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***  ATPASE/MYOSIN 21-MAR-03 1OE9  ***

elNémo ID: 20091111574324333

Job options:

ID        	=	 20091111574324333
JOBID     	=	 ATPASE/MYOSIN 21-MAR-03 1OE9
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


REMARK    File generated by Swiss-PdbViewer  4.00b0
REMARK    http://www.expasy.org/spdbv/
HEADER    ATPASE/MYOSIN                           21-MAR-03   1OE9              
TITLE     CRYSTAL STRUCTURE OF MYOSIN V MOTOR WITH ESSENTIAL LIGHT              
TITLE    2 CHAIN - NUCLEOTIDE-FREE                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOSIN VA;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: MOTOR DOMAIN, RESIDUES 1-792;                              
COMPND   5 SYNONYM: MYOSIN 5A, DILUTE MYOSIN HEAVY CHAIN, NON-MUSCLE,           
COMPND   6  MYOSIN HEAVY CHAIN P190, MYOSIN-V;                                  
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: MYOSIN LIGHT CHAIN 1, SLOW-TWITCH MUSCLE A                 
COMPND  10  ISOFORM;                                                            
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: RESIDUES 59-208;                                           
COMPND  13 SYNONYM: MLC1SA;                                                     
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE   3 ORGANISM_COMMON: CHICKEN;                                            
SOURCE   4 ORGANISM_TAXID: 9031;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    ATPASE/MYOSIN, UNCONVENTIONAL MYOSIN, MYOSIN V, CHICKEN,              
KEYWDS   2 MOLECULAR MOTOR, ATPASE, ELC, IQ MOTIF, MUSCLE PROTEIN,              
KEYWDS   3 ATP-BINDING                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.-D.COUREUX,A.L.WELLS,J.MENETREY,C.M.YENGO,C.A.MORRIS,               
AUTHOR   2 H.L.SWEENEY,A.HOUDUSSE                                               
REVDAT   2   24-FEB-09 1OE9    1       VERSN                                    
REVDAT   1   26-SEP-03 1OE9    0                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 65624                          
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) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3474                            
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) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4338                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2820                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 218                          
REMARK   3   BIN FREE R VALUE                    : 0.3240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6925                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 333                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.12000                                              
REMARK   3    B22 (A**2) : -0.91000                                             
REMARK   3    B33 (A**2) : -0.12000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.22000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.206         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.185         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.135         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.969         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7077 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  6387 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9557 ; 1.300 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14860 ; 0.791 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   860 ; 5.388 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1049 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7832 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1470 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1626 ; 0.203 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  7596 ; 0.237 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  4141 ; 0.085 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   370 ; 0.195 ; 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):    11 ; 0.135 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    41 ; 0.256 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.181 ; 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):  4327 ; 0.823 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6928 ; 1.509 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2750 ; 2.067 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2624 ; 3.416 ; 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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.DISORDERED REGIONS WERE NOT                        
REMARK   3  MODELED.DISORDERED SIDE-CHAINS WERE NOT MODELED.                    
REMARK   4                                                                      
REMARK   4 1OE9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-MAR-03.                  
REMARK 100 THE PDBE ID CODE IS EBI-12181.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9756                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69115                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.340                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 2MYS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 47.8                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG8000 (W/V), 50MM MOPS              
REMARK 280  PH 6.5, 2MM DTT, 2MM NAN3                                           
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       49.12350            
REMARK 290   SMTRY3   2  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 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  MYOSIN VA: PROCESSIVE ACTIN-BASED MOTOR THAT CAN MOVE IN            
REMARK 400  LARGE STEPS. POSSIBLY INVOLVED IN MELANOSOME TRANSPORT.             
REMARK 400  USUALLYASSOCIATED WITH MYOSIN LIGHT-CHAINS.                         
REMARK 400                                                                      
REMARK 400  MYOSIN LIGHT-CHAIN: THIS PROTEIN IS SIMILAR TO OTHER                
REMARK 400  EF-HAND CALCIUM-BINDING PROTEINS BUT DOES NOT BIND                  
REMARK 400  CALCIUM.                                                            
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     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     GLU A    43                                                      
REMARK 465     GLU A    44                                                      
REMARK 465     GLY A    45                                                      
REMARK 465     LYS A    46                                                      
REMARK 465     ASP A    53                                                      
REMARK 465     PRO A    54                                                      
REMARK 465     LYS A    55                                                      
REMARK 465     THR A    56                                                      
REMARK 465     GLY A   185                                                      
REMARK 465     SER A   186                                                      
REMARK 465     ALA A   187                                                      
REMARK 465     SER A   188                                                      
REMARK 465     GLU A   189                                                      
REMARK 465     ALA A   190                                                      
REMARK 465     THR A   382                                                      
REMARK 465     ALA A   383                                                      
REMARK 465     THR A   384                                                      
REMARK 465     GLU A   385                                                      
REMARK 465     TRP A   484                                                      
REMARK 465     THR A   485                                                      
REMARK 465     LEU A   486                                                      
REMARK 465     ILE A   487                                                      
REMARK 465     GLN A   594                                                      
REMARK 465     ASP A   595                                                      
REMARK 465     GLU A   596                                                      
REMARK 465     GLU A   597                                                      
REMARK 465     LYS A   598                                                      
REMARK 465     ALA A   599                                                      
REMARK 465     ILE A   600                                                      
REMARK 465     SER A   601                                                      
REMARK 465     PRO A   602                                                      
REMARK 465     THR A   603                                                      
REMARK 465     SER A   604                                                      
REMARK 465     ALA A   605                                                      
REMARK 465     THR A   606                                                      
REMARK 465     PRO A   607                                                      
REMARK 465     SER A   608                                                      
REMARK 465     GLY A   609                                                      
REMARK 465     ARG A   610                                                      
REMARK 465     VAL A   611                                                      
REMARK 465     PRO A   612                                                      
REMARK 465     LEU A   613                                                      
REMARK 465     SER A   614                                                      
REMARK 465     ARG A   615                                                      
REMARK 465     THR A   616                                                      
REMARK 465     PRO A   617                                                      
REMARK 465     VAL A   618                                                      
REMARK 465     LYS A   619                                                      
REMARK 465     PRO A   620                                                      
REMARK 465     ALA A   621                                                      
REMARK 465     LYS A   622                                                      
REMARK 465     ALA A   623                                                      
REMARK 465     ARG A   624                                                      
REMARK 465     PRO A   625                                                      
REMARK 465     GLY A   626                                                      
REMARK 465     GLN A   627                                                      
REMARK 465     THR A   628                                                      
REMARK 465     SER A   629                                                      
REMARK 465     LYS A   630                                                      
REMARK 465     GLU A   631                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ILE B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     ASN B    80                                                      
REMARK 465     ARG B    81                                                      
REMARK 465     GLY B    82                                                      
REMARK 465     GLN B    83                                                      
