CNRS Nantes University UFIP UFIP
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***  3gny  ***

elNémo ID: 19020821522730511

Job options:

ID        	=	 19020821522730511
JOBID     	=	 3gny
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 3gny

HEADER    ANTIMICROBIAL PROTEIN                   18-MAR-09   3GNY              
TITLE     CRYSTAL STRUCTURE OF HUMAN ALPHA-DEFENSIN 1 (HNP1)                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUTROPHIL DEFENSIN 1;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HNP-1, HP-1, HP1, DEFENSIN, ALPHA 1, HP 1-56, NEUTROPHIL    
COMPND   5 DEFENSIN 2, HNP-2, HP-2, HP2;                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   4 ORGANISM_COMMON: HUMAN;                                              
SOURCE   5 ORGANISM_TAXID: 9606                                                 
KEYWDS    ANTIMICROBIAL PEPTIDE, HUMAN ALPHA DEFENSIN 1, HUMAN NEUTROPHIL       
KEYWDS   2 PEPTIDE 1, HNP1, ANTIBIOTIC, ANTIMICROBIAL, ANTIVIRAL DEFENSE,       
KEYWDS   3 DEFENSIN, DISULFIDE BOND, FUNGICIDE, PHOSPHOPROTEIN, SECRETED,       
KEYWDS   4 ANTIMICROBIAL PROTEIN                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.PAZGIER,W.-Y.LU                                                     
REVDAT   5   07-FEB-18 3GNY    1       SOURCE                                   
REVDAT   4   24-JAN-18 3GNY    1       AUTHOR                                   
REVDAT   3   13-JUL-11 3GNY    1       VERSN                                    
REVDAT   2   02-FEB-10 3GNY    1       JRNL                                     
REVDAT   1   28-JUL-09 3GNY    0                                                
JRNL        AUTH   G.WEI,E.DE LEEUW,M.PAZGIER,W.YUAN,G.ZOU,J.WANG,B.ERICKSEN,   
JRNL        AUTH 2 W.Y.LU,R.I.LEHRER,W.LU                                       
JRNL        TITL   THROUGH THE LOOKING GLASS, MECHANISTIC INSIGHTS FROM         
JRNL        TITL 2 ENANTIOMERIC HUMAN DEFENSINS.                                
JRNL        REF    J.BIOL.CHEM.                  V. 284 29180 2009              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   19640840                                                     
JRNL        DOI    10.1074/JBC.M109.018085                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.56 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0070                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.56                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 7748                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 379                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.56                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.60                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 542                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1940                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 27                           
REMARK   3   BIN FREE R VALUE                    : 0.2660                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 476                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 13                                      
REMARK   3   SOLVENT ATOMS            : 60                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.41                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.59000                                              
REMARK   3    B22 (A**2) : 0.38000                                              
REMARK   3    B33 (A**2) : -0.98000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.087         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.084         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.047         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.816         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.953                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   504 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):   680 ; 1.423 ; 1.951       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):    58 ; 7.717 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    22 ;22.375 ;18.182       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):    72 ;10.824 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;18.063 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):    64 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   386 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   296 ; 0.688 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   466 ; 1.102 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   208 ; 1.733 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   214 ; 2.646 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   1    A    (A):    238 ;  0.59 ;  5.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):    238 ;  1.95 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    30                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0836   7.4056   6.0291              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0844 T22:   0.0795                                     
REMARK   3      T33:   0.0781 T12:   0.0065                                     
REMARK   3      T13:   0.0006 T23:  -0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3005 L22:   4.6970                                     
REMARK   3      L33:   2.0005 L12:  -1.0119                                     
REMARK   3      L13:  -0.3125 L23:   0.2226                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1011 S12:  -0.0412 S13:  -0.0416                       
REMARK   3      S21:   0.0810 S22:   0.0667 S23:  -0.0161                       
