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***  TOXIN (HEMOLYTIC POLYPEPTIDE) 04-OCT-90 2MLT  ***

elNémo ID: 210723142520129552

Job options:

ID        	=	 210723142520129552
JOBID     	=	 TOXIN (HEMOLYTIC POLYPEPTIDE) 04-OCT-90 2MLT
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TOXIN (HEMOLYTIC POLYPEPTIDE)           04-OCT-90   2MLT              
TITLE     MELITTIN                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MELITTIN;                                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: APIS MELLIFERA;                                 
SOURCE   3 ORGANISM_COMMON: HONEY BEE;                                          
SOURCE   4 ORGANISM_TAXID: 7460                                                 
KEYWDS    TOXIN (HEMOLYTIC POLYPEPTIDE)                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.EISENBERG,M.GRIBSKOV,T.C.TERWILLIGER                                
REVDAT   5   16-NOV-11 2MLT    1       HETATM                                   
REVDAT   4   13-JUL-11 2MLT    1       VERSN                                    
REVDAT   3   24-FEB-09 2MLT    1       VERSN                                    
REVDAT   2   15-JUL-92 2MLT    1       SPRSDE                                   
REVDAT   1   15-OCT-90 2MLT    0                                                
SPRSDE     15-OCT-90 2MLT      1MLT                                             
JRNL        AUTH   M.GRIBSKOV,L.WESSON,D.EISENBERG                              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.C.TERWILLIGER,D.EISENBERG                                  
REMARK   1  TITL   THE STRUCTURE OF MELITTIN. I. STRUCTURE DETERMINATION AND    
REMARK   1  TITL 2 PARTIAL REFINEMENT.                                          
REMARK   1  REF    J.BIOL.CHEM.                  V. 257  6010 1982              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   T.C.TERWILLIGER,D.EISENBERG                                  
REMARK   1  TITL   THE STRUCTURE OF MELITTIN. II. INTERPRETATION OF THE         
REMARK   1  TITL 2 STRUCTURE                                                    
REMARK   1  REF    J.BIOL.CHEM.                  V. 257  6016 1982              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   D.ANDERSON,T.C.TERWILLIGER,W.WICKNER,D.EISENBERG             
REMARK   1  TITL   MELITTIN FORMS CRYSTALS WHICH ARE SUITABLE FOR HIGH          
REMARK   1  TITL 2 RESOLUTION X-RAY STRUCTURAL ANALYSIS AND WHICH REVEAL A      
REMARK   1  TITL 3 MOLECULAR 2-FOLD AXIS OF SYMMETRY                            
REMARK   1  REF    J.BIOL.CHEM.                  V. 255  2578 1980              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROFFT                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON,FINZEL                           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 137                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 402                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 23                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.026 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.046 ; 0.030               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.073 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.016 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.244 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.189 ; 0.500               
REMARK   3    MULTIPLE TORSION                (A) : 0.209 ; 0.500               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : 0.544 ; 0.500               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 2.079 ; 1.500               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 2.913 ; 2.000               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 4.043 ; 2.000               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 6.281 ; 3.000               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2MLT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       21.10550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       21.10550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       30.41600            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       19.14650            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       30.41600            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       19.14650            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       21.10550            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       30.41600            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       19.14650            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       21.10550            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       30.41600            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       19.14650            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 5220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6280 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   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       42.21100            
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 A  36  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    VAL A   5   CA  -  CB  -  CG2 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    LEU A   6   CB  -  CA  -  C   ANGL. DEV. =  11.6 DEGREES          
REMARK 500    ARG A  22   NE  -  CZ  -  NH1 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    ARG A  24   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    GLN A  26   CA  -  C   -  O   ANGL. DEV. = -14.7 DEGREES          