REMARK 465     GLY B    84                                                      
REMARK 465     THR B    85                                                      
REMARK 465     LYS B    98                                                      
REMARK 465     GLU B    99                                                      
REMARK 465     VAL B   151                                                      
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     TYR A  10    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A  19    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  23    CG   CD   CE   NZ                                   
REMARK 470     LYS A  29    CG   CD   CE   NZ                                   
REMARK 470     LYS A  32    CG   CD   CE   NZ                                   
REMARK 470     LYS A  36    CG   CD   CE   NZ                                   
REMARK 470     ARG A  41    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A  47    CG   OD1  OD2                                       
REMARK 470     LYS A  57    CG   CD   CE   NZ                                   
REMARK 470     ASN A 191    CG   OD1  ND2                                       
REMARK 470     GLU A 193    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 194    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 195    CG   CD   CE   NZ                                   
REMARK 470     ARG A 231    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 303    CG   CD   CE   NZ                                   
REMARK 470     GLU A 574    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 584    CG   CD   CE   NZ                                   
REMARK 470     LYS A 587    CG   CD   CE   NZ                                   
REMARK 470     HIS A 632    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 633    CG   CD   CE   NZ                                   
REMARK 470     LYS A 634    CG   CD   CE   NZ                                   
REMARK 470     GLN A 717    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 718    CG   CD   CE   NZ                                   
REMARK 470     LYS A 739    CG   CD   CE   NZ                                   
REMARK 470     ASP A 740    CG   OD1  OD2                                       
REMARK 470     MET A 788    CG   SD   CE                                        
REMARK 470     ALA A 795    CA   C    O    CB                                   
REMARK 470     LYS B   6    CG   CD   CE   NZ                                   
REMARK 470     GLU B  10    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  14    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  58    CG   OD1  OD2                                       
REMARK 470     ARG B  63    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  87    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  88    CG   OD1  OD2                                       
REMARK 470     ARG B  94    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 101    CG   OD1  ND2                                       
REMARK 470     LYS B 103    CG   CD   CE   NZ                                   
REMARK 470     LYS B 146    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 301   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP A 674   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 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 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    TYR A  10      -42.39     84.63                                   
REMARK 500    VAL A  21      -45.03     67.02                                   
REMARK 500    LEU A  48      145.17    179.43                                   
REMARK 500    GLU A 154       71.69     42.02                                   
REMARK 500    ASP A 229     -169.12    -71.83                                   
REMARK 500    PRO A 351      148.00    -37.17                                   
REMARK 500    SER A 448     -160.90   -124.63                                   
REMARK 500    ASP A 555      163.37    179.51                                   
REMARK 500    ASP A 570       36.32   -162.13                                   
REMARK 500    LYS A 633      126.37     49.25                                   
REMARK 500    PHE A 671       68.34     21.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1796                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999  THE LAST THREE RESIDUES AT THE C-TERMINUS FOR CHAIN A               
REMARK 999  DERIVE FROM THE EXPRESSION VECTOR USED IN THE EXPERIMENT.           
DBREF  1OE9 A    1   792  UNP    Q02440   MY5A_CHICK       1    792             
DBREF  1OE9 A  793   795  PDB    1OE9     1OE9           793    795             
DBREF  1OE9 B    1     1  PDB    1OE9     1OE9             1      1             
DBREF  1OE9 B    2   151  UNP    P14649   MLEY_HUMAN      59    208             
CRYST1   53.933   98.247  111.378  90.00 101.43  90.00 P 1 21 1      2   
ATOM      1  N   PHE B   4      25.402  16.689 -18.317  1.00 49.86
ATOM      2  CA  PHE B   4      25.448  18.164 -18.577  1.00 50.06
ATOM      3  C   PHE B   4      26.445  18.519 -19.667  1.00 49.53
ATOM      4  O   PHE B   4      27.570  18.025 -19.666  1.00 50.42
ATOM      5  CB  PHE B   4      25.784  18.925 -17.289  1.00 49.71
ATOM      6  CG  PHE B   4      24.775  18.713 -16.184  1.00 50.17
ATOM      7  CD1 PHE B   4      23.407  18.706 -16.458  1.00 51.12
ATOM      8  CD2 PHE B   4      25.193  18.502 -14.881  1.00 51.20
ATOM      9  CE1 PHE B   4      22.470  18.508 -15.446  1.00 51.68
ATOM     10  CE2 PHE B   4      24.273  18.304 -13.864  1.00 51.37
ATOM     11  CZ  PHE B   4      22.904  18.305 -14.149  1.00 52.02
ATOM     12  N   ASN B   5      26.012  19.365 -20.599  1.00 49.15
ATOM     13  CA  ASN B   5      26.879  19.898 -21.645  1.00 48.35
ATOM     14  C   ASN B   5      27.632  21.136 -21.171  1.00 48.26
ATOM     15  O   ASN B   5      27.357  21.661 -20.084  1.00 47.66
ATOM     16  CB  ASN B   5      26.080  20.185 -22.927  1.00 48.29
ATOM     17  CG  ASN B   5      25.051  21.283 -22.758  1.00 48.25
ATOM     18  OD1 ASN B   5      25.344  22.354 -22.228  1.00 47.71
ATOM     19  ND2 ASN B   5      23.830  21.025 -23.224  1.00 47.17
ATOM     20  N   LYS B   6      28.564  21.604 -21.994  1.00 47.87
ATOM     21  CA  LYS B   6      29.410  22.750 -21.671  1.00 48.21
ATOM     22  C   LYS B   6      28.627  24.018 -21.307  1.00 48.16
ATOM     23  O   LYS B   6      29.004  24.731 -20.382  1.00 47.74
ATOM     24  CB  LYS B   6      30.345  23.072 -22.838  1.00 99.99
ATOM     25  CG  LYS B   6      29.627  23.462 -24.119  1.00 99.99
ATOM     26  CD  LYS B   6      30.614  23.768 -25.234  1.00 99.99
ATOM     27  CE  LYS B   6      29.896  24.158 -26.515  1.00 99.99
ATOM     28  NZ  LYS B   6      29.144  25.436 -26.363  1.00 99.99
ATOM     29  N   ASP B   7      27.555  24.302 -22.036  1.00 48.31
ATOM     30  CA  ASP B   7      26.759  25.493 -21.758  1.00 48.95
ATOM     31  C   ASP B   7      26.126  25.442 -20.364  1.00 48.89
ATOM     32  O   ASP B   7      26.188  26.416 -19.623  1.00 49.10
ATOM     33  CB  ASP B   7      25.677  25.703 -22.826  1.00 49.18
ATOM     34  CG  ASP B   7      26.240  26.254 -24.118  1.00 50.04
ATOM     35  OD1 ASP B   7      27.494  26.372 -24.251  1.00 52.67
ATOM     36  OD2 ASP B   7      25.501  26.586 -25.055  1.00 52.58
ATOM     37  N   GLN B   8      25.526  24.305 -20.025  1.00 48.44
ATOM     38  CA  GLN B   8      24.934  24.093 -18.712  1.00 48.11
ATOM     39  C   GLN B   8      26.008  24.235 -17.641  1.00 47.36
ATOM     40  O   GLN B   8      25.793  24.923 -16.662  1.00 47.31
ATOM     41  CB  GLN B   8      24.278  22.713 -18.631  1.00 48.28
ATOM     42  CG  GLN B   8      23.038  22.571 -19.508  1.00 49.62
ATOM     43  CD  GLN B   8      22.344  21.217 -19.334  1.00 51.08
ATOM     44  OE1 GLN B   8      22.863  20.187 -19.761  1.00 50.73
ATOM     45  NE2 GLN B   8      21.174  21.226 -18.708  1.00 51.60
ATOM     46  N   LEU B   9      27.160  23.615 -17.857  1.00 46.31
ATOM     47  CA  LEU B   9      28.269  23.687 -16.912  1.00 46.55
ATOM     48  C   LEU B   9      28.739  25.123 -16.704  1.00 46.41
ATOM     49  O   LEU B   9      29.150  25.470 -15.606  1.00 45.68
ATOM     50  CB  LEU B   9      29.458  22.813 -17.342  1.00 46.39
ATOM     51  CG  LEU B   9      29.310  21.275 -17.220  1.00 47.19
ATOM     52  CD1 LEU B   9      30.639  20.575 -17.468  1.00 47.11
ATOM     53  CD2 LEU B   9      28.727  20.838 -15.860  1.00 48.41
ATOM     54  N   GLU B  10      28.672  25.943 -17.748  1.00 46.24
ATOM     55  CA  GLU B  10      29.087  27.338 -17.657  1.00 46.82
ATOM     56  C   GLU B  10      28.074  28.090 -16.821  1.00 46.66
ATOM     57  O   GLU B  10      28.452  28.855 -15.955  1.00 47.38
ATOM     58  CB  GLU B  10      29.225  27.948 -19.053  1.00 99.99
ATOM     59  CG  GLU B  10      29.724  29.384 -19.056  1.00 99.99
ATOM     60  CD  GLU B  10      28.627  30.383 -18.746  1.00 99.99
ATOM     61  OE1 GLU B  10      27.445  30.061 -18.990  1.00 99.99
ATOM     62  OE2 GLU B  10      28.948  31.487 -18.257  1.00 99.99
ATOM     63  N   GLU B  11      26.797  27.836 -17.074  1.00 46.94
ATOM     64  CA  GLU B  11      25.705  28.454 -16.349  1.00 47.52
ATOM     65  C   GLU B  11      25.701  28.038 -14.875  1.00 46.98
ATOM     66  O   GLU B  11      25.476  28.852 -13.999  1.00 46.77
ATOM     67  CB  GLU B  11      24.380  28.073 -17.002  1.00 48.29
ATOM     68  CG  GLU B  11      23.156  28.552 -16.234  1.00 51.35
ATOM     69  CD  GLU B  11      21.866  28.411 -17.028  1.00 55.45
ATOM     70  OE1 GLU B  11      21.575  29.291 -17.883  1.00 58.13
ATOM     71  OE2 GLU B  11      21.136  27.430 -16.782  1.00 57.77
ATOM     72  N   PHE B  12      25.959  26.765 -14.604  1.00 46.51
ATOM     73  CA  PHE B  12      25.960  26.266 -13.237  1.00 46.06
ATOM     74  C   PHE B  12      27.157  26.842 -12.518  1.00 46.04
ATOM     75  O   PHE B  12      27.072  27.180 -11.343  1.00 45.47
ATOM     76  CB  PHE B  12      26.015  24.731 -13.207  1.00 45.78
ATOM     77  CG  PHE B  12      24.794  24.051 -13.802  1.00 44.80
ATOM     78  CD1 PHE B  12      23.617  24.753 -14.070  1.00 44.54
ATOM     79  CD2 PHE B  12      24.842  22.699 -14.115  1.00 43.65
ATOM     80  CE1 PHE B  12      22.505  24.106 -14.607  1.00 44.10
ATOM     81  CE2 PHE B  12      23.746  22.061 -14.660  1.00 42.79
ATOM     82  CZ  PHE B  12      22.581  22.752 -14.895  1.00 43.53
ATOM     83  N   LYS B  13      28.273  26.945 -13.235  1.00 45.54
ATOM     84  CA  LYS B  13      29.497  27.452 -12.654  1.00 46.33
ATOM     85  C   LYS B  13      29.334  28.940 -12.285  1.00 46.40
ATOM     86  O   LYS B  13      29.779  29.353 -11.217  1.00 45.40
ATOM     87  CB  LYS B  13      30.659  27.268 -13.615  1.00 46.28
ATOM     88  CG  LYS B  13      31.999  27.671 -13.070  1.00 48.39
ATOM     89  CD  LYS B  13      33.103  27.035 -13.896  1.00 50.35
ATOM     90  CE  LYS B  13      34.466  27.576 -13.514  1.00 52.14
ATOM     91  NZ  LYS B  13      34.698  27.445 -12.070  1.00 51.71
ATOM     92  N   GLU B  14      28.680  29.722 -13.147  1.00 46.58
ATOM     93  CA  GLU B  14      28.480  31.151 -12.876  1.00 47.20
ATOM     94  C   GLU B  14      27.694  31.295 -11.569  1.00 47.02
ATOM     95  O   GLU B  14      28.065  32.082 -10.706  1.00 46.91
ATOM     96  CB  GLU B  14      27.754  31.822 -14.044  1.00 99.99
ATOM     97  CG  GLU B  14      26.360  31.272 -14.306  1.00 99.99
ATOM     98  CD  GLU B  14      25.673  31.961 -15.468  1.00 99.99
ATOM     99  OE1 GLU B  14      26.210  31.906 -16.594  1.00 99.99
