CNRS Nantes University UFIP UFIP
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***  PROTEIN BINDING 23-JAN-01 1HZ6  ***

elNémo ID: 19010321093043919

Job options:

ID        	=	 19010321093043919
JOBID     	=	 PROTEIN BINDING 23-JAN-01 1HZ6
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    PROTEIN BINDING                         23-JAN-01   1HZ6              
TITLE     CRYSTAL STRUCTURES OF THE B1 DOMAIN OF PROTEIN L FROM                 
TITLE    2 PEPTOSTREPTOCOCCUS MAGNUS WITH A TYROSINE TO TRYPTOPHAN SUBSTITUTION 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN L;                                                 
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: B1 DOMAIN;                                                 
COMPND   5 SYNONYM: IG KAPPA LIGHT CHAIN-BINDING PROTEIN;                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: FINEGOLDIA MAGNA;                               
SOURCE   3 ORGANISM_TAXID: 334413;                                              
SOURCE   4 STRAIN: ATCC 29328;                                                  
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET3A                                     
KEYWDS    FOUR STRANDED BETA-SHEET WITH CENTRAL ALPHA HELIX, BINDS KAPPA LIGHT  
KEYWDS   2 CHAIN OF IMMUNOGLOBULINS, PROTEIN BINDING                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.W.O'NEILL,D.E.KIM,D.BAKER,K.Y.J.ZHANG                               
REVDAT   4   13-JUL-11 1HZ6    1       VERSN                                    
REVDAT   3   24-FEB-09 1HZ6    1       VERSN                                    
REVDAT   2   01-APR-03 1HZ6    1       JRNL                                     
REVDAT   1   04-APR-01 1HZ6    0                                                
JRNL        AUTH   J.W.O'NEILL,D.E.KIM,D.BAKER,K.Y.ZHANG                        
JRNL        TITL   STRUCTURES OF THE B1 DOMAIN OF PROTEIN L FROM                
JRNL        TITL 2 PEPTOSTREPTOCOCCUS MAGNUS WITH A TYROSINE TO TRYPTOPHAN      
JRNL        TITL 3 SUBSTITUTION.                                                
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  57   480 2001              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   11264576                                                     
JRNL        DOI    10.1107/S0907444901000373                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
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) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 923930.080                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 28825                          
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 SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1471                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.76                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4360                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2930                       
REMARK   3   BIN FREE R VALUE                    : 0.3230                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 141                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1488                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 299                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.55000                                              
REMARK   3    B22 (A**2) : 1.10000                                              
REMARK   3    B33 (A**2) : -1.65000                                             
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.19                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.10                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.21                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.14                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.22                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.68                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.670 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.480 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.870 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.280 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 51.29                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1HZ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB012705.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-OCT-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28825                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 4.940                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200   FOR THE DATA SET  : 17.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.25200                            
REMARK 200   FOR SHELL         : 6.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: EPMR                                                  
REMARK 200 STARTING MODEL: C3 DOMAIN OF PROTEIN L (UNPUBLISHED: T. WAN AND B.   
REMARK 200  SUTTON)                                                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30%PEG 8000, 0.2M AMMONIUM SULFATE, PH   
REMARK 280  5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.80550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.53450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       27.01000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.53450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.80550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       27.01000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7040 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     MET B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     MET C    -7                                                      
REMARK 465     HIS C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     HIS C    -2                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     ALA C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A  -2    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1HZ5   RELATED DB: PDB                                   
REMARK 900 1HZ5 IS PROTEIN L B1 DOMAIN (Y47W) WITH ZINC COORDINATED N-          
REMARK 900 TERMINAL 6X HISTIDINE-TAG.                                           
REMARK 900 RELATED ID: 2PTL   RELATED DB: PDB                                   
REMARK 900 NMR DERIVED B1 DOMAIN OF PROTEIN L                                   
DBREF  1HZ6 A    2    64  UNP    Q51912   Q51912_PEPMA   111    173             
DBREF  1HZ6 B    2    64  UNP    Q51912   Q51912_PEPMA   111    173             
