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***  TOXIN 30-AUG-12 4GV5  ***

elNémo ID: 23011323363465737

Job options:

ID        	=	 23011323363465737
JOBID     	=	 TOXIN 30-AUG-12 4GV5
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TOXIN                                   30-AUG-12   4GV5              
TITLE     X-RAY STRUCTURE OF CROTAMINE, A CELL-PENETRATING PEPTIDE FROM THE     
TITLE    2 BRAZILIAN SNAKE CROTALUS DURISSUS TERRIFICUS                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CROTAMINE ILE-19;                                          
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: CRO_ILE-19                                                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CROTALUS DURISSUS TERRIFICUS;                   
SOURCE   3 ORGANISM_COMMON: SOUTH AMERICAN RATTLESNAKE;                         
SOURCE   4 ORGANISM_TAXID: 8732                                                 
KEYWDS    ALPHA HELIX & BETA SHEET, ION CHANNEL INHIBITOR, ANTIBACTERIAL        
KEYWDS   2 PEPTIDE, EXTRACELLULAR REGION, TOXIN                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.CORONADO,A.GABDULKHAKOV,D.GEORGIEVA,B.SANKARAN,M.T.MURAKAMI,      
AUTHOR   2 R.K.ARNI,C.BETZEL                                                    
REVDAT   5   07-MAR-18 4GV5    1       REMARK                                   
REVDAT   4   23-OCT-13 4GV5    1       JRNL                                     
REVDAT   3   02-OCT-13 4GV5    1       DBREF  SOURCE                            
REVDAT   2   11-SEP-13 4GV5    1       REMARK                                   
REVDAT   1   04-SEP-13 4GV5    0                                                
JRNL        AUTH   M.A.CORONADO,A.GABDULKHAKOV,D.GEORGIEVA,B.SANKARAN,          
JRNL        AUTH 2 M.T.MURAKAMI,R.K.ARNI,C.BETZEL                               
JRNL        TITL   STRUCTURE OF THE POLYPEPTIDE CROTAMINE FROM THE BRAZILIAN    
JRNL        TITL 2 RATTLESNAKE CROTALUS DURISSUS TERRIFICUS.                    
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  69  1958 2013              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   24100315                                                     
JRNL        DOI    10.1107/S0907444913018003                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 20890                          
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) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1121                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1125                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.06                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5500                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 63                           
REMARK   3   BIN FREE R VALUE                    : 0.6910                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1014                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 51                                      
REMARK   3   SOLVENT ATOMS            : 62                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.67000                                             
REMARK   3    B22 (A**2) : -0.86000                                             
REMARK   3    B33 (A**2) : 1.53000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.096         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.092         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.064         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.493         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.975                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.958                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1116 ; 0.034 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1471 ; 2.856 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   127 ; 6.475 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    39 ;23.802 ;21.538       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   221 ;18.430 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;22.576 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   126 ; 0.196 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   784 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  1116 ;11.826 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    31 ;27.031 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  1122 ;36.112 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4GV5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-SEP-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000074671.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PETRA III, EMBL C/O DESY           
REMARK 200  BEAMLINE                       : P14 (MX2)                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.12                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20890                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: AUTOSOL                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM THIOCYANATE, 1.9 M          
REMARK 280  AMMONIUM SULPHATE, PH 6.1, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 293.0K                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y+1/2,Z                                             
REMARK 290       7555   -X+1/2,Y,-Z                                             
REMARK 290       8555   X,-Y,-Z+1/2                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       33.46100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.09950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.16500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.09950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.46100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.16500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       33.46100            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       37.16500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       40.09950            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       37.16500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.46100            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       40.09950            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -129.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       74.33000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       40.09950            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8100 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1 -1.000000  0.000000  0.000000       66.92200            
REMARK 350   BIOMT2   1  0.000000 -1.000000  0.000000       37.16500            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH C 212  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    MET A  28     -132.02     47.26                                   
REMARK 500    MET B  28     -130.86     48.04                                   
REMARK 500    MET C  28     -129.55     46.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN B 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN C 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 104                 
DBREF  4GV5 A    1    42  UNP    P01475   MYXC_CRODU       1     42             
DBREF  4GV5 B    1    42  UNP    P01475   MYXC_CRODU       1     42             
DBREF  4GV5 C    1    42  UNP    P01475   MYXC_CRODU       1     42             
SEQRES   1 A   42  TYR LYS GLN CYS HIS LYS LYS GLY GLY HIS CYS PHE PRO          
SEQRES   2 A   42  LYS GLU LYS ILE CYS LEU PRO PRO SER SER ASP PHE GLY          
SEQRES   3 A   42  LYS MET ASP CYS ARG TRP ARG TRP LYS CYS CYS LYS LYS          
SEQRES   4 A   42  GLY SER GLY                                                  
SEQRES   1 B   42  TYR LYS GLN CYS HIS LYS LYS GLY GLY HIS CYS PHE PRO          
SEQRES   2 B   42  LYS GLU LYS ILE CYS LEU PRO PRO SER SER ASP PHE GLY          
SEQRES   3 B   42  LYS MET ASP CYS ARG TRP ARG TRP LYS CYS CYS LYS LYS          
SEQRES   4 B   42  GLY SER GLY                                                  
SEQRES   1 C   42  TYR LYS GLN CYS HIS LYS LYS GLY GLY HIS CYS PHE PRO          
SEQRES   2 C   42  LYS GLU LYS ILE CYS LEU PRO PRO SER SER ASP PHE GLY          
SEQRES   3 C   42  LYS MET ASP CYS ARG TRP ARG TRP LYS CYS CYS LYS LYS          
SEQRES   4 C   42  GLY SER GLY                                                  
HET    SCN  A 101       3                                                       
HET    SCN  A 102       3                                                       
HET    GOL  A 103       6                                                       