ATOM    100  OE2 GLU B  14      24.593  32.554 -15.254  1.00 99.99
ATOM    101  N   ALA B  15      26.622  30.509 -11.442  1.00 46.71
ATOM    102  CA  ALA B  15      25.777  30.486 -10.256  1.00 46.88
ATOM    103  C   ALA B  15      26.558  30.077  -8.998  1.00 47.22
ATOM    104  O   ALA B  15      26.453  30.732  -7.959  1.00 46.70
ATOM    105  CB  ALA B  15      24.611  29.553 -10.480  1.00 46.94
ATOM    106  N   PHE B  16      27.358  29.016  -9.127  1.00 47.19
ATOM    107  CA  PHE B  16      28.236  28.498  -8.073  1.00 47.73
ATOM    108  C   PHE B  16      29.189  29.589  -7.566  1.00 48.68
ATOM    109  O   PHE B  16      29.373  29.750  -6.354  1.00 48.34
ATOM    110  CB  PHE B  16      29.017  27.282  -8.635  1.00 47.59
ATOM    111  CG  PHE B  16      29.995  26.643  -7.675  1.00 46.74
ATOM    112  CD1 PHE B  16      29.604  25.572  -6.875  1.00 46.05
ATOM    113  CD2 PHE B  16      31.312  27.063  -7.625  1.00 45.99
ATOM    114  CE1 PHE B  16      30.499  24.950  -6.012  1.00 46.01
ATOM    115  CE2 PHE B  16      32.223  26.440  -6.778  1.00 46.17
ATOM    116  CZ  PHE B  16      31.807  25.384  -5.956  1.00 46.24
ATOM    117  N   GLU B  17      29.736  30.364  -8.501  1.00 49.77
ATOM    118  CA  GLU B  17      30.712  31.407  -8.197  1.00 51.08
ATOM    119  C   GLU B  17      30.106  32.563  -7.406  1.00 50.83
ATOM    120  O   GLU B  17      30.800  33.179  -6.620  1.00 50.84
ATOM    121  CB  GLU B  17      31.379  31.948  -9.472  1.00 51.80
ATOM    122  CG  GLU B  17      32.109  30.894 -10.301  1.00 54.94
ATOM    123  CD  GLU B  17      33.542  30.666  -9.875  1.00 58.72
ATOM    124  OE1 GLU B  17      34.416  31.440 -10.338  1.00 62.52
ATOM    125  OE2 GLU B  17      33.795  29.705  -9.102  1.00 59.74
ATOM    126  N   LEU B  18      28.821  32.841  -7.604  1.00 50.78
ATOM    127  CA  LEU B  18      28.106  33.828  -6.790  1.00 51.08
ATOM    128  C   LEU B  18      28.071  33.465  -5.298  1.00 51.62
ATOM    129  O   LEU B  18      28.017  34.354  -4.446  1.00 52.07
ATOM    130  CB  LEU B  18      26.676  34.017  -7.309  1.00 50.49
ATOM    131  CG  LEU B  18      26.503  34.734  -8.656  1.00 50.59
ATOM    132  CD1 LEU B  18      25.003  34.911  -8.993  1.00 50.26
ATOM    133  CD2 LEU B  18      27.211  36.091  -8.693  1.00 50.92
ATOM    134  N   PHE B  19      28.107  32.169  -4.990  1.00 51.97
ATOM    135  CA  PHE B  19      28.080  31.679  -3.609  1.00 52.30
ATOM    136  C   PHE B  19      29.445  31.627  -2.941  1.00 53.48
ATOM    137  O   PHE B  19      29.555  31.332  -1.748  1.00 53.47
ATOM    138  CB  PHE B  19      27.453  30.294  -3.554  1.00 51.58
ATOM    139  CG  PHE B  19      25.987  30.310  -3.783  1.00 50.61
ATOM    140  CD1 PHE B  19      25.097  30.312  -2.709  1.00 49.13
ATOM    141  CD2 PHE B  19      25.485  30.364  -5.071  1.00 48.54
ATOM    142  CE1 PHE B  19      23.724  30.343  -2.926  1.00 48.78
ATOM    143  CE2 PHE B  19      24.119  30.394  -5.293  1.00 48.70
ATOM    144  CZ  PHE B  19      23.234  30.382  -4.212  1.00 48.32
ATOM    145  N   ASP B  20      30.485  31.902  -3.707  1.00 55.21
ATOM    146  CA  ASP B  20      31.826  31.930  -3.157  1.00 56.94
ATOM    147  C   ASP B  20      32.024  33.244  -2.376  1.00 57.88
ATOM    148  O   ASP B  20      32.138  34.307  -2.978  1.00 57.99
ATOM    149  CB  ASP B  20      32.833  31.770  -4.298  1.00 57.26
ATOM    150  CG  ASP B  20      34.243  32.068  -3.877  1.00 58.40
ATOM    151  OD1 ASP B  20      34.611  31.758  -2.721  1.00 60.60
ATOM    152  OD2 ASP B  20      35.051  32.622  -4.643  1.00 61.08
ATOM    153  N   ARG B  21      32.054  33.151  -1.043  1.00 59.21
ATOM    154  CA  ARG B  21      32.181  34.321  -0.155  1.00 60.17
ATOM    155  C   ARG B  21      33.615  34.582   0.304  1.00 60.50
ATOM    156  O   ARG B  21      33.847  35.435   1.160  1.00 60.55
ATOM    157  CB  ARG B  21      31.287  34.150   1.078  1.00 60.68
ATOM    158  CG  ARG B  21      29.805  34.398   0.817  1.00 62.58
ATOM    159  CD  ARG B  21      28.916  34.280   2.070  1.00 65.37
ATOM    160  NE  ARG B  21      29.066  32.991   2.766  1.00 67.40
ATOM    161  CZ  ARG B  21      29.633  32.811   3.971  1.00 70.14
ATOM    162  NH1 ARG B  21      30.141  33.834   4.666  1.00 70.16
ATOM    163  NH2 ARG B  21      29.700  31.584   4.489  1.00 70.80
ATOM    164  N   VAL B  22      34.570  33.854  -0.268  1.00 60.90
ATOM    165  CA  VAL B  22      35.986  33.979   0.101  1.00 61.17
ATOM    166  C   VAL B  22      36.910  34.307  -1.089  1.00 61.18
ATOM    167  O   VAL B  22      38.048  34.694  -0.875  1.00 61.80
ATOM    168  CB  VAL B  22      36.488  32.692   0.819  1.00 61.22
ATOM    169  CG1 VAL B  22      37.942  32.847   1.297  1.00 61.51
ATOM    170  CG2 VAL B  22      35.563  32.322   1.998  1.00 61.47
ATOM    171  N   GLY B  23      36.431  34.170  -2.328  1.00 61.17
ATOM    172  CA  GLY B  23      37.229  34.464  -3.516  1.00 60.71
ATOM    173  C   GLY B  23      38.146  33.372  -4.060  1.00 60.61
ATOM    174  O   GLY B  23      38.820  33.589  -5.070  1.00 60.63
ATOM    175  N   ASP B  24      38.183  32.207  -3.413  1.00 60.29
ATOM    176  CA  ASP B  24      39.049  31.089  -3.848  1.00 60.06
ATOM    177  C   ASP B  24      38.414  30.140  -4.894  1.00 59.40
ATOM    178  O   ASP B  24      38.954  29.075  -5.179  1.00 59.05
ATOM    179  CB  ASP B  24      39.538  30.276  -2.631  1.00 60.34
ATOM    180  CG  ASP B  24      38.399  29.585  -1.879  1.00 60.90
ATOM    181  OD1 ASP B  24      37.212  29.899  -2.139  1.00 60.02
ATOM    182  OD2 ASP B  24      38.603  28.723  -1.003  1.00 62.27
ATOM    183  N   GLY B  25      37.277  30.534  -5.462  1.00 58.56
ATOM    184  CA  GLY B  25      36.565  29.710  -6.422  1.00 58.12
ATOM    185  C   GLY B  25      35.837  28.532  -5.792  1.00 57.43
ATOM    186  O   GLY B  25      35.506  27.569  -6.482  1.00 57.18
ATOM    187  N   LYS B  26      35.582  28.619  -4.488  1.00 56.83
ATOM    188  CA  LYS B  26      35.023  27.509  -3.721  1.00 56.28
ATOM    189  C   LYS B  26      33.817  27.925  -2.897  1.00 55.53
ATOM    190  O   LYS B  26      33.626  29.104  -2.609  1.00 55.66
ATOM    191  CB  LYS B  26      36.073  26.933  -2.775  1.00 56.20
ATOM    192  CG  LYS B  26      37.273  26.355  -3.480  1.00 56.93
ATOM    193  CD  LYS B  26      38.233  25.696  -2.500  1.00 56.04
ATOM    194  CE  LYS B  26      39.508  25.255  -3.199  1.00 55.50
ATOM    195  NZ  LYS B  26      40.424  24.599  -2.244  1.00 55.92
ATOM    196  N   ILE B  27      33.008  26.936  -2.532  1.00 54.38
ATOM    197  CA  ILE B  27      31.968  27.101  -1.536  1.00 53.79
ATOM    198  C   ILE B  27      32.262  26.171  -0.364  1.00 53.87
ATOM    199  O   ILE B  27      33.112  25.279  -0.459  1.00 53.25
ATOM    200  CB  ILE B  27      30.569  26.788  -2.129  1.00 53.70
ATOM    201  CG1 ILE B  27      30.429  25.300  -2.482  1.00 52.92
ATOM    202  CG2 ILE B  27      30.294  27.659  -3.356  1.00 53.83
ATOM    203  CD1 ILE B  27      29.050  24.930  -2.954  1.00 53.13
ATOM    204  N   LEU B  28      31.539  26.385   0.730  1.00 53.57
ATOM    205  CA  LEU B  28      31.570  25.484   1.868  1.00 53.70
ATOM    206  C   LEU B  28      30.698  24.276   1.564  1.00 53.40
ATOM    207  O   LEU B  28      29.785  24.361   0.741  1.00 53.32
ATOM    208  CB  LEU B  28      31.016  26.168   3.117  1.00 53.91
ATOM    209  CG  LEU B  28      31.824  27.295   3.750  1.00 54.93
ATOM    210  CD1 LEU B  28      30.978  28.004   4.789  1.00 55.49
ATOM    211  CD2 LEU B  28      33.112  26.765   4.384  1.00 56.27
ATOM    212  N   TYR B  29      30.977  23.165   2.243  1.00 52.81
ATOM    213  CA  TYR B  29      30.103  21.998   2.224  1.00 52.72
ATOM    214  C   TYR B  29      28.677  22.408   2.558  1.00 51.81
ATOM    215  O   TYR B  29      27.732  21.943   1.932  1.00 51.83
ATOM    216  CB  TYR B  29      30.562  20.967   3.257  1.00 53.10
ATOM    217  CG  TYR B  29      31.376  19.809   2.721  1.00 55.82
ATOM    218  CD1 TYR B  29      32.405  20.003   1.801  1.00 57.77
ATOM    219  CD2 TYR B  29      31.131  18.504   3.169  1.00 59.47
ATOM    220  CE1 TYR B  29      33.168  18.925   1.338  1.00 59.81
ATOM    221  CE2 TYR B  29      31.881  17.421   2.701  1.00 60.97
ATOM    222  CZ  TYR B  29      32.903  17.639   1.793  1.00 61.31
ATOM    223  OH  TYR B  29      33.645  16.564   1.333  1.00 63.26
ATOM    224  N   SER B  30      28.537  23.290   3.551  1.00 50.74
ATOM    225  CA  SER B  30      27.224  23.712   4.053  1.00 49.70
ATOM    226  C   SER B  30      26.451  24.541   3.030  1.00 48.69
ATOM    227  O   SER B  30      25.240  24.689   3.137  1.00 48.53
ATOM    228  CB  SER B  30      27.372  24.500   5.375  1.00 49.62
ATOM    229  OG  SER B  30      28.514  25.350   5.343  1.00 49.60
ATOM    230  N   GLN B  31      27.155  25.087   2.047  1.00 47.89
ATOM    231  CA  GLN B  31      26.527  25.811   0.944  1.00 47.28
ATOM    232  C   GLN B  31      26.110  24.935  -0.231  1.00 46.81
ATOM    233  O   GLN B  31      25.351  25.383  -1.091  1.00 47.02
ATOM    234  CB  GLN B  31      27.472  26.866   0.435  1.00 47.45
ATOM    235  CG  GLN B  31      27.792  27.917   1.469  1.00 47.04
ATOM    236  CD  GLN B  31      28.529  29.056   0.855  1.00 47.09
ATOM    237  OE1 GLN B  31      29.743  28.975   0.655  1.00 48.60
ATOM    238  NE2 GLN B  31      27.805  30.113   0.511  1.00 46.54
ATOM    239  N   CYS B  32      26.597  23.697  -0.270  1.00 45.79
ATOM    240  CA  CYS B  32      26.347  22.822  -1.405  1.00 45.48
ATOM    241  C   CYS B  32      24.870  22.657  -1.675  1.00 44.94
ATOM    242  O   CYS B  32      24.442  22.788  -2.820  1.00 44.17
ATOM    243  CB  CYS B  32      27.033  21.476  -1.232  1.00 45.43
ATOM    244  SG  CYS B  32      28.803  21.648  -1.518  1.00 46.54
ATOM    245  N   GLY B  33      24.101  22.394  -0.621  1.00 44.56
ATOM    246  CA  GLY B  33      22.660  22.267  -0.731  1.00 44.66
ATOM    247  C   GLY B  33      21.988  23.500  -1.321  1.00 44.59
ATOM    248  O   GLY B  33      21.105  23.372  -2.150  1.00 44.52
ATOM    249  N   ASP B  34      22.418  24.686  -0.892  1.00 44.82
ATOM    250  CA  ASP B  34      21.872  25.955  -1.385  1.00 44.96
ATOM    251  C   ASP B  34      22.095  26.150  -2.871  1.00 43.98
ATOM    252  O   ASP B  34      21.217  26.661  -3.555  1.00 43.62
ATOM    253  CB  ASP B  34      22.511  27.152  -0.680  1.00 45.88
ATOM    254  CG  ASP B  34      22.244  27.170   0.807  1.00 47.76
ATOM    255  OD1 ASP B  34      21.214  26.600   1.247  1.00 48.77
ATOM    256  OD2 ASP B  34      23.039  27.722   1.597  1.00 51.02
ATOM    257  N   VAL B  35      23.283  25.778  -3.353  1.00 43.00
ATOM    258  CA  VAL B  35      23.614  25.911  -4.776  1.00 42.42
ATOM    259  C   VAL B  35      22.768  24.960  -5.617  1.00 41.62
ATOM    260  O   VAL B  35      22.264  25.348  -6.651  1.00 41.53
ATOM    261  CB  VAL B  35      25.103  25.690  -5.069  1.00 42.21
ATOM    262  CG1 VAL B  35      25.352  25.782  -6.564  1.00 42.52
ATOM    263  CG2 VAL B  35      25.953  26.724  -4.336  1.00 42.04
ATOM    264  N   MET B  36      22.573  23.734  -5.143  1.00 41.26
ATOM    265  CA  MET B  36      21.754  22.761  -5.864  1.00 41.28
ATOM    266  C   MET B  36      20.338  23.270  -6.013  1.00 40.28
ATOM    267  O   MET B  36      19.736  23.151  -7.073  1.00 40.12
ATOM    268  CB  MET B  36      21.747  21.418  -5.145  1.00 41.54
ATOM    269  CG  MET B  36      23.086  20.746  -5.156  1.00 43.85
ATOM    270  SD  MET B  36      23.084  19.233  -4.183  1.00 48.97
ATOM    271  CE  MET B  36      24.740  19.167  -3.726  1.00 48.84
ATOM    272  N   ARG B  37      19.823  23.852  -4.937  1.00 39.29
ATOM    273  CA  ARG B  37      18.472  24.407  -4.912  1.00 38.71