DBREF  1HZ6 C    2    64  UNP    Q51912   Q51912_PEPMA   111    173             
SEQADV 1HZ6 MET A   -7  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS A   -6  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS A   -5  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS A   -4  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS A   -3  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS A   -2  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS A   -1  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 ALA A    0  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 MET A    1  UNP  Q51912              CLONING ARTIFACT               
SEQADV 1HZ6 TRP A   47  UNP  Q51912    TYR   156 ENGINEERED                     
SEQADV 1HZ6 MET B   -7  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS B   -6  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS B   -5  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS B   -4  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS B   -3  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS B   -2  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS B   -1  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 ALA B    0  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 MET B    1  UNP  Q51912              CLONING ARTIFACT               
SEQADV 1HZ6 TRP B   47  UNP  Q51912    TYR   156 ENGINEERED                     
SEQADV 1HZ6 MET C   -7  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS C   -6  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS C   -5  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS C   -4  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS C   -3  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS C   -2  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 HIS C   -1  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 ALA C    0  UNP  Q51912              EXPRESSION TAG                 
SEQADV 1HZ6 MET C    1  UNP  Q51912              CLONING ARTIFACT               
SEQADV 1HZ6 TRP C   47  UNP  Q51912    TYR   156 ENGINEERED                     
SEQRES   1 A   72  MET HIS HIS HIS HIS HIS HIS ALA MET GLU GLU VAL THR          
SEQRES   2 A   72  ILE LYS ALA ASN LEU ILE PHE ALA ASN GLY SER THR GLN          
SEQRES   3 A   72  THR ALA GLU PHE LYS GLY THR PHE GLU LYS ALA THR SER          
SEQRES   4 A   72  GLU ALA TYR ALA TYR ALA ASP THR LEU LYS LYS ASP ASN          
SEQRES   5 A   72  GLY GLU TRP THR VAL ASP VAL ALA ASP LYS GLY TYR THR          
SEQRES   6 A   72  LEU ASN ILE LYS PHE ALA GLY                                  
SEQRES   1 B   72  MET HIS HIS HIS HIS HIS HIS ALA MET GLU GLU VAL THR          
SEQRES   2 B   72  ILE LYS ALA ASN LEU ILE PHE ALA ASN GLY SER THR GLN          
SEQRES   3 B   72  THR ALA GLU PHE LYS GLY THR PHE GLU LYS ALA THR SER          
SEQRES   4 B   72  GLU ALA TYR ALA TYR ALA ASP THR LEU LYS LYS ASP ASN          
SEQRES   5 B   72  GLY GLU TRP THR VAL ASP VAL ALA ASP LYS GLY TYR THR          
SEQRES   6 B   72  LEU ASN ILE LYS PHE ALA GLY                                  
SEQRES   1 C   72  MET HIS HIS HIS HIS HIS HIS ALA MET GLU GLU VAL THR          
SEQRES   2 C   72  ILE LYS ALA ASN LEU ILE PHE ALA ASN GLY SER THR GLN          
SEQRES   3 C   72  THR ALA GLU PHE LYS GLY THR PHE GLU LYS ALA THR SER          
SEQRES   4 C   72  GLU ALA TYR ALA TYR ALA ASP THR LEU LYS LYS ASP ASN          
SEQRES   5 C   72  GLY GLU TRP THR VAL ASP VAL ALA ASP LYS GLY TYR THR          
SEQRES   6 C   72  LEU ASN ILE LYS PHE ALA GLY                                  
HELIX    1   1 THR A   25  LEU A   40  1                                  16    
HELIX    2   2 LEU A   40  GLY A   45  1                                   6    
HELIX    3   3 ASP A   53  GLY A   55  5                                   3    
HELIX    4   4 THR B   25  LEU B   40  1                                  16    
HELIX    5   5 LEU B   40  GLY B   45  1                                   6    
HELIX    6   6 ASP B   53  GLY B   55  5                                   3    
HELIX    7   7 THR C   25  LEU C   40  1                                  16    
HELIX    8   8 LEU C   40  GLY C   45  1                                   6    
HELIX    9   9 ASP C   53  GLY C   55  5                                   3    
SHEET    1   A 4 THR A  17  GLY A  24  0                                        
SHEET    2   A 4 VAL A   4  ILE A  11 -1  N  VAL A   4   O  GLY A  24           
SHEET    3   A 4 THR A  57  PHE A  62  1  N  LEU A  58   O  LYS A   7           
SHEET    4   A 4 TRP A  47  ALA A  52 -1  O  THR A  48   N  LYS A  61           
SHEET    1   B 4 THR B  17  GLY B  24  0                                        
SHEET    2   B 4 VAL B   4  ILE B  11 -1  N  VAL B   4   O  GLY B  24           
SHEET    3   B 4 THR B  57  PHE B  62  1  N  LEU B  58   O  LYS B   7           
SHEET    4   B 4 TRP B  47  ALA B  52 -1  O  THR B  48   N  LYS B  61           
SHEET    1   C 4 THR C  17  GLY C  24  0                                        
SHEET    2   C 4 VAL C   4  ILE C  11 -1  N  VAL C   4   O  GLY C  24           
SHEET    3   C 4 THR C  57  PHE C  62  1  N  LEU C  58   O  LYS C   7           
SHEET    4   C 4 TRP C  47  ALA C  52 -1  O  THR C  48   N  LYS C  61           
CRYST1   51.611   54.020   95.069  90.00  90.00  90.00 P 21 21 21   12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019376  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018512  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010519        0.00000                          
ATOM     15  N   ALA A   0       7.059  -1.224   3.043  1.00 25.52           N  
ATOM     16  CA  ALA A   0       6.471  -2.448   3.575  1.00 25.58           C  
ATOM     17  C   ALA A   0       5.576  -2.165   4.768  1.00 25.01           C  
ATOM     18  O   ALA A   0       6.006  -1.541   5.737  1.00 27.23           O  
ATOM     19  CB  ALA A   0       7.572  -3.429   3.971  1.00 27.16           C  
ATOM     20  N   MET A   1       4.331  -2.627   4.691  1.00 23.62           N  
ATOM     21  CA  MET A   1       3.379  -2.414   5.770  1.00 23.56           C  
ATOM     22  C   MET A   1       2.879  -3.709   6.398  1.00 23.60           C  
ATOM     23  O   MET A   1       1.928  -3.704   7.179  1.00 23.11           O  
ATOM     24  CB  MET A   1       2.200  -1.573   5.271  1.00 22.69           C  
ATOM     25  CG  MET A   1       2.498  -0.075   5.218  1.00 20.47           C  
ATOM     26  SD  MET A   1       2.805   0.614   6.874  1.00 19.81           S  
ATOM     27  CE  MET A   1       1.175   0.471   7.577  1.00 20.49           C  
