK 465     THR A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     MET B   -32                                                      
REMARK 465     HIS B   -31                                                      
REMARK 465     HIS B   -30                                                      
REMARK 465     HIS B   -29                                                      
REMARK 465     HIS B   -28                                                      
REMARK 465     HIS B   -27                                                      
REMARK 465     HIS B   -26                                                      
REMARK 465     GLY B   -25                                                      
REMARK 465     LYS B   -24                                                      
REMARK 465     PRO B   -23                                                      
REMARK 465     ILE B   -22                                                      
REMARK 465     PRO B   -21                                                      
REMARK 465     ASN B   -20                                                      
REMARK 465     PRO B   -19                                                      
REMARK 465     LEU B   -18                                                      
REMARK 465     LEU B   -17                                                      
REMARK 465     GLY B   -16                                                      
REMARK 465     LEU B   -15                                                      
REMARK 465     ASP B   -14                                                      
REMARK 465     SER B   -13                                                      
REMARK 465     THR B   -12                                                      
REMARK 465     GLU B   -11                                                      
REMARK 465     ASN B   -10                                                      
REMARK 465     LEU B    -9                                                      
REMARK 465     TYR B    -8                                                      
REMARK 465     PHE B    -7                                                      
REMARK 465     GLN B    -6                                                      
REMARK 465     GLY B    -5                                                      
REMARK 465     ILE B    -4                                                      
REMARK 465     ASP B    -3                                                      
REMARK 465     PRO B    -2                                                      
REMARK 465     PHE B    -1                                                      
REMARK 465     THR B     0                                                      
REMARK 465     MET C   -32                                                      
REMARK 465     HIS C   -31                                                      
REMARK 465     HIS C   -30                                                      
REMARK 465     HIS C   -29                                                      
REMARK 465     HIS C   -28                                                      
REMARK 465     HIS C   -27                                                      
REMARK 465     HIS C   -26                                                      
REMARK 465     GLY C   -25                                                      
REMARK 465     LYS C   -24                                                      
REMARK 465     PRO C   -23                                                      
REMARK 465     ILE C   -22                                                      
REMARK 465     PRO C   -21                                                      
REMARK 465     ASN C   -20                                                      
REMARK 465     PRO C   -19                                                      
REMARK 465     LEU C   -18                                                      
REMARK 465     LEU C   -17                                                      
REMARK 465     GLY C   -16                                                      
REMARK 465     LEU C   -15                                                      
REMARK 465     ASP C   -14                                                      
REMARK 465     SER C   -13                                                      
REMARK 465     THR C   -12                                                      
REMARK 465     GLU C   -11                                                      
REMARK 465     ASN C   -10                                                      
REMARK 465     LEU C    -9                                                      
REMARK 465     TYR C    -8                                                      
REMARK 465     PHE C    -7                                                      
REMARK 465     GLN C    -6                                                      
REMARK 465     GLY C    -5                                                      
REMARK 465     ILE C    -4                                                      
REMARK 465     ASP C    -3                                                      
REMARK 465     MET D   -32                                                      
REMARK 465     HIS D   -31                                                      
REMARK 465     HIS D   -30                                                      
REMARK 465     HIS D   -29                                                      
REMARK 465     HIS D   -28                                                      
REMARK 465     HIS D   -27                                                      
REMARK 465     HIS D   -26                                                      
REMARK 465     GLY D   -25                                                      
REMARK 465     LYS D   -24                                                      
REMARK 465     PRO D   -23                                                      
REMARK 465     ILE D   -22                                                      
REMARK 465     PRO D   -21                                                      
REMARK 465     ASN D   -20                                                      
REMARK 465     PRO D   -19                                                      
REMARK 465     LEU D   -18                                                      
REMARK 465     LEU D   -17                                                      
REMARK 465     GLY D   -16                                                      
REMARK 465     LEU D   -15                                                      
REMARK 465     ASP D   -14                                                      
REMARK 465     SER D   -13                                                      
REMARK 465     THR D   -12                                                      
REMARK 465     GLU D   -11                                                      
REMARK 465     ASN D   -10                                                      
REMARK 465     LEU D    -9                                                      
REMARK 465     TYR D    -8                                                      
REMARK 465     PHE D    -7                                                      
REMARK 465     GLN D    -6                                                      
REMARK 465     GLY D    -5                                                      
REMARK 465     ILE D    -4                                                      
REMARK 465     ASP D    -3                                                      
REMARK 465     PRO D    -2                                                      
REMARK 465     PHE D    -1                                                      
REMARK 465     THR D     0                                                      
REMARK 465     MET E   -32                                                      
REMARK 465     HIS E   -31                                                      
REMARK 465     HIS E   -30                                                      
REMARK 465     HIS E   -29                                                      
REMARK 465     HIS E   -28                                                      