ATOM    274  C   ARG B  37      18.334  25.631  -5.803  1.00 38.18
ATOM    275  O   ARG B  37      17.324  25.809  -6.449  1.00 35.40
ATOM    276  CB  ARG B  37      18.085  24.792  -3.483  1.00 38.19
ATOM    277  CG  ARG B  37      17.921  23.608  -2.585  1.00 39.02
ATOM    278  CD  ARG B  37      17.675  23.946  -1.138  1.00 40.21
ATOM    279  NE  ARG B  37      17.382  22.726  -0.390  1.00 40.50
ATOM    280  CZ  ARG B  37      18.157  22.200   0.547  1.00 41.81
ATOM    281  NH1 ARG B  37      19.306  22.756   0.905  1.00 43.26
ATOM    282  NH2 ARG B  37      17.771  21.085   1.135  1.00 44.24
ATOM    283  N   ALA B  38      19.358  26.477  -5.780  1.00 39.28
ATOM    284  CA  ALA B  38      19.444  27.635  -6.650  1.00 40.84
ATOM    285  C   ALA B  38      19.477  27.246  -8.130  1.00 41.89
ATOM    286  O   ALA B  38      19.100  28.041  -8.963  1.00 43.00
ATOM    287  CB  ALA B  38      20.668  28.457  -6.307  1.00 41.00
ATOM    288  N   LEU B  39      19.932  26.033  -8.438  1.00 42.63
ATOM    289  CA  LEU B  39      20.026  25.538  -9.825  1.00 43.18
ATOM    290  C   LEU B  39      18.792  24.716 -10.213  1.00 42.87
ATOM    291  O   LEU B  39      18.782  24.078 -11.252  1.00 43.40
ATOM    292  CB  LEU B  39      21.303  24.698  -9.999  1.00 43.30
ATOM    293  CG  LEU B  39      22.600  25.436 -10.341  1.00 45.01
ATOM    294  CD1 LEU B  39      22.604  26.823  -9.792  1.00 48.05
ATOM    295  CD2 LEU B  39      23.844  24.679  -9.863  1.00 44.65
ATOM    296  N   GLY B  40      17.759  24.731  -9.371  1.00 42.53
ATOM    297  CA  GLY B  40      16.502  24.086  -9.688  1.00 42.26
ATOM    298  C   GLY B  40      16.219  22.745  -9.028  1.00 42.17
ATOM    299  O   GLY B  40      15.137  22.203  -9.210  1.00 41.88
ATOM    300  N   GLN B  41      17.168  22.194  -8.283  1.00 42.28
ATOM    301  CA  GLN B  41      16.921  20.931  -7.566  1.00 42.54
ATOM    302  C   GLN B  41      16.198  21.165  -6.228  1.00 42.58
ATOM    303  O   GLN B  41      16.298  22.238  -5.634  1.00 41.80
ATOM    304  CB  GLN B  41      18.233  20.202  -7.317  1.00 42.54
ATOM    305  CG  GLN B  41      19.009  19.859  -8.576  1.00 43.36
ATOM    306  CD  GLN B  41      18.205  18.991  -9.537  1.00 44.64
ATOM    307  OE1 GLN B  41      17.500  18.071  -9.111  1.00 44.61
ATOM    308  NE2 GLN B  41      18.287  19.303 -10.830  1.00 44.57
ATOM    309  N   ASN B  42      15.471  20.143  -5.774  1.00 43.00
ATOM    310  CA  ASN B  42      14.780  20.157  -4.476  1.00 42.99
ATOM    311  C   ASN B  42      15.129  18.936  -3.620  1.00 42.44
ATOM    312  O   ASN B  42      14.252  18.135  -3.284  1.00 42.26
ATOM    313  CB  ASN B  42      13.267  20.188  -4.687  1.00 42.84
ATOM    314  CG  ASN B  42      12.837  21.340  -5.542  1.00 45.51
ATOM    315  OD1 ASN B  42      13.107  22.492  -5.220  1.00 46.21
ATOM    316  ND2 ASN B  42      12.190  21.040  -6.656  1.00 47.77
ATOM    317  N   PRO B  43      16.393  18.800  -3.251  1.00 41.97
ATOM    318  CA  PRO B  43      16.821  17.655  -2.456  1.00 42.20
ATOM    319  C   PRO B  43      16.461  17.894  -0.992  1.00 42.30
ATOM    320  O   PRO B  43      16.453  19.049  -0.561  1.00 42.08
ATOM    321  CB  PRO B  43      18.330  17.667  -2.626  1.00 42.31
ATOM    322  CG  PRO B  43      18.660  19.126  -2.764  1.00 42.59
ATOM    323  CD  PRO B  43      17.497  19.742  -3.489  1.00 42.07
ATOM    324  N   THR B  44      16.189  16.830  -0.244  1.00 41.81
ATOM    325  CA  THR B  44      15.970  16.961   1.188  1.00 42.35
ATOM    326  C   THR B  44      17.349  17.202   1.769  1.00 42.84
ATOM    327  O   THR B  44      18.346  16.944   1.107  1.00 42.33
ATOM    328  CB  THR B  44      15.355  15.685   1.792  1.00 41.99
ATOM    329  OG1 THR B  44      16.256  14.585   1.618  1.00 41.71
ATOM    330  CG2 THR B  44      14.064  15.265   1.076  1.00 42.47
ATOM    331  N   ASN B  45      17.418  17.705   2.993  1.00 43.51
ATOM    332  CA  ASN B  45      18.710  17.871   3.648  1.00 44.29
ATOM    333  C   ASN B  45      19.451  16.573   3.778  1.00 44.48
ATOM    334  O   ASN B  45      20.678  16.557   3.681  1.00 44.31
ATOM    335  CB  ASN B  45      18.548  18.500   5.024  1.00 44.53
ATOM    336  CG  ASN B  45      18.161  19.952   4.937  1.00 45.80
ATOM    337  OD1 ASN B  45      18.426  20.598   3.923  1.00 46.83
ATOM    338  ND2 ASN B  45      17.520  20.477   5.989  1.00 46.10
ATOM    339  N   ALA B  46      18.702  15.494   3.990  1.00 45.01
ATOM    340  CA  ALA B  46      19.283  14.166   4.125  1.00 46.02
ATOM    341  C   ALA B  46      19.979  13.776   2.827  1.00 46.20
ATOM    342  O   ALA B  46      21.102  13.308   2.851  1.00 46.62
ATOM    343  CB  ALA B  46      18.202  13.121   4.512  1.00 45.70
ATOM    344  N   GLU B  47      19.315  14.007   1.701  1.00 46.88
ATOM    345  CA  GLU B  47      19.901  13.720   0.393  1.00 47.37
ATOM    346  C   GLU B  47      21.172  14.525   0.152  1.00 47.09
ATOM    347  O   GLU B  47      22.139  13.991  -0.367  1.00 46.06
ATOM    348  CB  GLU B  47      18.883  13.953  -0.726  1.00 47.80
ATOM    349  CG  GLU B  47      17.863  12.817  -0.836  1.00 49.48
ATOM    350  CD  GLU B  47      16.547  13.240  -1.478  1.00 51.77
ATOM    351  OE1 GLU B  47      16.495  14.350  -2.062  1.00 50.60
ATOM    352  OE2 GLU B  47      15.566  12.446  -1.414  1.00 53.38
ATOM    353  N   VAL B  48      21.179  15.788   0.572  1.00 47.17
ATOM    354  CA  VAL B  48      22.349  16.634   0.413  1.00 47.76
ATOM    355  C   VAL B  48      23.499  16.084   1.237  1.00 48.78
ATOM    356  O   VAL B  48      24.632  16.016   0.751  1.00 48.65
ATOM    357  CB  VAL B  48      22.095  18.097   0.823  1.00 47.72
ATOM    358  CG1 VAL B  48      23.383  18.903   0.766  1.00 47.63
ATOM    359  CG2 VAL B  48      21.030  18.744  -0.069  1.00 47.37
ATOM    360  N   LEU B  49      23.223  15.693   2.482  1.00 49.77
ATOM    361  CA  LEU B  49      24.275  15.149   3.332  1.00 50.62
ATOM    362  C   LEU B  49      24.806  13.825   2.761  1.00 50.98
ATOM    363  O   LEU B  49      25.992  13.562   2.840  1.00 51.06
ATOM    364  CB  LEU B  49      23.791  14.991   4.776  1.00 51.13
ATOM    365  CG  LEU B  49      23.550  16.336   5.488  1.00 52.22
ATOM    366  CD1 LEU B  49      22.683  16.148   6.724  1.00 53.26
ATOM    367  CD2 LEU B  49      24.868  17.005   5.865  1.00 52.83
ATOM    368  N   LYS B  50      23.945  13.027   2.140  1.00 51.65
ATOM    369  CA  LYS B  50      24.364  11.760   1.534  1.00 52.28
ATOM    370  C   LYS B  50      25.359  11.956   0.386  1.00 52.30
ATOM    371  O   LYS B  50      26.411  11.301   0.356  1.00 51.92
ATOM    372  CB  LYS B  50      23.162  10.949   1.046  1.00 52.73
ATOM    373  CG  LYS B  50      23.528   9.484   0.707  1.00 55.33
ATOM    374  CD  LYS B  50      22.316   8.570   0.531  1.00 58.18
ATOM    375  CE  LYS B  50      21.537   8.330   1.845  1.00 59.87
ATOM    376  NZ  LYS B  50      22.394   7.931   3.010  1.00 60.74
ATOM    377  N   VAL B  51      25.056  12.873  -0.538  1.00 52.49
ATOM    378  CA  VAL B  51      25.986  13.175  -1.636  1.00 52.73
ATOM    379  C   VAL B  51      27.270  13.826  -1.139  1.00 52.62
ATOM    380  O   VAL B  51      28.290  13.737  -1.801  1.00 52.58
ATOM    381  CB  VAL B  51      25.364  14.055  -2.750  1.00 52.68
ATOM    382  CG1 VAL B  51      24.141  13.375  -3.340  1.00 52.66
ATOM    383  CG2 VAL B  51      25.018  15.440  -2.227  1.00 53.60
ATOM    384  N   LEU B  52      27.208  14.490   0.013  1.00 52.89
ATOM    385  CA  LEU B  52      28.401  15.047   0.656  1.00 53.43
ATOM    386  C   LEU B  52      29.219  13.955   1.381  1.00 53.62
ATOM    387  O   LEU B  52      30.349  14.189   1.779  1.00 53.76
ATOM    388  CB  LEU B  52      28.017  16.160   1.646  1.00 53.21
ATOM    389  CG  LEU B  52      27.596  17.504   1.027  1.00 53.82
ATOM    390  CD1 LEU B  52      26.812  18.343   2.002  1.00 53.66
ATOM    391  CD2 LEU B  52      28.804  18.277   0.551  1.00 54.51
ATOM    392  N   GLY B  53      28.635  12.775   1.548  1.00 54.43
ATOM    393  CA  GLY B  53      29.298  11.650   2.194  1.00 55.03
ATOM    394  C   GLY B  53      29.008  11.606   3.690  1.00 55.59
ATOM    395  O   GLY B  53      29.825  11.108   4.463  1.00 55.81
ATOM    396  N   ASN B  54      27.840  12.121   4.082  1.00 55.88
ATOM    397  CA  ASN B  54      27.437  12.277   5.480  1.00 56.14
ATOM    398  C   ASN B  54      28.565  12.857   6.368  1.00 56.83
ATOM    399  O   ASN B  54      29.096  12.184   7.253  1.00 56.61
ATOM    400  CB  ASN B  54      26.898  10.949   5.999  1.00 55.94
ATOM    401  CG  ASN B  54      25.626  10.520   5.272  1.00 56.08
ATOM    402  OD1 ASN B  54      24.570  11.162   5.403  1.00 56.53
ATOM    403  ND2 ASN B  54      25.720   9.448   4.489  1.00 54.01
ATOM    404  N   PRO B  55      28.937  14.112   6.107  1.00 57.17
ATOM    405  CA  PRO B  55      30.046  14.757   6.827  1.00 57.53
ATOM    406  C   PRO B  55      29.762  14.997   8.310  1.00 58.11
ATOM    407  O   PRO B  55      28.604  15.104   8.719  1.00 57.66
ATOM    408  CB  PRO B  55      30.194  16.101   6.102  1.00 57.38
ATOM    409  CG  PRO B  55      28.842  16.364   5.520  1.00 57.06
ATOM    410  CD  PRO B  55      28.342  15.012   5.103  1.00 57.04
ATOM    411  N   LYS B  56      30.829  15.073   9.100  1.00 58.87
ATOM    412  CA  LYS B  56      30.720  15.442  10.505  1.00 59.68
ATOM    413  C   LYS B  56      30.565  16.956  10.612  1.00 60.52
ATOM    414  O   LYS B  56      30.908  17.681   9.683  1.00 60.37
ATOM    415  CB  LYS B  56      31.953  14.970  11.293  1.00 59.64
ATOM    416  CG  LYS B  56      32.266  13.459  11.170  1.00 58.84
ATOM    417  CD  LYS B  56      31.094  12.568  11.620  1.00 57.85
ATOM    418  CE  LYS B  56      31.059  11.248  10.852  1.00 56.96
ATOM    419  NZ  LYS B  56      32.387  10.601  10.848  1.00 56.19
ATOM    420  N   SER B  57      30.045  17.421  11.747  1.00 61.58
ATOM    421  CA  SER B  57      29.823  18.850  11.978  1.00 62.41
ATOM    422  C   SER B  57      31.016  19.689  11.527  1.00 62.79
ATOM    423  O   SER B  57      30.831  20.718  10.883  1.00 63.18
ATOM    424  CB  SER B  57      29.491  19.129  13.459  1.00 62.61
ATOM    425  OG  SER B  57      30.478  18.588  14.346  1.00 63.62
ATOM    426  N   ASP B  58      32.227  19.217  11.834  1.00 63.37
ATOM    427  CA  ASP B  58      33.470  19.968  11.609  1.00 63.65
ATOM    428  C   ASP B  58      33.781  20.187  10.132  1.00 64.02
ATOM    429  O   ASP B  58      34.146  21.298   9.726  1.00 63.90
ATOM    430  CB  ASP B  58      34.653  19.256  12.267  1.00 99.99
ATOM    431  CG  ASP B  58      34.896  17.876  11.690  1.00 99.99
ATOM    432  OD1 ASP B  58      34.040  17.394  10.917  1.00 99.99
ATOM    433  OD2 ASP B  58      35.944  17.274  12.008  1.00 99.99
ATOM    434  N   GLU B  59      33.661  19.131   9.329  1.00 64.30
ATOM    435  CA  GLU B  59      33.955  19.265   7.908  1.00 64.68
ATOM    436  C   GLU B  59      32.800  19.966   7.168  1.00 64.35
ATOM    437  O   GLU B  59      33.024  20.633   6.168  1.00 64.03
ATOM    438  CB  GLU B  59      34.361  17.924   7.284  1.00 64.98
ATOM    439  CG  GLU B  59      33.240  16.976   6.932  1.00 66.77
ATOM    440  CD  GLU B  59      33.773  15.631   6.482  1.00 69.23
ATOM    441  OE1 GLU B  59      34.065  14.790   7.366  1.00 70.46
ATOM    442  OE2 GLU B  59      33.920  15.427   5.249  1.00 70.54
ATOM    443  N   LEU B  60      31.584  19.844   7.691  1.00 64.07
ATOM    444  CA  LEU B  60      30.429  20.532   7.130  1.00 64.12
ATOM    445  C   LEU B  60      30.584  22.061   7.223  1.00 64.36
ATOM    446  O   LEU B  60      30.119  22.790   6.339  1.00 64.57
ATOM    447  CB  LEU B  60      29.147  20.078   7.843  1.00 63.96