ATOM     28  N   GLU A   2       3.523  -4.823   6.062  1.00 23.10           N  
ATOM     29  CA  GLU A   2       3.136  -6.101   6.637  1.00 22.12           C  
ATOM     30  C   GLU A   2       3.493  -6.086   8.114  1.00 23.11           C  
ATOM     31  O   GLU A   2       4.392  -5.360   8.534  1.00 21.62           O  
ATOM     32  CB  GLU A   2       3.901  -7.258   5.980  1.00 26.58           C  
ATOM     33  CG  GLU A   2       3.585  -7.516   4.520  1.00 32.60           C  
ATOM     34  CD  GLU A   2       4.000  -6.377   3.617  1.00 36.31           C  
ATOM     35  OE1 GLU A   2       5.129  -5.866   3.782  1.00 35.11           O  
ATOM     36  OE2 GLU A   2       3.198  -6.002   2.734  1.00 40.96           O  
ATOM     37  N   GLU A   3       2.781  -6.882   8.902  1.00 23.72           N  
ATOM     38  CA  GLU A   3       3.081  -6.984  10.321  1.00 23.93           C  
ATOM     39  C   GLU A   3       4.260  -7.956  10.348  1.00 21.81           C  
ATOM     40  O   GLU A   3       4.171  -9.053   9.790  1.00 23.24           O  
ATOM     41  CB  GLU A   3       1.890  -7.580  11.078  1.00 29.55           C  
ATOM     42  CG  GLU A   3       1.955  -7.397  12.588  1.00 38.26           C  
ATOM     43  CD  GLU A   3       1.248  -6.133  13.064  1.00 42.66           C  
ATOM     44  OE1 GLU A   3       1.418  -5.065  12.436  1.00 41.82           O  
ATOM     45  OE2 GLU A   3       0.522  -6.207  14.078  1.00 46.48           O  
ATOM     46  N   VAL A   4       5.369  -7.551  10.957  1.00 18.93           N  
ATOM     47  CA  VAL A   4       6.542  -8.413  11.021  1.00 18.23           C  
ATOM     48  C   VAL A   4       6.999  -8.605  12.460  1.00 17.73           C  
ATOM     49  O   VAL A   4       6.422  -8.042  13.389  1.00 17.29           O  
ATOM     50  CB  VAL A   4       7.717  -7.828  10.205  1.00 19.26           C  
ATOM     51  CG1 VAL A   4       7.313  -7.671   8.740  1.00 22.75           C  
ATOM     52  CG2 VAL A   4       8.136  -6.490  10.784  1.00 21.33           C  
ATOM     53  N   THR A   5       8.030  -9.419  12.640  1.00 17.64           N  
ATOM     54  CA  THR A   5       8.569  -9.661  13.967  1.00 18.00           C  
ATOM     55  C   THR A   5      10.057  -9.357  13.949  1.00 18.22           C  
ATOM     56  O   THR A   5      10.794  -9.877  13.112  1.00 20.02           O  
ATOM     57  CB  THR A   5       8.371 -11.125  14.407  1.00 20.21           C  
ATOM     58  OG1 THR A   5       6.972 -11.447  14.392  1.00 23.81           O  
ATOM     59  CG2 THR A   5       8.919 -11.328  15.815  1.00 20.95           C  
ATOM     60  N   ILE A   6      10.487  -8.489  14.858  1.00 16.46           N  
ATOM     61  CA  ILE A   6      11.889  -8.123  14.975  1.00 17.25           C  
ATOM     62  C   ILE A   6      12.410  -8.895  16.177  1.00 18.21           C  
ATOM     63  O   ILE A   6      11.895  -8.746  17.284  1.00 18.67           O  
ATOM     64  CB  ILE A   6      12.058  -6.611  15.239  1.00 16.89           C  
ATOM     65  CG1 ILE A   6      11.399  -5.805  14.115  1.00 16.88           C  
ATOM     66  CG2 ILE A   6      13.540  -6.265  15.370  1.00 17.87           C  
ATOM     67  CD1 ILE A   6      11.986  -6.045  12.720  1.00 17.20           C  
ATOM     68  N   LYS A   7      13.424  -9.725  15.959  1.00 18.01           N  
ATOM     69  CA  LYS A   7      13.991 -10.519  17.039  1.00 18.17           C  
ATOM     70  C   LYS A   7      15.199  -9.831  17.650  1.00 17.57           C  
ATOM     71  O   LYS A   7      16.136  -9.475  16.946  1.00 19.56           O  
ATOM     72  CB  LYS A   7      14.395 -11.898  16.514  1.00 21.49           C  
ATOM     73  CG  LYS A   7      15.024 -12.822  17.555  1.00 26.73           C  
ATOM     74  CD  LYS A   7      15.315 -14.177  16.927  1.00 31.46           C  
ATOM     75  CE  LYS A   7      15.955 -15.138  17.905  1.00 37.24           C  
ATOM     76  NZ  LYS A   7      16.296 -16.429  17.237  1.00 42.58           N  
ATOM     77  N   ALA A   8      15.159  -9.630  18.962  1.00 16.83           N  
ATOM     78  CA  ALA A   8      16.271  -9.008  19.660  1.00 18.23           C  
ATOM     79  C   ALA A   8      17.038 -10.073  20.437  1.00 20.25           C  
ATOM     80  O   ALA A   8      16.502 -10.677  21.366  1.00 19.48           O  
ATOM     81  CB  ALA A   8      15.759  -7.927  20.612  1.00 19.43           C  
ATOM     82  N   ASN A   9      18.281 -10.330  20.035  1.00 18.45           N  
ATOM     83  CA  ASN A   9      19.112 -11.291  20.750  1.00 21.70           C  
ATOM     84  C   ASN A   9      19.957 -10.440  21.680  1.00 22.01           C  
ATOM     85  O   ASN A   9      20.902  -9.787  21.244  1.00 22.61           O  
ATOM     86  CB  ASN A   9      20.024 -12.075  19.800  1.00 21.97           C  
ATOM     87  CG  ASN A   9      19.266 -13.072  18.949  1.00 24.07           C  
ATOM     88  OD1 ASN A   9      18.373 -13.774  19.437  1.00 26.57           O  
ATOM     89  ND2 ASN A   9      19.624 -13.150  17.669  1.00 22.99           N  
ATOM     90  N   LEU A  10      19.593 -10.430  22.956  1.00 20.87           N  
ATOM     91  CA  LEU A  10      20.301  -9.652  23.956  1.00 23.06           C  
ATOM     92  C   LEU A  10      21.463 -10.467  24.510  1.00 25.47           C  
ATOM     93  O   LEU A  10      21.292 -11.605  24.952  1.00 26.41           O  
ATOM     94  CB  LEU A  10      19.336  -9.263  25.074  1.00 23.49           C  
ATOM     95  CG  LEU A  10      18.031  -8.634  24.569  1.00 23.91           C  
ATOM     96  CD1 LEU A  10      17.006  -8.591  25.688  1.00 27.01           C  
ATOM     97  CD2 LEU A  10      18.307  -7.246  24.015  1.00 26.20           C  
ATOM     98  N   ILE A  11      22.651  -9.877  24.468  1.00 24.78           N  
ATOM     99  CA  ILE A  11      23.857 -10.533  24.953  1.00 25.39           C  
ATOM    100  C   ILE A  11      24.446  -9.660  26.053  1.00 23.92           C  
ATOM    101  O   ILE A  11      24.775  -8.497  25.816  1.00 24.29           O  
ATOM    102  CB  ILE A  11      24.879 -10.680  23.813  1.00 28.71           C  
ATOM    103  CG1 ILE A  11      24.208 -11.357  22.613  1.00 32.11           C  
ATOM    104  CG2 ILE A  11      26.079 -11.480  24.292  1.00 27.74           C  
ATOM    105  CD1 ILE A  11      25.054 -11.378  21.358  1.00 38.10           C  
ATOM    106  N   PHE A  12      24.570 -10.215  27.252  1.00 23.02           N  
ATOM    107  CA  PHE A  12      25.094  -9.453  28.377  1.00 25.20           C  
ATOM    108  C   PHE A  12      26.597  -9.611  28.551  1.00 25.52           C  