HET    GOL  A 104       6                                                       
HET    SO4  B 101       5                                                       
HET    SO4  B 102       5                                                       
HET    SCN  B 103       3                                                       
HET    SO4  C 101       5                                                       
HET    SCN  C 102       3                                                       
HET    GOL  C 103       6                                                       
HET    GOL  C 104       6                                                       
HETNAM     SCN THIOCYANATE ION                                                  
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   4  SCN    4(C N S 1-)                                                  
FORMUL   6  GOL    4(C3 H8 O3)                                                  
FORMUL   8  SO4    3(O4 S 2-)                                                   
FORMUL  15  HOH   *62(H2 O)                                                     
HELIX    1   1 TYR A    1  LYS A    7  1                                   7
HELIX    2   2 PRO A   20  ASP A   24  1                                   5
SHEET    1   1 1 GLY A   9  PRO A  13  0
SHEET    2   2 1 TRP A  34  LYS A  38  0
SSBOND   1 CYS A    4    CYS A   36                          1555   1555  2.13  
SSBOND   2 CYS A   11    CYS A   30                          1555   1555  2.13  
SSBOND   3 CYS A   18    CYS A   37                          1555   1555  2.02  
SSBOND   4 CYS B    4    CYS B   36                          1555   1555  2.05  
SSBOND   5 CYS B   11    CYS B   30                          1555   1555  2.06  
SSBOND   6 CYS B   18    CYS B   37                          1555   1555  2.00  
SSBOND   7 CYS C    4    CYS C   36                          1555   1555  2.13  
SSBOND   8 CYS C   11    CYS C   30                          1555   1555  2.08  
LINK         SG  CYS C  18                 SG  CYS C  37     1555   1555  1.70  
CISPEP   1 LEU A   19    PRO A   20          0        -3.40                     
CISPEP   2 LEU B   19    PRO B   20          0         0.95                     
CISPEP   3 LEU C   19    PRO C   20          0        10.95                     
SITE     1 AC1  4 ILE A  17  HOH A 204  TYR C   1  TRP C  34                    
SITE     1 AC2  5 PRO A  13  LYS A  14  GLU A  15  PRO B  21                    
SITE     2 AC2  5 PRO C  13                                                     
SITE     1 AC3  5 LYS A  14  TRP A  32  ARG A  33  PRO B  21                    
SITE     2 AC3  5 SER B  22                                                     
SITE     1 AC4  4 GLN A   3  TRP A  32  ARG A  33  HOH A 215                    
SITE     1 AC5  6 LYS B   2  GLN B   3  TRP B  32  ARG B  33                    
SITE     2 AC5  6 HOH B 209  HOH B 211                                          
SITE     1 AC6  6 TYR B   1  HIS B  10  CYS B  11  HOH B 213                    
SITE     2 AC6  6 ARG C  31  TRP C  32                                          
SITE     1 AC7  5 PHE B  12  PRO B  13  ILE B  17  GLY B  42                    
SITE     2 AC7  5 GOL C 103                                                     
SITE     1 AC8  6 PHE A  12  PRO A  13  LYS A  16  HIS C  10                    
SITE     2 AC8  6 CYS C  11  HOH C 204                                          
SITE     1 AC9  2 TRP C  32  ARG C  33                                          
SITE     1 BC1  7 PHE B  12  GLY B  42  SCN B 103  ARG C  31                    
SITE     2 BC1  7 TRP C  32  ARG C  33  TRP C  34                               
SITE     1 BC2  7 LEU B  19  PRO B  20  PRO B  21  PRO C  13                    
SITE     2 BC2  7 LYS C  14  GLU C  15  LYS C  16                               
CRYST1   66.922   74.330   80.199  90.00  90.00  90.00 I 21 21 21   24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014943  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013454  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012469        0.00000                         
ATOM      1  N   TYR A   1      24.311  40.954  45.768  1.00 48.43           N
ANISOU    1  N   TYR A   1     6674   7165   4561  -1383   1803   -302       N
ATOM      2  CA  TYR A   1      22.901  40.559  45.929  1.00 46.14           C
ANISOU    2  CA  TYR A   1     6349   4789   6394   -158   1927  -1208       C
ATOM      3  C   TYR A   1      22.740  39.866  47.274  1.00 50.30           C
ANISOU    3  C   TYR A   1     6924   6579   5608    897    489   -947       C
ATOM      4  O   TYR A   1      23.578  39.023  47.619  1.00 48.29           O
ANISOU    4  O   TYR A   1     6325   5751   6271    196   -141   -688       O
ATOM      5  CB  TYR A   1      22.554  39.627  44.799  1.00 46.55           C
ANISOU    5  CB  TYR A   1     8175   4578   4932  -1960  -1004    486       C
ATOM      6  CG  TYR A   1      22.522  40.362  43.516  1.00 39.39           C
ANISOU    6  CG  TYR A   1     6216   5801   2947     22   1429     72       C
ATOM      7  CD1 TYR A   1      21.545  41.330  43.290  1.00 64.59           C
ANISOU    7  CD1 TYR A   1     6778   8253   9507   -365   -736   2417       C
ATOM      8  CD2 TYR A   1      23.481  40.137  42.519  1.00 42.00           C
ANISOU    8  CD2 TYR A   1     7965   5930   2064   1402   2007    250       C
ATOM      9  CE1 TYR A   1      21.507  42.019  42.090  1.00 84.67           C
ANISOU    9  CE1 TYR A   1    12819   8250  11100   -653   3177   3303       C
ATOM     10  CE2 TYR A   1      23.428  40.798  41.291  1.00 42.01           C
ANISOU   10  CE2 TYR A   1     8103   4983   2875    963   -142    537       C
ATOM     11  CZ  TYR A   1      22.470  41.761  41.105  1.00 58.47           C
ANISOU   11  CZ  TYR A   1     9210   6541   6463   -368   -949    771       C
ATOM     12  OH  TYR A   1      22.402  42.469  39.919  1.00 62.09           O
ANISOU   12  OH  TYR A   1    11715   6953   4923   -396    801   -864       O
ATOM     13  N   LYS A   2      21.671  40.199  48.001  1.00 41.64           N
ANISOU   13  N   LYS A   2     5750   4508   5563   -149    700  -1120       N
ATOM     14  CA  LYS A   2      21.496  39.794  49.427  1.00 41.06           C
ANISOU   14  CA  LYS A   2     4983   5356   5259    149   2324  -1046       C
ATOM     15  C   LYS A   2      21.742  38.292  49.675  1.00 37.57           C
ANISOU   15  C   LYS A   2     3562   5711   5000     79    248  -1697       C
ATOM     16  O   LYS A   2      22.587  37.955  50.467  1.00 42.63           O
ANISOU   16  O   LYS A   2     5395   5518   5285    653   -256  -2190       O
ATOM     17  CB  LYS A   2      20.069  40.193  49.936  1.00 47.38           C
ANISOU   17  CB  LYS A   2     5466   5424   7109   1213   3447  -1822       C
ATOM     18  CG  LYS A   2      19.769  40.064  51.444  1.00 72.13           C
ANISOU   18  CG  LYS A   2     6964  11056   9386  -2051   2264  -4277       C
ATOM     19  CD  LYS A   2      18.363  40.553  51.803  1.00 63.74           C
ANISOU   19  CD  LYS A   2     6635   8674   8906    128  -1773  -4014       C
ATOM     20  CE  LYS A   2      18.211  40.865  53.306  1.00 85.58           C
ANISOU   20  CE  LYS A   2     7630  16059   8826    539   2270  -1666       C
ATOM     21  NZ  LYS A   2      16.785  40.750  53.766  1.00114.43           N
ANISOU   21  NZ  LYS A   2    13291  21439   8747   4159   3598   2752       N
ATOM     22  N   GLN A   3      20.983  37.403  49.013  1.00 37.10           N
ANISOU   22  N   GLN A   3     5055   5047   3992   -779   1012  -1367       N
ATOM     23  CA  GLN A   3      20.983  35.955  49.346  1.00 40.92           C
ANISOU   23  CA  GLN A   3     4805   5768   4972    289    161  -1255       C
ATOM     24  C   GLN A   3      22.294  35.285  48.988  1.00 33.20           C
ANISOU   24  C   GLN A   3     4323   4546   3745   -501    277   -874       C
ATOM     25  O   GLN A   3      22.844  34.461  49.802  1.00 35.66           O
ANISOU   25  O   GLN A   3     5161   5226   3161    -65    537   -733       O
ATOM     26  CB  GLN A   3      19.767  35.192  48.794  1.00 37.76           C
ANISOU   26  CB  GLN A   3     3789   6107   4450   -644    459  -1001       C
ATOM     27  CG  GLN A   3      18.456  35.922  49.091  1.00 37.23           C
ANISOU   27  CG  GLN A   3     3844   5878   4423   -521   -357     -9       C
ATOM     28  CD  GLN A   3      18.133  35.872  50.562  1.00 42.35           C
ANISOU   28  CD  GLN A   3     4680   5983   5428   1106    527    -68       C
ATOM     29  OE1 GLN A   3      18.730  35.029  51.312  1.00 40.67           O