ATOM    448  CG  LEU B  60      27.812  20.632   7.333  1.00 63.82
ATOM    449  CD1 LEU B  60      27.486  20.066   5.965  1.00 63.50
ATOM    450  CD2 LEU B  60      26.679  20.341   8.313  1.00 63.64
ATOM    451  N   LYS B  61      31.252  22.538   8.276  1.00 64.37
ATOM    452  CA  LYS B  61      31.356  23.973   8.540  1.00 64.30
ATOM    453  C   LYS B  61      32.599  24.612   7.930  1.00 63.91
ATOM    454  O   LYS B  61      32.655  25.829   7.795  1.00 64.17
ATOM    455  CB  LYS B  61      31.287  24.257  10.053  1.00 64.58
ATOM    456  CG  LYS B  61      32.453  23.722  10.883  1.00 65.50
ATOM    457  CD  LYS B  61      32.745  24.599  12.115  1.00 67.23
ATOM    458  CE  LYS B  61      33.901  24.032  12.963  1.00 68.45
ATOM    459  NZ  LYS B  61      35.182  23.866  12.189  1.00 69.01
ATOM    460  N   SER B  62      33.582  23.804   7.546  1.00 63.43
ATOM    461  CA  SER B  62      34.876  24.342   7.113  1.00 63.20
ATOM    462  C   SER B  62      35.503  23.749   5.842  1.00 62.38
ATOM    463  O   SER B  62      36.397  24.371   5.270  1.00 62.36
ATOM    464  CB  SER B  62      35.880  24.236   8.274  1.00 63.52
ATOM    465  OG  SER B  62      36.033  25.492   8.925  1.00 64.33
ATOM    466  N   ARG B  63      35.078  22.563   5.406  1.00 61.70
ATOM    467  CA  ARG B  63      35.605  21.982   4.161  1.00 61.26
ATOM    468  C   ARG B  63      35.066  22.750   2.958  1.00 60.52
ATOM    469  O   ARG B  63      33.876  23.056   2.885  1.00 60.41
ATOM    470  CB  ARG B  63      35.241  20.499   4.065  1.00 99.99
ATOM    471  CG  ARG B  63      35.808  19.798   2.842  1.00 99.99
ATOM    472  CD  ARG B  63      35.408  18.332   2.811  1.00 99.99
ATOM    473  NE  ARG B  63      35.986  17.584   3.922  1.00 99.99
ATOM    474  CZ  ARG B  63      37.204  17.054   3.912  1.00 99.99
ATOM    475  NH1 ARG B  63      37.977  17.189   2.843  1.00 99.99
ATOM    476  NH2 ARG B  63      37.646  16.388   4.970  1.00 99.99
ATOM    477  N   ARG B  64      35.963  23.082   2.034  1.00 59.85
ATOM    478  CA  ARG B  64      35.637  23.904   0.873  1.00 59.32
ATOM    479  C   ARG B  64      35.828  23.093  -0.418  1.00 58.75
ATOM    480  O   ARG B  64      36.785  22.330  -0.542  1.00 58.85
ATOM    481  CB  ARG B  64      36.510  25.168   0.861  1.00 59.17
ATOM    482  CG  ARG B  64      36.351  26.050   2.101  1.00 58.96
ATOM    483  CD  ARG B  64      37.041  27.412   2.009  1.00 58.28
ATOM    484  NE  ARG B  64      36.460  28.277   0.976  1.00 57.63
ATOM    485  CZ  ARG B  64      35.319  28.967   1.103  1.00 58.19
ATOM    486  NH1 ARG B  64      34.588  28.912   2.215  1.00 58.14
ATOM    487  NH2 ARG B  64      34.893  29.717   0.095  1.00 58.80
ATOM    488  N   VAL B  65      34.908  23.244  -1.366  1.00 58.00
ATOM    489  CA  VAL B  65      34.982  22.513  -2.627  1.00 57.29
ATOM    490  C   VAL B  65      34.923  23.467  -3.807  1.00 56.65
ATOM    491  O   VAL B  65      34.176  24.442  -3.792  1.00 55.58
ATOM    492  CB  VAL B  65      33.852  21.461  -2.777  1.00 57.56
ATOM    493  CG1 VAL B  65      34.102  20.271  -1.861  1.00 57.97
ATOM    494  CG2 VAL B  65      32.468  22.061  -2.512  1.00 57.90
ATOM    495  N   ASP B  66      35.734  23.180  -4.825  1.00 56.10
ATOM    496  CA  ASP B  66      35.683  23.916  -6.088  1.00 55.61
ATOM    497  C   ASP B  66      34.531  23.368  -6.922  1.00 54.61
ATOM    498  O   ASP B  66      33.890  22.398  -6.522  1.00 54.12
ATOM    499  CB  ASP B  66      37.026  23.858  -6.843  1.00 56.07
ATOM    500  CG  ASP B  66      37.586  22.435  -6.996  1.00 56.99
ATOM    501  OD1 ASP B  66      36.817  21.453  -6.922  1.00 57.43
ATOM    502  OD2 ASP B  66      38.803  22.213  -7.207  1.00 58.98
ATOM    503  N   PHE B  67      34.251  23.999  -8.063  1.00 53.86
ATOM    504  CA  PHE B  67      33.116  23.591  -8.897  1.00 52.98
ATOM    505  C   PHE B  67      33.204  22.126  -9.327  1.00 52.66
ATOM    506  O   PHE B  67      32.198  21.436  -9.368  1.00 52.27
ATOM    507  CB  PHE B  67      32.978  24.489 -10.134  1.00 52.95
ATOM    508  CG  PHE B  67      31.789  24.148 -10.996  1.00 51.39
ATOM    509  CD1 PHE B  67      30.508  24.430 -10.565  1.00 49.60
ATOM    510  CD2 PHE B  67      31.955  23.517 -12.222  1.00 51.67
ATOM    511  CE1 PHE B  67      29.403  24.117 -11.340  1.00 49.18
ATOM    512  CE2 PHE B  67      30.851  23.182 -13.011  1.00 51.22
ATOM    513  CZ  PHE B  67      29.569  23.486 -12.571  1.00 50.84
ATOM    514  N   GLU B  68      34.417  21.655  -9.599  1.00 52.89
ATOM    515  CA  GLU B  68      34.647  20.330 -10.197  1.00 53.07
ATOM    516  C   GLU B  68      34.249  19.218  -9.224  1.00 52.20
ATOM    517  O   GLU B  68      33.745  18.177  -9.622  1.00 51.82
ATOM    518  CB  GLU B  68      36.122  20.164 -10.615  1.00 53.55
ATOM    519  CG  GLU B  68      36.543  20.900 -11.891  1.00 55.11
ATOM    520  CD  GLU B  68      36.099  22.358 -11.942  1.00 57.28
ATOM    521  OE1 GLU B  68      36.445  23.142 -11.021  1.00 56.46
ATOM    522  OE2 GLU B  68      35.395  22.722 -12.913  1.00 59.90
ATOM    523  N   THR B  69      34.455  19.474  -7.942  1.00 51.70
ATOM    524  CA  THR B  69      34.113  18.531  -6.895  1.00 51.28
ATOM    525  C   THR B  69      32.625  18.626  -6.569  1.00 51.04
ATOM    526  O   THR B  69      31.974  17.622  -6.265  1.00 51.58
ATOM    527  CB  THR B  69      34.964  18.841  -5.656  1.00 51.88
ATOM    528  OG1 THR B  69      36.336  19.024  -6.045  1.00 50.44
ATOM    529  CG2 THR B  69      34.975  17.667  -4.663  1.00 52.00
ATOM    530  N   PHE B  70      32.080  19.838  -6.652  1.00 50.49
ATOM    531  CA  PHE B  70      30.647  20.069  -6.454  1.00 49.77
ATOM    532  C   PHE B  70      29.807  19.335  -7.492  1.00 49.30
ATOM    533  O   PHE B  70      28.756  18.795  -7.172  1.00 48.27
ATOM    534  CB  PHE B  70      30.338  21.570  -6.530  1.00 49.69
ATOM    535  CG  PHE B  70      28.870  21.895  -6.537  1.00 48.79
ATOM    536  CD1 PHE B  70      28.147  21.894  -5.355  1.00 48.88
ATOM    537  CD2 PHE B  70      28.217  22.217  -7.713  1.00 48.40
ATOM    538  CE1 PHE B  70      26.787  22.196  -5.345  1.00 48.07
ATOM    539  CE2 PHE B  70      26.858  22.528  -7.714  1.00 48.33
ATOM    540  CZ  PHE B  70      26.146  22.514  -6.522  1.00 48.66
ATOM    541  N   LEU B  71      30.292  19.318  -8.731  1.00 49.10
ATOM    542  CA  LEU B  71      29.512  18.859  -9.880  1.00 48.99
ATOM    543  C   LEU B  71      28.949  17.440  -9.750  1.00 48.27
ATOM    544  O   LEU B  71      27.757  17.252  -9.944  1.00 47.88
ATOM    545  CB  LEU B  71      30.326  19.000 -11.185  1.00 49.60
ATOM    546  CG  LEU B  71      29.649  18.392 -12.416  1.00 50.14
ATOM    547  CD1 LEU B  71      28.424  19.243 -12.809  1.00 51.28
ATOM    548  CD2 LEU B  71      30.643  18.235 -13.561  1.00 51.39
ATOM    549  N   PRO B  72      29.775  16.440  -9.460  1.00 47.94
ATOM    550  CA  PRO B  72      29.252  15.087  -9.241  1.00 48.20
ATOM    551  C   PRO B  72      28.105  15.048  -8.219  1.00 48.07
ATOM    552  O   PRO B  72      27.193  14.256  -8.377  1.00 48.40
ATOM    553  CB  PRO B  72      30.472  14.302  -8.730  1.00 48.31
ATOM    554  CG  PRO B  72      31.636  15.027  -9.185  1.00 48.11
ATOM    555  CD  PRO B  72      31.243  16.472  -9.364  1.00 48.61
ATOM    556  N   MET B  73      28.156  15.902  -7.203  1.00 47.85
ATOM    557  CA  MET B  73      27.103  15.960  -6.188  1.00 47.68
ATOM    558  C   MET B  73      25.804  16.482  -6.770  1.00 46.85
ATOM    559  O   MET B  73      24.756  15.939  -6.509  1.00 45.85
ATOM    560  CB  MET B  73      27.505  16.860  -5.027  1.00 48.06
ATOM    561  CG  MET B  73      28.808  16.491  -4.321  1.00 49.78
ATOM    562  SD  MET B  73      29.338  17.805  -3.175  1.00 55.06
ATOM    563  CE  MET B  73      27.818  18.491  -2.654  1.00 56.33
ATOM    564  N   LEU B  74      25.890  17.551  -7.549  1.00 46.71
ATOM    565  CA  LEU B  74      24.744  18.085  -8.274  1.00 46.95
ATOM    566  C   LEU B  74      24.135  17.040  -9.216  1.00 47.60
ATOM    567  O   LEU B  74      22.913  16.873  -9.255  1.00 46.76
ATOM    568  CB  LEU B  74      25.169  19.316  -9.085  1.00 47.24
ATOM    569  CG  LEU B  74      24.091  19.945  -9.967  1.00 46.76
ATOM    570  CD1 LEU B  74      22.990  20.518  -9.087  1.00 47.34
ATOM    571  CD2 LEU B  74      24.680  21.020 -10.864  1.00 46.65
ATOM    572  N   GLN B  75      25.003  16.366  -9.979  1.00 48.46
ATOM    573  CA  GLN B  75      24.603  15.286 -10.887  1.00 49.29
ATOM    574  C   GLN B  75      23.841  14.213 -10.115  1.00 49.33
ATOM    575  O   GLN B  75      22.751  13.801 -10.518  1.00 48.62
ATOM    576  CB  GLN B  75      25.833  14.646 -11.561  1.00 49.54
ATOM    577  CG  GLN B  75      26.573  15.553 -12.532  1.00 51.44
ATOM    578  CD  GLN B  75      27.808  14.906 -13.153  1.00 54.55
ATOM    579  OE1 GLN B  75      28.108  15.143 -14.322  1.00 56.65
ATOM    580  NE2 GLN B  75      28.524  14.101 -12.376  1.00 57.69
ATOM    581  N   ALA B  76      24.406  13.782  -8.988  1.00 49.97
ATOM    582  CA  ALA B  76      23.839  12.668  -8.227  1.00 50.82
ATOM    583  C   ALA B  76      22.441  13.009  -7.728  1.00 51.58
ATOM    584  O   ALA B  76      21.528  12.189  -7.824  1.00 52.20
ATOM    585  CB  ALA B  76      24.763  12.277  -7.071  1.00 50.82
ATOM    586  N   VAL B  77      22.269  14.241  -7.247  1.00 52.12
ATOM    587  CA  VAL B  77      20.967  14.749  -6.830  1.00 52.62
ATOM    588  C   VAL B  77      19.995  14.825  -8.002  1.00 53.19
ATOM    589  O   VAL B  77      18.823  14.468  -7.865  1.00 53.22
ATOM    590  CB  VAL B  77      21.105  16.150  -6.172  1.00 52.63
ATOM    591  CG1 VAL B  77      19.744  16.795  -5.942  1.00 52.88
ATOM    592  CG2 VAL B  77      21.872  16.031  -4.867  1.00 53.56
ATOM    593  N   ALA B  78      20.477  15.300  -9.147  1.00 53.79
ATOM    594  CA  ALA B  78      19.643  15.441 -10.338  1.00 54.54
ATOM    595  C   ALA B  78      19.101  14.094 -10.862  1.00 55.43
ATOM    596  O   ALA B  78      17.971  14.036 -11.337  1.00 55.28
ATOM    597  CB  ALA B  78      20.421  16.178 -11.445  1.00 54.60
ATOM    598  N   LYS B  79      19.893  13.023 -10.762  1.00 56.53
ATOM    599  CA  LYS B  79      19.479  11.681 -11.223  1.00 57.57
ATOM    600  C   LYS B  79      18.794  10.860 -10.120  1.00 57.77
ATOM    601  O   LYS B  79      18.118  11.414  -9.242  1.00 58.49
ATOM    602  CB  LYS B  79      20.678  10.910 -11.810  1.00 57.89
ATOM    603  CG  LYS B  79      21.621  10.248 -10.790  1.00 59.37
ATOM    604  CD  LYS B  79      22.969   9.797 -11.435  1.00 60.72
ATOM    605  CE  LYS B  79      23.946  10.966 -11.695  1.00 60.91
ATOM    606  NZ  LYS B  79      25.392  10.645 -11.414  1.00 60.70
ATOM    607  N   TYR B  86       3.428  15.678  -9.312  1.00 64.86
ATOM    608  CA  TYR B  86       2.552  16.735  -8.805  1.00 64.83
ATOM    609  C   TYR B  86       1.352  16.187  -8.017  1.00 64.95
ATOM    610  O   TYR B  86       0.876  16.832  -7.075  1.00 64.86
ATOM    611  CB  TYR B  86       2.049  17.615  -9.959  1.00 64.74
ATOM    612  CG  TYR B  86       1.143  18.770  -9.533  1.00 64.43
ATOM    613  CD1 TYR B  86      -0.234  18.589  -9.396  1.00 64.40
ATOM    614  CD2 TYR B  86       1.663  20.041  -9.287  1.00 64.05
ATOM    615  CE1 TYR B  86      -1.070  19.638  -9.012  1.00 64.56
ATOM    616  CE2 TYR B  86       0.837  21.099  -8.900  1.00 63.71
ATOM    617  CZ  TYR B  86      -0.532  20.892  -8.765  1.00 64.43
ATOM    618  OH  TYR B  86      -1.372  21.927  -8.380  1.00 64.22
ATOM    619  N   GLU B  87       0.838  15.022  -8.410  1.00 64.90
ATOM    620  CA  GLU B  87      -0.370  14.479  -7.771  1.00 64.67
ATOM    621  C   GLU B  87      -0.099  14.085  -6.315  1.00 64.62