REMARK   3      S31:   0.1639 S32:   0.0559 S33:   0.0344                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B    30                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.6306  17.0670  14.1975              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0639 T22:   0.1058                                     
REMARK   3      T33:   0.0815 T12:   0.0169                                     
REMARK   3      T13:  -0.0045 T23:  -0.0091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6305 L22:   3.5465                                     
REMARK   3      L33:   2.8542 L12:   2.6039                                     
REMARK   3      L13:   0.5567 L23:  -0.0811                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0091 S12:  -0.0177 S13:  -0.1505                       
REMARK   3      S21:   0.1158 S22:   0.0551 S23:  -0.2080                       
REMARK   3      S31:  -0.0111 S32:   0.2582 S33:  -0.0460                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3GNY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAR-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000052097.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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 MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : CONFOCAL                           
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   : 8119                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.560                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.466                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : 0.10800                            
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.15200                            
REMARK 200   FOR SHELL         : 13.90                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1DFN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M IMIDAZOLE, PH 6.5, 1.0 M SODIUM    
REMARK 280  ACETATE TRIHYDRATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       22.73300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       15.66950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.73300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       15.66950            
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                                                    
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                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7580 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 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       31.33900            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 4180 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 31                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 32                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 31                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DFN   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ALPHA-DEFENSIN 3 (HNP3)                   
REMARK 900 RELATED ID: 2PM1   RELATED DB: PDB                                   
REMARK 900 DERIVATIVE OF HUMAN ALPHA-DEFENSIN 1                                 
REMARK 900 RELATED ID: 2PM4   RELATED DB: PDB                                   
REMARK 900 HUMAN ALPHA-DEFENSIN 1 (MULTIPLE ARG TO LYS MUTANT)                  
REMARK 900 RELATED ID: 2PM5   RELATED DB: PDB                                   
REMARK 900 HUMAN ALPHA-DEFENSIN 1 DERIVATIVE                                    
REMARK 900 RELATED ID: 3GO0   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF D-ENANTIOMER OF HUMAN ALPHA-DEFENSIN 1 (D-HNP1) 
DBREF  3GNY A    1    30  UNP    P59665   DEF1_HUMAN      65     94             
DBREF  3GNY B    1    30  UNP    P59665   DEF1_HUMAN      65     94             
SEQRES   1 A   30  ALA CYS TYR CYS ARG ILE PRO ALA CYS ILE ALA GLY GLU          
SEQRES   2 A   30  ARG ARG TYR GLY THR CYS ILE TYR GLN GLY ARG LEU TRP          
SEQRES   3 A   30  ALA PHE CYS CYS                                              
SEQRES   1 B   30  ALA CYS TYR CYS ARG ILE PRO ALA CYS ILE ALA GLY GLU          
SEQRES   2 B   30  ARG ARG TYR GLY THR CYS ILE TYR GLN GLY ARG LEU TRP          
SEQRES   3 B   30  ALA PHE CYS CYS                                              
HET     CL  A  31       1                                                       
HET    GOL  A  32       6                                                       
HET    GOL  B  31       6                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  GOL    2(C3 H8 O3)                                                  
FORMUL   6  HOH   *60(H2 O)                                                     
SHEET    1   A 6 TYR A   3  ARG A   5  0                                        
SHEET    2   A 6 ARG A  24  CYS A  30 -1  O  CYS A  29   N  TYR A   3           
SHEET    3   A 6 ARG A  14  TYR A  21 -1  N  TYR A  16   O  PHE A  28           
SHEET    4   A 6 ARG B  14  TYR B  21 -1  O  ILE B  20   N  THR A  18           
SHEET    5   A 6 ARG B  24  CYS B  30 -1  O  PHE B  28   N  TYR B  16           
SHEET    6   A 6 TYR B   3  ARG B   5 -1  N  TYR B   3   O  CYS B  29           
SSBOND   1 CYS A    2    CYS A   30                          1555   1555  2.05  
SSBOND   2 CYS A    4    CYS A   19                          1555   1555  2.01  
SSBOND   3 CYS A    9    CYS A   29                          1555   1555  2.04  
SSBOND   4 CYS B    2    CYS B   30                          1555   1555  2.05  
SSBOND   5 CYS B    4    CYS B   19                          1555   1555  2.03  
SSBOND   6 CYS B    9    CYS B   29                          1555   1555  2.02  
CISPEP   1 ILE A    6    PRO A    7          0         7.39                     
CISPEP   2 ILE B    6    PRO B    7          0         1.47                     
SITE     1 AC1  2 ARG B  14  HOH B  51                                          
SITE     1 AC2  4 PRO A   7  ARG A  15  LEU A  25  HOH A  57                    