REMARK 500    ARG B  22   CD  -  NE  -  CZ  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    GLN B  25   CB  -  CG  -  CD  ANGL. DEV. =  18.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  11      -41.83   -130.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B  34        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH B  35        DISTANCE = 14.69 ANGSTROMS                       
REMARK 525    HOH B  38        DISTANCE =  8.69 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 28                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 29                  
DBREF  2MLT A    1    26  UNP    P01501   MEL_APIME       44     69             
DBREF  2MLT B    1    26  UNP    P01501   MEL_APIME       44     69             
SEQRES   1 A   27  GLY ILE GLY ALA VAL LEU LYS VAL LEU THR THR GLY LEU          
SEQRES   2 A   27  PRO ALA LEU ILE SER TRP ILE LYS ARG LYS ARG GLN GLN          
SEQRES   3 A   27  NH2                                                          
SEQRES   1 B   27  GLY ILE GLY ALA VAL LEU LYS VAL LEU THR THR GLY LEU          
SEQRES   2 B   27  PRO ALA LEU ILE SER TRP ILE LYS ARG LYS ARG GLN GLN          
SEQRES   3 B   27  NH2                                                          
HET    NH2  A  27       1                                                       
HET    NH2  B  27       1                                                       
HET    SO4  B  28       5                                                       
HET    SO4  B  29       5                                                       
HETNAM     NH2 AMINO GROUP                                                      
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  NH2    2(H2 N)                                                      
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  HOH   *23(H2 O)                                                     
HELIX    1  AA GLY A    1  THR A   11  1                                  11    
HELIX    2  BA PRO A   14  GLN A   26  1                                  13    
HELIX    3  AB GLY B    1  THR B   11  1                                  11    
HELIX    4  BB PRO B   14  GLN B   26  1                                  13    
LINK         C   GLN A  26                 N   NH2 A  27     1555   1555  1.32  
LINK         C   GLN B  26                 N   NH2 B  27     1555   1555  1.30  
SITE     1 AC1  4 ILE A   2  GLY A   3  TRP A  19  ARG B  24                    
SITE     1 AC2  7 ARG A  24  ILE B   2  GLY B   3  TRP B  19                    
SITE     2 AC2  7 LYS B  23  ARG B  24  HOH B  31                               
CRYST1   60.832   38.293   42.211  90.00  90.00  90.00 C 2 2 21     16          
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      0.016439  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.026114  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023691        0.00000                         
MTRIX1   1 -0.996310 -0.033870 -0.078870       71.25100    1                    
MTRIX2   1  0.048050 -0.981470 -0.185470        2.71100    1                    
MTRIX3   1 -0.071130 -0.188580  0.979480        2.05300    1                    
ATOM      1  N   GLY A   1      42.375 -12.180  24.780  1.00 35.31           N  
ATOM      2  CA  GLY A   1      43.603 -11.488  24.325  1.00 35.57           C  
ATOM      3  C   GLY A   1      43.288 -10.171  23.615  1.00 34.64           C  
ATOM      4  O   GLY A   1      42.111  -9.896  23.277  1.00 35.82           O  
ATOM      5  N   ILE A   2      44.323  -9.391  23.299  1.00 32.23           N  
ATOM      6  CA  ILE A   2      44.200  -8.183  22.475  1.00 27.55           C  
ATOM      7  C   ILE A   2      43.750  -8.629  21.119  1.00 24.92           C  
ATOM      8  O   ILE A   2      43.068  -7.904  20.409  1.00 23.73           O  
ATOM      9  CB  ILE A   2      45.525  -7.320  22.425  1.00 30.10           C  
ATOM     10  CG1 ILE A   2      45.924  -6.837  23.820  1.00 29.64           C  
ATOM     11  CG2 ILE A   2      45.555  -6.173  21.386  1.00 30.54           C  
ATOM     12  CD1 ILE A   2      44.837  -6.338  24.762  1.00 32.44           C  
ATOM     13  N   GLY A   3      44.161  -9.867  20.749  1.00 22.69           N  
ATOM     14  CA  GLY A   3      43.999 -10.264  19.329  1.00 21.05           C  
ATOM     15  C   GLY A   3      42.433 -10.405  19.166  1.00 22.08           C  
ATOM     16  O   GLY A   3      41.912 -10.061  18.096  1.00 22.86           O  
ATOM     17  N   ALA A   4      41.862 -10.961  20.191  1.00 21.60           N  
ATOM     18  CA  ALA A   4      40.378 -11.260  20.106  1.00 21.80           C  
ATOM     19  C   ALA A   4      39.584  -9.950  20.087  1.00 21.67           C  
ATOM     20  O   ALA A   4      38.676  -9.747  19.278  1.00 22.21           O  
ATOM     21  CB  ALA A   4      40.061 -12.080  21.350  1.00 22.97           C  
ATOM     22  N   VAL A   5      39.936  -9.001  20.956  1.00 22.13           N  
ATOM     23  CA  VAL A   5      39.355  -7.658  21.083  1.00 19.34           C  
ATOM     24  C   VAL A   5      39.536  -6.896  19.795  1.00 18.81           C  
ATOM     25  O   VAL A   5      38.626  -6.314  19.126  1.00 17.22           O  
ATOM     26  CB  VAL A   5      39.843  -6.933  22.338  1.00 20.40           C  
ATOM     27  CG1 VAL A   5      39.237  -5.519  22.413  1.00 23.06           C  
ATOM     28  CG2 VAL A   5      39.745  -7.587  23.653  1.00 21.67           C  
ATOM     29  N   LEU A   6      40.752  -7.021  19.222  1.00 16.05           N  
ATOM     30  CA  LEU A   6      41.062  -6.432  17.957  1.00 17.59           C  
ATOM     31  C   LEU A   6      40.230  -6.935  16.870  1.00 20.01           C  
ATOM     32  O   LEU A   6      39.649  -6.121  16.029  1.00 21.90           O  