ATOM    109  O   PHE A  12      27.201 -10.521  27.997  1.00 28.97           O  
ATOM    110  CB  PHE A  12      24.353  -9.842  29.654  1.00 26.31           C  
ATOM    111  CG  PHE A  12      22.864  -9.654  29.552  1.00 25.90           C  
ATOM    112  CD1 PHE A  12      22.318  -8.375  29.546  1.00 26.59           C  
ATOM    113  CD2 PHE A  12      22.018 -10.747  29.395  1.00 27.69           C  
ATOM    114  CE1 PHE A  12      20.945  -8.183  29.380  1.00 29.97           C  
ATOM    115  CE2 PHE A  12      20.645 -10.567  29.229  1.00 30.83           C  
ATOM    116  CZ  PHE A  12      20.108  -9.283  29.222  1.00 26.60           C  
ATOM    117  N   ALA A  13      27.178  -8.700  29.324  1.00 29.00           N  
ATOM    118  CA  ALA A  13      28.617  -8.662  29.578  1.00 31.10           C  
ATOM    119  C   ALA A  13      29.276  -9.997  29.914  1.00 32.05           C  
ATOM    120  O   ALA A  13      30.368 -10.295  29.422  1.00 32.70           O  
ATOM    121  CB  ALA A  13      28.906  -7.657  30.685  1.00 30.39           C  
ATOM    122  N   ASN A  14      28.627 -10.798  30.751  1.00 30.66           N  
ATOM    123  CA  ASN A  14      29.199 -12.078  31.147  1.00 31.03           C  
ATOM    124  C   ASN A  14      28.913 -13.208  30.161  1.00 31.87           C  
ATOM    125  O   ASN A  14      29.247 -14.364  30.419  1.00 33.50           O  
ATOM    126  CB  ASN A  14      28.703 -12.457  32.541  1.00 30.69           C  
ATOM    127  CG  ASN A  14      27.290 -12.992  32.529  1.00 32.60           C  
ATOM    128  OD1 ASN A  14      26.475 -12.607  31.690  1.00 31.93           O  
ATOM    129  ND2 ASN A  14      26.986 -13.879  33.471  1.00 34.42           N  
ATOM    130  N   GLY A  15      28.289 -12.876  29.035  1.00 31.27           N  
ATOM    131  CA  GLY A  15      28.005 -13.891  28.036  1.00 30.42           C  
ATOM    132  C   GLY A  15      26.614 -14.491  28.071  1.00 30.39           C  
ATOM    133  O   GLY A  15      26.231 -15.200  27.138  1.00 31.40           O  
ATOM    134  N   SER A  16      25.864 -14.231  29.138  1.00 28.03           N  
ATOM    135  CA  SER A  16      24.506 -14.753  29.244  1.00 28.09           C  
ATOM    136  C   SER A  16      23.652 -14.080  28.173  1.00 25.42           C  
ATOM    137  O   SER A  16      23.999 -13.012  27.673  1.00 24.30           O  
ATOM    138  CB  SER A  16      23.928 -14.490  30.639  1.00 27.86           C  
ATOM    139  OG  SER A  16      23.953 -13.113  30.973  1.00 30.03           O  
ATOM    140  N   THR A  17      22.530 -14.700  27.829  1.00 25.90           N  
ATOM    141  CA  THR A  17      21.671 -14.156  26.788  1.00 23.54           C  
ATOM    142  C   THR A  17      20.191 -14.184  27.129  1.00 22.91           C  
ATOM    143  O   THR A  17      19.758 -14.887  28.043  1.00 23.39           O  
ATOM    144  CB  THR A  17      21.849 -14.936  25.484  1.00 27.24           C  
ATOM    145  OG1 THR A  17      21.606 -16.325  25.734  1.00 29.79           O  
ATOM    146  CG2 THR A  17      23.266 -14.760  24.941  1.00 27.64           C  
ATOM    147  N   GLN A  18      19.428 -13.410  26.365  1.00 20.97           N  
ATOM    148  CA  GLN A  18      17.979 -13.321  26.515  1.00 20.62           C  
ATOM    149  C   GLN A  18      17.431 -12.945  25.144  1.00 19.97           C  
ATOM    150  O   GLN A  18      18.030 -12.137  24.436  1.00 20.66           O  
ATOM    151  CB  GLN A  18      17.604 -12.227  27.516  1.00 20.41           C  
ATOM    152  CG  GLN A  18      16.101 -12.068  27.750  1.00 24.50           C  
ATOM    153  CD  GLN A  18      15.764 -10.793  28.521  1.00 25.96           C  
ATOM    154  OE1 GLN A  18      16.489 -10.402  29.438  1.00 25.61           O  
ATOM    155  NE2 GLN A  18      14.655 -10.149  28.157  1.00 19.31           N  
ATOM    156  N   THR A  19      16.300 -13.530  24.765  1.00 18.24           N  
ATOM    157  CA  THR A  19      15.701 -13.204  23.481  1.00 17.01           C  
ATOM    158  C   THR A  19      14.298 -12.665  23.691  1.00 15.81           C  
ATOM    159  O   THR A  19      13.528 -13.218  24.470  1.00 17.26           O  
ATOM    160  CB  THR A  19      15.624 -14.442  22.563  1.00 21.02           C  
ATOM    161  OG1 THR A  19      16.953 -14.883  22.261  1.00 25.67           O  
ATOM    162  CG2 THR A  19      14.904 -14.102  21.253  1.00 21.65           C  
ATOM    163  N   ALA A  20      13.997 -11.561  23.019  1.00 16.73           N  
ATOM    164  CA  ALA A  20      12.677 -10.944  23.079  1.00 15.05           C  
ATOM    165  C   ALA A  20      12.321 -10.592  21.635  1.00 17.23           C  
ATOM    166  O   ALA A  20      13.209 -10.374  20.813  1.00 19.36           O  
ATOM    167  CB  ALA A  20      12.715  -9.682  23.945  1.00 18.86           C  
ATOM    168  N   GLU A  21      11.031 -10.554  21.313  1.00 15.95           N  
ATOM    169  CA  GLU A  21      10.604 -10.233  19.952  1.00 17.38           C  
ATOM    170  C   GLU A  21       9.549  -9.144  19.970  1.00 16.43           C  
ATOM    171  O   GLU A  21       8.768  -9.040  20.915  1.00 17.29           O  
ATOM    172  CB  GLU A  21      10.066 -11.478  19.246  1.00 20.76           C  
ATOM    173  CG  GLU A  21      11.093 -12.595  19.177  1.00 29.47           C  
ATOM    174  CD  GLU A  21      10.809 -13.586  18.076  1.00 32.74           C  
ATOM    175  OE1 GLU A  21       9.779 -14.285  18.146  1.00 38.76           O  
ATOM    176  OE2 GLU A  21      11.622 -13.659  17.133  1.00 42.47           O  
ATOM    177  N   PHE A  22       9.533  -8.339  18.914  1.00 15.47           N  
ATOM    178  CA  PHE A  22       8.615  -7.216  18.824  1.00 15.41           C  
ATOM    179  C   PHE A  22       7.836  -7.276  17.521  1.00 16.16           C  
ATOM    180  O   PHE A  22       8.410  -7.342  16.437  1.00 16.78           O  
ATOM    181  CB  PHE A  22       9.435  -5.934  18.978  1.00 16.82           C  
ATOM    182  CG  PHE A  22      10.276  -5.938  20.223  1.00 15.54           C  
ATOM    183  CD1 PHE A  22      11.479  -6.647  20.268  1.00 15.37           C  
ATOM    184  CD2 PHE A  22       9.789  -5.381  21.398  1.00 16.77           C  
ATOM    185  CE1 PHE A  22      12.166  -6.808  21.465  1.00 16.24           C  
ATOM    186  CE2 PHE A  22      10.473  -5.536  22.604  1.00 18.46           C  
ATOM    187  CZ  PHE A  22      11.666  -6.256  22.634  1.00 17.89           C  
ATOM    188  N   LYS A  23       6.512  -7.263  17.650  1.00 16.35           N  
ATOM    189  CA  LYS A  23       5.624  -7.392  16.505  1.00 17.23           C  
ATOM    190  C   LYS A  23       4.863  -6.138  16.106  1.00 18.77           C  