ATOM    622  O   GLU B  87      -0.978  14.226  -5.449  1.00 64.32
ATOM    623  CB  GLU B  87      -0.894  13.273  -8.553  1.00 99.99
ATOM    624  CG  GLU B  87      -2.185  12.690  -8.002  1.00 99.99
ATOM    625  CD  GLU B  87      -1.954  11.791  -6.803  1.00 99.99
ATOM    626  OE1 GLU B  87      -0.839  11.242  -6.679  1.00 99.99
ATOM    627  OE2 GLU B  87      -2.886  11.637  -5.986  1.00 99.99
ATOM    628  N   ASP B  88       1.118  13.593  -6.059  1.00 64.32
ATOM    629  CA  ASP B  88       1.573  13.302  -4.703  1.00 64.31
ATOM    630  C   ASP B  88       1.756  14.588  -3.868  1.00 64.16
ATOM    631  O   ASP B  88       1.433  14.603  -2.685  1.00 64.43
ATOM    632  CB  ASP B  88       2.885  12.516  -4.735  1.00 99.99
ATOM    633  CG  ASP B  88       4.012  13.291  -5.389  1.00 99.99
ATOM    634  OD1 ASP B  88       4.003  14.537  -5.308  1.00 99.99
ATOM    635  OD2 ASP B  88       4.906  12.651  -5.984  1.00 99.99
ATOM    636  N   TYR B  89       2.271  15.653  -4.482  1.00 63.75
ATOM    637  CA  TYR B  89       2.491  16.923  -3.785  1.00 63.35
ATOM    638  C   TYR B  89       1.190  17.512  -3.260  1.00 63.18
ATOM    639  O   TYR B  89       1.148  18.080  -2.167  1.00 62.72
ATOM    640  CB  TYR B  89       3.188  17.933  -4.700  1.00 63.39
ATOM    641  CG  TYR B  89       4.670  17.669  -4.846  1.00 64.04
ATOM    642  CD1 TYR B  89       5.151  16.709  -5.743  1.00 64.77
ATOM    643  CD2 TYR B  89       5.589  18.365  -4.077  1.00 64.12
ATOM    644  CE1 TYR B  89       6.516  16.465  -5.872  1.00 65.26
ATOM    645  CE2 TYR B  89       6.948  18.128  -4.192  1.00 64.79
ATOM    646  CZ  TYR B  89       7.410  17.182  -5.087  1.00 65.27
ATOM    647  OH  TYR B  89       8.764  16.957  -5.183  1.00 66.27
ATOM    648  N   LEU B  90       0.130  17.352  -4.046  1.00 63.09
ATOM    649  CA  LEU B  90      -1.183  17.853  -3.688  1.00 62.94
ATOM    650  C   LEU B  90      -1.731  17.051  -2.516  1.00 62.91
ATOM    651  O   LEU B  90      -2.246  17.629  -1.559  1.00 62.91
ATOM    652  CB  LEU B  90      -2.135  17.770  -4.886  1.00 63.09
ATOM    653  CG  LEU B  90      -3.096  18.948  -5.079  1.00 63.80
ATOM    654  CD1 LEU B  90      -2.368  20.192  -5.590  1.00 63.98
ATOM    655  CD2 LEU B  90      -4.237  18.573  -6.025  1.00 64.04
ATOM    656  N   GLU B  91      -1.621  15.724  -2.597  1.00 62.74
ATOM    657  CA  GLU B  91      -2.131  14.833  -1.553  1.00 62.93
ATOM    658  C   GLU B  91      -1.405  15.104  -0.244  1.00 62.51
ATOM    659  O   GLU B  91      -2.020  15.079   0.820  1.00 62.37
ATOM    660  CB  GLU B  91      -1.965  13.359  -1.946  1.00 63.34
ATOM    661  CG  GLU B  91      -2.808  12.386  -1.123  1.00 64.88
ATOM    662  CD  GLU B  91      -4.300  12.461  -1.440  1.00 66.74
ATOM    663  OE1 GLU B  91      -4.652  12.683  -2.616  1.00 67.20
ATOM    664  OE2 GLU B  91      -5.123  12.295  -0.508  1.00 68.24
ATOM    665  N   GLY B  92      -0.103  15.376  -0.349  1.00 61.77
ATOM    666  CA  GLY B  92       0.721  15.783   0.769  1.00 61.68
ATOM    667  C   GLY B  92       0.180  16.981   1.535  1.00 61.21
ATOM    668  O   GLY B  92       0.267  17.006   2.758  1.00 61.13
ATOM    669  N   PHE B  93      -0.362  17.970   0.826  1.00 60.68
ATOM    670  CA  PHE B  93      -1.038  19.101   1.471  1.00 60.11
ATOM    671  C   PHE B  93      -2.416  18.715   2.010  1.00 60.40
ATOM    672  O   PHE B  93      -2.871  19.282   3.003  1.00 61.06
ATOM    673  CB  PHE B  93      -1.174  20.291   0.510  1.00 59.82
ATOM    674  CG  PHE B  93       0.050  21.169   0.441  1.00 58.41
ATOM    675  CD1 PHE B  93       0.190  22.258   1.290  1.00 57.07
ATOM    676  CD2 PHE B  93       1.055  20.906  -0.472  1.00 57.34
ATOM    677  CE1 PHE B  93       1.305  23.068   1.219  1.00 56.22
ATOM    678  CE2 PHE B  93       2.174  21.710  -0.542  1.00 56.74
ATOM    679  CZ  PHE B  93       2.305  22.787   0.307  1.00 56.02
ATOM    680  N   ARG B  94      -3.077  17.759   1.359  1.00 60.66
ATOM    681  CA  ARG B  94      -4.413  17.290   1.773  1.00 60.96
ATOM    682  C   ARG B  94      -4.406  16.504   3.096  1.00 60.93
ATOM    683  O   ARG B  94      -5.452  16.305   3.711  1.00 60.96
ATOM    684  CB  ARG B  94      -5.036  16.416   0.683  1.00 99.99
ATOM    685  CG  ARG B  94      -5.374  17.165  -0.595  1.00 99.99
ATOM    686  CD  ARG B  94      -5.988  16.239  -1.633  1.00 99.99
ATOM    687  NE  ARG B  94      -6.318  16.942  -2.867  1.00 99.99
ATOM    688  CZ  ARG B  94      -7.453  17.604  -3.069  1.00 99.99
ATOM    689  NH1 ARG B  94      -8.371  17.653  -2.113  1.00 99.99
ATOM    690  NH2 ARG B  94      -7.668  18.215  -4.227  1.00 99.99
ATOM    691  N   VAL B  95      -3.222  16.069   3.517  1.00 60.90
ATOM    692  CA  VAL B  95      -3.007  15.484   4.836  1.00 60.56
ATOM    693  C   VAL B  95      -3.437  16.466   5.934  1.00 60.47
ATOM    694  O   VAL B  95      -4.073  16.070   6.912  1.00 60.27
ATOM    695  CB  VAL B  95      -1.500  15.097   5.002  1.00 60.61
ATOM    696  CG1 VAL B  95      -1.137  14.791   6.450  1.00 60.87
ATOM    697  CG2 VAL B  95      -1.152  13.916   4.104  1.00 60.15
ATOM    698  N   PHE B  96      -3.110  17.746   5.744  1.00 60.16
ATOM    699  CA  PHE B  96      -3.287  18.773   6.767  1.00 59.98
ATOM    700  C   PHE B  96      -4.547  19.607   6.603  1.00 60.17
ATOM    701  O   PHE B  96      -4.723  20.602   7.308  1.00 60.09
ATOM    702  CB  PHE B  96      -2.073  19.702   6.770  1.00 59.92
ATOM    703  CG  PHE B  96      -0.773  18.978   6.896  1.00 59.22
ATOM    704  CD1 PHE B  96      -0.381  18.448   8.120  1.00 59.33
ATOM    705  CD2 PHE B  96       0.045  18.793   5.791  1.00 58.07
ATOM    706  CE1 PHE B  96       0.814  17.759   8.241  1.00 58.57
ATOM    707  CE2 PHE B  96       1.247  18.107   5.903  1.00 57.80
ATOM    708  CZ  PHE B  96       1.630  17.588   7.125  1.00 58.64
ATOM    709  N   ASP B  97      -5.420  19.208   5.682  1.00 60.36
ATOM    710  CA  ASP B  97      -6.670  19.931   5.435  1.00 60.57
ATOM    711  C   ASP B  97      -7.626  19.851   6.640  1.00 60.60
ATOM    712  O   ASP B  97      -8.527  19.007   6.691  1.00 60.94
ATOM    713  CB  ASP B  97      -7.345  19.399   4.161  1.00 60.56
ATOM    714  CG  ASP B  97      -8.435  20.327   3.636  1.00 60.78
ATOM    715  OD1 ASP B  97      -9.119  20.993   4.451  1.00 60.07
ATOM    716  OD2 ASP B  97      -8.676  20.448   2.418  1.00 60.10
ATOM    717  N   GLY B 100     -12.482  19.506   4.252  1.00 64.72
ATOM    718  CA  GLY B 100     -11.945  19.181   2.941  1.00 64.79
ATOM    719  C   GLY B 100     -12.269  20.252   1.910  1.00 64.92
ATOM    720  O   GLY B 100     -12.576  19.945   0.751  1.00 64.77
ATOM    721  N   ASN B 101     -12.177  21.512   2.335  1.00 65.05
ATOM    722  CA  ASN B 101     -12.563  22.656   1.512  1.00 65.08
ATOM    723  C   ASN B 101     -11.391  23.252   0.718  1.00 65.12
ATOM    724  O   ASN B 101     -11.507  24.355   0.185  1.00 65.50
ATOM    725  CB  ASN B 101     -13.188  23.752   2.377  1.00 99.99
ATOM    726  CG  ASN B 101     -12.225  24.297   3.412  1.00 99.99
ATOM    727  OD1 ASN B 101     -11.012  24.300   3.206  1.00 99.99
ATOM    728  ND2 ASN B 101     -12.764  24.763   4.533  1.00 99.99
ATOM    729  N   GLY B 102     -10.281  22.518   0.617  1.00 64.92
ATOM    730  CA  GLY B 102      -9.132  22.935  -0.178  1.00 64.51
ATOM    731  C   GLY B 102      -8.218  23.932   0.523  1.00 64.28
ATOM    732  O   GLY B 102      -7.407  24.616  -0.118  1.00 63.78
ATOM    733  N   LYS B 103      -8.350  24.009   1.844  1.00 64.01
ATOM    734  CA  LYS B 103      -7.573  24.935   2.655  1.00 63.92
ATOM    735  C   LYS B 103      -6.756  24.188   3.724  1.00 63.85
ATOM    736  O   LYS B 103      -6.940  22.987   3.947  1.00 63.91
ATOM    737  CB  LYS B 103      -8.489  25.965   3.318  1.00 99.99
ATOM    738  CG  LYS B 103      -9.247  26.844   2.337  1.00 99.99
ATOM    739  CD  LYS B 103      -8.307  27.776   1.590  1.00 99.99
ATOM    740  CE  LYS B 103      -7.711  28.819   2.520  1.00 99.99
ATOM    741  NZ  LYS B 103      -6.788  29.741   1.801  1.00 99.99
ATOM    742  N   VAL B 104      -5.842  24.927   4.348  1.00 63.62
ATOM    743  CA  VAL B 104      -5.002  24.463   5.451  1.00 63.36
ATOM    744  C   VAL B 104      -4.801  25.668   6.356  1.00 63.05
ATOM    745  O   VAL B 104      -4.462  26.743   5.860  1.00 63.48
ATOM    746  CB  VAL B 104      -3.611  24.023   4.944  1.00 63.46
ATOM    747  CG1 VAL B 104      -2.638  23.799   6.109  1.00 64.13
ATOM    748  CG2 VAL B 104      -3.703  22.764   4.086  1.00 63.29
ATOM    749  N   MET B 105      -4.995  25.522   7.664  1.00 62.34
ATOM    750  CA  MET B 105      -4.687  26.635   8.570  1.00 62.03
ATOM    751  C   MET B 105      -3.230  27.060   8.391  1.00 61.02
ATOM    752  O   MET B 105      -2.360  26.227   8.201  1.00 60.57
ATOM    753  CB  MET B 105      -4.931  26.265  10.041  1.00 62.35
ATOM    754  CG  MET B 105      -6.340  26.532  10.575  1.00 63.91
ATOM    755  SD  MET B 105      -7.355  27.667   9.559  1.00 68.80
ATOM    756  CE  MET B 105      -8.197  26.438   8.484  1.00 67.53
ATOM    757  N   GLY B 106      -2.974  28.360   8.430  1.00 60.33
ATOM    758  CA  GLY B 106      -1.616  28.865   8.374  1.00 59.89
ATOM    759  C   GLY B 106      -0.878  28.497   9.652  1.00 59.27
ATOM    760  O   GLY B 106       0.299  28.140   9.618  1.00 59.08
ATOM    761  N   ALA B 107      -1.589  28.573  10.774  1.00 58.44
ATOM    762  CA  ALA B 107      -1.052  28.174  12.070  1.00 58.11
ATOM    763  C   ALA B 107      -0.634  26.698  12.097  1.00 57.67
ATOM    764  O   ALA B 107       0.432  26.390  12.611  1.00 57.51
ATOM    765  CB  ALA B 107      -2.060  28.465  13.174  1.00 58.03
ATOM    766  N   GLU B 108      -1.453  25.798  11.543  1.00 57.25
ATOM    767  CA  GLU B 108      -1.136  24.360  11.571  1.00 57.10
ATOM    768  C   GLU B 108       0.034  24.041  10.654  1.00 55.84
ATOM    769  O   GLU B 108       0.918  23.291  11.028  1.00 55.76
ATOM    770  CB  GLU B 108      -2.335  23.450  11.207  1.00 57.65
ATOM    771  CG  GLU B 108      -1.946  21.954  11.214  1.00 59.58
ATOM    772  CD  GLU B 108      -3.086  20.976  10.935  1.00 62.80
ATOM    773  OE1 GLU B 108      -4.012  21.296  10.152  1.00 66.29
ATOM    774  OE2 GLU B 108      -3.047  19.855  11.495  1.00 63.72
ATOM    775  N   LEU B 109       0.026  24.608   9.454  1.00 54.67
ATOM    776  CA  LEU B 109       1.141  24.464   8.535  1.00 53.35
ATOM    777  C   LEU B 109       2.444  25.009   9.120  1.00 52.19
ATOM    778  O   LEU B 109       3.501  24.405   8.950  1.00 51.71
ATOM    779  CB  LEU B 109       0.843  25.167   7.212  1.00 53.48
ATOM    780  CG  LEU B 109       1.837  24.886   6.086  1.00 52.83
ATOM    781  CD1 LEU B 109       1.867  23.404   5.766  1.00 51.93
ATOM    782  CD2 LEU B 109       1.479  25.696   4.861  1.00 53.30
ATOM    783  N   ARG B 110       2.368  26.144   9.799  1.00 51.04
ATOM    784  CA  ARG B 110       3.540  26.735  10.445  1.00 50.59
ATOM    785  C   ARG B 110       4.102  25.778  11.483  1.00 49.57
ATOM    786  O   ARG B 110       5.291  25.554  11.532  1.00 49.32
ATOM    787  CB  ARG B 110       3.192  28.039  11.155  1.00 50.86
ATOM    788  CG  ARG B 110       3.110  29.262  10.288  1.00 51.84
ATOM    789  CD  ARG B 110       2.504  30.436  11.054  1.00 53.95
ATOM    790  NE  ARG B 110       2.025  31.527  10.209  1.00 56.46
ATOM    791  CZ  ARG B 110       2.810  32.368   9.541  1.00 58.10
ATOM    792  NH1 ARG B 110       4.139  32.253   9.587  1.00 58.33
ATOM    793  NH2 ARG B 110       2.264  33.332   8.814  1.00 57.69
ATOM    794  N   HIS B 111       3.220  25.217  12.304  1.00 48.92
ATOM    795  CA  HIS B 111       3.605  24.285  13.355  1.00 48.08