ATOM     33  CB  LEU A   6      42.627  -6.461  17.880  1.00 24.58           C  
ATOM     34  CG  LEU A   6      43.125  -6.023  16.524  1.00 23.91           C  
ATOM     35  CD1 LEU A   6      42.706  -4.584  16.210  1.00 27.44           C  
ATOM     36  CD2 LEU A   6      44.669  -6.152  16.638  1.00 29.31           C  
ATOM     37  N   LYS A   7      39.981  -8.229  16.721  1.00 19.83           N  
ATOM     38  CA  LYS A   7      39.079  -8.646  15.636  1.00 22.55           C  
ATOM     39  C   LYS A   7      37.648  -8.063  15.784  1.00 19.04           C  
ATOM     40  O   LYS A   7      37.031  -7.839  14.731  1.00 21.18           O  
ATOM     41  CB  LYS A   7      38.854 -10.176  15.616  1.00 27.62           C  
ATOM     42  CG  LYS A   7      40.011 -10.993  15.144  1.00 40.15           C  
ATOM     43  CD  LYS A   7      39.691 -12.487  15.325  1.00 47.84           C  
ATOM     44  CE  LYS A   7      40.599 -13.394  14.493  1.00 53.11           C  
ATOM     45  NZ  LYS A   7      39.966 -14.755  14.319  1.00 55.47           N  
ATOM     46  N   VAL A   8      37.111  -7.988  16.981  1.00 19.69           N  
ATOM     47  CA  VAL A   8      35.792  -7.369  17.211  1.00 20.52           C  
ATOM     48  C   VAL A   8      35.776  -5.881  16.885  1.00 20.31           C  
ATOM     49  O   VAL A   8      34.775  -5.402  16.257  1.00 20.12           O  
ATOM     50  CB  VAL A   8      35.113  -7.600  18.562  1.00 23.09           C  
ATOM     51  CG1 VAL A   8      34.774  -9.045  18.851  1.00 24.22           C  
ATOM     52  CG2 VAL A   8      35.769  -6.970  19.726  1.00 27.95           C  
ATOM     53  N   LEU A   9      36.860  -5.176  17.216  1.00 19.55           N  
ATOM     54  CA  LEU A   9      36.899  -3.759  16.725  1.00 16.83           C  
ATOM     55  C   LEU A   9      36.778  -3.644  15.254  1.00 19.11           C  
ATOM     56  O   LEU A   9      36.328  -2.551  14.694  1.00 19.69           O  
ATOM     57  CB  LEU A   9      38.227  -3.088  17.147  1.00 16.57           C  
ATOM     58  CG  LEU A   9      38.462  -3.091  18.615  1.00 18.69           C  
ATOM     59  CD1 LEU A   9      39.783  -2.288  18.873  1.00 24.09           C  
ATOM     60  CD2 LEU A   9      37.265  -2.535  19.351  1.00 22.17           C  
ATOM     61  N   THR A  10      37.320  -4.627  14.530  1.00 19.39           N  
ATOM     62  CA  THR A  10      37.338  -4.508  13.084  1.00 19.41           C  
ATOM     63  C   THR A  10      36.072  -5.022  12.458  1.00 21.08           C  
ATOM     64  O   THR A  10      35.694  -4.554  11.333  1.00 21.48           O  
ATOM     65  CB  THR A  10      38.687  -5.179  12.486  1.00 24.07           C  
ATOM     66  OG1 THR A  10      38.285  -6.538  12.354  1.00 31.20           O  
ATOM     67  CG2 THR A  10      39.877  -5.049  13.451  1.00 20.75           C  
ATOM     68  N   THR A  11      35.315  -5.870  13.113  1.00 21.12           N  
ATOM     69  CA  THR A  11      34.132  -6.405  12.343  1.00 24.14           C  
ATOM     70  C   THR A  11      32.874  -6.299  13.140  1.00 24.13           C  
ATOM     71  O   THR A  11      31.823  -5.889  12.630  1.00 27.78           O  
ATOM     72  CB  THR A  11      34.462  -7.925  11.935  1.00 27.78           C  
ATOM     73  OG1 THR A  11      34.702  -8.591  13.199  1.00 31.22           O  
ATOM     74  CG2 THR A  11      35.695  -7.959  11.047  1.00 30.31           C  
ATOM     75  N   GLY A  12      32.918  -6.606  14.420  1.00 23.00           N  
ATOM     76  CA  GLY A  12      31.584  -6.595  15.140  1.00 24.17           C  
ATOM     77  C   GLY A  12      31.264  -5.168  15.584  1.00 24.45           C  
ATOM     78  O   GLY A  12      30.060  -4.914  15.603  1.00 23.79           O  
ATOM     79  N   LEU A  13      32.195  -4.276  15.948  1.00 22.05           N  
ATOM     80  CA  LEU A  13      31.923  -2.919  16.364  1.00 23.24           C  
ATOM     81  C   LEU A  13      31.251  -2.004  15.324  1.00 21.24           C  
ATOM     82  O   LEU A  13      30.232  -1.308  15.679  1.00 23.02           O  
ATOM     83  CB  LEU A  13      33.146  -2.183  17.008  1.00 25.55           C  
ATOM     84  CG  LEU A  13      32.913  -1.523  18.351  1.00 27.01           C  
ATOM     85  CD1 LEU A  13      33.999  -0.517  18.760  1.00 27.53           C  
ATOM     86  CD2 LEU A  13      31.587  -0.842  18.531  1.00 24.54           C  
ATOM     87  N   PRO A  14      31.689  -1.979  14.106  1.00 17.38           N  
ATOM     88  CA  PRO A  14      31.026  -1.278  13.030  1.00 17.52           C  
ATOM     89  C   PRO A  14      29.521  -1.670  12.857  1.00 18.98           C  
ATOM     90  O   PRO A  14      28.657  -0.801  12.744  1.00 16.75           O  
ATOM     91  CB  PRO A  14      31.845  -1.614  11.816  1.00 17.80           C  
ATOM     92  CG  PRO A  14      33.118  -2.205  12.303  1.00 18.05           C  
ATOM     93  CD  PRO A  14      33.098  -2.363  13.769  1.00 17.96           C  
ATOM     94  N   ALA A  15      29.207  -2.952  12.868  1.00 16.39           N  
ATOM     95  CA  ALA A  15      27.822  -3.418  12.724  1.00 17.10           C  
ATOM     96  C   ALA A  15      27.023  -3.016  13.951  1.00 16.98           C  
ATOM     97  O   ALA A  15      25.872  -2.551  13.769  1.00 16.78           O  
ATOM     98  CB  ALA A  15      27.741  -4.906  12.502  1.00 19.58           C  
ATOM     99  N   LEU A  16      27.570  -3.117  15.127  1.00 15.97           N  
ATOM    100  CA  LEU A  16      26.958  -2.649  16.351  1.00 18.20           C  
ATOM    101  C   LEU A  16      26.614  -1.169  16.344  1.00 20.28           C  
ATOM    102  O   LEU A  16      25.599  -0.734  16.933  1.00 18.32           O  