ATOM    191  O   LYS A  23       4.216  -5.497  16.940  1.00 19.89           O  
ATOM    192  CB  LYS A  23       4.626  -8.524  16.766  1.00 21.85           C  
ATOM    193  CG  LYS A  23       5.190  -9.922  16.542  1.00 32.02           C  
ATOM    194  CD  LYS A  23       4.078 -10.969  16.577  1.00 37.49           C  
ATOM    195  CE  LYS A  23       4.508 -12.277  15.911  1.00 40.04           C  
ATOM    196  NZ  LYS A  23       5.706 -12.895  16.549  1.00 34.28           N  
ATOM    197  N   GLY A  24       4.938  -5.814  14.817  1.00 16.60           N  
ATOM    198  CA  GLY A  24       4.254  -4.646  14.284  1.00 18.44           C  
ATOM    199  C   GLY A  24       4.858  -4.275  12.941  1.00 17.84           C  
ATOM    200  O   GLY A  24       5.627  -5.054  12.370  1.00 17.08           O  
ATOM    201  N   THR A  25       4.507  -3.110  12.405  1.00 15.75           N  
ATOM    202  CA  THR A  25       5.110  -2.712  11.136  1.00 16.16           C  
ATOM    203  C   THR A  25       6.608  -2.557  11.412  1.00 16.11           C  
ATOM    204  O   THR A  25       7.004  -2.260  12.536  1.00 16.96           O  
ATOM    205  CB  THR A  25       4.489  -1.407  10.605  1.00 15.88           C  
ATOM    206  OG1 THR A  25       4.474  -0.420  11.643  1.00 17.52           O  
ATOM    207  CG2 THR A  25       3.051  -1.668  10.147  1.00 18.98           C  
ATOM    208  N   PHE A  26       7.433  -2.756  10.385  1.00 15.42           N  
ATOM    209  CA  PHE A  26       8.889  -2.740  10.538  1.00 15.66           C  
ATOM    210  C   PHE A  26       9.565  -1.673  11.397  1.00 15.10           C  
ATOM    211  O   PHE A  26      10.244  -2.002  12.368  1.00 16.47           O  
ATOM    212  CB  PHE A  26       9.568  -2.753   9.162  1.00 16.46           C  
ATOM    213  CG  PHE A  26      11.052  -3.016   9.228  1.00 17.54           C  
ATOM    214  CD1 PHE A  26      11.539  -4.319   9.303  1.00 18.99           C  
ATOM    215  CD2 PHE A  26      11.955  -1.960   9.258  1.00 22.07           C  
ATOM    216  CE1 PHE A  26      12.917  -4.561   9.408  1.00 21.31           C  
ATOM    217  CE2 PHE A  26      13.329  -2.189   9.363  1.00 22.77           C  
ATOM    218  CZ  PHE A  26      13.808  -3.496   9.439  1.00 21.07           C  
ATOM    219  N   GLU A  27       9.414  -0.403  11.044  1.00 16.95           N  
ATOM    220  CA  GLU A  27      10.094   0.631  11.815  1.00 15.93           C  
ATOM    221  C   GLU A  27       9.513   0.818  13.213  1.00 14.91           C  
ATOM    222  O   GLU A  27      10.252   1.102  14.156  1.00 15.44           O  
ATOM    223  CB  GLU A  27      10.101   1.959  11.045  1.00 15.62           C  
ATOM    224  CG  GLU A  27      10.841   1.911   9.695  1.00 17.28           C  
ATOM    225  CD  GLU A  27      12.342   1.631   9.811  1.00 19.55           C  
ATOM    226  OE1 GLU A  27      12.860   1.488  10.937  1.00 18.49           O  
ATOM    227  OE2 GLU A  27      13.013   1.560   8.753  1.00 20.87           O  
ATOM    228  N   LYS A  28       8.200   0.653  13.356  1.00 15.92           N  
ATOM    229  CA  LYS A  28       7.572   0.796  14.667  1.00 16.81           C  
ATOM    230  C   LYS A  28       8.099  -0.285  15.607  1.00 16.56           C  
ATOM    231  O   LYS A  28       8.491  -0.001  16.738  1.00 16.18           O  
ATOM    232  CB  LYS A  28       6.044   0.675  14.558  1.00 15.39           C  
ATOM    233  CG  LYS A  28       5.314   0.742  15.910  1.00 17.69           C  
ATOM    234  CD  LYS A  28       3.796   0.601  15.727  1.00 18.64           C  
ATOM    235  CE  LYS A  28       3.018   0.820  17.032  1.00 21.36           C  
ATOM    236  NZ  LYS A  28       3.122  -0.307  18.013  1.00 22.16           N  
ATOM    237  N   ALA A  29       8.109  -1.526  15.127  1.00 14.87           N  
ATOM    238  CA  ALA A  29       8.587  -2.651  15.921  1.00 15.39           C  
ATOM    239  C   ALA A  29      10.081  -2.547  16.211  1.00 15.30           C  
ATOM    240  O   ALA A  29      10.534  -2.912  17.291  1.00 15.52           O  
ATOM    241  CB  ALA A  29       8.290  -3.958  15.198  1.00 14.36           C  
ATOM    242  N   THR A  30      10.849  -2.047  15.247  1.00 15.01           N  
ATOM    243  CA  THR A  30      12.290  -1.924  15.445  1.00 16.88           C  
ATOM    244  C   THR A  30      12.563  -0.914  16.559  1.00 16.56           C  
ATOM    245  O   THR A  30      13.391  -1.149  17.448  1.00 16.01           O  
ATOM    246  CB  THR A  30      13.003  -1.491  14.137  1.00 15.96           C  
ATOM    247  OG1 THR A  30      12.890  -2.538  13.161  1.00 17.23           O  
ATOM    248  CG2 THR A  30      14.491  -1.214  14.405  1.00 15.91           C  
ATOM    249  N   SER A  31      11.846   0.204  16.525  1.00 16.65           N  
ATOM    250  CA  SER A  31      12.016   1.232  17.543  1.00 17.13           C  
ATOM    251  C   SER A  31      11.644   0.668  18.915  1.00 16.70           C  
ATOM    252  O   SER A  31      12.284   0.973  19.921  1.00 16.29           O  
ATOM    253  CB  SER A  31      11.140   2.447  17.225  1.00 18.04           C  
ATOM    254  OG  SER A  31      11.415   3.509  18.127  1.00 22.00           O  
ATOM    255  N   GLU A  32      10.604  -0.159  18.950  1.00 15.83           N  
ATOM    256  CA  GLU A  32      10.170  -0.763  20.202  1.00 15.54           C  
ATOM    257  C   GLU A  32      11.227  -1.727  20.744  1.00 13.81           C  
ATOM    258  O   GLU A  32      11.433  -1.816  21.953  1.00 15.95           O  
ATOM    259  CB  GLU A  32       8.821  -1.453  19.989  1.00 14.92           C  
ATOM    260  CG  GLU A  32       7.696  -0.423  19.929  1.00 14.72           C  
ATOM    261  CD  GLU A  32       6.407  -0.930  19.311  1.00 16.24           C  
ATOM    262  OE1 GLU A  32       6.374  -2.080  18.824  1.00 19.69           O  
ATOM    263  OE2 GLU A  32       5.425  -0.156  19.311  1.00 18.69           O  
ATOM    264  N   ALA A  33      11.916  -2.426  19.850  1.00 15.09           N  
ATOM    265  CA  ALA A  33      12.963  -3.346  20.279  1.00 16.69           C  
ATOM    266  C   ALA A  33      14.078  -2.567  20.980  1.00 17.47           C  
ATOM    267  O   ALA A  33      14.541  -2.954  22.053  1.00 16.56           O  
ATOM    268  CB  ALA A  33      13.532  -4.104  19.077  1.00 16.87           C  
ATOM    269  N   TYR A  34      14.508  -1.464  20.374  1.00 18.22           N  
ATOM    270  CA  TYR A  34      15.563  -0.664  20.982  1.00 18.50           C  
ATOM    271  C   TYR A  34      15.091  -0.036  22.284  1.00 19.71           C  
ATOM    272  O   TYR A  34      15.860   0.065  23.236  1.00 18.51           O  