ANISOU   29  OE1 GLN A   3     4827   7604   3021   -224   1036   -225       O
ATOM     30  NE2 GLN A   3      17.205  36.737  51.025  1.00 43.32           N
ANISOU   30  NE2 GLN A   3     4856   6446   5154   1051    881   -878       N
ATOM     31  N   CYS A   4      22.849  35.700  47.831  1.00 32.29           N
ANISOU   31  N   CYS A   4     3390   4970   3906   -653   1725  -1370       N
ATOM     32  CA  CYS A   4      24.146  35.145  47.360  1.00 30.30           C
ANISOU   32  CA  CYS A   4     3075   6031   2404    137    791   -976       C
ATOM     33  C   CYS A   4      25.199  35.612  48.402  1.00 34.59           C
ANISOU   33  C   CYS A   4     3847   4753   4540    -39     23    -55       C
ATOM     34  O   CYS A   4      26.002  34.803  48.928  1.00 32.96           O
ANISOU   34  O   CYS A   4     4162   5573   2787    202    -21   -560       O
ATOM     35  CB  CYS A   4      24.440  35.634  45.905  1.00 35.65           C
ANISOU   35  CB  CYS A   4     4232   6271   3040    414    724    -10       C
ATOM     36  SG  CYS A   4      26.087  35.012  45.476  1.00 36.57           S
ANISOU   36  SG  CYS A   4     4536   5491   3865   -134    172   -292       S
ATOM     37  N   HIS A   5      25.194  36.900  48.725  1.00 37.49           N
ANISOU   37  N   HIS A   5     4979   5176   4089     95     93   -846       N
ATOM     38  CA  HIS A   5      26.136  37.437  49.682  1.00 41.85           C
ANISOU   38  CA  HIS A   5     6452   6092   3355   -816   -454  -1159       C
ATOM     39  C   HIS A   5      25.998  36.741  51.028  1.00 40.69           C
ANISOU   39  C   HIS A   5     4767   6478   4215      7   -569  -1451       C
ATOM     40  O   HIS A   5      27.002  36.376  51.657  1.00 45.98           O
ANISOU   40  O   HIS A   5     5604   7178   4688    158  -1067  -2206       O
ATOM     41  CB  HIS A   5      26.026  38.939  49.775  1.00 44.11           C
ANISOU   41  CB  HIS A   5     4445   5872   6442   -859   -528  -1782       C
ATOM     42  CG  HIS A   5      26.928  39.550  50.871  1.00 57.48           C
ANISOU   42  CG  HIS A   5     6701   7413   7727   -373  -2095  -1205       C
ATOM     43  ND1 HIS A   5      28.234  39.827  50.664  1.00 67.20           N
ANISOU   43  ND1 HIS A   5    10382   8416   6733   -653   3779  -2316       N
ATOM     44  CD2 HIS A   5      26.671  39.883  52.205  1.00 90.63           C
ANISOU   44  CD2 HIS A   5    15993   8861   9578   1646   -914  -2745       C
ATOM     45  CE1 HIS A   5      28.776  40.320  51.783  1.00 76.90           C
ANISOU   45  CE1 HIS A   5    15191   7451   6575   1811  -2888   -846       C
ATOM     46  NE2 HIS A   5      27.823  40.341  52.724  1.00 97.10           N
ANISOU   46  NE2 HIS A   5    19438   7906   9547   3097  -3044  -6890       N
ATOM     47  N   LYS A   6      24.755  36.526  51.464  1.00 46.68           N
ANISOU   47  N   LYS A   6     5815   6908   5010   -987   -503   -213       N
ATOM     48  CA  LYS A   6      24.518  35.839  52.689  1.00 39.78           C
ANISOU   48  CA  LYS A   6     4100   6960   4052   -714   -406    -39       C
ATOM     49  C   LYS A   6      25.116  34.478  52.820  1.00 45.96           C
ANISOU   49  C   LYS A   6     7453   6632   3378   -666  -1255  -1097       C
ATOM     50  O   LYS A   6      25.550  34.166  53.947  1.00 48.22           O
ANISOU   50  O   LYS A   6     6194  10004   2123    -54   -217   -204       O
ATOM     51  CB  LYS A   6      23.079  35.774  53.044  1.00 39.75           C
ANISOU   51  CB  LYS A   6     3769   6920   4412   -841    121  -1715       C
ATOM     52  CG  LYS A   6      22.520  37.020  53.717  1.00 71.12           C
ANISOU   52  CG  LYS A   6     9494  13997   3531   3120   -190  -4676       C
ATOM     53  CD  LYS A   6      20.980  36.875  53.824  1.00101.25           C
ANISOU   53  CD  LYS A   6    10214  17126  11127  -3208  -1625  -1690       C
ATOM     54  CE  LYS A   6      20.445  35.459  54.200  1.00 57.85           C
ANISOU   54  CE  LYS A   6     7555  12061   2365    742     86  -1620       C
ATOM     55  NZ  LYS A   6      20.202  35.394  55.645  1.00105.66           N
ANISOU   55  NZ  LYS A   6    15040  21576   3529   2381   -835   -745       N
ATOM     56  N   LYS A   7      25.155  33.716  51.709  1.00 43.85           N
ANISOU   56  N   LYS A   7     6452   6383   3825   -151   -226   -603       N
ATOM     57  CA  LYS A   7      25.844  32.434  51.605  1.00 41.04           C
ANISOU   57  CA  LYS A   7     5724   6338   3527   -119   -817   -381       C
ATOM     58  C   LYS A   7      27.349  32.559  51.571  1.00 35.16           C
ANISOU   58  C   LYS A   7     4781   5253   3323   -284  -1027    305       C
ATOM     59  O   LYS A   7      28.021  31.526  51.573  1.00 50.63           O
ANISOU   59  O   LYS A   7     6476   7405   5356    678  -1274    610       O
ATOM     60  CB  LYS A   7      25.436  31.670  50.329  1.00 44.44           C
ANISOU   60  CB  LYS A   7     6222   6378   4285    451   -194  -1700       C
ATOM     61  CG  LYS A   7      24.163  30.975  50.626  1.00 51.82           C
ANISOU   61  CG  LYS A   7     5679   6483   7525     95     87    517       C
ATOM     62  CD  LYS A   7      23.931  29.824  49.732  1.00 56.90           C
ANISOU   62  CD  LYS A   7     6939  10555   4123   -660   2015   -825       C
ATOM     63  CE  LYS A   7      22.866  28.970  50.368  1.00 58.37           C
ANISOU   63  CE  LYS A   7     8212  11305   2659    806    109    828       C
ATOM     64  NZ  LYS A   7      23.298  28.071  51.436  1.00 64.97           N
ANISOU   64  NZ  LYS A   7    11743   9019   3920  -2041  -2024   1425       N
ATOM     65  N   GLY A   8      27.891  33.791  51.546  1.00 40.18           N
ANISOU   65  N   GLY A   8     6137   6403   2726  -1156    269    103       N
ATOM     66  CA  GLY A   8      29.340  33.966  51.457  1.00 41.87           C
ANISOU   66  CA  GLY A   8     5407   7262   3238   -350    264  -1078       C
ATOM     67  C   GLY A   8      29.807  33.862  49.988  1.00 35.66           C
ANISOU   67  C   GLY A   8     4315   6029   3204    805    -76   -125       C
ATOM     68  O   GLY A   8      30.971  33.632  49.687  1.00 39.22           O
ANISOU   68  O   GLY A   8     4612   7283   3007   1034   -728  -1671       O
ATOM     69  N   GLY A   9      28.880  34.025  49.058  1.00 36.96           N
ANISOU   69  N   GLY A   9     5608   5403   3030      5   -915   -350       N
ATOM     70  CA  GLY A   9      29.219  33.864  47.600  1.00 34.94           C
ANISOU   70  CA  GLY A   9     5397   4960   2917     56   -612    168       C
ATOM     71  C   GLY A   9      29.298  35.198  46.859  1.00 33.03           C
ANISOU   71  C   GLY A   9     4610   4036   3903   -549    -78  -1257       C
ATOM     72  O   GLY A   9      29.119  36.303  47.455  1.00 35.49           O
ANISOU   72  O   GLY A   9     4989   4966   3529   -419    326  -1567       O
ATOM     73  N   HIS A  10      29.573  35.078  45.555  1.00 33.72           N
ANISOU   73  N   HIS A  10     3933   5242   3634    -96     34   -904       N
ATOM     74  CA  HIS A  10      29.513  36.162  44.662  1.00 35.30           C
ANISOU   74  CA  HIS A  10     5416   4481   3512  -1671   -389   -351       C
ATOM     75  C   HIS A  10      28.930  35.691  43.353  1.00 32.80           C
ANISOU   75  C   HIS A  10     4251   3695   4514    109   -682   -496       C
ATOM     76  O   HIS A  10      28.965  34.505  43.080  1.00 31.47           O
ANISOU   76  O   HIS A  10     4305   4039   3614   -566     36   -501       O
ATOM     77  CB  HIS A  10      30.920  36.687  44.430  1.00 40.09           C
ANISOU   77  CB  HIS A  10     4769   5543   4918  -2130   1528   -835       C
ATOM     78  CG  HIS A  10      30.938  38.043  43.862  1.00 79.21           C
ANISOU   78  CG  HIS A  10     8249   7844  14001  -2619  -1548    722       C
ATOM     79  ND1 HIS A  10      31.410  38.306  42.609  1.00 98.22           N
ANISOU   79  ND1 HIS A  10     4672  13315  19329   -750   -104  -2633       N
ATOM     80  CD2 HIS A  10      30.508  39.255  44.396  1.00 86.29           C
ANISOU   80  CD2 HIS A  10    10291  10522  11973  -4653   4378  -3111       C
ATOM     81  CE1 HIS A  10      31.279  39.611  42.353  1.00113.21           C
ANISOU   81  CE1 HIS A  10    24953  11844   6216 -10717  -1280     95       C
ATOM     82  NE2 HIS A  10      30.731  40.200  43.457  1.00 97.62           N
ANISOU   82  NE2 HIS A  10    11069   8215  17804  -2304  -4237  -3975       N
ATOM     83  N   CYS A  11      28.407  36.589  42.524  1.00 32.14           N
ANISOU   83  N   CYS A  11     5108   4435   2667     77    179   -870       N
ATOM     84  CA  CYS A  11      27.831  36.192  41.252  1.00 28.45           C