ATOM    103  CB  LEU A  16      27.811  -3.027  17.542  1.00 19.70           C  
ATOM    104  CG  LEU A  16      27.384  -2.550  18.921  1.00 22.23           C  
ATOM    105  CD1 LEU A  16      26.031  -3.234  19.257  1.00 27.80           C  
ATOM    106  CD2 LEU A  16      28.445  -2.970  19.933  1.00 21.91           C  
ATOM    107  N   ILE A  17      27.514  -0.365  15.791  1.00 20.97           N  
ATOM    108  CA  ILE A  17      27.343   1.056  15.618  1.00 20.41           C  
ATOM    109  C   ILE A  17      26.081   1.392  14.758  1.00 18.17           C  
ATOM    110  O   ILE A  17      25.380   2.240  15.282  1.00 16.46           O  
ATOM    111  CB  ILE A  17      28.579   1.847  15.132  1.00 21.10           C  
ATOM    112  CG1 ILE A  17      29.586   1.858  16.352  1.00 25.66           C  
ATOM    113  CG2 ILE A  17      28.268   3.288  14.691  1.00 22.04           C  
ATOM    114  CD1 ILE A  17      30.856   2.696  16.161  1.00 27.00           C  
ATOM    115  N   SER A  18      25.930   0.759  13.657  1.00 16.97           N  
ATOM    116  CA  SER A  18      24.825   0.827  12.744  1.00 19.98           C  
ATOM    117  C   SER A  18      23.499   0.405  13.438  1.00 18.89           C  
ATOM    118  O   SER A  18      22.557   1.165  13.352  1.00 18.37           O  
ATOM    119  CB  SER A  18      25.076   0.039  11.491  1.00 20.39           C  
ATOM    120  OG  SER A  18      23.902   0.046  10.670  1.00 23.87           O  
ATOM    121  N   TRP A  19      23.512  -0.661  14.161  1.00 17.71           N  
ATOM    122  CA  TRP A  19      22.492  -1.085  15.081  1.00 15.72           C  
ATOM    123  C   TRP A  19      22.083   0.004  16.012  1.00 18.02           C  
ATOM    124  O   TRP A  19      20.820   0.244  16.160  1.00 16.93           O  
ATOM    125  CB  TRP A  19      22.854  -2.410  15.767  1.00 15.59           C  
ATOM    126  CG  TRP A  19      21.803  -2.993  16.678  1.00 17.94           C  
ATOM    127  CD1 TRP A  19      20.917  -3.950  16.210  1.00 18.03           C  
ATOM    128  CD2 TRP A  19      21.448  -2.745  18.041  1.00 16.03           C  
ATOM    129  NE1 TRP A  19      20.060  -4.304  17.222  1.00 21.28           N  
ATOM    130  CE2 TRP A  19      20.357  -3.624  18.372  1.00 20.45           C  
ATOM    131  CE3 TRP A  19      21.879  -1.892  19.048  1.00 14.41           C  
ATOM    132  CZ2 TRP A  19      19.784  -3.690  19.612  1.00 17.15           C  
ATOM    133  CZ3 TRP A  19      21.292  -1.950  20.288  1.00 17.24           C  
ATOM    134  CH2 TRP A  19      20.230  -2.805  20.601  1.00 15.13           C  
ATOM    135  N   ILE A  20      22.930   0.594  16.823  1.00 14.82           N  
ATOM    136  CA  ILE A  20      22.628   1.633  17.766  1.00 15.67           C  
ATOM    137  C   ILE A  20      21.917   2.819  17.080  1.00 17.51           C  
ATOM    138  O   ILE A  20      20.942   3.365  17.655  1.00 17.70           O  
ATOM    139  CB  ILE A  20      23.902   2.192  18.499  1.00 16.25           C  
ATOM    140  CG1 ILE A  20      24.481   0.986  19.363  1.00 15.50           C  
ATOM    141  CG2 ILE A  20      23.599   3.421  19.390  1.00 14.54           C  
ATOM    142  CD1 ILE A  20      26.033   1.304  19.637  1.00 18.18           C  
ATOM    143  N   LYS A  21      22.464   3.177  15.957  1.00 16.61           N  
ATOM    144  CA  LYS A  21      21.888   4.236  15.157  1.00 19.84           C  
ATOM    145  C   LYS A  21      20.436   3.910  14.752  1.00 21.02           C  
ATOM    146  O   LYS A  21      19.685   4.899  14.971  1.00 22.80           O  
ATOM    147  CB  LYS A  21      22.699   4.646  13.935  1.00 16.73           C  
ATOM    148  CG  LYS A  21      23.944   5.416  14.471  1.00 22.19           C  
ATOM    149  CD  LYS A  21      24.919   5.669  13.300  1.00 25.86           C  
ATOM    150  CE  LYS A  21      26.173   6.287  13.908  1.00 32.91           C  
ATOM    151  NZ  LYS A  21      27.199   6.564  12.863  1.00 39.11           N  
ATOM    152  N   ARG A  22      20.075   2.728  14.351  1.00 19.18           N  
ATOM    153  CA  ARG A  22      18.740   2.273  14.020  1.00 20.38           C  
ATOM    154  C   ARG A  22      17.807   2.365  15.177  1.00 22.46           C  
ATOM    155  O   ARG A  22      16.648   2.899  15.096  1.00 23.24           O  
ATOM    156  CB  ARG A  22      18.733   0.860  13.418  1.00 22.73           C  
ATOM    157  CG  ARG A  22      19.309   0.956  12.004  1.00 22.29           C  
ATOM    158  CD  ARG A  22      19.117  -0.300  11.254  1.00 25.78           C  
ATOM    159  NE  ARG A  22      19.382  -1.562  11.991  1.00 28.94           N  
ATOM    160  CZ  ARG A  22      20.624  -2.104  11.889  1.00 33.77           C  
ATOM    161  NH1 ARG A  22      21.664  -1.554  11.252  1.00 31.21           N  
ATOM    162  NH2 ARG A  22      20.870  -3.271  12.498  1.00 33.11           N  
ATOM    163  N   LYS A  23      18.257   1.937  16.323  1.00 20.49           N  
ATOM    164  CA  LYS A  23      17.500   1.928  17.550  1.00 22.62           C  
ATOM    165  C   LYS A  23      17.216   3.361  18.100  1.00 25.47           C  
ATOM    166  O   LYS A  23      16.204   3.554  18.811  1.00 24.62           O  
ATOM    167  CB  LYS A  23      18.257   1.128  18.589  1.00 24.16           C  
ATOM    168  CG  LYS A  23      17.979  -0.388  18.463  1.00 31.03           C  
ATOM    169  CD  LYS A  23      16.858  -0.657  19.514  1.00 38.52           C  
ATOM    170  CE  LYS A  23      16.197  -1.986  19.278  1.00 44.05           C  
ATOM    171  NZ  LYS A  23      15.412  -2.493  20.477  1.00 48.30           N  
ATOM    172  N   ARG A  24      18.155   4.268  17.844  1.00 23.99           N  
ATOM    173  CA  ARG A  24      18.059   5.674  18.276  1.00 27.11           C  