ATOM    273  CB  TYR A  34      16.052   0.416  20.013  1.00 18.38           C  
ATOM    274  CG  TYR A  34      16.856  -0.131  18.854  1.00 18.59           C  
ATOM    275  CD1 TYR A  34      17.999  -0.905  19.076  1.00 20.45           C  
ATOM    276  CD2 TYR A  34      16.494   0.142  17.538  1.00 19.67           C  
ATOM    277  CE1 TYR A  34      18.763  -1.388  18.013  1.00 20.69           C  
ATOM    278  CE2 TYR A  34      17.251  -0.339  16.464  1.00 21.90           C  
ATOM    279  CZ  TYR A  34      18.385  -1.102  16.711  1.00 22.60           C  
ATOM    280  OH  TYR A  34      19.141  -1.569  15.656  1.00 22.33           O  
ATOM    281  N   ALA A  35      13.825   0.375  22.329  1.00 18.37           N  
ATOM    282  CA  ALA A  35      13.255   0.962  23.539  1.00 18.55           C  
ATOM    283  C   ALA A  35      13.327  -0.060  24.671  1.00 17.89           C  
ATOM    284  O   ALA A  35      13.590   0.293  25.820  1.00 17.50           O  
ATOM    285  CB  ALA A  35      11.804   1.367  23.296  1.00 19.77           C  
ATOM    286  N   TYR A  36      13.091  -1.331  24.346  1.00 17.01           N  
ATOM    287  CA  TYR A  36      13.158  -2.368  25.364  1.00 16.80           C  
ATOM    288  C   TYR A  36      14.609  -2.530  25.828  1.00 18.66           C  
ATOM    289  O   TYR A  36      14.879  -2.607  27.023  1.00 19.19           O  
ATOM    290  CB  TYR A  36      12.639  -3.701  24.828  1.00 17.87           C  
ATOM    291  CG  TYR A  36      12.751  -4.798  25.857  1.00 17.48           C  
ATOM    292  CD1 TYR A  36      11.935  -4.798  26.989  1.00 17.13           C  
ATOM    293  CD2 TYR A  36      13.741  -5.777  25.755  1.00 17.35           C  
ATOM    294  CE1 TYR A  36      12.109  -5.739  28.000  1.00 16.12           C  
ATOM    295  CE2 TYR A  36      13.922  -6.724  26.758  1.00 17.71           C  
ATOM    296  CZ  TYR A  36      13.106  -6.697  27.879  1.00 18.91           C  
ATOM    297  OH  TYR A  36      13.303  -7.617  28.882  1.00 17.96           O  
ATOM    298  N   ALA A  37      15.536  -2.581  24.878  1.00 17.42           N  
ATOM    299  CA  ALA A  37      16.952  -2.718  25.216  1.00 17.58           C  
ATOM    300  C   ALA A  37      17.360  -1.608  26.179  1.00 19.84           C  
ATOM    301  O   ALA A  37      18.123  -1.839  27.120  1.00 19.19           O  
ATOM    302  CB  ALA A  37      17.807  -2.649  23.950  1.00 19.40           C  
ATOM    303  N   ASP A  38      16.847  -0.404  25.936  1.00 20.77           N  
ATOM    304  CA  ASP A  38      17.162   0.745  26.779  1.00 22.28           C  
ATOM    305  C   ASP A  38      16.765   0.546  28.243  1.00 22.78           C  
ATOM    306  O   ASP A  38      17.440   1.051  29.142  1.00 23.46           O  
ATOM    307  CB  ASP A  38      16.491   2.004  26.230  1.00 23.54           C  
ATOM    308  CG  ASP A  38      17.245   2.611  25.056  1.00 25.92           C  
ATOM    309  OD1 ASP A  38      18.437   2.287  24.866  1.00 25.00           O  
ATOM    310  OD2 ASP A  38      16.639   3.426  24.327  1.00 26.00           O  
ATOM    311  N   THR A  39      15.682  -0.186  28.498  1.00 20.69           N  
ATOM    312  CA  THR A  39      15.264  -0.412  29.879  1.00 22.14           C  
ATOM    313  C   THR A  39      16.233  -1.329  30.624  1.00 22.39           C  
ATOM    314  O   THR A  39      16.180  -1.422  31.848  1.00 25.37           O  
ATOM    315  CB  THR A  39      13.859  -1.055  29.974  1.00 22.19           C  
ATOM    316  OG1 THR A  39      13.915  -2.411  29.509  1.00 20.47           O  
ATOM    317  CG2 THR A  39      12.851  -0.262  29.156  1.00 21.41           C  
ATOM    318  N   LEU A  40      17.123  -1.993  29.894  1.00 21.40           N  
ATOM    319  CA  LEU A  40      18.070  -2.910  30.517  1.00 21.63           C  
ATOM    320  C   LEU A  40      19.438  -2.284  30.787  1.00 22.66           C  
ATOM    321  O   LEU A  40      20.307  -2.924  31.379  1.00 23.97           O  
ATOM    322  CB  LEU A  40      18.236  -4.164  29.646  1.00 20.10           C  
ATOM    323  CG  LEU A  40      16.945  -4.942  29.344  1.00 20.59           C  
ATOM    324  CD1 LEU A  40      17.272  -6.218  28.581  1.00 22.11           C  
ATOM    325  CD2 LEU A  40      16.228  -5.282  30.645  1.00 23.16           C  
ATOM    326  N   LYS A  41      19.620  -1.035  30.364  1.00 23.21           N  
ATOM    327  CA  LYS A  41      20.898  -0.348  30.553  1.00 25.06           C  
ATOM    328  C   LYS A  41      21.227  -0.064  32.014  1.00 28.43           C  
ATOM    329  O   LYS A  41      22.394  -0.094  32.411  1.00 28.17           O  
ATOM    330  CB  LYS A  41      20.921   0.962  29.757  1.00 27.19           C  
ATOM    331  CG  LYS A  41      20.898   0.760  28.249  1.00 26.10           C  
ATOM    332  CD  LYS A  41      21.218   2.042  27.489  1.00 30.57           C  
ATOM    333  CE  LYS A  41      20.210   3.146  27.768  1.00 33.29           C  
ATOM    334  NZ  LYS A  41      20.584   4.403  27.056  1.00 33.03           N  
ATOM    335  N   LYS A  42      20.201   0.207  32.813  1.00 28.46           N  
ATOM    336  CA  LYS A  42      20.393   0.507  34.226  1.00 31.84           C  
ATOM    337  C   LYS A  42      21.166  -0.596  34.946  1.00 32.85           C  
ATOM    338  O   LYS A  42      22.062  -0.316  35.746  1.00 34.11           O  
ATOM    339  CB  LYS A  42      19.035   0.716  34.902  1.00 35.41           C  
ATOM    340  CG  LYS A  42      19.109   1.123  36.370  1.00 40.97           C  
ATOM    341  CD  LYS A  42      17.718   1.401  36.938  1.00 44.45           C  
ATOM    342  CE  LYS A  42      17.041   2.559  36.213  1.00 47.40           C  
ATOM    343  NZ  LYS A  42      15.672   2.840  36.733  1.00 49.44           N  
ATOM    344  N   ASP A  43      20.833  -1.848  34.653  1.00 29.96           N  
ATOM    345  CA  ASP A  43      21.497  -2.972  35.300  1.00 32.17           C  
ATOM    346  C   ASP A  43      22.562  -3.658  34.453  1.00 31.78           C  
ATOM    347  O   ASP A  43      23.369  -4.423  34.979  1.00 32.57           O  
ATOM    348  CB  ASP A  43      20.458  -4.013  35.723  1.00 35.50           C  
ATOM    349  CG  ASP A  43      19.479  -3.477  36.744  1.00 37.97           C  
ATOM    350  OD1 ASP A  43      19.932  -3.014  37.810  1.00 41.59           O  
ATOM    351  OD2 ASP A  43      18.259  -3.520  36.484  1.00 43.76           O  
ATOM    352  N   ASN A  44      22.581  -3.378  33.153  1.00 28.92           N  
ATOM    353  CA  ASN A  44      23.534  -4.035  32.266  1.00 29.72           C  