SITE     1 AC3  6 PRO B   7  ARG B  15  LEU B  25  TRP B  26                    
SITE     2 AC3  6 ALA B  27  HOH B  63                                          
CRYST1   45.466   31.339   40.205  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021994  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.031909  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.024873        0.00000                         
ATOM      1  N   ALA A   1      17.625   3.093  12.353  1.00 17.24           N  
ATOM      2  CA  ALA A   1      17.139   4.498  12.276  1.00 16.12           C  
ATOM      3  C   ALA A   1      15.730   4.529  11.685  1.00 15.65           C  
ATOM      4  O   ALA A   1      15.235   3.524  11.196  1.00 16.70           O  
ATOM      5  CB  ALA A   1      18.115   5.358  11.443  1.00 16.78           C  
ATOM      6  N   CYS A   2      15.078   5.678  11.782  1.00 13.75           N  
ATOM      7  CA  CYS A   2      13.779   5.857  11.145  1.00 12.72           C  
ATOM      8  C   CYS A   2      13.891   6.799   9.966  1.00 12.32           C  
ATOM      9  O   CYS A   2      14.765   7.665   9.924  1.00 12.90           O  
ATOM     10  CB  CYS A   2      12.736   6.397  12.139  1.00 12.63           C  
ATOM     11  SG  CYS A   2      12.438   5.372  13.623  1.00 12.85           S  
ATOM     12  N   TYR A   3      12.960   6.642   9.027  1.00 11.55           N  
ATOM     13  CA  TYR A   3      12.961   7.406   7.797  1.00 11.17           C  
ATOM     14  C   TYR A   3      11.563   7.842   7.411  1.00 10.36           C  
ATOM     15  O   TYR A   3      10.617   7.043   7.483  1.00 10.83           O  
ATOM     16  CB  TYR A   3      13.508   6.539   6.652  1.00 11.21           C  
ATOM     17  CG  TYR A   3      14.913   6.066   6.894  1.00 12.04           C  
ATOM     18  CD1 TYR A   3      15.991   6.881   6.584  1.00 15.77           C  
ATOM     19  CD2 TYR A   3      15.161   4.822   7.466  1.00 12.47           C  
ATOM     20  CE1 TYR A   3      17.297   6.456   6.820  1.00 15.68           C  
ATOM     21  CE2 TYR A   3      16.452   4.385   7.709  1.00 13.61           C  
ATOM     22  CZ  TYR A   3      17.512   5.205   7.383  1.00 14.86           C  
ATOM     23  OH  TYR A   3      18.802   4.794   7.613  1.00 18.34           O  
ATOM     24  N   CYS A   4      11.441   9.083   6.951  1.00  9.39           N  
ATOM     25  CA  CYS A   4      10.230   9.495   6.224  1.00  9.71           C  
ATOM     26  C   CYS A   4      10.380   9.074   4.763  1.00  9.47           C  
ATOM     27  O   CYS A   4      11.389   9.420   4.105  1.00 11.82           O  
ATOM     28  CB  CYS A   4      10.036  11.021   6.305  1.00 10.12           C  
ATOM     29  SG  CYS A   4       9.774  11.630   7.974  1.00 10.68           S  
ATOM     30  N   ARG A   5       9.398   8.316   4.259  1.00  9.36           N  
ATOM     31  CA  ARG A   5       9.478   7.726   2.912  1.00  9.27           C  
ATOM     32  C   ARG A   5       8.262   7.990   2.048  1.00  9.37           C  
ATOM     33  O   ARG A   5       7.137   7.991   2.538  1.00  9.36           O  
ATOM     34  CB  ARG A   5       9.695   6.212   2.995  1.00  8.74           C  
ATOM     35  CG  ARG A   5      11.003   5.781   3.670  1.00  8.10           C  
ATOM     36  CD  ARG A   5      11.223   4.323   3.343  1.00  8.10           C  
ATOM     37  NE  ARG A   5      12.357   3.754   4.052  1.00  8.19           N  
ATOM     38  CZ  ARG A   5      13.634   3.971   3.723  1.00  8.47           C  
ATOM     39  NH1 ARG A   5      13.946   4.759   2.688  1.00  8.81           N  
ATOM     40  NH2 ARG A   5      14.613   3.411   4.436  1.00  9.23           N  
ATOM     41  N   ILE A   6       8.513   8.202   0.761  1.00  8.59           N  
ATOM     42  CA  ILE A   6       7.496   8.125  -0.272  1.00  8.78           C  
ATOM     43  C   ILE A   6       8.024   7.130  -1.303  1.00  8.62           C  
ATOM     44  O   ILE A   6       9.181   7.244  -1.704  1.00  9.64           O  
ATOM     45  CB  ILE A   6       7.257   9.505  -0.915  1.00  8.23           C  
ATOM     46  CG1 ILE A   6       6.539  10.437   0.080  1.00  9.50           C  
ATOM     47  CG2 ILE A   6       6.476   9.382  -2.215  1.00  9.13           C  
ATOM     48  CD1 ILE A   6       6.551  11.898  -0.387  1.00 10.12           C  
ATOM     49  N   PRO A   7       7.185   6.167  -1.745  1.00  9.59           N  
ATOM     50  CA  PRO A   7       5.743   6.008  -1.482  1.00  9.92           C  
ATOM     51  C   PRO A   7       5.382   5.146  -0.278  1.00 10.58           C  
ATOM     52  O   PRO A   7       4.220   5.131   0.117  1.00 12.65           O  
ATOM     53  CB  PRO A   7       5.248   5.295  -2.748  1.00  9.70           C  
ATOM     54  CG  PRO A   7       6.401   4.451  -3.166  1.00 11.10           C  
ATOM     55  CD  PRO A   7       7.632   5.300  -2.853  1.00  8.70           C  
ATOM     56  N   ALA A   8       6.351   4.439   0.305  1.00 10.51           N  
ATOM     57  CA  ALA A   8       6.025   3.447   1.335  1.00 10.01           C  
ATOM     58  C   ALA A   8       7.258   3.053   2.099  1.00  9.55           C  
ATOM     59  O   ALA A   8       8.383   3.273   1.630  1.00  9.81           O  
ATOM     60  CB  ALA A   8       5.408   2.181   0.664  1.00 10.45           C  
ATOM     61  N   CYS A   9       7.070   2.461   3.283  1.00  9.16           N  
ATOM     62  CA  CYS A   9       8.181   1.796   3.974  1.00  9.40           C  
ATOM     63  C   CYS A   9       8.707   0.632   3.154  1.00  9.40           C  
ATOM     64  O   CYS A   9       8.009   0.082   2.285  1.00  9.95           O  
ATOM     65  CB  CYS A   9       7.760   1.294   5.362  1.00  8.99           C  
ATOM     66  SG  CYS A   9       7.016   2.551   6.400  1.00 10.72           S  
ATOM     67  N   ILE A  10       9.946   0.258   3.444  1.00  8.34           N  