ATOM    174  C   ARG A  24      16.996   6.355  17.441  1.00 28.34           C  
ATOM    175  O   ARG A  24      16.224   7.166  18.029  1.00 31.82           O  
ATOM    176  CB  ARG A  24      19.446   6.379  18.188  1.00 22.24           C  
ATOM    177  CG  ARG A  24      20.182   6.236  19.542  1.00 20.01           C  
ATOM    178  CD  ARG A  24      21.577   6.742  19.433  1.00 25.00           C  
ATOM    179  NE  ARG A  24      21.715   8.115  18.950  1.00 24.24           N  
ATOM    180  CZ  ARG A  24      21.745   9.136  19.837  1.00 22.72           C  
ATOM    181  NH1 ARG A  24      21.508   8.848  21.086  1.00 24.10           N  
ATOM    182  NH2 ARG A  24      22.134  10.375  19.512  1.00 24.09           N  
ATOM    183  N   GLN A  25      16.889   6.080  16.192  1.00 29.90           N  
ATOM    184  CA  GLN A  25      15.836   6.730  15.339  1.00 37.50           C  
ATOM    185  C   GLN A  25      14.463   6.162  15.554  1.00 39.92           C  
ATOM    186  O   GLN A  25      13.435   6.799  15.227  1.00 42.39           O  
ATOM    187  CB  GLN A  25      16.283   6.713  13.874  1.00 40.82           C  
ATOM    188  CG  GLN A  25      17.607   7.505  13.800  1.00 46.91           C  
ATOM    189  CD  GLN A  25      18.413   7.205  12.564  1.00 50.89           C  
ATOM    190  OE1 GLN A  25      19.596   7.559  12.477  1.00 54.23           O  
ATOM    191  NE2 GLN A  25      17.757   6.512  11.624  1.00 51.61           N  
ATOM    192  N   GLN A  26      14.363   4.945  16.064  1.00 43.06           N  
ATOM    193  CA  GLN A  26      13.132   4.360  16.583  1.00 46.66           C  
ATOM    194  C   GLN A  26      12.618   5.071  17.837  1.00 48.00           C  
ATOM    195  O   GLN A  26      11.409   5.344  17.597  1.00 50.85           O  
ATOM    196  CB  GLN A  26      13.144   2.874  16.862  1.00 49.14           C  
ATOM    197  CG  GLN A  26      13.166   1.972  15.625  1.00 54.49           C  
ATOM    198  CD  GLN A  26      13.506   0.551  16.116  1.00 58.10           C  
ATOM    199  OE1 GLN A  26      13.083   0.180  17.239  1.00 59.27           O  
ATOM    200  NE2 GLN A  26      14.304  -0.117  15.290  1.00 57.61           N  
HETATM  201  N   NH2 A  27      13.279   5.297  18.956  1.00 48.71           N  
TER     202      NH2 A  27                                                      
ATOM    203  N   GLY B   1      26.991  12.460  25.488  1.00 32.45           N  
ATOM    204  CA  GLY B   1      26.196  11.215  25.772  1.00 31.28           C  
ATOM    205  C   GLY B   1      26.428  10.365  24.501  1.00 31.22           C  
ATOM    206  O   GLY B   1      27.472  10.631  23.867  1.00 29.98           O  
ATOM    207  N   ILE B   2      25.518   9.469  24.174  1.00 28.85           N  
ATOM    208  CA  ILE B   2      25.695   8.457  23.127  1.00 26.61           C  
ATOM    209  C   ILE B   2      26.147   9.009  21.812  1.00 24.79           C  
ATOM    210  O   ILE B   2      27.068   8.454  21.126  1.00 23.51           O  
ATOM    211  CB  ILE B   2      24.434   7.537  22.864  1.00 28.06           C  
ATOM    212  CG1 ILE B   2      23.912   6.874  24.136  1.00 32.06           C  
ATOM    213  CG2 ILE B   2      24.666   6.469  21.761  1.00 26.41           C  
ATOM    214  CD1 ILE B   2      24.958   6.136  24.975  1.00 33.88           C  
ATOM    215  N   GLY B   3      25.522  10.110  21.347  1.00 24.09           N  
ATOM    216  CA  GLY B   3      25.775  10.608  19.984  1.00 20.83           C  
ATOM    217  C   GLY B   3      27.283  11.062  19.756  1.00 19.38           C  
ATOM    218  O   GLY B   3      27.758  10.922  18.648  1.00 20.22           O  
ATOM    219  N   ALA B   4      27.870  11.673  20.705  1.00 19.33           N  
ATOM    220  CA  ALA B   4      29.261  12.192  20.662  1.00 22.19           C  
ATOM    221  C   ALA B   4      30.169  10.886  20.673  1.00 20.97           C  
ATOM    222  O   ALA B   4      31.002  10.887  19.804  1.00 27.69           O  
ATOM    223  CB  ALA B   4      29.492  12.908  21.991  1.00 20.68           C  
ATOM    224  N   VAL B   5      29.883   9.951  21.550  1.00 21.99           N  
ATOM    225  CA  VAL B   5      30.560   8.605  21.561  1.00 20.43           C  
ATOM    226  C   VAL B   5      30.579   7.954  20.234  1.00 19.18           C  
ATOM    227  O   VAL B   5      31.601   7.654  19.529  1.00 18.23           O  
ATOM    228  CB  VAL B   5      29.986   7.705  22.706  1.00 22.41           C  
ATOM    229  CG1 VAL B   5      30.651   6.314  22.587  1.00 20.25           C  
ATOM    230  CG2 VAL B   5      30.132   8.211  24.092  1.00 19.72           C  
ATOM    231  N   LEU B   6      29.331   7.820  19.609  1.00 13.46           N  
ATOM    232  CA  LEU B   6      29.339   7.258  18.306  1.00 15.03           C  
ATOM    233  C   LEU B   6      30.192   8.006  17.351  1.00 17.62           C  
ATOM    234  O   LEU B   6      30.715   7.431  16.369  1.00 18.19           O  
ATOM    235  CB  LEU B   6      27.869   7.237  17.745  1.00 17.96           C  
ATOM    236  CG  LEU B   6      26.957   6.450  18.727  1.00 18.65           C  
ATOM    237  CD1 LEU B   6      25.498   6.501  18.145  1.00 20.72           C  
ATOM    238  CD2 LEU B   6      27.440   4.996  18.656  1.00 19.24           C  
ATOM    239  N   LYS B   7      30.129   9.328  17.515  1.00 18.17           N  
ATOM    240  CA  LYS B   7      30.789  10.122  16.413  1.00 20.35           C  
ATOM    241  C   LYS B   7      32.344   9.943  16.549  1.00 19.60           C  
ATOM    242  O   LYS B   7      33.030   9.923  15.516  1.00 20.24           O  
ATOM    243  CB  LYS B   7      30.507  11.588  16.732  1.00 26.90           C  