ATOM    354  C   ASN A  44      24.483  -3.128  31.489  1.00 28.66           C  
ATOM    355  O   ASN A  44      25.329  -3.611  30.730  1.00 28.66           O  
ATOM    356  CB  ASN A  44      22.760  -4.929  31.299  1.00 28.75           C  
ATOM    357  CG  ASN A  44      21.927  -5.969  32.024  1.00 31.48           C  
ATOM    358  OD1 ASN A  44      22.459  -6.939  32.562  1.00 32.11           O  
ATOM    359  ND2 ASN A  44      20.613  -5.761  32.059  1.00 30.11           N  
ATOM    360  N   GLY A  45      24.345  -1.820  31.670  1.00 28.66           N  
ATOM    361  CA  GLY A  45      25.215  -0.890  30.976  1.00 28.86           C  
ATOM    362  C   GLY A  45      24.746  -0.534  29.579  1.00 28.93           C  
ATOM    363  O   GLY A  45      23.675  -0.963  29.140  1.00 26.90           O  
ATOM    364  N   GLU A  46      25.556   0.255  28.879  1.00 28.56           N  
ATOM    365  CA  GLU A  46      25.242   0.690  27.526  1.00 27.34           C  
ATOM    366  C   GLU A  46      25.322  -0.474  26.550  1.00 26.39           C  
ATOM    367  O   GLU A  46      26.000  -1.466  26.812  1.00 26.96           O  
ATOM    368  CB  GLU A  46      26.217   1.788  27.101  1.00 31.38           C  
ATOM    369  CG  GLU A  46      26.281   2.942  28.087  1.00 37.24           C  
ATOM    370  CD  GLU A  46      24.979   3.715  28.168  1.00 42.78           C  
ATOM    371  OE1 GLU A  46      24.146   3.582  27.249  1.00 47.10           O  
ATOM    372  OE2 GLU A  46      24.794   4.468  29.146  1.00 47.64           O  
ATOM    373  N   TRP A  47      24.630  -0.349  25.423  1.00 26.40           N  
ATOM    374  CA  TRP A  47      24.645  -1.402  24.419  1.00 25.10           C  
ATOM    375  C   TRP A  47      25.037  -0.921  23.029  1.00 25.52           C  
ATOM    376  O   TRP A  47      24.992   0.272  22.722  1.00 26.96           O  
ATOM    377  CB  TRP A  47      23.272  -2.103  24.338  1.00 25.31           C  
ATOM    378  CG  TRP A  47      22.100  -1.186  24.071  1.00 23.40           C  
ATOM    379  CD1 TRP A  47      21.253  -0.652  24.998  1.00 23.70           C  
ATOM    380  CD2 TRP A  47      21.661  -0.691  22.794  1.00 23.95           C  
ATOM    381  NE1 TRP A  47      20.314   0.145  24.382  1.00 24.34           N  
ATOM    382  CE2 TRP A  47      20.541   0.140  23.032  1.00 21.36           C  
ATOM    383  CE3 TRP A  47      22.105  -0.867  21.475  1.00 20.33           C  
ATOM    384  CZ2 TRP A  47      19.857   0.795  21.998  1.00 22.32           C  
ATOM    385  CZ3 TRP A  47      21.423  -0.212  20.445  1.00 25.32           C  
ATOM    386  CH2 TRP A  47      20.312   0.608  20.717  1.00 23.22           C  
ATOM    387  N   THR A  48      25.450  -1.877  22.205  1.00 25.91           N  
ATOM    388  CA  THR A  48      25.815  -1.633  20.818  1.00 26.99           C  
ATOM    389  C   THR A  48      25.027  -2.680  20.041  1.00 26.50           C  
ATOM    390  O   THR A  48      24.593  -3.686  20.613  1.00 25.96           O  
ATOM    391  CB  THR A  48      27.324  -1.842  20.560  1.00 26.80           C  
ATOM    392  OG1 THR A  48      27.709  -3.157  20.980  1.00 31.65           O  
ATOM    393  CG2 THR A  48      28.140  -0.802  21.309  1.00 29.99           C  
ATOM    394  N   VAL A  49      24.834  -2.459  18.747  1.00 24.84           N  
ATOM    395  CA  VAL A  49      24.075  -3.415  17.964  1.00 24.48           C  
ATOM    396  C   VAL A  49      24.667  -3.766  16.606  1.00 26.75           C  
ATOM    397  O   VAL A  49      25.349  -2.961  15.963  1.00 25.17           O  
ATOM    398  CB  VAL A  49      22.618  -2.920  17.747  1.00 24.53           C  
ATOM    399  CG1 VAL A  49      22.621  -1.620  16.953  1.00 25.02           C  
ATOM    400  CG2 VAL A  49      21.804  -3.986  17.020  1.00 24.27           C  
ATOM    401  N   ASP A  50      24.400  -5.000  16.200  1.00 25.49           N  
ATOM    402  CA  ASP A  50      24.810  -5.529  14.916  1.00 26.66           C  
ATOM    403  C   ASP A  50      23.505  -6.024  14.316  1.00 25.46           C  
ATOM    404  O   ASP A  50      22.890  -6.960  14.835  1.00 25.33           O  
ATOM    405  CB  ASP A  50      25.791  -6.685  15.096  1.00 30.02           C  
ATOM    406  CG  ASP A  50      27.152  -6.216  15.559  1.00 37.30           C  
ATOM    407  OD1 ASP A  50      27.796  -5.452  14.810  1.00 40.88           O  
ATOM    408  OD2 ASP A  50      27.577  -6.602  16.670  1.00 42.94           O  
ATOM    409  N   VAL A  51      23.073  -5.367  13.245  1.00 25.11           N  
ATOM    410  CA  VAL A  51      21.832  -5.719  12.570  1.00 25.80           C  
ATOM    411  C   VAL A  51      22.058  -6.879  11.607  1.00 27.64           C  
ATOM    412  O   VAL A  51      22.950  -6.829  10.756  1.00 27.71           O  
ATOM    413  CB  VAL A  51      21.274  -4.509  11.795  1.00 24.55           C  
ATOM    414  CG1 VAL A  51      19.931  -4.851  11.183  1.00 24.93           C  
ATOM    415  CG2 VAL A  51      21.150  -3.311  12.730  1.00 25.04           C  
ATOM    416  N   ALA A  52      21.243  -7.921  11.740  1.00 24.47           N  
ATOM    417  CA  ALA A  52      21.360  -9.103  10.891  1.00 25.23           C  
ATOM    418  C   ALA A  52      20.030  -9.511  10.267  1.00 27.28           C  
ATOM    419  O   ALA A  52      18.990  -8.898  10.523  1.00 24.47           O  
ATOM    420  CB  ALA A  52      21.930 -10.267  11.702  1.00 26.41           C  
ATOM    421  N   ASP A  53      20.077 -10.558   9.447  1.00 26.85           N  
ATOM    422  CA  ASP A  53      18.893 -11.084   8.777  1.00 29.70           C  
ATOM    423  C   ASP A  53      18.043 -10.015   8.093  1.00 29.47           C  
ATOM    424  O   ASP A  53      16.824  -9.977   8.256  1.00 29.30           O  
ATOM    425  CB  ASP A  53      18.042 -11.880   9.775  1.00 30.50           C  
ATOM    426  CG  ASP A  53      18.780 -13.086  10.329  1.00 34.25           C  
ATOM    427  OD1 ASP A  53      19.303 -13.881   9.518  1.00 38.38           O  
ATOM    428  OD2 ASP A  53      18.840 -13.245  11.567  1.00 33.56           O  
ATOM    429  N   LYS A  54      18.704  -9.161   7.314  1.00 30.00           N  
ATOM    430  CA  LYS A  54      18.048  -8.082   6.579  1.00 31.75           C  
ATOM    431  C   LYS A  54      17.308  -7.102   7.482  1.00 30.51           C  
ATOM    432  O   LYS A  54      16.349  -6.458   7.050  1.00 32.37           O  
ATOM    433  CB  LYS A  54      17.066  -8.642   5.544  1.00 35.48           C  
ATOM    434  CG  LYS A  54      17.654  -9.653   4.569  1.00 42.02           C  
ATOM    435  CD  LYS A  54      17.620 -11.064   5.142  1.00 45.27           C  