ATOM     68  CA  ILE A  10      10.598  -0.807   2.688  1.00  7.92           C  
ATOM     69  C   ILE A  10      10.686  -2.080   3.518  1.00  6.77           C  
ATOM     70  O   ILE A  10      10.388  -2.081   4.719  1.00  8.00           O  
ATOM     71  CB  ILE A  10      11.998  -0.375   2.154  1.00  8.32           C  
ATOM     72  CG1 ILE A  10      13.017  -0.148   3.284  1.00  8.93           C  
ATOM     73  CG2 ILE A  10      11.870   0.831   1.209  1.00  8.94           C  
ATOM     74  CD1 ILE A  10      14.446  -0.120   2.766  1.00  9.73           C  
ATOM     75  N   ALA A  11      11.097  -3.166   2.865  1.00  7.36           N  
ATOM     76  CA  ALA A  11      11.321  -4.434   3.516  1.00  7.20           C  
ATOM     77  C   ALA A  11      12.136  -4.270   4.796  1.00  7.78           C  
ATOM     78  O   ALA A  11      13.164  -3.603   4.808  1.00  8.60           O  
ATOM     79  CB  ALA A  11      12.032  -5.401   2.551  1.00  6.81           C  
ATOM     80  N   GLY A  12      11.669  -4.885   5.869  1.00  6.86           N  
ATOM     81  CA  GLY A  12      12.388  -4.829   7.135  1.00  7.35           C  
ATOM     82  C   GLY A  12      11.989  -3.667   8.015  1.00  7.79           C  
ATOM     83  O   GLY A  12      12.467  -3.541   9.142  1.00  8.76           O  
ATOM     84  N   GLU A  13      11.099  -2.829   7.493  1.00  7.45           N  
ATOM     85  CA  GLU A  13      10.578  -1.678   8.235  1.00  8.30           C  
ATOM     86  C   GLU A  13       9.093  -1.804   8.522  1.00  9.13           C  
ATOM     87  O   GLU A  13       8.364  -2.523   7.812  1.00  9.45           O  
ATOM     88  CB  GLU A  13      10.803  -0.387   7.448  1.00  8.88           C  
ATOM     89  CG  GLU A  13      12.244  -0.035   7.222  1.00  8.51           C  
ATOM     90  CD  GLU A  13      12.387   1.254   6.428  1.00  8.67           C  
ATOM     91  OE1 GLU A  13      11.441   1.631   5.701  1.00  8.27           O  
ATOM     92  OE2 GLU A  13      13.477   1.857   6.522  1.00 10.45           O  
ATOM     93  N   ARG A  14       8.652  -1.081   9.553  1.00  9.65           N  
ATOM     94  CA  ARG A  14       7.238  -0.976   9.869  1.00 11.25           C  
ATOM     95  C   ARG A  14       6.848   0.506   9.842  1.00 10.33           C  
ATOM     96  O   ARG A  14       7.658   1.364  10.185  1.00 10.72           O  
ATOM     97  CB  ARG A  14       6.969  -1.611  11.247  1.00 11.64           C  
ATOM     98  CG  ARG A  14       5.560  -1.396  11.805  1.00 16.54           C  
ATOM     99  CD  ARG A  14       5.104  -2.635  12.579  1.00 21.96           C  
ATOM    100  NE  ARG A  14       4.150  -2.414  13.679  1.00 26.54           N  
ATOM    101  CZ  ARG A  14       3.814  -1.249  14.243  1.00 29.32           C  
ATOM    102  NH1 ARG A  14       4.322  -0.095  13.830  1.00 30.25           N  
ATOM    103  NH2 ARG A  14       2.936  -1.242  15.247  1.00 30.53           N  
ATOM    104  N   ARG A  15       5.617   0.796   9.425  1.00  9.99           N  
ATOM    105  CA  ARG A  15       5.112   2.155   9.479  1.00  9.94           C  
ATOM    106  C   ARG A  15       4.620   2.479  10.891  1.00  9.75           C  
ATOM    107  O   ARG A  15       3.744   1.800  11.437  1.00 10.82           O  
ATOM    108  CB  ARG A  15       3.995   2.406   8.453  1.00  9.74           C  
ATOM    109  CG  ARG A  15       3.520   3.857   8.485  1.00 11.89           C  
ATOM    110  CD  ARG A  15       2.621   4.194   7.313  1.00 12.63           C  
ATOM    111  NE  ARG A  15       2.240   5.599   7.327  1.00 12.53           N  
ATOM    112  CZ  ARG A  15       1.702   6.254   6.303  1.00 13.49           C  
ATOM    113  NH1 ARG A  15       1.496   5.637   5.141  1.00 15.97           N  
ATOM    114  NH2 ARG A  15       1.376   7.537   6.435  1.00 12.99           N  
ATOM    115  N   TYR A  16       5.200   3.518  11.484  1.00  9.24           N  
ATOM    116  CA  TYR A  16       4.819   3.957  12.820  1.00  8.62           C  
ATOM    117  C   TYR A  16       4.090   5.298  12.834  1.00  8.44           C  
ATOM    118  O   TYR A  16       3.613   5.719  13.882  1.00  9.32           O  
ATOM    119  CB  TYR A  16       6.035   4.048  13.749  1.00  8.30           C  
ATOM    120  CG  TYR A  16       6.623   2.721  14.142  1.00  9.22           C  
ATOM    121  CD1 TYR A  16       6.262   2.112  15.318  1.00 12.91           C  
ATOM    122  CD2 TYR A  16       7.571   2.114  13.340  1.00 10.68           C  
ATOM    123  CE1 TYR A  16       6.820   0.909  15.688  1.00 12.24           C  
ATOM    124  CE2 TYR A  16       8.141   0.911  13.685  1.00 12.33           C  
ATOM    125  CZ  TYR A  16       7.760   0.312  14.860  1.00 12.65           C  
ATOM    126  OH  TYR A  16       8.320  -0.891  15.219  1.00 17.28           O  
ATOM    127  N   GLY A  17       4.006   5.981  11.687  1.00  8.26           N  
ATOM    128  CA  GLY A  17       3.297   7.259  11.623  1.00  8.39           C  
ATOM    129  C   GLY A  17       3.462   7.915  10.279  1.00  8.31           C  
ATOM    130  O   GLY A  17       3.630   7.252   9.259  1.00  7.89           O  
ATOM    131  N   THR A  18       3.410   9.242  10.301  1.00  7.94           N  
ATOM    132  CA  THR A  18       3.345  10.055   9.103  1.00  8.34           C  
ATOM    133  C   THR A  18       4.219  11.278   9.260  1.00  9.21           C  
ATOM    134  O   THR A  18       4.320  11.824  10.350  1.00  9.01           O  
ATOM    135  CB  THR A  18       1.895  10.528   8.861  1.00  8.75           C  
ATOM    136  OG1 THR A  18       1.070   9.365   8.695  1.00  9.88           O  
ATOM    137  CG2 THR A  18       1.779  11.408   7.609  1.00 11.34           C  
ATOM    138  N   CYS A  19       4.879  11.686   8.185  1.00  8.63           N  
ATOM    139  CA  CYS A  19       5.600  12.970   8.169  1.00  8.78           C  
ATOM    140  C   CYS A  19       4.909  13.931   7.227  1.00  8.20           C  