ANISOU   84  CA  CYS A  11     3097   5806   1906    217    649  -1586       C
ATOM     85  C   CYS A  11      28.786  36.113  40.145  1.00 27.67           C
ANISOU   85  C   CYS A  11     2929   3917   3667   -369   1195    -86       C
ATOM     86  O   CYS A  11      29.536  37.067  39.892  1.00 33.89           O
ANISOU   86  O   CYS A  11     4625   3845   4404   -991   1245   -800       O
ATOM     87  CB  CYS A  11      26.616  37.067  40.894  1.00 36.38           C
ANISOU   87  CB  CYS A  11     3932   4926   4965    289    992   -617       C
ATOM     88  SG  CYS A  11      25.267  37.101  42.146  1.00 40.25           S
ANISOU   88  SG  CYS A  11     5604   5513   4174   1082    590   -360       S
ATOM     89  N   PHE A  12      28.633  35.036  39.378  1.00 32.24           N
ANISOU   89  N   PHE A  12     3957   4644   3649     41   -281   -189       N
ATOM     90  CA  PHE A  12      29.570  34.775  38.195  1.00 32.65           C
ANISOU   90  CA  PHE A  12     3654   4868   3882    525    164   -175       C
ATOM     91  C   PHE A  12      28.715  34.319  37.052  1.00 31.75           C
ANISOU   91  C   PHE A  12     4425   4789   2850   -826    566    692       C
ATOM     92  O   PHE A  12      27.615  33.842  37.275  1.00 27.78           O
ANISOU   92  O   PHE A  12     3399   4103   3053   -161    135    -93       O
ATOM     93  CB  PHE A  12      30.663  33.679  38.504  1.00 29.06           C
ANISOU   93  CB  PHE A  12     3207   4561   3271    536   -823     71       C
ATOM     94  CG  PHE A  12      31.522  33.999  39.638  1.00 29.31           C
ANISOU   94  CG  PHE A  12     3592   4086   3456    -62   -365   -358       C
ATOM     95  CD1 PHE A  12      32.666  34.792  39.463  1.00 37.03           C
ANISOU   95  CD1 PHE A  12     4271   5571   4227  -1375   -612   -290       C
ATOM     96  CD2 PHE A  12      31.209  33.529  40.955  1.00 33.56           C
ANISOU   96  CD2 PHE A  12     4411   5127   3211    316   -793    -19       C
ATOM     97  CE1 PHE A  12      33.473  35.117  40.543  1.00 39.65           C
ANISOU   97  CE1 PHE A  12     4844   6238   3982   -507   -614  -1873       C
ATOM     98  CE2 PHE A  12      32.086  33.851  42.056  1.00 28.52           C
ANISOU   98  CE2 PHE A  12     3643   4135   3057   -541   -516   -282       C
ATOM     99  CZ  PHE A  12      33.189  34.642  41.833  1.00 42.76           C
ANISOU   99  CZ  PHE A  12     4539   6381   5327  -1425    -82   -226       C
ATOM    100  N   PRO A  13      29.226  34.432  35.819  1.00 26.59           N
ANISOU  100  N   PRO A  13     3436   3754   2911   -142    627    378       N
ATOM    101  CA  PRO A  13      28.435  33.933  34.648  1.00 27.48           C
ANISOU  101  CA  PRO A  13     3693   3718   3028   -193    572    106       C
ATOM    102  C   PRO A  13      28.022  32.464  34.862  1.00 25.85           C
ANISOU  102  C   PRO A  13     3138   3995   2687     57    544    103       C
ATOM    103  O   PRO A  13      28.815  31.683  35.520  1.00 28.16           O
ANISOU  103  O   PRO A  13     3760   3718   3221    173     42   -344       O
ATOM    104  CB  PRO A  13      29.474  34.079  33.497  1.00 25.68           C
ANISOU  104  CB  PRO A  13     3521   3408   2827   -786    605   -119       C
ATOM    105  CG  PRO A  13      30.238  35.310  33.908  1.00 25.50           C
ANISOU  105  CG  PRO A  13     3705   3754   2230   -681     76    -80       C
ATOM    106  CD  PRO A  13      30.511  35.051  35.412  1.00 26.83           C
ANISOU  106  CD  PRO A  13     3117   4371   2705   -480    376    494       C
ATOM    107  N   LYS A  14      26.854  32.055  34.347  1.00 26.33           N
ANISOU  107  N   LYS A  14     3293   3255   3455   -293    -86   -282       N
ATOM    108  CA  LYS A  14      26.279  30.739  34.482  1.00 27.75           C
ANISOU  108  CA  LYS A  14     3928   3248   3365    378   -658    151       C
ATOM    109  C   LYS A  14      27.302  29.546  34.237  1.00 23.33           C
ANISOU  109  C   LYS A  14     2356   3507   3001   -347   -575    402       C
ATOM    110  O   LYS A  14      27.215  28.529  34.923  1.00 26.09           O
ANISOU  110  O   LYS A  14     3426   3632   2855   -199    -40    276       O
ATOM    111  CB  LYS A  14      25.120  30.702  33.415  1.00 35.18           C
ANISOU  111  CB  LYS A  14     3478   4098   5791    399   -966    195       C
ATOM    112  CG  LYS A  14      24.369  29.433  33.341  1.00 32.85           C
ANISOU  112  CG  LYS A  14     4227   4728   3527     83   -200    387       C
ATOM    113  CD  LYS A  14      23.168  29.611  32.433  1.00 34.75           C
ANISOU  113  CD  LYS A  14     4472   4455   4275    701   -772    565       C
ATOM    114  CE  LYS A  14      22.754  28.197  32.200  1.00 35.26           C
ANISOU  114  CE  LYS A  14     4327   5660   3411    401   -671   -288       C
ATOM    115  NZ  LYS A  14      21.546  28.155  31.278  1.00 33.56           N
ANISOU  115  NZ  LYS A  14     3520   4953   4277    -74   -630    -49       N
ATOM    116  N   GLU A  15      28.205  29.639  33.234  1.00 25.69           N
ANISOU  116  N   GLU A  15     3240   3693   2826     64    491   -581       N
ATOM    117  CA  GLU A  15      29.101  28.568  32.854  1.00 22.99           C
ANISOU  117  CA  GLU A  15     2943   3714   2075    382   -117   -121       C
ATOM    118  C   GLU A  15      30.485  28.643  33.540  1.00 20.90           C
ANISOU  118  C   GLU A  15     2784   3231   1924     73    -32   -108       C
ATOM    119  O   GLU A  15      31.349  27.815  33.271  1.00 25.28           O
ANISOU  119  O   GLU A  15     3307   3526   2772    129     48   -243       O
ATOM    120  CB  GLU A  15      29.322  28.533  31.287  1.00 24.15           C
ANISOU  120  CB  GLU A  15     3529   3899   1745   -520   -408   -512       C
ATOM    121  CG  GLU A  15      28.034  28.205  30.567  1.00 25.42           C
ANISOU  121  CG  GLU A  15     3502   3291   2862   -829   -589    156       C
ATOM    122  CD  GLU A  15      27.316  26.985  31.106  1.00 29.32           C
ANISOU  122  CD  GLU A  15     3532   3551   4055    187     93     19       C
ATOM    123  OE1 GLU A  15      27.977  25.944  31.319  1.00 27.54           O
ANISOU  123  OE1 GLU A  15     4047   3686   2728    -27   -252   -301       O
ATOM    124  OE2 GLU A  15      26.099  27.103  31.385  1.00 28.80           O
ANISOU  124  OE2 GLU A  15     3652   4152   3138     66    376   -129       O
ATOM    125  N   LYS A  16      30.678  29.655  34.429  1.00 25.81           N
ANISOU  125  N   LYS A  16     3756   3276   2771   -362   -535   -160       N
ATOM    126  CA  LYS A  16      31.976  29.797  35.068  1.00 27.99           C
ANISOU  126  CA  LYS A  16     3220   3637   3777   -162   -613   -110       C
ATOM    127  C   LYS A  16      32.199  28.509  35.874  1.00 26.13           C
ANISOU  127  C   LYS A  16     3026   3764   3135   -191   -285   -181       C
ATOM    128  O   LYS A  16      31.270  28.098  36.665  1.00 27.73           O
ANISOU  128  O   LYS A  16     3871   3850   2815     -2   -127    252       O
ATOM    129  CB  LYS A  16      32.087  31.039  35.966  1.00 27.26           C
ANISOU  129  CB  LYS A  16     3502   3746   3110   -506    759    293       C
ATOM    130  CG  LYS A  16      33.519  31.148  36.534  1.00 30.53           C
ANISOU  130  CG  LYS A  16     3701   4291   3605   -323    170   -708       C
ATOM    131  CD  LYS A  16      33.721  31.926  37.759  1.00 36.38           C
ANISOU  131  CD  LYS A  16     4304   5071   4448    664    -82  -1527       C
ATOM    132  CE  LYS A  16      35.089  31.586  38.360  1.00 52.43           C
ANISOU  132  CE  LYS A  16     4691   8021   7207  -2454  -2881  -1257       C
ATOM    133  NZ  LYS A  16      35.923  32.646  37.688  1.00 73.14           N
ANISOU  133  NZ  LYS A  16     6132   9584  12074  -2200  -3950   3405       N
ATOM    134  N   ILE A  17      33.402  27.896  35.772  1.00 25.50           N
ANISOU  134  N   ILE A  17     3413   3626   2649    323   -497    137       N
ATOM    135  CA  ILE A  17      33.706  26.701  36.624  1.00 24.57           C
ANISOU  135  CA  ILE A  17     3747   3497   2090    443   -742   -277       C
ATOM    136  C   ILE A  17      33.942  27.163  38.045  1.00 26.08           C
ANISOU  136  C   ILE A  17     3675   3780   2454   -440   -152   -582       C
ATOM    137  O   ILE A  17      34.786  28.096  38.293  1.00 27.01           O
ANISOU  137  O   ILE A  17     3850   4078   2335   -350     93   -104       O
ATOM    138  CB  ILE A  17      34.925  25.963  36.079  1.00 26.88           C
ANISOU  138  CB  ILE A  17     4035   3263   2914    463   -575    117       C
ATOM    139  CG1 ILE A  17      34.550  25.348  34.606  1.00 26.49           C