ATOM    796  C   HIS B 111       4.244  23.029  12.777  1.00 47.22
ATOM    797  O   HIS B 111       5.287  22.592  13.266  1.00 46.05
ATOM    798  CB  HIS B 111       2.392  23.902  14.211  1.00 48.11
ATOM    799  CG  HIS B 111       2.683  22.855  15.244  1.00 49.46
ATOM    800  ND1 HIS B 111       2.424  21.513  15.041  1.00 50.29
ATOM    801  CD2 HIS B 111       3.206  22.951  16.492  1.00 48.85
ATOM    802  CE1 HIS B 111       2.777  20.832  16.117  1.00 49.35
ATOM    803  NE2 HIS B 111       3.247  21.682  17.013  1.00 48.64
ATOM    804  N   VAL B 112       3.631  22.445  11.742  1.00 46.45
ATOM    805  CA  VAL B 112       4.138  21.166  11.228  1.00 46.10
ATOM    806  C   VAL B 112       5.458  21.338  10.497  1.00 44.74
ATOM    807  O   VAL B 112       6.351  20.498  10.613  1.00 45.07
ATOM    808  CB  VAL B 112       3.120  20.375  10.352  1.00 46.42
ATOM    809  CG1 VAL B 112       1.889  19.986  11.173  1.00 46.85
ATOM    810  CG2 VAL B 112       2.741  21.133   9.077  1.00 46.98
ATOM    811  N   LEU B 113       5.611  22.443   9.783  1.00 44.30
ATOM    812  CA  LEU B 113       6.841  22.700   9.039  1.00 43.53
ATOM    813  C   LEU B 113       8.006  23.018   9.985  1.00 43.09
ATOM    814  O   LEU B 113       9.153  22.725   9.683  1.00 41.89
ATOM    815  CB  LEU B 113       6.629  23.815   8.016  1.00 43.64
ATOM    816  CG  LEU B 113       5.584  23.575   6.903  1.00 44.72
ATOM    817  CD1 LEU B 113       5.398  24.835   6.100  1.00 45.84
ATOM    818  CD2 LEU B 113       5.943  22.412   5.981  1.00 45.41
ATOM    819  N   THR B 114       7.708  23.590  11.147  1.00 43.35
ATOM    820  CA  THR B 114       8.758  23.885  12.138  1.00 43.22
ATOM    821  C   THR B 114       8.977  22.800  13.202  1.00 43.44
ATOM    822  O   THR B 114       9.910  22.926  13.985  1.00 44.00
ATOM    823  CB  THR B 114       8.473  25.215  12.849  1.00 43.18
ATOM    824  OG1 THR B 114       7.216  25.146  13.518  1.00 42.39
ATOM    825  CG2 THR B 114       8.297  26.336  11.835  1.00 44.52
ATOM    826  N   THR B 115       8.154  21.752  13.253  1.00 43.94
ATOM    827  CA  THR B 115       8.296  20.737  14.318  1.00 44.67
ATOM    828  C   THR B 115       8.389  19.278  13.855  1.00 44.85
ATOM    829  O   THR B 115       8.828  18.411  14.625  1.00 44.90
ATOM    830  CB  THR B 115       7.158  20.832  15.364  1.00 44.72
ATOM    831  OG1 THR B 115       5.913  20.495  14.757  1.00 47.25
ATOM    832  CG2 THR B 115       6.943  22.246  15.880  1.00 44.87
ATOM    833  N   LEU B 116       7.956  18.986  12.636  1.00 44.33
ATOM    834  CA  LEU B 116       8.086  17.636  12.098  1.00 44.43
ATOM    835  C   LEU B 116       9.050  17.641  10.933  1.00 44.04
ATOM    836  O   LEU B 116       9.382  18.690  10.387  1.00 43.28
ATOM    837  CB  LEU B 116       6.728  17.087  11.650  1.00 44.83
ATOM    838  CG  LEU B 116       5.562  17.249  12.624  1.00 46.03
ATOM    839  CD1 LEU B 116       4.282  16.760  11.968  1.00 45.79
ATOM    840  CD2 LEU B 116       5.817  16.500  13.943  1.00 45.92
ATOM    841  N   GLY B 117       9.503  16.455  10.568  1.00 44.29
ATOM    842  CA  GLY B 117      10.320  16.270   9.385  1.00 44.22
ATOM    843  C   GLY B 117      11.656  16.964   9.505  1.00 44.36
ATOM    844  O   GLY B 117      12.299  16.918  10.566  1.00 43.55
ATOM    845  N   GLU B 118      12.071  17.598   8.408  1.00 43.79
ATOM    846  CA  GLU B 118      13.306  18.363   8.356  1.00 44.41
ATOM    847  C   GLU B 118      12.944  19.793   8.720  1.00 44.87
ATOM    848  O   GLU B 118      12.720  20.650   7.845  1.00 43.89
ATOM    849  CB  GLU B 118      13.925  18.256   6.960  1.00 44.57
ATOM    850  CG  GLU B 118      14.227  16.811   6.586  1.00 46.26
ATOM    851  CD  GLU B 118      15.068  16.650   5.330  1.00 47.74
ATOM    852  OE1 GLU B 118      15.045  17.575   4.493  1.00 46.27
ATOM    853  OE2 GLU B 118      15.717  15.574   5.180  1.00 46.92
ATOM    854  N   LYS B 119      12.850  20.022  10.028  1.00 45.15
ATOM    855  CA  LYS B 119      12.212  21.219  10.578  1.00 45.91
ATOM    856  C   LYS B 119      12.832  22.472  10.000  1.00 45.66
ATOM    857  O   LYS B 119      14.041  22.566   9.856  1.00 45.41
ATOM    858  CB  LYS B 119      12.359  21.269  12.103  1.00 46.57
ATOM    859  CG  LYS B 119      11.863  20.031  12.846  1.00 48.78
ATOM    860  CD  LYS B 119      11.959  20.203  14.379  1.00 52.17
ATOM    861  CE  LYS B 119      13.403  20.201  14.859  1.00 53.33
ATOM    862  NZ  LYS B 119      13.817  18.830  15.252  1.00 55.83
ATOM    863  N   MET B 120      11.988  23.430   9.666  1.00 45.89
ATOM    864  CA  MET B 120      12.425  24.703   9.139  1.00 46.42
ATOM    865  C   MET B 120      12.288  25.736  10.230  1.00 46.63
ATOM    866  O   MET B 120      11.541  25.546  11.185  1.00 45.85
ATOM    867  CB  MET B 120      11.539  25.120   7.966  1.00 46.34
ATOM    868  CG  MET B 120      11.278  24.016   6.962  1.00 46.95
ATOM    869  SD  MET B 120      10.562  24.691   5.435  1.00 48.61
ATOM    870  CE  MET B 120       9.018  24.707   5.800  1.00 48.73
ATOM    871  N   THR B 121      12.999  26.839  10.069  1.00 47.53
ATOM    872  CA  THR B 121      12.880  27.950  10.999  1.00 48.64
ATOM    873  C   THR B 121      11.562  28.624  10.736  1.00 49.57
ATOM    874  O   THR B 121      11.024  28.511   9.640  1.00 48.98
ATOM    875  CB  THR B 121      14.022  28.980  10.815  1.00 48.67
ATOM    876  OG1 THR B 121      14.021  29.465   9.474  1.00 49.13
ATOM    877  CG2 THR B 121      15.403  28.337  10.981  1.00 48.61
ATOM    878  N   GLU B 122      11.064  29.340  11.748  1.00 50.50
ATOM    879  CA  GLU B 122       9.827  30.121  11.663  1.00 51.18
ATOM    880  C   GLU B 122       9.952  31.232  10.626  1.00 50.56
ATOM    881  O   GLU B 122       8.966  31.639  10.026  1.00 50.60
ATOM    882  CB  GLU B 122       9.486  30.745  13.035  1.00 51.63
ATOM    883  CG  GLU B 122       8.116  30.369  13.599  1.00 54.71
ATOM    884  CD  GLU B 122       8.109  30.355  15.125  1.00 57.97
ATOM    885  OE1 GLU B 122       8.132  31.455  15.733  1.00 59.19
ATOM    886  OE2 GLU B 122       8.110  29.246  15.711  1.00 60.28
ATOM    887  N   GLU B 123      11.169  31.720  10.451  1.00 50.27
ATOM    888  CA  GLU B 123      11.474  32.800   9.522  1.00 50.55
ATOM    889  C   GLU B 123      11.449  32.303   8.076  1.00 50.32
ATOM    890  O   GLU B 123      10.974  32.998   7.185  1.00 49.93
ATOM    891  CB  GLU B 123      12.859  33.388   9.825  1.00 50.66
ATOM    892  CG  GLU B 123      12.919  34.275  11.072  1.00 53.00
ATOM    893  CD  GLU B 123      13.061  33.500  12.386  1.00 54.68
ATOM    894  OE1 GLU B 123      12.592  34.029  13.417  1.00 57.39
ATOM    895  OE2 GLU B 123      13.636  32.379  12.395  1.00 54.01
ATOM    896  N   GLU B 124      11.991  31.110   7.847  1.00 49.77
ATOM    897  CA  GLU B 124      11.907  30.481   6.542  1.00 49.39
ATOM    898  C   GLU B 124      10.434  30.298   6.186  1.00 48.96
ATOM    899  O   GLU B 124      10.023  30.628   5.071  1.00 48.08
ATOM    900  CB  GLU B 124      12.626  29.133   6.534  1.00 49.65
ATOM    901  CG  GLU B 124      14.130  29.255   6.344  1.00 50.85
ATOM    902  CD  GLU B 124      14.860  27.932   6.540  1.00 52.28
ATOM    903  OE1 GLU B 124      14.300  27.011   7.169  1.00 54.25
ATOM    904  OE2 GLU B 124      16.000  27.811   6.067  1.00 52.50
ATOM    905  N   VAL B 125       9.650  29.818   7.153  1.00 48.46
ATOM    906  CA  VAL B 125       8.234  29.523   6.953  1.00 49.12
ATOM    907  C   VAL B 125       7.429  30.806   6.743  1.00 49.50
ATOM    908  O   VAL B 125       6.540  30.836   5.915  1.00 49.13
ATOM    909  CB  VAL B 125       7.640  28.698   8.122  1.00 49.27
ATOM    910  CG1 VAL B 125       6.143  28.484   7.960  1.00 48.66
ATOM    911  CG2 VAL B 125       8.329  27.351   8.214  1.00 49.85
ATOM    912  N   GLU B 126       7.784  31.860   7.465  1.00 50.32
ATOM    913  CA  GLU B 126       7.122  33.159   7.353  1.00 51.35
ATOM    914  C   GLU B 126       7.331  33.756   5.968  1.00 50.81
ATOM    915  O   GLU B 126       6.432  34.369   5.409  1.00 50.65
ATOM    916  CB  GLU B 126       7.675  34.120   8.404  1.00 52.04
ATOM    917  CG  GLU B 126       7.096  35.534   8.371  1.00 54.98
ATOM    918  CD  GLU B 126       5.700  35.643   8.962  1.00 60.10
ATOM    919  OE1 GLU B 126       5.339  34.814   9.834  1.00 62.34
ATOM    920  OE2 GLU B 126       4.960  36.585   8.566  1.00 64.61
ATOM    921  N   THR B 127       8.524  33.561   5.421  1.00 50.69
ATOM    922  CA  THR B 127       8.889  34.148   4.146  1.00 50.57
ATOM    923  C   THR B 127       8.049  33.537   3.031  1.00 50.43
ATOM    924  O   THR B 127       7.462  34.261   2.220  1.00 50.27
ATOM    925  CB  THR B 127      10.373  33.934   3.883  1.00 50.49
ATOM    926  OG1 THR B 127      11.136  34.641   4.868  1.00 49.73
ATOM    927  CG2 THR B 127      10.796  34.564   2.537  1.00 51.02
ATOM    928  N   VAL B 128       7.980  32.211   3.009  1.00 50.07
ATOM    929  CA  VAL B 128       7.231  31.517   1.980  1.00 50.56
ATOM    930  C   VAL B 128       5.716  31.692   2.143  1.00 51.29
ATOM    931  O   VAL B 128       4.983  31.702   1.153  1.00 51.14
ATOM    932  CB  VAL B 128       7.626  30.008   1.909  1.00 50.46
ATOM    933  CG1 VAL B 128       7.178  29.250   3.139  1.00 50.74
ATOM    934  CG2 VAL B 128       7.085  29.362   0.634  1.00 50.08
ATOM    935  N   LEU B 129       5.248  31.823   3.380  1.00 52.17
ATOM    936  CA  LEU B 129       3.815  31.922   3.653  1.00 53.27
ATOM    937  C   LEU B 129       3.286  33.346   3.500  1.00 54.29
ATOM    938  O   LEU B 129       2.076  33.535   3.497  1.00 54.39
ATOM    939  CB  LEU B 129       3.480  31.446   5.070  1.00 53.46
ATOM    940  CG  LEU B 129       3.559  29.968   5.474  1.00 54.40
ATOM    941  CD1 LEU B 129       2.842  29.796   6.811  1.00 54.45
ATOM    942  CD2 LEU B 129       2.983  29.018   4.426  1.00 54.74
ATOM    943  N   ALA B 130       4.167  34.340   3.374  1.00 55.38
ATOM    944  CA  ALA B 130       3.734  35.743   3.298  1.00 56.54
ATOM    945  C   ALA B 130       2.849  36.033   2.075  1.00 57.46
ATOM    946  O   ALA B 130       3.226  35.749   0.936  1.00 56.76
ATOM    947  CB  ALA B 130       4.933  36.679   3.308  1.00 56.62
ATOM    948  N   GLY B 131       1.660  36.578   2.342  1.00 58.93
ATOM    949  CA  GLY B 131       0.711  36.954   1.307  1.00 59.94
ATOM    950  C   GLY B 131      -0.210  35.848   0.790  1.00 61.20
ATOM    951  O   GLY B 131      -1.076  36.129  -0.039  1.00 61.63
ATOM    952  N   HIS B 132      -0.052  34.608   1.264  1.00 61.98
ATOM    953  CA  HIS B 132      -0.848  33.486   0.754  1.00 62.71
ATOM    954  C   HIS B 132      -2.009  33.098   1.631  1.00 63.55
ATOM    955  O   HIS B 132      -2.881  32.349   1.190  1.00 63.79
ATOM    956  CB  HIS B 132       0.013  32.246   0.565  1.00 62.76
ATOM    957  CG  HIS B 132       1.042  32.394  -0.504  1.00 63.01
ATOM    958  ND1 HIS B 132       2.190  33.134  -0.326  1.00 62.66
ATOM    959  CD2 HIS B 132       1.103  31.891  -1.759  1.00 63.32
ATOM    960  CE1 HIS B 132       2.919  33.075  -1.426  1.00 63.98
ATOM    961  NE2 HIS B 132       2.282  32.330  -2.312  1.00 64.02
ATOM    962  N   GLU B 133      -2.024  33.582   2.867  1.00 64.47
ATOM    963  CA  GLU B 133      -3.119  33.283   3.776  1.00 65.44
ATOM    964  C   GLU B 133      -4.090  34.453   3.797  1.00 66.05
ATOM    965  O   GLU B 133      -3.684  35.610   3.667  1.00 65.93
ATOM    966  CB  GLU B 133      -2.626  32.956   5.194  1.00 65.67
ATOM    967  CG  GLU B 133      -1.471  33.809   5.704  1.00 66.78
ATOM    968  CD  GLU B 133      -0.717  33.152   6.844  1.00 67.85
ATOM    969  OE1 GLU B 133       0.480  33.471   6.979  1.00 69.49