ATOM    244  CG  LYS B   7      30.878  12.436  15.490  1.00 34.77           C  
ATOM    245  CD  LYS B   7      30.876  13.915  15.970  1.00 43.62           C  
ATOM    246  CE  LYS B   7      30.843  14.830  14.734  1.00 48.81           C  
ATOM    247  NZ  LYS B   7      30.356  16.214  15.122  1.00 53.62           N  
ATOM    248  N   VAL B   8      32.749   9.846  17.787  1.00 20.60           N  
ATOM    249  CA  VAL B   8      34.238   9.637  18.027  1.00 23.38           C  
ATOM    250  C   VAL B   8      34.622   8.283  17.475  1.00 22.25           C  
ATOM    251  O   VAL B   8      35.704   8.215  16.813  1.00 25.53           O  
ATOM    252  CB  VAL B   8      34.638   9.946  19.449  1.00 23.61           C  
ATOM    253  CG1 VAL B   8      36.085   9.410  19.742  1.00 28.23           C  
ATOM    254  CG2 VAL B   8      34.614  11.408  19.841  1.00 25.53           C  
ATOM    255  N   LEU B   9      33.880   7.234  17.693  1.00 21.03           N  
ATOM    256  CA  LEU B   9      34.150   5.918  17.183  1.00 20.22           C  
ATOM    257  C   LEU B   9      34.207   5.848  15.710  1.00 22.83           C  
ATOM    258  O   LEU B   9      35.162   5.179  15.183  1.00 23.58           O  
ATOM    259  CB  LEU B   9      33.288   4.796  17.839  1.00 18.69           C  
ATOM    260  CG  LEU B   9      33.288   4.714  19.315  1.00 20.80           C  
ATOM    261  CD1 LEU B   9      32.271   3.699  19.895  1.00 23.06           C  
ATOM    262  CD2 LEU B   9      34.691   4.315  19.813  1.00 22.83           C  
ATOM    263  N   THR B  10      33.259   6.407  14.989  1.00 21.66           N  
ATOM    264  CA  THR B  10      33.081   6.344  13.562  1.00 23.85           C  
ATOM    265  C   THR B  10      34.316   6.945  12.911  1.00 24.74           C  
ATOM    266  O   THR B  10      34.780   6.421  11.899  1.00 24.91           O  
ATOM    267  CB  THR B  10      31.815   7.271  13.137  1.00 26.65           C  
ATOM    268  OG1 THR B  10      30.705   6.522  13.750  1.00 32.91           O  
ATOM    269  CG2 THR B  10      31.689   7.389  11.657  1.00 29.78           C  
ATOM    270  N   THR B  11      34.731   8.059  13.555  1.00 24.75           N  
ATOM    271  CA  THR B  11      35.833   8.796  12.896  1.00 26.41           C  
ATOM    272  C   THR B  11      37.184   8.189  13.384  1.00 25.22           C  
ATOM    273  O   THR B  11      38.145   8.224  12.597  1.00 26.25           O  
ATOM    274  CB  THR B  11      35.923  10.328  13.252  1.00 32.59           C  
ATOM    275  OG1 THR B  11      34.599  10.871  13.482  1.00 38.37           O  
ATOM    276  CG2 THR B  11      36.692  11.118  12.167  1.00 35.60           C  
ATOM    277  N   GLY B  12      37.201   7.812  14.632  1.00 22.04           N  
ATOM    278  CA  GLY B  12      38.482   7.602  15.318  1.00 22.53           C  
ATOM    279  C   GLY B  12      38.861   6.145  15.351  1.00 22.17           C  
ATOM    280  O   GLY B  12      40.092   5.870  15.453  1.00 20.26           O  
ATOM    281  N   LEU B  13      37.903   5.244  15.252  1.00 20.94           N  
ATOM    282  CA  LEU B  13      38.268   3.810  15.278  1.00 23.61           C  
ATOM    283  C   LEU B  13      39.152   3.341  14.158  1.00 21.75           C  
ATOM    284  O   LEU B  13      40.108   2.585  14.527  1.00 26.77           O  
ATOM    285  CB  LEU B  13      37.051   2.957  15.502  1.00 27.83           C  
ATOM    286  CG  LEU B  13      37.111   1.608  16.159  1.00 33.51           C  
ATOM    287  CD1 LEU B  13      37.653   1.658  17.581  1.00 33.01           C  
ATOM    288  CD2 LEU B  13      35.605   1.185  16.218  1.00 37.40           C  
ATOM    289  N   PRO B  14      39.058   3.664  12.901  1.00 21.06           N  
ATOM    290  CA  PRO B  14      39.945   3.149  11.872  1.00 20.15           C  
ATOM    291  C   PRO B  14      41.412   3.421  12.212  1.00 23.00           C  
ATOM    292  O   PRO B  14      42.252   2.506  12.061  1.00 20.49           O  
ATOM    293  CB  PRO B  14      39.436   3.687  10.568  1.00 21.45           C  
ATOM    294  CG  PRO B  14      38.010   4.121  10.875  1.00 20.47           C  
ATOM    295  CD  PRO B  14      37.874   4.382  12.318  1.00 20.25           C  
ATOM    296  N   ALA B  15      41.741   4.643  12.629  1.00 21.33           N  
ATOM    297  CA  ALA B  15      43.145   4.994  13.009  1.00 22.26           C  
ATOM    298  C   ALA B  15      43.672   4.181  14.187  1.00 20.80           C  
ATOM    299  O   ALA B  15      44.848   3.870  14.307  1.00 18.74           O  
ATOM    300  CB  ALA B  15      43.156   6.478  13.445  1.00 20.43           C  
ATOM    301  N   LEU B  16      42.767   3.925  15.159  1.00 18.52           N  
ATOM    302  CA  LEU B  16      43.070   3.167  16.352  1.00 18.86           C  
ATOM    303  C   LEU B  16      43.461   1.747  15.872  1.00 18.82           C  
ATOM    304  O   LEU B  16      44.523   1.273  16.334  1.00 19.64           O  
ATOM    305  CB  LEU B  16      41.982   3.125  17.390  1.00 24.28           C  
ATOM    306  CG  LEU B  16      42.242   2.752  18.850  1.00 28.45           C  
ATOM    307  CD1 LEU B  16      41.204   1.811  19.434  1.00 27.45           C  
ATOM    308  CD2 LEU B  16      43.612   2.243  19.154  1.00 31.46           C  
ATOM    309  N   ILE B  17      42.681   1.161  15.028  1.00 14.59           N  
ATOM    310  CA  ILE B  17      42.952  -0.212  14.601  1.00 14.88           C  
ATOM    311  C   ILE B  17      44.368  -0.233  13.934  1.00 15.79           C  
ATOM    312  O   ILE B  17      45.145  -1.102  14.164  1.00 15.07           O  
ATOM    313  CB  ILE B  17      41.840  -0.664  13.603  1.00 12.63           C  
ATOM    314  CG1 ILE B  17      40.537  -0.811  14.509  1.00 16.37           C  