ANISOU  139  CG1 ILE A  17     3104   3901   3058   -501     76    -52       C
ATOM    140  CG2 ILE A  17      35.517  24.937  37.074  1.00 25.14           C
ANISOU  140  CG2 ILE A  17     3599   3907   2043     -2   -622    523       C
ATOM    141  CD1 ILE A  17      35.782  24.956  33.853  1.00 26.74           C
ANISOU  141  CD1 ILE A  17     3359   4842   1956    281   -357    213       C
ATOM    142  N   CYS A  18      33.172  26.546  38.962  1.00 27.48           N
ANISOU  142  N   CYS A  18     3708   4467   2264    523   -175    -83       N
ATOM    143  CA  CYS A  18      33.350  26.853  40.436  1.00 26.84           C
ANISOU  143  CA  CYS A  18     4068   3996   2133    107    297   -375       C
ATOM    144  C   CYS A  18      33.710  25.551  41.117  1.00 27.06           C
ANISOU  144  C   CYS A  18     3608   3683   2988   -214    668   -320       C
ATOM    145  O   CYS A  18      32.870  24.623  41.132  1.00 27.52           O
ANISOU  145  O   CYS A  18     3638   4149   2668   -657     -5     46       O
ATOM    146  CB  CYS A  18      32.081  27.410  41.069  1.00 30.58           C
ANISOU  146  CB  CYS A  18     3044   4480   4092    570    463   -107       C
ATOM    147  SG  CYS A  18      31.611  29.009  40.348  1.00 34.75           S
ANISOU  147  SG  CYS A  18     4467   4710   4026    532   -224   -458       S
ATOM    148  N   LEU A  19      34.953  25.430  41.598  1.00 28.69           N
ANISOU  148  N   LEU A  19     3281   3899   3721    541    226   -126       N
ATOM    149  CA  LEU A  19      35.363  24.164  42.196  1.00 28.16           C
ANISOU  149  CA  LEU A  19     4444   4108   2148   1197   -196   -568       C
ATOM    150  C   LEU A  19      35.750  24.517  43.689  1.00 28.48           C
ANISOU  150  C   LEU A  19     4548   3577   2694    -27   -543   -737       C
ATOM    151  O   LEU A  19      36.330  25.565  43.951  1.00 33.45           O
ANISOU  151  O   LEU A  19     4324   5040   3344   -124  -1212   -823       O
ATOM    152  CB  LEU A  19      36.561  23.511  41.440  1.00 30.83           C
ANISOU  152  CB  LEU A  19     4602   4119   2989    814   -277   -816       C
ATOM    153  CG  LEU A  19      36.291  23.120  39.979  1.00 27.37           C
ANISOU  153  CG  LEU A  19     3892   3776   2729      4   -233   -481       C
ATOM    154  CD1 LEU A  19      37.523  22.588  39.294  1.00 31.43           C
ANISOU  154  CD1 LEU A  19     3517   4939   3486    190   -296    -28       C
ATOM    155  CD2 LEU A  19      35.207  22.089  39.947  1.00 29.17           C
ANISOU  155  CD2 LEU A  19     3936   4101   3045   -162   -947   -693       C
ATOM    156  N   PRO A  20      35.463  23.630  44.629  1.00 28.75           N
ANISOU  156  N   PRO A  20     4115   4449   2358   -184   -395    171       N
ATOM    157  CA  PRO A  20      34.756  22.376  44.430  1.00 28.91           C
ANISOU  157  CA  PRO A  20     4645   4067   2273    514  -1290     37       C
ATOM    158  C   PRO A  20      33.291  22.691  44.049  1.00 26.55           C
ANISOU  158  C   PRO A  20     4391   3474   2223    455    -67    267       C
ATOM    159  O   PRO A  20      32.817  23.799  44.328  1.00 30.48           O
ANISOU  159  O   PRO A  20     5135   3929   2514    472   -233   -324       O
ATOM    160  CB  PRO A  20      34.861  21.703  45.854  1.00 30.59           C
ANISOU  160  CB  PRO A  20     5377   4521   1724    430    -50   -319       C
ATOM    161  CG  PRO A  20      34.803  22.886  46.808  1.00 37.12           C
ANISOU  161  CG  PRO A  20     5769   4996   3338    136   -430   -686       C
ATOM    162  CD  PRO A  20      35.662  23.927  46.109  1.00 35.75           C
ANISOU  162  CD  PRO A  20     5481   5625   2477     90   -211   -339       C
ATOM    163  N   PRO A  21      32.577  21.722  43.415  1.00 25.71           N
ANISOU  163  N   PRO A  21     3622   3735   2410    181   -489    206       N
ATOM    164  CA  PRO A  21      31.212  22.033  42.961  1.00 25.19           C
ANISOU  164  CA  PRO A  21     2723   4032   2813   -359    316   -497       C
ATOM    165  C   PRO A  21      30.246  22.311  44.159  1.00 23.68           C
ANISOU  165  C   PRO A  21     3049   3698   2249    444     94     17       C
ATOM    166  O   PRO A  21      29.226  23.013  43.962  1.00 28.87           O
ANISOU  166  O   PRO A  21     3768   4148   3052    491    378   -234       O
ATOM    167  CB  PRO A  21      30.778  20.746  42.222  1.00 28.78           C
ANISOU  167  CB  PRO A  21     3367   3813   3752    132    122   -894       C
ATOM    168  CG  PRO A  21      32.090  20.090  41.793  1.00 28.36           C
ANISOU  168  CG  PRO A  21     3677   4369   2726    789   -941   -262       C
ATOM    169  CD  PRO A  21      33.022  20.376  43.010  1.00 27.23           C
ANISOU  169  CD  PRO A  21     4150   3424   2770    244  -1003   -258       C
ATOM    170  N   SER A  22      30.613  21.892  45.408  1.00 29.20           N
ANISOU  170  N   SER A  22     4165   4621   2308    154    595      0       N
ATOM    171  CA  SER A  22      29.698  22.257  46.459  1.00 32.57           C
ANISOU  171  CA  SER A  22     4881   4703   2791    126   1197    727       C
ATOM    172  C   SER A  22      29.736  23.725  46.793  1.00 33.60           C
ANISOU  172  C   SER A  22     4307   4695   3762   -112    166    315       C
ATOM    173  O   SER A  22      28.883  24.216  47.546  1.00 43.28           O
ANISOU  173  O   SER A  22     5314   7439   3692   -271    861    208       O
ATOM    174  CB  SER A  22      30.092  21.502  47.706  1.00 35.37           C
ANISOU  174  CB  SER A  22     4535   6243   2659   -790    489    534       C
ATOM    175  OG  SER A  22      31.487  21.706  47.955  1.00 34.56           O
ANISOU  175  OG  SER A  22     5200   5544   2387    105   -490    198       O
ATOM    176  N   SER A  23      30.754  24.446  46.266  1.00 29.75           N
ANISOU  176  N   SER A  23     4162   4914   2224     19    -91     77       N
ATOM    177  CA  SER A  23      30.853  25.937  46.461  1.00 32.81           C
ANISOU  177  CA  SER A  23     4619   4656   3189    -22   1049    863       C
ATOM    178  C   SER A  23      29.973  26.677  45.455  1.00 29.72           C
ANISOU  178  C   SER A  23     4945   3784   2563   -480    807   -420       C
ATOM    179  O   SER A  23      29.886  27.911  45.479  1.00 32.78           O
ANISOU  179  O   SER A  23     4896   4368   3189     52    334   -455       O
ATOM    180  CB  SER A  23      32.292  26.372  46.499  1.00 39.34           C
ANISOU  180  CB  SER A  23     4196   4678   6072   -246   2404  -2253       C
ATOM    181  OG  SER A  23      32.789  26.233  45.124  1.00 49.06           O
ANISOU  181  OG  SER A  23     5452   5360   7828    -38    295    356       O
ATOM    182  N   ASP A  24      29.331  25.932  44.548  1.00 26.87           N
ANISOU  182  N   ASP A  24     3773   4495   1940     -4   -443   -330       N
ATOM    183  CA  ASP A  24      28.407  26.581  43.520  1.00 27.91           C
ANISOU  183  CA  ASP A  24     3113   5004   2487    -40   -116  -1112       C
ATOM    184  C   ASP A  24      27.010  26.410  44.126  1.00 24.15           C
ANISOU  184  C   ASP A  24     3638   3481   2055    -77    670   -516       C
ATOM    185  O   ASP A  24      26.495  25.279  44.215  1.00 32.06           O
ANISOU  185  O   ASP A  24     4001   4048   4130   -324    579   -287       O
ATOM    186  CB  ASP A  24      28.632  25.803  42.204  1.00 28.86           C
ANISOU  186  CB  ASP A  24     4783   3434   2748    555    251   -454       C
ATOM    187  CG  ASP A  24      27.697  26.200  41.080  1.00 32.50           C
ANISOU  187  CG  ASP A  24     4485   4684   3176    332    445   -235       C
ATOM    188  OD1 ASP A  24      26.671  26.872  41.317  1.00 32.26           O
ANISOU  188  OD1 ASP A  24     4156   4055   4046   -210    252    -16       O
ATOM    189  OD2 ASP A  24      27.962  25.809  39.848  1.00 31.25           O
ANISOU  189  OD2 ASP A  24     4175   4312   3386    171    871   -410       O
ATOM    190  N   PHE A  25      26.347  27.542  44.425  1.00 28.18           N
ANISOU  190  N   PHE A  25     3452   4113   3142    273    554  -1067       N
ATOM    191  CA  PHE A  25      25.004  27.549  45.172  1.00 27.24           C
ANISOU  191  CA  PHE A  25     3128   4175   3047     68    300  -1136       C
ATOM    192  C   PHE A  25      23.919  27.741  44.194  1.00 31.22           C
ANISOU  192  C   PHE A  25     3185   4888   3786    856    557  -1005       C
ATOM    193  O   PHE A  25      22.779  27.946  44.576  1.00 31.84           O
ANISOU  193  O   PHE A  25     3748   4976   3372   -121    135  -1068       O
ATOM    194  CB  PHE A  25      25.010  28.644  46.214  1.00 30.77           C