ATOM    141  O   CYS A  19       4.357  13.526   6.185  1.00  9.25           O  
ATOM    142  CB  CYS A  19       7.049  12.824   7.711  1.00  9.77           C  
ATOM    143  SG  CYS A  19       7.816  11.317   8.328  1.00  9.79           S  
ATOM    144  N   ILE A  20       4.982  15.207   7.573  1.00  7.44           N  
ATOM    145  CA  ILE A  20       4.496  16.307   6.746  1.00  7.59           C  
ATOM    146  C   ILE A  20       5.744  17.129   6.410  1.00  6.96           C  
ATOM    147  O   ILE A  20       6.411  17.654   7.302  1.00  6.91           O  
ATOM    148  CB  ILE A  20       3.506  17.202   7.524  1.00  7.76           C  
ATOM    149  CG1 ILE A  20       2.261  16.417   7.925  1.00  8.18           C  
ATOM    150  CG2 ILE A  20       3.153  18.462   6.703  1.00  9.19           C  
ATOM    151  CD1 ILE A  20       1.375  17.155   8.946  1.00  9.89           C  
ATOM    152  N   TYR A  21       6.083  17.200   5.117  1.00  6.68           N  
ATOM    153  CA  TYR A  21       7.347  17.791   4.686  1.00  6.92           C  
ATOM    154  C   TYR A  21       7.259  18.065   3.180  1.00  6.74           C  
ATOM    155  O   TYR A  21       6.768  17.234   2.398  1.00  7.22           O  
ATOM    156  CB  TYR A  21       8.489  16.833   5.034  1.00  6.72           C  
ATOM    157  CG  TYR A  21       9.863  17.166   4.477  1.00  7.40           C  
ATOM    158  CD1 TYR A  21      10.543  18.323   4.865  1.00  7.39           C  
ATOM    159  CD2 TYR A  21      10.496  16.296   3.576  1.00  7.47           C  
ATOM    160  CE1 TYR A  21      11.835  18.611   4.359  1.00  6.50           C  
ATOM    161  CE2 TYR A  21      11.764  16.579   3.062  1.00  6.97           C  
ATOM    162  CZ  TYR A  21      12.427  17.727   3.453  1.00  7.70           C  
ATOM    163  OH  TYR A  21      13.670  18.001   2.942  1.00  8.61           O  
ATOM    164  N   GLN A  22       7.693  19.253   2.783  1.00  6.31           N  
ATOM    165  CA  GLN A  22       7.730  19.662   1.362  1.00  6.49           C  
ATOM    166  C   GLN A  22       6.360  19.564   0.677  1.00  6.54           C  
ATOM    167  O   GLN A  22       6.269  19.215  -0.506  1.00  7.72           O  
ATOM    168  CB  GLN A  22       8.788  18.863   0.597  1.00  6.71           C  
ATOM    169  CG  GLN A  22      10.225  19.067   1.069  1.00  7.11           C  
ATOM    170  CD  GLN A  22      10.767  20.446   0.787  1.00  7.51           C  
ATOM    171  OE1 GLN A  22      10.440  21.078  -0.224  1.00  7.60           O  
ATOM    172  NE2 GLN A  22      11.627  20.927   1.679  1.00  8.42           N  
ATOM    173  N   GLY A  23       5.300  19.857   1.431  1.00  7.57           N  
ATOM    174  CA  GLY A  23       3.964  19.841   0.867  1.00  7.91           C  
ATOM    175  C   GLY A  23       3.386  18.468   0.612  1.00  8.10           C  
ATOM    176  O   GLY A  23       2.330  18.346  -0.045  1.00  9.04           O  
ATOM    177  N   ARG A  24       4.075  17.441   1.129  1.00  7.89           N  
ATOM    178  CA  ARG A  24       3.667  16.055   0.950  1.00  8.40           C  
ATOM    179  C   ARG A  24       3.555  15.269   2.259  1.00  8.59           C  
ATOM    180  O   ARG A  24       4.149  15.640   3.308  1.00  8.02           O  
ATOM    181  CB  ARG A  24       4.678  15.347   0.057  1.00  9.68           C  
ATOM    182  CG  ARG A  24       4.736  15.917  -1.366  1.00 10.20           C  
ATOM    183  CD  ARG A  24       3.473  15.582  -2.204  1.00 13.69           C  
ATOM    184  NE  ARG A  24       3.320  14.130  -2.307  1.00 13.14           N  
ATOM    185  CZ  ARG A  24       4.019  13.363  -3.150  1.00 15.04           C  
ATOM    186  NH1 ARG A  24       4.866  13.923  -4.021  1.00 14.86           N  
ATOM    187  NH2 ARG A  24       3.834  12.048  -3.158  1.00 14.02           N  
ATOM    188  N   LEU A  25       2.750  14.209   2.180  1.00  8.31           N  
ATOM    189  CA  LEU A  25       2.670  13.189   3.211  1.00  7.94           C  
ATOM    190  C   LEU A  25       3.675  12.072   2.949  1.00  8.61           C  
ATOM    191  O   LEU A  25       3.824  11.584   1.805  1.00  9.28           O  
ATOM    192  CB  LEU A  25       1.252  12.604   3.247  1.00  8.43           C  
ATOM    193  CG  LEU A  25       0.194  13.612   3.727  1.00  7.53           C  
ATOM    194  CD1 LEU A  25      -1.208  13.173   3.380  1.00 11.82           C  
ATOM    195  CD2 LEU A  25       0.300  13.816   5.215  1.00 11.25           C  
ATOM    196  N   TRP A  26       4.333  11.654   4.033  1.00  8.07           N  
ATOM    197  CA  TRP A  26       5.349  10.601   4.001  1.00  8.61           C  
ATOM    198  C   TRP A  26       5.023   9.531   5.038  1.00  8.75           C  
ATOM    199  O   TRP A  26       4.482   9.829   6.089  1.00  9.26           O  
ATOM    200  CB  TRP A  26       6.733  11.173   4.347  1.00  9.05           C  
ATOM    201  CG  TRP A  26       7.173  12.354   3.541  1.00  8.93           C  
ATOM    202  CD1 TRP A  26       6.574  13.582   3.484  1.00  9.24           C  
ATOM    203  CD2 TRP A  26       8.293  12.405   2.658  1.00  7.58           C  
ATOM    204  NE1 TRP A  26       7.267  14.410   2.626  1.00  8.87           N  
ATOM    205  CE2 TRP A  26       8.320  13.707   2.086  1.00  7.79           C  
ATOM    206  CE3 TRP A  26       9.296  11.476   2.298  1.00  8.87           C  
ATOM    207  CZ2 TRP A  26       9.316  14.111   1.194  1.00  8.58           C  
ATOM    208  CZ3 TRP A  26      10.283  11.875   1.407  1.00  8.35           C  
ATOM    209  CH2 TRP A  26      10.281  13.183   0.849  1.00  9.36           C  
ATOM    210  N   ALA A  27       5.357   8.276   4.742  1.00  8.02           N  
ATOM    211  CA  ALA A  27       5.288   7.246   5.768  1.00  8.09           C  
ATOM    212  C   ALA A  27       6.474   7.413   6.696  1.00  8.29           C  
ATOM    213  O   ALA A  27       7.596   7.559   6.237  1.00  9.63           O  