ATOM    315  CG2 ILE B  17      42.230  -1.972  12.943  1.00 14.40           C  
ATOM    316  CD1 ILE B  17      39.333  -0.748  13.479  1.00 20.77           C  
ATOM    317  N   SER B  18      44.643   0.713  13.076  1.00 14.90           N  
ATOM    318  CA  SER B  18      45.891   0.689  12.345  1.00 17.71           C  
ATOM    319  C   SER B  18      47.069   0.713  13.345  1.00 17.07           C  
ATOM    320  O   SER B  18      48.090   0.093  13.118  1.00 19.11           O  
ATOM    321  CB  SER B  18      45.979   1.870  11.385  1.00 20.62           C  
ATOM    322  OG  SER B  18      45.145   1.481  10.284  1.00 30.58           O  
ATOM    323  N   TRP B  19      46.881   1.600  14.284  1.00 16.87           N  
ATOM    324  CA  TRP B  19      47.907   1.909  15.276  1.00 17.53           C  
ATOM    325  C   TRP B  19      48.220   0.667  16.036  1.00 18.31           C  
ATOM    326  O   TRP B  19      49.363   0.303  16.406  1.00 15.07           O  
ATOM    327  CB  TRP B  19      47.453   3.048  16.206  1.00 15.45           C  
ATOM    328  CG  TRP B  19      48.377   3.522  17.288  1.00 14.83           C  
ATOM    329  CD1 TRP B  19      49.313   4.509  17.156  1.00 19.28           C  
ATOM    330  CD2 TRP B  19      48.499   3.077  18.627  1.00 14.65           C  
ATOM    331  NE1 TRP B  19      49.999   4.714  18.342  1.00 20.44           N  
ATOM    332  CE2 TRP B  19      49.514   3.836  19.266  1.00 18.09           C  
ATOM    333  CE3 TRP B  19      47.887   2.064  19.370  1.00 13.60           C  
ATOM    334  CZ2 TRP B  19      49.859   3.667  20.587  1.00 15.12           C  
ATOM    335  CZ3 TRP B  19      48.223   1.830  20.663  1.00 14.58           C  
ATOM    336  CH2 TRP B  19      49.185   2.683  21.275  1.00 18.33           C  
ATOM    337  N   ILE B  20      47.155   0.040  16.529  1.00 14.87           N  
ATOM    338  CA  ILE B  20      47.296  -1.149  17.359  1.00 14.07           C  
ATOM    339  C   ILE B  20      47.996  -2.229  16.567  1.00 14.90           C  
ATOM    340  O   ILE B  20      48.951  -2.923  17.095  1.00 17.33           O  
ATOM    341  CB  ILE B  20      45.897  -1.693  17.846  1.00 16.32           C  
ATOM    342  CG1 ILE B  20      45.178  -0.728  18.867  1.00 17.61           C  
ATOM    343  CG2 ILE B  20      46.172  -3.127  18.507  1.00 17.08           C  
ATOM    344  CD1 ILE B  20      43.655  -1.168  19.001  1.00 19.42           C  
ATOM    345  N   LYS B  21      47.633  -2.483  15.357  1.00 15.82           N  
ATOM    346  CA  LYS B  21      48.314  -3.437  14.512  1.00 20.04           C  
ATOM    347  C   LYS B  21      49.808  -3.171  14.344  1.00 23.80           C  
ATOM    348  O   LYS B  21      50.655  -4.117  14.467  1.00 24.68           O  
ATOM    349  CB  LYS B  21      47.701  -3.481  13.108  1.00 22.25           C  
ATOM    350  CG  LYS B  21      46.486  -4.396  13.363  1.00 28.65           C  
ATOM    351  CD  LYS B  21      45.497  -4.210  12.230  1.00 36.60           C  
ATOM    352  CE  LYS B  21      44.389  -5.239  12.647  1.00 42.81           C  
ATOM    353  NZ  LYS B  21      43.119  -4.724  12.052  1.00 48.93           N  
ATOM    354  N   ARG B  22      50.104  -1.918  13.997  1.00 23.75           N  
ATOM    355  CA  ARG B  22      51.517  -1.513  14.068  1.00 25.56           C  
ATOM    356  C   ARG B  22      52.243  -1.800  15.330  1.00 24.43           C  
ATOM    357  O   ARG B  22      53.398  -2.400  15.256  1.00 27.20           O  
ATOM    358  CB  ARG B  22      51.651  -0.007  13.797  1.00 34.10           C  
ATOM    359  CG  ARG B  22      52.190   0.192  12.389  1.00 45.35           C  
ATOM    360  CD  ARG B  22      52.407   1.661  12.194  1.00 53.40           C  
ATOM    361  NE  ARG B  22      51.258   2.432  12.624  1.00 61.00           N  
ATOM    362  CZ  ARG B  22      51.056   3.289  13.620  1.00 63.11           C  
ATOM    363  NH1 ARG B  22      49.892   3.972  13.631  1.00 63.30           N  
ATOM    364  NH2 ARG B  22      51.985   3.512  14.556  1.00 64.86           N  
ATOM    365  N   LYS B  23      51.848  -1.342  16.458  1.00 21.70           N  
ATOM    366  CA  LYS B  23      52.367  -1.651  17.742  1.00 23.85           C  
ATOM    367  C   LYS B  23      52.563  -3.167  17.982  1.00 25.31           C  
ATOM    368  O   LYS B  23      53.543  -3.564  18.672  1.00 23.77           O  
ATOM    369  CB  LYS B  23      51.452  -1.187  18.865  1.00 26.71           C  
ATOM    370  CG  LYS B  23      51.808   0.115  19.510  1.00 35.14           C  
ATOM    371  CD  LYS B  23      52.544   1.057  18.527  1.00 40.49           C  
ATOM    372  CE  LYS B  23      53.467   1.929  19.371  1.00 45.02           C  
ATOM    373  NZ  LYS B  23      53.821   3.216  18.689  1.00 50.38           N  
ATOM    374  N   ARG B  24      51.599  -3.966  17.607  1.00 23.50           N  
ATOM    375  CA  ARG B  24      51.670  -5.431  17.781  1.00 28.09           C  
ATOM    376  C   ARG B  24      52.815  -6.031  16.955  1.00 30.44           C  
ATOM    377  O   ARG B  24      53.499  -6.990  17.415  1.00 32.18           O  
ATOM    378  CB  ARG B  24      50.305  -6.080  17.417  1.00 22.87           C  
ATOM    379  CG  ARG B  24      49.242  -5.834  18.448  1.00 22.47           C  
ATOM    380  CD  ARG B  24      49.488  -6.584  19.723  1.00 24.97           C  
ATOM    381  NE  ARG B  24      48.819  -7.903  19.436  1.00 29.63           N  
ATOM    382  CZ  ARG B  24      48.624  -8.836  20.356  1.00 27.74           C  
ATOM    383  NH1 ARG B  24      49.012  -8.693  21.616  1.00 29.32           N  
ATOM    384  NH2 ARG B  24      47.972  -9.950  19.985  1.00 28.55           N  