ANISOU  194  CB  PHE A  25     4720   4528   2442   -215    -87   -804       C
ATOM    195  CG  PHE A  25      26.182  28.527  47.215  1.00 31.66           C
ANISOU  195  CG  PHE A  25     4747   4983   2297   -174    -19   -243       C
ATOM    196  CD1 PHE A  25      26.460  27.331  47.892  1.00 39.96           C
ANISOU  196  CD1 PHE A  25     6064   5536   3581    729   -701   -442       C
ATOM    197  CD2 PHE A  25      26.953  29.667  47.531  1.00 35.35           C
ANISOU  197  CD2 PHE A  25     4372   5282   3778   -393   -265    126       C
ATOM    198  CE1 PHE A  25      27.513  27.278  48.895  1.00 42.96           C
ANISOU  198  CE1 PHE A  25     6169   5879   4273   -617  -1013   -894       C
ATOM    199  CE2 PHE A  25      28.017  29.628  48.451  1.00 36.05           C
ANISOU  199  CE2 PHE A  25     4367   5365   3964    466   -322     95       C
ATOM    200  CZ  PHE A  25      28.270  28.414  49.175  1.00 35.44           C
ANISOU  200  CZ  PHE A  25     4707   4999   3759    368    230   -172       C
ATOM    201  N   GLY A  26      24.230  27.563  42.922  1.00 30.26           N
ANISOU  201  N   GLY A  26     4368   4131   2998   -405    279  -1047       N
ATOM    202  CA  GLY A  26      23.206  27.793  41.839  1.00 29.80           C
ANISOU  202  CA  GLY A  26     3485   5040   2797   -547    120     77       C
ATOM    203  C   GLY A  26      22.789  29.269  41.682  1.00 28.84           C
ANISOU  203  C   GLY A  26     3421   5107   2427   -210   -314   -415       C
ATOM    204  O   GLY A  26      23.485  30.197  42.130  1.00 30.66           O
ANISOU  204  O   GLY A  26     3575   4746   3328   -383    261   -325       O
ATOM    205  N   LYS A  27      21.660  29.527  41.022  1.00 36.73           N
ANISOU  205  N   LYS A  27     3749   5733   4474    827  -1058  -1978       N
ATOM    206  CA  LYS A  27      21.327  30.914  40.686  1.00 31.87           C
ANISOU  206  CA  LYS A  27     4015   5372   2719    763   -485   -859       C
ATOM    207  C   LYS A  27      21.191  31.846  41.944  1.00 31.66           C
ANISOU  207  C   LYS A  27     4214   4501   3312    167    177   -956       C
ATOM    208  O   LYS A  27      21.539  33.002  41.861  1.00 33.11           O
ANISOU  208  O   LYS A  27     4723   4832   3025    804    546   -518       O
ATOM    209  CB  LYS A  27      20.084  31.042  39.819  1.00 37.60           C
ANISOU  209  CB  LYS A  27     4243   6466   3575   1233  -1181  -1221       C
ATOM    210  CG  LYS A  27      19.863  32.529  39.242  1.00 50.76           C
ANISOU  210  CG  LYS A  27     6414   6658   6213   1868   -361  -2817       C
ATOM    211  CD  LYS A  27      18.581  32.755  38.355  1.00 67.15           C
ANISOU  211  CD  LYS A  27     5020   5673  14820   -287   -651   4825       C
ATOM    212  CE  LYS A  27      18.369  34.217  37.977  1.00 62.44           C
ANISOU  212  CE  LYS A  27    11590   5131   7002  -2070   5173   -659       C
ATOM    213  NZ  LYS A  27      17.834  34.922  39.228  1.00 61.86           N
ANISOU  213  NZ  LYS A  27     3212   9962  10329  -2170   3715  -4506       N
ATOM    214  N   MET A  28      20.671  31.350  43.060  1.00 34.78           N
ANISOU  214  N   MET A  28     4187   5786   3241     23     30   -806       N
ATOM    215  CA  MET A  28      20.352  32.230  44.213  1.00 32.44           C
ANISOU  215  CA  MET A  28     4236   4646   3441    196     87  -1299       C
ATOM    216  C   MET A  28      19.597  33.435  43.677  1.00 32.83           C
ANISOU  216  C   MET A  28     4029   5730   2714   -510    510   -753       C
ATOM    217  O   MET A  28      18.621  33.244  42.963  1.00 37.44           O
ANISOU  217  O   MET A  28     3682   6637   3906    719   -403  -1558       O
ATOM    218  CB  MET A  28      21.631  32.569  45.087  1.00 29.53           C
ANISOU  218  CB  MET A  28     3248   4892   3078    391   -219   -295       C
ATOM    219  CG  MET A  28      22.419  31.334  45.616  1.00 32.34           C
ANISOU  219  CG  MET A  28     3146   4351   4788    249   1593    667       C
ATOM    220  SD  MET A  28      21.348  30.424  46.741  1.00 39.94           S
ANISOU  220  SD  MET A  28     5202   5776   4195    -27    732   -301       S
ATOM    221  CE  MET A  28      21.001  31.625  48.066  1.00 39.29           C
ANISOU  221  CE  MET A  28     4708   5653   4564    819   1391  -1497       C
ATOM    222  N   ASP A  29      19.978  34.658  44.064  1.00 34.87           N
ANISOU  222  N   ASP A  29     4772   4868   3607    -32   1049   -138       N
ATOM    223  CA  ASP A  29      19.353  35.839  43.561  1.00 40.25           C
ANISOU  223  CA  ASP A  29     4913   5179   5201    656   1224   -611       C
ATOM    224  C   ASP A  29      20.299  36.631  42.655  1.00 33.84           C
ANISOU  224  C   ASP A  29     4839   4139   3878    680    856   -789       C
ATOM    225  O   ASP A  29      20.166  37.880  42.500  1.00 35.01           O
ANISOU  225  O   ASP A  29     4610   4257   4434    995   1102   -237       O
ATOM    226  CB  ASP A  29      18.862  36.695  44.699  1.00 37.25           C
ANISOU  226  CB  ASP A  29     3834   5219   5099    781    469  -1013       C
ATOM    227  CG  ASP A  29      19.936  37.051  45.713  1.00 41.30           C
ANISOU  227  CG  ASP A  29     4760   6420   4511   1085    182  -1037       C
ATOM    228  OD1 ASP A  29      21.041  36.519  45.714  1.00 34.87           O
ANISOU  228  OD1 ASP A  29     4278   4720   4249    392    934   -338       O
ATOM    229  OD2 ASP A  29      19.655  37.927  46.600  1.00 41.36           O
ANISOU  229  OD2 ASP A  29     6097   5134   4481   -283   1029   -296       O
ATOM    230  N   CYS A  30      21.253  35.925  42.058  1.00 34.07           N
ANISOU  230  N   CYS A  30     4340   5204   3401    516   1452     59       N
ATOM    231  CA  CYS A  30      22.038  36.567  40.976  1.00 32.82           C
ANISOU  231  CA  CYS A  30     3457   4753   4257    488   1078    588       C
ATOM    232  C   CYS A  30      21.148  36.832  39.770  1.00 37.97           C
ANISOU  232  C   CYS A  30     4911   5344   4171    -78    675    441       C
ATOM    233  O   CYS A  30      20.031  36.258  39.618  1.00 36.29           O
ANISOU  233  O   CYS A  30     4113   5087   4588    982    985    694       O
ATOM    234  CB  CYS A  30      23.163  35.645  40.522  1.00 34.14           C
ANISOU  234  CB  CYS A  30     3540   4901   4532   1144    164    104       C
ATOM    235  SG  CYS A  30      24.316  35.214  41.859  1.00 35.27           S
ANISOU  235  SG  CYS A  30     4714   4864   3823    558    705   -169       S
ATOM    236  N   ARG A  31      21.632  37.651  38.858  1.00 33.17           N
ANISOU  236  N   ARG A  31     4456   4064   4083    441     38    138       N
ATOM    237  CA  ARG A  31      20.859  37.915  37.629  1.00 30.62           C
ANISOU  237  CA  ARG A  31     3494   4862   3276   -207   -297    325       C
ATOM    238  C   ARG A  31      20.707  36.690  36.742  1.00 35.27           C
ANISOU  238  C   ARG A  31     4999   3770   4629    449   -754   1059       C
ATOM    239  O   ARG A  31      21.414  35.717  36.871  1.00 32.90           O
ANISOU  239  O   ARG A  31     4204   4115   4181    585    224    255       O
ATOM    240  CB  ARG A  31      21.465  39.043  36.810  1.00 35.70           C
ANISOU  240  CB  ARG A  31     4862   4298   4402   -609     83     59       C
ATOM    241  CG  ARG A  31      21.196  40.408  37.318  1.00 43.93           C
ANISOU  241  CG  ARG A  31     5854   5347   5490    143   -880   -898       C
ATOM    242  CD  ARG A  31      22.438  41.240  37.175  1.00 61.51           C
ANISOU  242  CD  ARG A  31     7859   7971   7541  -2079   -838  -1352       C
ATOM    243  NE  ARG A  31      22.813  41.426  35.807  1.00 59.75           N
ANISOU  243  NE  ARG A  31     7529   6426   8746  -1205   -288   2136       N
ATOM    244  CZ  ARG A  31      24.061  41.610  35.356  1.00 87.97           C
ANISOU  244  CZ  ARG A  31     5764  12438  15220   -279  -4814   -306       C
ATOM    245  NH1 ARG A  31      25.092  41.636  36.192  1.00 53.60           N
ANISOU  245  NH1 ARG A  31     8614   4875   6874    997  -3286   -261       N
ATOM    246  NH2 ARG A  31      24.286  41.759  34.042  1.00103.81           N
ANISOU  246  NH2 ARG A  31    14859   7236  17348    922  -1123   4652       N
ATOM    247  N   TRP A  32      19.786  36.761  35.803  1.00 29.99           N
ANISOU  247  N   TRP A  32     3451   4619   3323    842    150    597       N
ATOM    248  CA  TRP A  32      19.607  35.746  34.817  1.00 35.04           C
ANISOU  248  CA  TRP A  32     3939   5205   4169    703    433   -652       C
ATOM    249  C   TRP A  32      20.923  35.499  34.143  1.00 28.56           C