ATOM    214  CB  ALA A  27       5.298   5.874   5.141  1.00  9.08           C  
ATOM    215  N   PHE A  28       6.231   7.374   8.003  1.00  8.04           N  
ATOM    216  CA  PHE A  28       7.320   7.305   8.969  1.00  7.71           C  
ATOM    217  C   PHE A  28       7.633   5.848   9.313  1.00  7.71           C  
ATOM    218  O   PHE A  28       6.783   5.137   9.872  1.00  8.05           O  
ATOM    219  CB  PHE A  28       6.970   8.101  10.220  1.00  7.81           C  
ATOM    220  CG  PHE A  28       8.062   8.120  11.248  1.00  8.42           C  
ATOM    221  CD1 PHE A  28       9.210   8.885  11.050  1.00  9.61           C  
ATOM    222  CD2 PHE A  28       7.949   7.365  12.405  1.00  9.69           C  
ATOM    223  CE1 PHE A  28      10.216   8.895  12.010  1.00  9.10           C  
ATOM    224  CE2 PHE A  28       8.949   7.371  13.351  1.00 11.27           C  
ATOM    225  CZ  PHE A  28      10.074   8.136  13.144  1.00  9.84           C  
ATOM    226  N   CYS A  29       8.854   5.428   8.949  1.00  8.54           N  
ATOM    227  CA  CYS A  29       9.232   4.018   8.911  1.00  9.20           C  
ATOM    228  C   CYS A  29      10.416   3.727   9.796  1.00  9.30           C  
ATOM    229  O   CYS A  29      11.389   4.457   9.764  1.00  9.74           O  
ATOM    230  CB  CYS A  29       9.618   3.681   7.476  1.00  9.37           C  
ATOM    231  SG  CYS A  29       8.343   4.095   6.249  1.00 10.48           S  
ATOM    232  N   CYS A  30      10.331   2.665  10.593  1.00  9.47           N  
ATOM    233  CA  CYS A  30      11.450   2.260  11.439  1.00 11.02           C  
ATOM    234  C   CYS A  30      11.670   0.753  11.369  1.00 11.43           C  
ATOM    235  O   CYS A  30      10.744  -0.045  11.120  1.00 11.63           O  
ATOM    236  CB  CYS A  30      11.237   2.654  12.906  1.00 10.82           C  
ATOM    237  SG  CYS A  30      10.730   4.327  13.193  1.00 12.29           S  
ATOM    238  OXT CYS A  30      12.810   0.325  11.597  1.00 13.13           O  
TER     239      CYS A  30                                                      
ATOM    240  N   ALA B   1      21.097  14.362   6.773  1.00 18.79           N  
ATOM    241  CA  ALA B   1      19.841  13.647   7.135  1.00 17.88           C  
ATOM    242  C   ALA B   1      18.868  14.549   7.883  1.00 17.26           C  
ATOM    243  O   ALA B   1      19.266  15.540   8.513  1.00 17.93           O  
ATOM    244  CB  ALA B   1      20.162  12.405   7.964  1.00 18.32           C  
ATOM    245  N   CYS B   2      17.584  14.209   7.804  1.00 15.61           N  
ATOM    246  CA  CYS B   2      16.577  14.895   8.600  1.00 14.34           C  
ATOM    247  C   CYS B   2      16.191  14.045   9.779  1.00 13.98           C  
ATOM    248  O   CYS B   2      16.312  12.826   9.731  1.00 14.76           O  
ATOM    249  CB  CYS B   2      15.341  15.220   7.782  1.00 13.94           C  
ATOM    250  SG  CYS B   2      15.664  16.240   6.350  1.00 14.56           S  
ATOM    251  N   TYR B   3      15.716  14.702  10.832  1.00 12.85           N  
ATOM    252  CA  TYR B   3      15.397  14.070  12.105  1.00 12.85           C  
ATOM    253  C   TYR B   3      14.114  14.617  12.690  1.00 12.04           C  
ATOM    254  O   TYR B   3      13.881  15.831  12.663  1.00 12.15           O  
ATOM    255  CB  TYR B   3      16.522  14.323  13.111  1.00 13.14           C  
ATOM    256  CG  TYR B   3      17.815  13.682  12.685  1.00 15.45           C  
ATOM    257  CD1 TYR B   3      18.039  12.328  12.916  1.00 18.45           C  
ATOM    258  CD2 TYR B   3      18.774  14.405  11.992  1.00 16.69           C  
ATOM    259  CE1 TYR B   3      19.219  11.702  12.504  1.00 20.19           C  
ATOM    260  CE2 TYR B   3      19.976  13.788  11.568  1.00 19.09           C  
ATOM    261  CZ  TYR B   3      20.178  12.435  11.831  1.00 20.43           C  
ATOM    262  OH  TYR B   3      21.339  11.802  11.427  1.00 21.85           O  
ATOM    263  N   CYS B   4      13.283  13.714  13.216  1.00 11.98           N  
ATOM    264  CA  CYS B   4      12.134  14.092  14.048  1.00 11.75           C  
ATOM    265  C   CYS B   4      12.610  14.371  15.471  1.00 12.31           C  
ATOM    266  O   CYS B   4      13.217  13.490  16.093  1.00 13.51           O  
ATOM    267  CB  CYS B   4      11.064  12.996  14.048  1.00 11.83           C  
ATOM    268  SG  CYS B   4      10.420  12.583  12.413  1.00 11.64           S  
ATOM    269  N   ARG B   5      12.347  15.572  15.988  1.00 13.22           N  
ATOM    270  CA  ARG B   5      12.867  15.974  17.307  1.00 14.03           C  
ATOM    271  C   ARG B   5      11.816  16.555  18.258  1.00 14.53           C  
ATOM    272  O   ARG B   5      10.902  17.253  17.834  1.00 14.96           O  
ATOM    273  CB  ARG B   5      13.989  17.011  17.161  1.00 13.09           C  
ATOM    274  CG  ARG B   5      15.131  16.630  16.239  1.00 13.72           C  
ATOM    275  CD  ARG B   5      16.347  17.472  16.560  1.00 13.03           C  
ATOM    276  NE  ARG B   5      17.450  17.229  15.635  1.00 12.59           N  
ATOM    277  CZ  ARG B   5      18.373  16.276  15.786  1.00 15.17           C  
ATOM    278  NH1 ARG B   5      18.326  15.439  16.813  1.00 16.25           N  
ATOM    279  NH2 ARG B   5      19.335  16.150  14.889  1.00 14.62           N  
ATOM    280  N   ILE B   6      11.977  16.255  19.547  1.00 15.36           N  
ATOM    281  CA  ILE B   6      11.331  16.987  20.634  1.00 16.14           C  
ATOM    282  C   ILE B   6      12.518  17.496  21.488  1.00 16.64           C  
ATOM    283  O   ILE B   6      13.505  16.763  21.669  1.00 17.80           O  
ATOM    284  CB  ILE B   6      10.335  16.074  21.430  1.00 16.42           C  
ATOM    285  CG1 ILE B   6       9.044  15.874  20.622  1.00 17.18           C  