ATOM    436  CE  LYS A  54      16.190 -11.500   5.460  1.00 47.99           C  
ATOM    437  NZ  LYS A  54      16.128 -12.867   6.056  1.00 49.33           N  
ATOM    438  N   GLY A  55      17.752  -6.991   8.730  1.00 26.14           N  
ATOM    439  CA  GLY A  55      17.119  -6.073   9.659  1.00 26.88           C  
ATOM    440  C   GLY A  55      16.108  -6.708  10.598  1.00 23.32           C  
ATOM    441  O   GLY A  55      15.581  -6.038  11.484  1.00 26.15           O  
ATOM    442  N   TYR A  56      15.838  -7.996  10.427  1.00 23.47           N  
ATOM    443  CA  TYR A  56      14.868  -8.662  11.290  1.00 21.81           C  
ATOM    444  C   TYR A  56      15.457  -9.239  12.566  1.00 21.61           C  
ATOM    445  O   TYR A  56      14.728  -9.712  13.438  1.00 20.40           O  
ATOM    446  CB  TYR A  56      14.121  -9.741  10.511  1.00 22.95           C  
ATOM    447  CG  TYR A  56      13.262  -9.148   9.423  1.00 23.33           C  
ATOM    448  CD1 TYR A  56      13.818  -8.764   8.201  1.00 24.09           C  
ATOM    449  CD2 TYR A  56      11.906  -8.902   9.637  1.00 25.97           C  
ATOM    450  CE1 TYR A  56      13.047  -8.148   7.221  1.00 26.69           C  
ATOM    451  CE2 TYR A  56      11.126  -8.286   8.663  1.00 27.07           C  
ATOM    452  CZ  TYR A  56      11.702  -7.912   7.459  1.00 27.25           C  
ATOM    453  OH  TYR A  56      10.936  -7.299   6.493  1.00 31.07           O  
ATOM    454  N   THR A  57      16.779  -9.207  12.676  1.00 19.85           N  
ATOM    455  CA  THR A  57      17.440  -9.690  13.877  1.00 20.70           C  
ATOM    456  C   THR A  57      18.377  -8.608  14.392  1.00 21.67           C  
ATOM    457  O   THR A  57      19.205  -8.079  13.644  1.00 22.89           O  
ATOM    458  CB  THR A  57      18.261 -10.970  13.612  1.00 21.22           C  
ATOM    459  OG1 THR A  57      17.375 -12.052  13.299  1.00 24.80           O  
ATOM    460  CG2 THR A  57      19.093 -11.332  14.844  1.00 22.60           C  
ATOM    461  N   LEU A  58      18.227  -8.262  15.665  1.00 20.03           N  
ATOM    462  CA  LEU A  58      19.082  -7.260  16.282  1.00 18.74           C  
ATOM    463  C   LEU A  58      19.924  -7.934  17.357  1.00 21.44           C  
ATOM    464  O   LEU A  58      19.401  -8.394  18.371  1.00 19.48           O  
ATOM    465  CB  LEU A  58      18.246  -6.137  16.909  1.00 21.29           C  
ATOM    466  CG  LEU A  58      17.241  -5.430  15.994  1.00 20.21           C  
ATOM    467  CD1 LEU A  58      16.456  -4.405  16.802  1.00 18.86           C  
ATOM    468  CD2 LEU A  58      17.967  -4.762  14.833  1.00 21.78           C  
ATOM    469  N   ASN A  59      21.229  -8.024  17.119  1.00 19.82           N  
ATOM    470  CA  ASN A  59      22.120  -8.620  18.102  1.00 22.43           C  
ATOM    471  C   ASN A  59      22.635  -7.463  18.942  1.00 23.32           C  
ATOM    472  O   ASN A  59      23.530  -6.724  18.531  1.00 24.60           O  
ATOM    473  CB  ASN A  59      23.260  -9.360  17.404  1.00 22.95           C  
ATOM    474  CG  ASN A  59      22.775 -10.596  16.678  1.00 23.67           C  
ATOM    475  OD1 ASN A  59      22.062 -11.420  17.254  1.00 26.26           O  
ATOM    476  ND2 ASN A  59      23.158 -10.738  15.412  1.00 25.99           N  
ATOM    477  N   ILE A  60      22.031  -7.312  20.117  1.00 21.77           N  
ATOM    478  CA  ILE A  60      22.339  -6.235  21.040  1.00 22.49           C  
ATOM    479  C   ILE A  60      23.231  -6.698  22.185  1.00 24.56           C  
ATOM    480  O   ILE A  60      22.830  -7.522  23.009  1.00 23.00           O  
ATOM    481  CB  ILE A  60      21.018  -5.645  21.587  1.00 21.76           C  
ATOM    482  CG1 ILE A  60      20.172  -5.143  20.411  1.00 22.90           C  
ATOM    483  CG2 ILE A  60      21.301  -4.522  22.571  1.00 20.81           C  
ATOM    484  CD1 ILE A  60      18.782  -4.679  20.791  1.00 21.06           C  
ATOM    485  N   LYS A  61      24.446  -6.155  22.231  1.00 25.55           N  
ATOM    486  CA  LYS A  61      25.419  -6.515  23.258  1.00 25.14           C  
ATOM    487  C   LYS A  61      25.619  -5.415  24.294  1.00 25.09           C  
ATOM    488  O   LYS A  61      25.901  -4.267  23.948  1.00 25.37           O  
ATOM    489  CB  LYS A  61      26.763  -6.847  22.599  1.00 29.74           C  
ATOM    490  CG  LYS A  61      27.921  -7.038  23.575  1.00 34.25           C  
ATOM    491  CD  LYS A  61      27.725  -8.243  24.491  1.00 39.57           C  
ATOM    492  CE  LYS A  61      28.903  -8.390  25.449  1.00 42.01           C  
ATOM    493  NZ  LYS A  61      28.851  -9.643  26.255  1.00 45.22           N  
ATOM    494  N   PHE A  62      25.480  -5.774  25.567  1.00 23.73           N  
ATOM    495  CA  PHE A  62      25.659  -4.810  26.647  1.00 25.66           C  
ATOM    496  C   PHE A  62      27.091  -4.874  27.170  1.00 27.99           C  
ATOM    497  O   PHE A  62      27.671  -5.952  27.289  1.00 26.47           O  
ATOM    498  CB  PHE A  62      24.668  -5.080  27.781  1.00 25.34           C  
ATOM    499  CG  PHE A  62      23.230  -4.874  27.387  1.00 24.37           C  
ATOM    500  CD1 PHE A  62      22.575  -5.802  26.584  1.00 24.81           C  
ATOM    501  CD2 PHE A  62      22.539  -3.739  27.804  1.00 24.95           C  
ATOM    502  CE1 PHE A  62      21.243  -5.602  26.202  1.00 23.74           C  
ATOM    503  CE2 PHE A  62      21.209  -3.531  27.426  1.00 22.73           C  
ATOM    504  CZ  PHE A  62      20.563  -4.465  26.625  1.00 23.89           C  
ATOM    505  N   ALA A  63      27.650  -3.711  27.483  1.00 30.43           N  
ATOM    506  CA  ALA A  63      29.023  -3.628  27.964  1.00 35.45           C  
ATOM    507  C   ALA A  63      29.145  -3.731  29.478  1.00 38.41           C  
ATOM    508  O   ALA A  63      28.150  -3.890  30.190  1.00 36.72           O  
ATOM    509  CB  ALA A  63      29.652  -2.329  27.483  1.00 36.45           C  
ATOM    510  N   GLY A  64      30.381  -3.645  29.959  1.00 41.22           N  
ATOM    511  CA  GLY A  64      30.635  -3.712  31.386  1.00 48.36           C  
ATOM    512  C   GLY A  64      31.344  -4.981  31.813  1.00 50.10           C  
ATOM    513  O   GLY A  64      30.831  -5.665  32.726  1.00 53.63           O  
ATOM    514  OXT GLY A  64      32.412  -5.290  31.244  1.00 52.95           O  
TER     515      GLY A  64                                                                       
MASTER      317    0    0    9   12    0    0    6 1787    3    0   18          
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.