ANISOU  249  C   TRP A  32     3740   3204   3908    292    262    -87       C
ATOM    250  O   TRP A  32      21.601  36.446  33.802  1.00 32.06           O
ANISOU  250  O   TRP A  32     3743   3989   4447     79    323     61       O
ATOM    251  CB  TRP A  32      18.563  36.198  33.811  1.00 31.20           C
ANISOU  251  CB  TRP A  32     4077   4691   3084    350    379   -479       C
ATOM    252  CG  TRP A  32      18.236  35.194  32.756  1.00 34.56           C
ANISOU  252  CG  TRP A  32     4206   4630   4294    273  -1157    -21       C
ATOM    253  CD1 TRP A  32      18.609  35.208  31.430  1.00 41.54           C
ANISOU  253  CD1 TRP A  32     4625   6478   4677    286     23     84       C
ATOM    254  CD2 TRP A  32      17.449  33.989  32.904  1.00 35.16           C
ANISOU  254  CD2 TRP A  32     4294   4608   4455    191     86    431       C
ATOM    255  NE1 TRP A  32      18.128  34.130  30.777  1.00 35.76           N
ANISOU  255  NE1 TRP A  32     4514   5529   3543   -121    316    128       N
ATOM    256  CE2 TRP A  32      17.430  33.356  31.599  1.00 43.39           C
ANISOU  256  CE2 TRP A  32     5094   6506   4884   -787   1357   -357       C
ATOM    257  CE3 TRP A  32      16.785  33.390  33.947  1.00 38.51           C
ANISOU  257  CE3 TRP A  32     5133   4680   4819   -569   1150   -350       C
ATOM    258  CZ2 TRP A  32      16.766  32.186  31.376  1.00 47.64           C
ANISOU  258  CZ2 TRP A  32     6487   5881   5732   -412    755   -478       C
ATOM    259  CZ3 TRP A  32      16.126  32.209  33.710  1.00 40.13           C
ANISOU  259  CZ3 TRP A  32     4408   5920   4918  -1219   1708   -765       C
ATOM    260  CH2 TRP A  32      16.117  31.619  32.454  1.00 47.20           C
ANISOU  260  CH2 TRP A  32     5452   6594   5886   -370   1795  -1615       C
ATOM    261  N   ARG A  33      21.290  34.244  33.983  1.00 30.43           N
ANISOU  261  N   ARG A  33     4070   4056   3435    853    353    -46       N
ATOM    262  CA  ARG A  33      22.535  33.856  33.352  1.00 27.90           C
ANISOU  262  CA  ARG A  33     3038   4827   2734    427   -820    697       C
ATOM    263  C   ARG A  33      23.758  34.041  34.235  1.00 26.61           C
ANISOU  263  C   ARG A  33     3113   4073   2923    459   -375   -327       C
ATOM    264  O   ARG A  33      24.871  34.001  33.773  1.00 30.40           O
ANISOU  264  O   ARG A  33     4144   4414   2991    366    799    234       O
ATOM    265  CB  ARG A  33      22.741  34.558  32.005  1.00 30.49           C
ANISOU  265  CB  ARG A  33     4781   4762   2040    792    614    377       C
ATOM    266  CG  ARG A  33      23.371  33.668  30.979  1.00 33.24           C
ANISOU  266  CG  ARG A  33     4557   5530   2542    106   1069    301       C
ATOM    267  CD  ARG A  33      23.498  34.343  29.627  1.00 44.19           C
ANISOU  267  CD  ARG A  33     5497   6483   4807    373    187   1380       C
ATOM    268  NE  ARG A  33      22.226  34.602  28.995  1.00 38.66           N
ANISOU  268  NE  ARG A  33     4749   5413   4526   1137    305    541       N
ATOM    269  CZ  ARG A  33      21.652  35.782  28.973  1.00 34.93           C
ANISOU  269  CZ  ARG A  33     4922   4863   3486   1000    913   1262       C
ATOM    270  NH1 ARG A  33      22.236  36.792  29.544  1.00 43.29           N
ANISOU  270  NH1 ARG A  33     5053   5590   5803    173     85   1004       N
ATOM    271  NH2 ARG A  33      20.490  35.938  28.392  1.00 46.67           N
ANISOU  271  NH2 ARG A  33     4806   7732   5192   2065   -219   1418       N
ATOM    272  N   TRP A  34      23.525  34.226  35.519  1.00 32.53           N
ANISOU  272  N   TRP A  34     4724   4332   3301    315    162    -16       N
ATOM    273  CA  TRP A  34      24.573  34.253  36.496  1.00 27.58           C
ANISOU  273  CA  TRP A  34     3721   3123   3633    220    161    418       C
ATOM    274  C   TRP A  34      24.279  33.242  37.566  1.00 25.40           C
ANISOU  274  C   TRP A  34     2629   3273   3747   -229    291    448       C
ATOM    275  O   TRP A  34      23.183  32.748  37.669  1.00 28.51           O
ANISOU  275  O   TRP A  34     3163   4259   3408   -281    192    438       O
ATOM    276  CB  TRP A  34      24.724  35.642  37.108  1.00 28.74           C
ANISOU  276  CB  TRP A  34     3615   3047   4259   -495    102    224       C
ATOM    277  CG  TRP A  34      25.159  36.680  36.136  1.00 29.83           C
ANISOU  277  CG  TRP A  34     3320   4028   3985    125    229   -130       C
ATOM    278  CD1 TRP A  34      24.446  37.197  35.092  1.00 30.48           C
ANISOU  278  CD1 TRP A  34     4453   3766   3362    507    655    216       C
ATOM    279  CD2 TRP A  34      26.436  37.346  36.070  1.00 30.97           C
ANISOU  279  CD2 TRP A  34     3672   4560   3535   -388    283   -831       C
ATOM    280  NE1 TRP A  34      25.160  38.106  34.425  1.00 32.82           N
ANISOU  280  NE1 TRP A  34     4024   4401   4044   -557    533    366       N
ATOM    281  CE2 TRP A  34      26.360  38.238  34.943  1.00 32.72           C
ANISOU  281  CE2 TRP A  34     4094   3706   4629   -251   -206   -542       C
ATOM    282  CE3 TRP A  34      27.592  37.289  36.795  1.00 29.00           C
ANISOU  282  CE3 TRP A  34     3291   3466   4262   -353    188   -171       C
ATOM    283  CZ2 TRP A  34      27.405  39.022  34.573  1.00 32.14           C
ANISOU  283  CZ2 TRP A  34     4561   4059   3589     -5    657   -288       C
ATOM    284  CZ3 TRP A  34      28.642  38.103  36.417  1.00 32.58           C
ANISOU  284  CZ3 TRP A  34     4409   3718   4250   -563    764    -28       C
ATOM    285  CH2 TRP A  34      28.546  38.942  35.331  1.00 32.73           C
ANISOU  285  CH2 TRP A  34     5085   3759   3591   -144    371   -145       C
ATOM    286  N   LYS A  35      25.273  32.932  38.366  1.00 29.36           N
ANISOU  286  N   LYS A  35     3932   3861   3362    689   -125    495       N
ATOM    287  CA  LYS A  35      25.115  31.988  39.482  1.00 31.35           C
ANISOU  287  CA  LYS A  35     4356   3709   3846   -135   -729    294       C
ATOM    288  C   LYS A  35      26.046  32.393  40.608  1.00 25.86           C
ANISOU  288  C   LYS A  35     3940   3096   2788    -44    379    -18       C
ATOM    289  O   LYS A  35      27.024  33.145  40.435  1.00 30.66           O
ANISOU  289  O   LYS A  35     4468   3551   3628   -311    937   -381       O
ATOM    290  CB  LYS A  35      25.387  30.534  39.048  1.00 26.30           C
ANISOU  290  CB  LYS A  35     3945   3381   2667   -110    318     55       C
ATOM    291  CG  LYS A  35      26.871  30.297  38.601  1.00 27.24           C
ANISOU  291  CG  LYS A  35     3388   3653   3307    360    525     40       C
ATOM    292  CD  LYS A  35      27.178  28.846  38.350  1.00 29.26           C
ANISOU  292  CD  LYS A  35     3499   4077   3539    433    877    250       C
ATOM    293  CE  LYS A  35      28.609  28.696  37.826  1.00 26.92           C
ANISOU  293  CE  LYS A  35     3433   3775   3018    479    230   -349       C
ATOM    294  NZ  LYS A  35      28.947  27.245  37.651  1.00 26.80           N
ANISOU  294  NZ  LYS A  35     3515   3537   3130     90    109   -327       N
ATOM    295  N   CYS A  36      25.712  31.909  41.794  1.00 26.98           N
ANISOU  295  N   CYS A  36     3938   4167   2144     56     56   -124       N
ATOM    296  CA  CYS A  36      26.403  32.315  43.066  1.00 26.70           C
ANISOU  296  CA  CYS A  36     3827   4387   1930    437    766   -546       C
ATOM    297  C   CYS A  36      27.416  31.214  43.391  1.00 24.99           C
ANISOU  297  C   CYS A  36     3073   3548   2874   -166    176   -964       C
ATOM    298  O   CYS A  36      27.045  30.004  43.596  1.00 29.97           O
ANISOU  298  O   CYS A  36     4602   3845   2938    179    282    -71       O
ATOM    299  CB  CYS A  36      25.280  32.402  44.168  1.00 27.09           C
ANISOU  299  CB  CYS A  36     2989   4768   2535    -96    510   -452       C
ATOM    300  SG  CYS A  36      26.051  32.900  45.709  1.00 34.74           S
ANISOU  300  SG  CYS A  36     4724   5367   3106     44    214   -748       S
ATOM    301  N   CYS A  37      28.727  31.586  43.510  1.00 25.71           N
ANISOU  301  N   CYS A  37     3133   3960   2674    -98    214   -942       N
ATOM    302  CA  CYS A  37      29.757  30.613  43.926  1.00 28.33           C
ANISOU  302  CA  CYS A  37     3355   4489   2919    311   -205   -823       C
ATOM    303  C   CYS A  37      30.466  31.245  45.108  1.00 31.03           C
ANISOU  303  C   CYS A  37     4507   3823   3461   -286    -31   -645       C
ATOM    304  O   CYS A  37      30.678  32.503  45.171  1.00 32.26           O