ATOM    286  CG2 ILE B   6      10.014  16.653  22.821  1.00 17.08           C  
ATOM    287  CD1 ILE B   6       8.142  14.728  21.109  1.00 17.58           C  
ATOM    288  N   PRO B   7      12.468  18.754  21.987  1.00 16.15           N  
ATOM    289  CA  PRO B   7      11.424  19.781  21.887  1.00 15.26           C  
ATOM    290  C   PRO B   7      11.495  20.663  20.635  1.00 14.70           C  
ATOM    291  O   PRO B   7      10.488  21.283  20.286  1.00 15.95           O  
ATOM    292  CB  PRO B   7      11.670  20.639  23.133  1.00 15.06           C  
ATOM    293  CG  PRO B   7      13.150  20.537  23.379  1.00 15.68           C  
ATOM    294  CD  PRO B   7      13.574  19.177  22.880  1.00 15.98           C  
ATOM    295  N   ALA B   8      12.651  20.706  19.967  1.00 13.04           N  
ATOM    296  CA  ALA B   8      12.898  21.651  18.873  1.00 11.41           C  
ATOM    297  C   ALA B   8      14.124  21.206  18.073  1.00 10.68           C  
ATOM    298  O   ALA B   8      14.900  20.355  18.537  1.00 10.84           O  
ATOM    299  CB  ALA B   8      13.111  23.089  19.449  1.00 11.19           C  
ATOM    300  N   CYS B   9      14.308  21.796  16.887  1.00  9.78           N  
ATOM    301  CA  CYS B   9      15.495  21.553  16.081  1.00 10.00           C  
ATOM    302  C   CYS B   9      16.738  22.108  16.779  1.00 10.09           C  
ATOM    303  O   CYS B   9      16.651  23.021  17.632  1.00  9.92           O  
ATOM    304  CB  CYS B   9      15.317  22.155  14.695  1.00 10.05           C  
ATOM    305  SG  CYS B   9      13.851  21.524  13.852  1.00 10.28           S  
ATOM    306  N   ILE B  10      17.904  21.561  16.445  1.00 10.19           N  
ATOM    307  CA  ILE B  10      19.104  22.035  17.105  1.00 10.62           C  
ATOM    308  C   ILE B  10      19.740  23.121  16.253  1.00 10.00           C  
ATOM    309  O   ILE B  10      19.452  23.216  15.059  1.00 10.24           O  
ATOM    310  CB  ILE B  10      20.096  20.906  17.378  1.00 11.62           C  
ATOM    311  CG1 ILE B  10      20.614  20.324  16.084  1.00 12.73           C  
ATOM    312  CG2 ILE B  10      19.453  19.838  18.231  1.00 12.42           C  
ATOM    313  CD1 ILE B  10      21.945  19.605  16.260  1.00 16.63           C  
ATOM    314  N   ALA B  11      20.603  23.930  16.860  1.00 10.36           N  
ATOM    315  CA  ALA B  11      21.322  24.943  16.108  1.00 10.23           C  
ATOM    316  C   ALA B  11      21.965  24.321  14.867  1.00 10.46           C  
ATOM    317  O   ALA B  11      22.536  23.249  14.946  1.00 11.05           O  
ATOM    318  CB  ALA B  11      22.373  25.591  16.985  1.00  9.85           C  
ATOM    319  N   GLY B  12      21.848  25.000  13.737  1.00 10.30           N  
ATOM    320  CA  GLY B  12      22.359  24.486  12.469  1.00 11.63           C  
ATOM    321  C   GLY B  12      21.318  23.746  11.656  1.00 12.14           C  
ATOM    322  O   GLY B  12      21.569  23.420  10.491  1.00 13.43           O  
ATOM    323  N   GLU B  13      20.166  23.474  12.271  1.00 11.51           N  
ATOM    324  CA  GLU B  13      19.028  22.871  11.573  1.00 10.64           C  
ATOM    325  C   GLU B  13      17.919  23.888  11.467  1.00 10.72           C  
ATOM    326  O   GLU B  13      17.912  24.875  12.201  1.00 11.61           O  
ATOM    327  CB  GLU B  13      18.483  21.673  12.349  1.00 10.61           C  
ATOM    328  CG  GLU B  13      19.463  20.517  12.491  1.00 10.60           C  
ATOM    329  CD  GLU B  13      18.899  19.383  13.299  1.00 12.81           C  
ATOM    330  OE1 GLU B  13      17.997  19.600  14.145  1.00 10.87           O  
ATOM    331  OE2 GLU B  13      19.351  18.248  13.081  1.00 15.86           O  
ATOM    332  N   ARG B  14      16.976  23.634  10.558  1.00 10.38           N  
ATOM    333  CA  ARG B  14      15.709  24.372  10.524  1.00 10.46           C  
ATOM    334  C   ARG B  14      14.573  23.375  10.574  1.00 10.36           C  
ATOM    335  O   ARG B  14      14.759  22.213  10.213  1.00 10.83           O  
ATOM    336  CB  ARG B  14      15.583  25.187   9.237  1.00 10.93           C  
ATOM    337  CG  ARG B  14      16.749  26.134   9.017  1.00 12.88           C  
ATOM    338  CD  ARG B  14      16.756  27.271  10.025  1.00 16.82           C  
ATOM    339  NE  ARG B  14      15.754  28.272   9.669  1.00 22.95           N  
ATOM    340  CZ  ARG B  14      15.026  28.955  10.550  1.00 27.03           C  
ATOM    341  NH1 ARG B  14      15.180  28.745  11.865  1.00 29.67           N  
ATOM    342  NH2 ARG B  14      14.136  29.847  10.118  1.00 25.69           N  
ATOM    343  N   ARG B  15      13.398  23.842  10.996  1.00  9.41           N  
ATOM    344  CA  ARG B  15      12.195  23.013  11.024  1.00  9.53           C  
ATOM    345  C   ARG B  15      11.501  23.137   9.678  1.00  8.79           C  
ATOM    346  O   ARG B  15      11.086  24.232   9.265  1.00  9.92           O  
ATOM    347  CB  ARG B  15      11.233  23.429  12.138  1.00  9.25           C  
ATOM    348  CG  ARG B  15      10.083  22.486  12.218  1.00 10.07           C  
ATOM    349  CD  ARG B  15       9.143  22.825  13.325  1.00 12.15           C  
ATOM    350  NE  ARG B  15       7.994  21.926  13.306  1.00 11.98           N  
ATOM    351  CZ  ARG B  15       7.228  21.681  14.361  1.00 13.83           C  
ATOM    352  NH1 ARG B  15       7.511  22.263  15.524  1.00 14.25           N  
ATOM    353  NH2 ARG B  15       6.191  20.841  14.268  1.00 14.49           N  
ATOM    354  N   TYR B  16      11.404  22.016   8.969  1.00  7.65           N  
ATOM    355  CA  TYR B  16      10.766  21.980   7.655  1.00  7.52           C  
ATOM    356  C   TYR B  16       9.444  21.237   7.643  1.00  6.91           C  
ATOM    357  O   TYR B  16       8.786  21.151   6.606  1.00  8.40           O  
ATOM    358  CB  TYR B  16      11.697  21.319   6.627  1.00  6.15           C  