REMARK 465     HIS E   -27                                                      
REMARK 465     HIS E   -26                                                      
REMARK 465     GLY E   -25                                                      
REMARK 465     LYS E   -24                                                      
REMARK 465     PRO E   -23                                                      
REMARK 465     ILE E   -22                                                      
REMARK 465     PRO E   -21                                                      
REMARK 465     ASN E   -20                                                      
REMARK 465     PRO E   -19                                                      
REMARK 465     LEU E   -18                                                      
REMARK 465     LEU E   -17                                                      
REMARK 465     GLY E   -16                                                      
REMARK 465     LEU E   -15                                                      
REMARK 465     ASP E   -14                                                      
REMARK 465     SER E   -13                                                      
REMARK 465     THR E   -12                                                      
REMARK 465     GLU E   -11                                                      
REMARK 465     ASN E   -10                                                      
REMARK 465     LEU E    -9                                                      
REMARK 465     TYR E    -8                                                      
REMARK 465     PHE E    -7                                                      
REMARK 465     GLN E    -6                                                      
REMARK 465     GLY E    -5                                                      
REMARK 465     ILE E    -4                                                      
REMARK 465     ASP E    -3                                                      
REMARK 465     PRO E    -2                                                      
REMARK 465     PHE E    -1                                                      
REMARK 465     THR E     0                                                      
REMARK 465     MET F   -32                                                      
REMARK 465     HIS F   -31                                                      
REMARK 465     HIS F   -30                                                      
REMARK 465     HIS F   -29                                                      
REMARK 465     HIS F   -28                                                      
REMARK 465     HIS F   -27                                                      
REMARK 465     HIS F   -26                                                      
REMARK 465     GLY F   -25                                                      
REMARK 465     LYS F   -24                                                      
REMARK 465     PRO F   -23                                                      
REMARK 465     ILE F   -22                                                      
REMARK 465     PRO F   -21                                                      
REMARK 465     ASN F   -20                                                      
REMARK 465     PRO F   -19                                                      
REMARK 465     LEU F   -18                                                      
REMARK 465     LEU F   -17                                                      
REMARK 465     GLY F   -16                                                      
REMARK 465     LEU F   -15                                                      
REMARK 465     ASP F   -14                                                      
REMARK 465     SER F   -13                                                      
REMARK 465     THR F   -12                                                      
REMARK 465     GLU F   -11                                                      
REMARK 465     ASN F   -10                                                      
REMARK 465     LEU F    -9                                                      
REMARK 465     TYR F    -8                                                      
REMARK 465     PHE F    -7                                                      
REMARK 465     GLN F    -6                                                      
REMARK 465     GLY F    -5                                                      
REMARK 465     ILE F    -4                                                      
REMARK 465     ASP F    -3                                                      
REMARK 465     PRO F    -2                                                      
REMARK 465     PHE F    -1                                                      
REMARK 465     THR F     0                                                      
REMARK 465     MET F     1                                                      
REMARK 465     LYS F   167                                                      
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     GLN A  20    CD   OE1  NE2                                       
REMARK 470     GLN A  70    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 124    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 167    CE   NZ                                             
REMARK 470     MET B   1    CB   CG   SD   CE                                   
REMARK 470     LYS B  17    CD   CE   NZ                                        
REMARK 470     LYS C  26    CD   CE   NZ                                        
REMARK 470     LYS D  26    CD   CE   NZ                                        
REMARK 470     GLU D 124    CD   OE1  OE2                                       
REMARK 470     MET E   1    CG   SD   CE                                        
REMARK 470     LYS E  17    CB   CG   CD   CE   NZ                              
REMARK 470     LYS E  26    CG   CD   CE   NZ                                   
REMARK 470     GLU E  76    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 124    CD   OE1  OE2                                       
REMARK 470     GLN F   8    CG   CD   OE1  NE2                                  
REMARK 470     LYS F  17    CG   CD   CE   NZ                                   
REMARK 470     LYS F  24    CG   CD   CE   NZ                                   
REMARK 470     LEU F  75    CB   CG   CD1  CD2                                  
REMARK 470     GLU F  76    CB   CG   CD   OE1  OE2                             
REMARK 470     TYR F 146    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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   NH2  ARG D    47     O    LEU D   166              1.96            
REMARK 500   NH2  ARG E    47     O    GLU E    76              2.05            
REMARK 500   NH2  ARG C    47     O    LEU C   166              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    SER B 101   CB  -  CA  -  C   ANGL. DEV. = -11.7 DEGREES          
REMARK 500    ARG C  47   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ARG D  47   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG D  47   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A   5     -162.92   -122.44                                   
REMARK 500    GLN B   8       51.40     30.97                                   
REMARK 500    LEU B  35        9.16     82.21                                   
REMARK 500    ASP B 113       -8.14    -57.44                                   
REMARK 500    ASP B 142       30.19     71.71                                   
REMARK 500    PHE C  -1        6.67    -63.70                                   
REMARK 500    VAL E   5     -166.19   -116.10                                   
REMARK 500    SER E  55      126.03   -172.83                                   
REMARK 500    GLU E  74       47.71   -104.34                                   
REMARK 500    ALA E 132      172.05    -53.61                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA



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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.