ATOM    970  OE2 GLU B 133      -1.309  32.333   7.593  1.00 67.46
ATOM    971  N   ASP B 134      -5.370  34.132   3.981  1.00 66.98
ATOM    972  CA  ASP B 134      -6.448  35.118   3.949  1.00 67.75
ATOM    973  C   ASP B 134      -6.742  35.643   5.367  1.00 68.34
ATOM    974  O   ASP B 134      -5.909  35.479   6.277  1.00 68.22
ATOM    975  CB  ASP B 134      -7.693  34.538   3.233  1.00 67.87
ATOM    976  CG  ASP B 134      -8.316  33.358   3.961  1.00 68.15
ATOM    977  OD1 ASP B 134      -8.423  33.390   5.204  1.00 68.95
ATOM    978  OD2 ASP B 134      -8.746  32.355   3.356  1.00 68.33
ATOM    979  N   SER B 135      -7.898  36.293   5.538  1.00 68.88
ATOM    980  CA  SER B 135      -8.268  36.944   6.809  1.00 69.28
ATOM    981  C   SER B 135      -8.607  35.943   7.928  1.00 69.69
ATOM    982  O   SER B 135      -8.288  36.189   9.100  1.00 70.02
ATOM    983  CB  SER B 135      -9.441  37.915   6.599  1.00 69.24
ATOM    984  OG  SER B 135     -10.500  37.296   5.882  1.00 68.75
ATOM    985  N   ASN B 136      -9.250  34.829   7.570  1.00 69.72
ATOM    986  CA  ASN B 136      -9.450  33.716   8.508  1.00 69.91
ATOM    987  C   ASN B 136      -8.145  33.019   8.939  1.00 69.93
ATOM    988  O   ASN B 136      -8.128  32.302   9.941  1.00 69.86
ATOM    989  CB  ASN B 136     -10.397  32.669   7.906  1.00 70.03
ATOM    990  CG  ASN B 136     -11.767  33.231   7.602  1.00 70.29
ATOM    991  OD1 ASN B 136     -12.345  33.951   8.410  1.00 71.01
ATOM    992  ND2 ASN B 136     -12.290  32.913   6.423  1.00 71.21
ATOM    993  N   GLY B 137      -7.066  33.231   8.180  1.00 69.82
ATOM    994  CA  GLY B 137      -5.808  32.539   8.387  1.00 69.55
ATOM    995  C   GLY B 137      -5.832  31.189   7.698  1.00 69.37
ATOM    996  O   GLY B 137      -5.494  30.185   8.305  1.00 69.32
ATOM    997  N   CYS B 138      -6.258  31.170   6.435  1.00 69.54
ATOM    998  CA  CYS B 138      -6.297  29.950   5.617  1.00 69.49
ATOM    999  C   CYS B 138      -5.547  30.129   4.306  1.00 69.07
ATOM   1000  O   CYS B 138      -5.639  31.175   3.665  1.00 68.73
ATOM   1001  CB  CYS B 138      -7.732  29.564   5.264  1.00 69.63
ATOM   1002  SG  CYS B 138      -8.812  29.312   6.669  1.00 71.37
ATOM   1003  N   ILE B 139      -4.855  29.072   3.892  1.00 68.53
ATOM   1004  CA  ILE B 139      -4.084  29.071   2.669  1.00 68.18
ATOM   1005  C   ILE B 139      -4.727  28.121   1.688  1.00 67.81
ATOM   1006  O   ILE B 139      -4.953  26.953   2.001  1.00 67.50
ATOM   1007  CB  ILE B 139      -2.645  28.614   2.948  1.00 68.30
ATOM   1008  CG1 ILE B 139      -1.944  29.631   3.853  1.00 68.68
ATOM   1009  CG2 ILE B 139      -1.886  28.421   1.637  1.00 68.41
ATOM   1010  CD1 ILE B 139      -0.600  29.177   4.350  1.00 69.16
ATOM   1011  N   ASN B 140      -5.022  28.634   0.502  1.00 67.25
ATOM   1012  CA  ASN B 140      -5.365  27.797  -0.623  1.00 67.07
ATOM   1013  C   ASN B 140      -4.078  27.085  -1.026  1.00 67.01
ATOM   1014  O   ASN B 140      -3.172  27.706  -1.582  1.00 66.65
ATOM   1015  CB  ASN B 140      -5.914  28.655  -1.770  1.00 67.05
ATOM   1016  CG  ASN B 140      -6.499  27.829  -2.885  1.00 66.72
ATOM   1017  OD1 ASN B 140      -6.017  26.732  -3.179  1.00 66.08
ATOM   1018  ND2 ASN B 140      -7.554  28.351  -3.522  1.00 66.59
ATOM   1019  N   TYR B 141      -3.997  25.788  -0.722  1.00 66.85
ATOM   1020  CA  TYR B 141      -2.745  25.046  -0.875  1.00 66.78
ATOM   1021  C   TYR B 141      -2.447  24.614  -2.305  1.00 66.24
ATOM   1022  O   TYR B 141      -1.280  24.422  -2.667  1.00 65.99
ATOM   1023  CB  TYR B 141      -2.671  23.839   0.075  1.00 67.11
ATOM   1024  CG  TYR B 141      -3.748  22.781  -0.073  1.00 68.08
ATOM   1025  CD1 TYR B 141      -3.655  21.788  -1.043  1.00 69.02
ATOM   1026  CD2 TYR B 141      -4.831  22.749   0.794  1.00 69.63
ATOM   1027  CE1 TYR B 141      -4.628  20.808  -1.157  1.00 70.68
ATOM   1028  CE2 TYR B 141      -5.809  21.778   0.688  1.00 70.64
ATOM   1029  CZ  TYR B 141      -5.708  20.811  -0.287  1.00 71.41
ATOM   1030  OH  TYR B 141      -6.690  19.845  -0.386  1.00 73.79
ATOM   1031  N   GLU B 142      -3.492  24.436  -3.107  1.00 65.72
ATOM   1032  CA  GLU B 142      -3.308  24.120  -4.521  1.00 65.33
ATOM   1033  C   GLU B 142      -2.646  25.337  -5.164  1.00 64.15
ATOM   1034  O   GLU B 142      -1.722  25.196  -5.963  1.00 63.71
ATOM   1035  CB  GLU B 142      -4.640  23.752  -5.209  1.00 65.82
ATOM   1036  CG  GLU B 142      -5.528  22.835  -4.361  1.00 67.16
ATOM   1037  CD  GLU B 142      -6.301  21.779  -5.150  1.00 69.13
ATOM   1038  OE1 GLU B 142      -6.060  21.617  -6.377  1.00 70.19
ATOM   1039  OE2 GLU B 142      -7.153  21.097  -4.518  1.00 68.74
ATOM   1040  N   ALA B 143      -3.095  26.522  -4.755  1.00 62.93
ATOM   1041  CA  ALA B 143      -2.530  27.787  -5.218  1.00 62.24
ATOM   1042  C   ALA B 143      -1.136  28.016  -4.638  1.00 61.27
ATOM   1043  O   ALA B 143      -0.226  28.452  -5.348  1.00 60.86
ATOM   1044  CB  ALA B 143      -3.450  28.951  -4.843  1.00 62.14
ATOM   1045  N   PHE B 144      -0.986  27.719  -3.350  1.00 60.22
ATOM   1046  CA  PHE B 144       0.301  27.823  -2.655  1.00 59.38
ATOM   1047  C   PHE B 144       1.322  26.857  -3.239  1.00 58.79
ATOM   1048  O   PHE B 144       2.509  27.158  -3.301  1.00 58.76
ATOM   1049  CB  PHE B 144       0.135  27.523  -1.159  1.00 59.26
ATOM   1050  CG  PHE B 144       1.437  27.513  -0.398  1.00 58.87
ATOM   1051  CD1 PHE B 144       2.100  28.707  -0.115  1.00 58.27
ATOM   1052  CD2 PHE B 144       2.016  26.315   0.005  1.00 58.17
ATOM   1053  CE1 PHE B 144       3.306  28.700   0.564  1.00 58.00
ATOM   1054  CE2 PHE B 144       3.224  26.305   0.698  1.00 58.32
ATOM   1055  CZ  PHE B 144       3.866  27.497   0.979  1.00 57.82
ATOM   1056  N   LEU B 145       0.851  25.697  -3.668  1.00 58.11
ATOM   1057  CA  LEU B 145       1.732  24.669  -4.188  1.00 58.00
ATOM   1058  C   LEU B 145       2.257  25.083  -5.553  1.00 57.73
ATOM   1059  O   LEU B 145       3.452  24.960  -5.820  1.00 57.58
ATOM   1060  CB  LEU B 145       1.011  23.324  -4.267  1.00 57.91
ATOM   1061  CG  LEU B 145       1.771  22.207  -4.975  1.00 59.13
ATOM   1062  CD1 LEU B 145       3.128  21.948  -4.302  1.00 59.43
ATOM   1063  CD2 LEU B 145       0.912  20.941  -5.030  1.00 59.19
ATOM   1064  N   LYS B 146       1.369  25.581  -6.416  1.00 57.19
ATOM   1065  CA  LYS B 146       1.774  26.031  -7.748  1.00 56.83
ATOM   1066  C   LYS B 146       2.842  27.117  -7.615  1.00 56.38
ATOM   1067  O   LYS B 146       3.840  27.108  -8.339  1.00 55.70
ATOM   1068  CB  LYS B 146       0.564  26.543  -8.532  1.00 99.99
ATOM   1069  CG  LYS B 146      -0.448  25.466  -8.885  1.00 99.99
ATOM   1070  CD  LYS B 146      -1.621  26.042  -9.661  1.00 99.99
ATOM   1071  CE  LYS B 146      -2.633  24.965 -10.013  1.00 99.99
ATOM   1072  NZ  LYS B 146      -3.276  24.387  -8.800  1.00 99.99
ATOM   1073  N   HIS B 147       2.640  28.017  -6.656  1.00 56.22
ATOM   1074  CA  HIS B 147       3.562  29.130  -6.408  1.00 56.46
ATOM   1075  C   HIS B 147       4.978  28.677  -6.036  1.00 55.99
ATOM   1076  O   HIS B 147       5.949  29.165  -6.610  1.00 55.86
ATOM   1077  CB  HIS B 147       2.998  30.039  -5.308  1.00 56.68
ATOM   1078  CG  HIS B 147       3.843  31.242  -5.011  1.00 58.32
ATOM   1079  ND1 HIS B 147       4.005  32.286  -5.901  1.00 59.99
ATOM   1080  CD2 HIS B 147       4.550  31.577  -3.907  1.00 59.81
ATOM   1081  CE1 HIS B 147       4.783  33.208  -5.358  1.00 59.74
ATOM   1082  NE2 HIS B 147       5.122  32.806  -4.146  1.00 60.22
ATOM   1083  N   ILE B 148       5.101  27.750  -5.087  1.00 55.63
ATOM   1084  CA  ILE B 148       6.433  27.300  -4.658  1.00 55.56
ATOM   1085  C   ILE B 148       7.068  26.336  -5.642  1.00 55.89
ATOM   1086  O   ILE B 148       8.249  26.040  -5.525  1.00 55.69
ATOM   1087  CB  ILE B 148       6.439  26.704  -3.220  1.00 55.05
ATOM   1088  CG1 ILE B 148       5.664  25.390  -3.138  1.00 54.61
ATOM   1089  CG2 ILE B 148       5.906  27.734  -2.218  1.00 55.34
ATOM   1090  CD1 ILE B 148       5.787  24.698  -1.779  1.00 54.34
ATOM   1091  N   LEU B 149       6.283  25.856  -6.608  1.00 56.63
ATOM   1092  CA  LEU B 149       6.779  24.959  -7.657  1.00 57.32
ATOM   1093  C   LEU B 149       7.167  25.727  -8.915  1.00 57.67
ATOM   1094  O   LEU B 149       7.900  25.201  -9.747  1.00 57.78
ATOM   1095  CB  LEU B 149       5.725  23.896  -7.998  1.00 57.46
ATOM   1096  CG  LEU B 149       6.059  22.403  -7.852  1.00 58.09
ATOM   1097  CD1 LEU B 149       7.124  22.110  -6.795  1.00 57.90
ATOM   1098  CD2 LEU B 149       4.777  21.625  -7.555  1.00 58.17
ATOM   1099  N   SER B 150       6.691  26.969  -9.035  1.00 58.17
ATOM   1100  CA  SER B 150       6.916  27.806 -10.222  1.00 58.55
ATOM   1101  C   SER B 150       8.394  28.022 -10.521  1.00 58.63
ATOM   1102  O   SER B 150       9.193  28.213  -9.599  1.00 59.17
ATOM   1103  CB  SER B 150       6.253  29.175 -10.043  1.00 58.62
ATOM   1104  OG  SER B 150       4.840  29.062 -10.009  1.00 59.90
SPDBVT        1.0000000000         0.0000000000         0.0000000000 
SPDBVT        0.0000000000         1.0000000000         0.0000000000 
SPDBVT        0.0000000000         0.0000000000         1.0000000000 
SPDBVT        0.0000000000         0.0000000000         0.0000000000 
SPDBVT        0.0000000000         0.0000000000         0.0000000000 
SPDBVV default;
SPDBVV      3.489880453777    1134.256363923542      20.000000000000
SPDBVV       -0.0308433079        -0.8778251574         0.4779871164 
SPDBVV       -0.7905656843         0.3140402722         0.5257229368 
SPDBVV       -0.6116000238        -0.3616651774        -0.7036644871 
SPDBVV        3.0889999866         4.5114998817        37.9123115540 
SPDBVV        0.0000000000         0.0000000000         0.0000000000 
SPDBVf  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3
SPDBVf  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3
SPDBVf  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3
SPDBVf  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3
SPDBVf  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3
SPDBVf  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3
SPDBVf  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 1.00 0.00 1.00 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 1.00 0.00 1.00 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 1.00 0.00 1.00 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 1.00 0.00 1.00 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 1.00 0.00 1.00 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 1.00 0.00 1.00 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 1.00 0.00 1.00 0.00 0.00 0.20 1.00 0.00 1.00 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 1.00 0.00 1.00 0.00 0.00 0.20 
SPDBVc 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 1.00 0.00 1.00 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 1.00 0.00 1.00 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 1.00 0.00 1.00 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 1.00 0.00 1.00 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 1.00 0.00 1.00 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 1.00 0.00 1.00 0.00 0.00 0.20 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 1.00 0.00 1.00 0.00 0.00 0.20 
SPDBVC 0.00 0.00 0.20 0.00 0.00 0.20 0.00 0.00 0.20 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVb 0.00 0.00 0.20
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64
SPDBVi        1 1 1 0 1 0 1 1 0 1 0 1 1 0  0
SPDBVp     9606
END



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