ATOM    385  N   GLN B  25      53.033  -5.532  15.767  1.00 33.47           N  
ATOM    386  CA  GLN B  25      54.153  -6.012  14.932  1.00 40.40           C  
ATOM    387  C   GLN B  25      55.486  -5.682  15.548  1.00 42.71           C  
ATOM    388  O   GLN B  25      56.520  -6.321  15.227  1.00 45.76           O  
ATOM    389  CB  GLN B  25      53.969  -5.608  13.454  1.00 45.46           C  
ATOM    390  CG  GLN B  25      52.870  -6.466  12.903  1.00 56.98           C  
ATOM    391  CD  GLN B  25      52.067  -6.296  11.682  1.00 64.02           C  
ATOM    392  OE1 GLN B  25      51.210  -7.164  11.306  1.00 68.36           O  
ATOM    393  NE2 GLN B  25      52.181  -5.192  10.928  1.00 66.24           N  
ATOM    394  N   GLN B  26      55.545  -4.753  16.483  1.00 44.62           N  
ATOM    395  CA  GLN B  26      56.818  -4.124  16.883  1.00 45.23           C  
ATOM    396  C   GLN B  26      57.128  -4.641  18.290  1.00 45.26           C  
ATOM    397  O   GLN B  26      56.154  -5.162  18.880  1.00 45.82           O  
ATOM    398  CB  GLN B  26      56.818  -2.626  16.958  1.00 48.74           C  
ATOM    399  CG  GLN B  26      56.957  -1.837  15.657  1.00 52.76           C  
ATOM    400  CD  GLN B  26      56.502  -0.407  15.923  1.00 55.74           C  
ATOM    401  OE1 GLN B  26      56.561   0.036  17.088  1.00 56.64           O  
ATOM    402  NE2 GLN B  26      56.038   0.260  14.875  1.00 56.30           N  
HETATM  403  N   NH2 B  27      58.362  -4.410  18.635  1.00 46.88           N  
TER     404      NH2 B  27                                                      
HETATM  405  S   SO4 B  28      47.622 -11.933  23.048  1.00 54.28           S  
HETATM  406  O1  SO4 B  28      49.109 -12.130  22.840  1.00 56.09           O  
HETATM  407  O2  SO4 B  28      47.166 -12.772  24.177  1.00 55.25           O  
HETATM  408  O3  SO4 B  28      47.506 -10.492  23.505  1.00 54.75           O  
HETATM  409  O4  SO4 B  28      46.835 -12.165  21.792  1.00 53.20           O  
HETATM  410  S   SO4 B  29      22.437  12.193  22.820  1.00 38.32           S  
HETATM  411  O1  SO4 B  29      22.929  13.331  23.656  1.00 40.06           O  
HETATM  412  O2  SO4 B  29      22.548  10.994  23.652  1.00 38.96           O  
HETATM  413  O3  SO4 B  29      21.029  12.357  22.374  1.00 42.43           O  
HETATM  414  O4  SO4 B  29      23.246  12.262  21.572  1.00 40.29           O  
HETATM  415  O   HOH A  28      12.913   9.491  15.366  1.00 51.66           O  
HETATM  416  O   HOH A  29      16.198   4.369  11.741  1.00 35.82           O  
HETATM  417  O   HOH A  30      36.989 -12.282  18.725  1.00 39.33           O  
HETATM  418  O   HOH A  31      23.976  -3.849  12.132  1.00 32.70           O  
HETATM  419  O   HOH A  32      33.508  -9.399  15.211  1.00 54.46           O  
HETATM  420  O   HOH A  33      28.879   1.778  11.179  1.00 42.18           O  
HETATM  421  O   HOH A  34      22.304   8.730  16.425  1.00 41.52           O  
HETATM  422  O   HOH A  35      36.230  -0.269  12.860  1.00 34.42           O  
HETATM  423  O   HOH A  36      30.395  -5.197  10.564  0.50 68.01           O  
HETATM  424  O   HOH B  30      40.366   7.292  11.900  1.00 23.82           O  
HETATM  425  O   HOH B  31      25.812  13.318  22.889  1.00 35.47           O  
HETATM  426  O   HOH B  32      47.549  -8.830  17.433  1.00 42.65           O  
HETATM  427  O   HOH B  33      46.802   5.128  12.939  1.00 35.28           O  
HETATM  428  O   HOH B  34      21.822   6.903  28.372  1.00 56.77           O  
HETATM  429  O   HOH B  35      26.850  -1.560  33.783  1.00 46.57           O  
HETATM  430  O   HOH B  36      55.151  -1.817  20.390  1.00 56.34           O  
HETATM  431  O   HOH B  37      48.665  -0.671  11.047  1.00 43.80           O  
HETATM  432  O   HOH B  38      19.236   6.875  30.548  1.00 60.32           O  
HETATM  433  O   HOH B  39      38.184  10.506  16.661  1.00 40.04           O  
HETATM  434  O   HOH B  40      57.240   3.245  19.995  1.00 50.49           O  
HETATM  435  O   HOH B  41      27.110  10.370  16.093  1.00 55.11           O  
HETATM  436  O   HOH B  42      32.023  13.960  20.062  1.00 54.46           O  
HETATM  437  O   HOH B  43      41.599   8.035  16.427  1.00 43.57           O  
CONECT  194  201                                                                
CONECT  201  194                                                                
CONECT  396  403                                                                
CONECT  403  396                                                                
CONECT  405  406  407  408  409                                                 
CONECT  406  405                                                                
CONECT  407  405                                                                
CONECT  408  405                                                                
CONECT  409  405                                                                
CONECT  410  411  412  413  414                                                 
CONECT  411  410                                                                
CONECT  412  410                                                                
CONECT  413  410                                                                
CONECT  414  410                                                                
MASTER      311    0    4    4    0    0    3    9  435    2   14    6          
END                                                                             



If you find results from this site helpful for your research, please cite one of our papers:

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.