ANISOU  304  O   CYS A  37     4453   4556   3246   -643   -125   -781       O
ATOM    305  CB  CYS A  37      30.788  30.376  42.856  1.00 27.72           C
ANISOU  305  CB  CYS A  37     3550   3766   3213   -248     12   -701       C
ATOM    306  SG  CYS A  37      30.010  29.569  41.441  1.00 31.23           S
ANISOU  306  SG  CYS A  37     3864   4976   3023    369     24   -855       S
ATOM    307  N   LYS A  38      30.877  30.368  46.042  1.00 31.84           N
ANISOU  307  N   LYS A  38     4065   5204   2826     56   -321  -1079       N
ATOM    308  CA  LYS A  38      31.503  30.837  47.245  1.00 41.75           C
ANISOU  308  CA  LYS A  38     5655   6294   3912    153  -1743   -977       C
ATOM    309  C   LYS A  38      32.777  31.539  46.860  1.00 54.07           C
ANISOU  309  C   LYS A  38     6533   8731   5277  -1160   -864  -1305       C
ATOM    310  O   LYS A  38      33.537  31.020  46.039  1.00 51.47           O
ANISOU  310  O   LYS A  38     5649   8768   5139   -149  -1014  -2411       O
ATOM    311  CB  LYS A  38      31.777  29.652  48.227  1.00 35.15           C
ANISOU  311  CB  LYS A  38     4870   5967   2516   -201    164   -755       C
ATOM    312  CG  LYS A  38      32.204  30.176  49.572  1.00 46.27           C
ANISOU  312  CG  LYS A  38     8966   5667   2948   -167  -1533   -606       C
ATOM    313  CD  LYS A  38      32.044  29.080  50.546  1.00 55.16           C
ANISOU  313  CD  LYS A  38     8150  10691   2117   -632  -1123   1594       C
ATOM    314  CE  LYS A  38      32.197  29.672  51.994  1.00 74.58           C
ANISOU  314  CE  LYS A  38    12603  11866   3865  -1128    198    504       C
ATOM    315  NZ  LYS A  38      32.194  28.546  52.930  1.00 77.08           N
ANISOU  315  NZ  LYS A  38    13981   9943   5360   -384   -270   1135       N
ATOM    316  N   LYS A  39      33.006  32.703  47.487  1.00 61.07           N
ANISOU  316  N   LYS A  39     7681   7341   8180   -760  -3625    165       N
ATOM    317  CA  LYS A  39      34.265  33.456  47.412  1.00 65.62           C
ANISOU  317  CA  LYS A  39     8428   9271   7231  -2047  -2598  -3239       C
ATOM    318  C   LYS A  39      35.498  32.512  47.522  1.00 71.53           C
ANISOU  318  C   LYS A  39     7199  11911   8068   -577    743   1225       C
ATOM    319  O   LYS A  39      35.579  31.671  48.441  1.00 75.35           O
ANISOU  319  O   LYS A  39    13936  10757   3937   -128  -2607  -1310       O
ATOM    320  CB  LYS A  39      34.272  34.525  48.495  1.00 68.88           C
ANISOU  320  CB  LYS A  39    10983   6184   9002  -1563   2869  -3216       C
ATOM    321  CG  LYS A  39      33.466  35.758  48.131  1.00102.97           C
ANISOU  321  CG  LYS A  39    11741   9807  17572   1346   3970  -1130       C
ATOM    322  CD  LYS A  39      33.905  37.046  48.852  1.00 94.23           C
ANISOU  322  CD  LYS A  39    11515  11033  13252  -2164   7236  -1449       C
ATOM    323  CE  LYS A  39      32.782  38.077  48.838  1.00 97.93           C
ANISOU  323  CE  LYS A  39    13910   6725  16573  -1571   4265  -4939       C
ATOM    324  NZ  LYS A  39      32.137  38.304  47.500  1.00120.68           N
ANISOU  324  NZ  LYS A  39     3043  14906  27904  -1538    464   8037       N
ATOM    325  N   GLY A  40      36.419  32.649  46.557  1.00 74.62           N
ANISOU  325  N   GLY A  40     8370  12915   7065   -368   2072  -4565       N
ATOM    326  CA  GLY A  40      37.575  31.740  46.370  1.00 63.68           C
ANISOU  326  CA  GLY A  40     7899   9215   7079   -734   -867   -894       C
ATOM    327  C   GLY A  40      37.343  30.554  45.399  1.00118.78           C
ANISOU  327  C   GLY A  40    20484   9807  14841   2762   1032  -4159       C
ATOM    328  O   GLY A  40      38.084  29.556  45.492  1.00 93.93           O
ANISOU  328  O   GLY A  40    12769   8163  14755  -3003  -5138   4627       O
ATOM    329  N   SER A  41      36.353  30.656  44.477  1.00113.51           N
ANISOU  329  N   SER A  41    16288   6097  20744  -1466   1417  -4899       N
ATOM    330  CA  SER A  41      35.838  29.525  43.657  1.00 84.04           C
ANISOU  330  CA  SER A  41     8115  11028  12786   2108   2310  -5960       C
ATOM    331  C   SER A  41      36.352  29.358  42.248  1.00 98.00           C
ANISOU  331  C   SER A  41    17099  13583   6550  -5880   1782  -3611       C
ATOM    332  O   SER A  41      36.486  30.378  41.554  1.00 97.25           O
ANISOU  332  O   SER A  41    18547   7086  11316  -1866    213  -1285       O
ATOM    333  CB  SER A  41      34.321  29.562  43.556  1.00 77.71           C
ANISOU  333  CB  SER A  41     8239  10976  10309  -4612  -3125   1382       C
ATOM    334  OG  SER A  41      33.805  28.617  44.426  1.00 57.24           O
ANISOU  334  OG  SER A  41     6830   7445   7475  -2048   -410    735       O
ATOM    335  N   GLY A  42      36.520  28.064  41.836  1.00 77.95           N
ANISOU  335  N   GLY A  42     9329  11087   9200  -5044   1875    957       N
ATOM    336  CA  GLY A  42      37.230  27.538  40.578  1.00 40.16           C
ANISOU  336  CA  GLY A  42     4993   6071   4194   -486  -1369   1192       C
ATOM    337  C   GLY A  42      38.752  27.782  40.768  1.00 86.71           C
ANISOU  337  C   GLY A  42     5684  12664  14596    701   1185  -1744       C
ATOM    338  O   GLY A  42      39.600  26.870  40.826  1.00 65.58           O
ANISOU  338  O   GLY A  42     6600  11041   7273     84    487  -1703       O
TER     339      GLY A  42
HETATM  340  O   HOH A 201      15.588  39.140  44.473  1.00 38.59           O
ANISOU  340  O   HOH A 201     3898   4857   5907   -622    271   -326       O
HETATM  341  O   HOH A 202      24.922  25.994  39.405  1.00 34.65           O
ANISOU  341  O   HOH A 202     4093   6634   2438   -455   -710   -683       O
HETATM  342  O   HOH A 203      21.005  33.143  51.282  1.00 45.62           O
ANISOU  342  O   HOH A 203     6024   6584   4723   -715   1173  -1045       O
HETATM  343  O   HOH A 205      24.714  37.501  30.725  1.00 39.43           O
ANISOU  343  O   HOH A 205     5397   5743   3840    176    924    670       O
HETATM  344  O   HOH A 207      19.998  31.757  34.653  1.00 41.15           O
ANISOU  344  O   HOH A 207     6211   4398   5024   -888    291    939       O
HETATM  345  O   HOH A 208      28.221  25.644  35.347  1.00 31.59           O
ANISOU  345  O   HOH A 208     4438   5036   2528   -709   -282    -10       O
HETATM  346  O   HOH A 209      20.248  28.595  43.911  1.00 43.84           O
ANISOU  346  O   HOH A 209     6129   5556   4971   -530   1116  -1181       O
HETATM  347  O   HOH A 210      22.323  30.872  35.787  1.00 43.01           O
ANISOU  347  O   HOH A 210     5103   5577   5660     -7   -542   -305       O
HETATM  348  O   HOH A 211      25.274  26.507  35.440  1.00 36.19           O
ANISOU  348  O   HOH A 211     4408   4924   4419   -226    567    755       O
HETATM  349  O   HOH A 212      23.052  28.004  36.687  1.00 45.34           O
ANISOU  349  O   HOH A 212     6139   5362   5725   -283   1415   -232       O
HETATM  350  O   HOH A 213      21.932  26.735  46.908  1.00 49.79           O
ANISOU  350  O   HOH A 213     6746   7339   4830  -1465   2010    689       O
HETATM  351  O   HOH A 214      24.316  38.617  38.881  1.00 34.93           O
ANISOU  351  O   HOH A 214     4527   4871   3870    531    268    233       O
HETATM  352  O   HOH A 215      17.238  39.118  46.800  1.00 45.64           O
ANISOU  352  O   HOH A 215     5530   5652   6157    564    606  -1828       O
HETATM  353  O   HOH A 216      31.998  19.078  45.942  1.00 42.50           O
ANISOU  353  O   HOH A 216     7040   5227   3878    277   1717    881       O
HETATM  354  O   HOH A 217      38.652  33.069  38.370  1.00 52.70           O
ANISOU  354  O   HOH A 217     7714   7880   4428     72    -49   -433       O
HETATM  355  O   HOH A 218      28.062  28.919  52.721  1.00 65.74           O
ANISOU  355  O   HOH A 218    10995   8863   5119    399     22   -541       O
HETATM  356  O   HOH A 219      27.907  39.552  43.400  1.00 47.12           O
ANISOU  356  O   HOH A 219     6091   6126   5686   1454   -151  -1939       O
HETATM  357  O   HOH A 220      26.409  38.723  45.658  1.00 39.44           O
ANISOU  357  O   HOH A 220     5661   4714   4607    286    286   -450       O
HETATM  358  O   HOH A 221      31.913  24.195  49.670  1.00 43.35           O
ANISOU  358  O   HOH A 221     5540   5714   5214   -123   -258    360       O
CONECT   36   35  300
CONECT   88   87  235
CONECT  147  146  306
CONECT  235   88  234
CONECT  300   36  299
CONECT  306  147  305
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.