ATOM    359  CG  TYR B  16      12.951  22.110   6.376  1.00  7.01           C  
ATOM    360  CD1 TYR B  16      12.961  23.161   5.461  1.00  7.62           C  
ATOM    361  CD2 TYR B  16      14.123  21.819   7.055  1.00  9.07           C  
ATOM    362  CE1 TYR B  16      14.103  23.905   5.244  1.00  8.26           C  
ATOM    363  CE2 TYR B  16      15.291  22.548   6.825  1.00  9.51           C  
ATOM    364  CZ  TYR B  16      15.273  23.591   5.913  1.00  8.45           C  
ATOM    365  OH  TYR B  16      16.403  24.330   5.691  1.00  9.77           O  
ATOM    366  N   GLY B  17       9.045  20.692   8.789  1.00  7.36           N  
ATOM    367  CA  GLY B  17       7.800  19.988   8.825  1.00  8.00           C  
ATOM    368  C   GLY B  17       7.534  19.393  10.170  1.00  8.67           C  
ATOM    369  O   GLY B  17       8.067  19.848  11.171  1.00  8.78           O  
ATOM    370  N   THR B  18       6.687  18.365  10.176  1.00  9.18           N  
ATOM    371  CA  THR B  18       6.182  17.743  11.408  1.00  9.48           C  
ATOM    372  C   THR B  18       6.124  16.230  11.246  1.00  9.66           C  
ATOM    373  O   THR B  18       5.744  15.747  10.188  1.00 11.03           O  
ATOM    374  CB  THR B  18       4.773  18.279  11.718  1.00  9.37           C  
ATOM    375  OG1 THR B  18       4.848  19.700  11.841  1.00 10.77           O  
ATOM    376  CG2 THR B  18       4.207  17.665  13.011  1.00 10.54           C  
ATOM    377  N   CYS B  19       6.504  15.497  12.290  1.00  9.84           N  
ATOM    378  CA  CYS B  19       6.300  14.040  12.308  1.00 10.37           C  
ATOM    379  C   CYS B  19       5.176  13.720  13.280  1.00 10.90           C  
ATOM    380  O   CYS B  19       5.040  14.364  14.334  1.00 10.70           O  
ATOM    381  CB  CYS B  19       7.548  13.312  12.776  1.00 10.58           C  
ATOM    382  SG  CYS B  19       9.033  14.015  12.046  1.00 11.25           S  
ATOM    383  N   ILE B  20       4.368  12.740  12.917  1.00 10.30           N  
ATOM    384  CA  ILE B  20       3.332  12.228  13.803  1.00  9.87           C  
ATOM    385  C   ILE B  20       3.602  10.756  14.024  1.00 10.79           C  
ATOM    386  O   ILE B  20       3.533   9.966  13.085  1.00 10.32           O  
ATOM    387  CB  ILE B  20       1.927  12.362  13.181  1.00 10.92           C  
ATOM    388  CG1 ILE B  20       1.631  13.815  12.837  1.00 11.99           C  
ATOM    389  CG2 ILE B  20       0.860  11.807  14.148  1.00 11.48           C  
ATOM    390  CD1 ILE B  20       0.321  13.938  12.118  1.00 16.61           C  
ATOM    391  N   TYR B  21       3.929  10.393  15.256  1.00 11.33           N  
ATOM    392  CA  TYR B  21       4.043   8.976  15.587  1.00 12.97           C  
ATOM    393  C   TYR B  21       3.962   8.697  17.052  1.00 13.71           C  
ATOM    394  O   TYR B  21       4.255   9.563  17.870  1.00 14.54           O  
ATOM    395  CB  TYR B  21       5.277   8.320  14.948  1.00 13.79           C  
ATOM    396  CG  TYR B  21       6.621   8.874  15.354  1.00 15.32           C  
ATOM    397  CD1 TYR B  21       7.175   9.961  14.687  1.00 17.83           C  
ATOM    398  CD2 TYR B  21       7.355   8.276  16.378  1.00 17.10           C  
ATOM    399  CE1 TYR B  21       8.433  10.471  15.051  1.00 18.87           C  
ATOM    400  CE2 TYR B  21       8.614   8.774  16.755  1.00 18.83           C  
ATOM    401  CZ  TYR B  21       9.146   9.867  16.082  1.00 18.02           C  
ATOM    402  OH  TYR B  21      10.392  10.341  16.447  1.00 19.08           O  
ATOM    403  N   GLN B  22       3.527   7.480  17.372  1.00 14.16           N  
ATOM    404  CA  GLN B  22       3.336   7.058  18.754  1.00 13.72           C  
ATOM    405  C   GLN B  22       2.391   8.059  19.470  1.00 13.73           C  
ATOM    406  O   GLN B  22       2.559   8.329  20.648  1.00 13.60           O  
ATOM    407  CB  GLN B  22       4.714   6.939  19.464  1.00 14.29           C  
ATOM    408  CG  GLN B  22       5.743   5.950  18.822  1.00 13.92           C  
ATOM    409  CD  GLN B  22       5.295   4.495  18.918  1.00 16.11           C  
ATOM    410  OE1 GLN B  22       4.399   4.055  18.184  1.00 17.51           O  
ATOM    411  NE2 GLN B  22       5.900   3.747  19.829  1.00 14.43           N  
ATOM    412  N   GLY B  23       1.425   8.612  18.722  1.00 13.47           N  
ATOM    413  CA  GLY B  23       0.436   9.611  19.221  1.00 12.54           C  
ATOM    414  C   GLY B  23       0.985  10.986  19.584  1.00 11.37           C  
ATOM    415  O   GLY B  23       0.363  11.749  20.302  1.00 11.24           O  
ATOM    416  N   ARG B  24       2.168  11.300  19.075  1.00 10.64           N  
ATOM    417  CA  ARG B  24       2.905  12.499  19.474  1.00  9.45           C  
ATOM    418  C   ARG B  24       3.330  13.288  18.257  1.00  8.76           C  
ATOM    419  O   ARG B  24       3.523  12.726  17.175  1.00  8.60           O  
ATOM    420  CB  ARG B  24       4.158  12.125  20.297  1.00  9.34           C  
ATOM    421  CG  ARG B  24       3.807  11.304  21.521  1.00  9.01           C  
ATOM    422  CD  ARG B  24       4.996  10.545  22.086  1.00 12.19           C  
ATOM    423  NE  ARG B  24       6.028  11.467  22.515  1.00 10.81           N  
ATOM    424  CZ  ARG B  24       7.252  11.098  22.887  1.00 11.97           C  
ATOM    425  NH1 ARG B  24       8.114  12.015  23.284  1.00 14.48           N  
ATOM    426  NH2 ARG B  24       7.624   9.819  22.869  1.00 11.93           N  
ATOM    427  N   LEU B  25       3.516  14.588  18.479  1.00  8.92           N  
ATOM    428  CA  LEU B  25       3.981  15.533  17.467  1.00  9.55           C  
ATOM    429  C   LEU B  25       5.455  15.841  17.664  1.00 10.02           C  
ATOM    430  O   LEU B  25       5.888  16.092  18.797  1.00 11.31           O  
ATOM    431  CB  LEU B  25       3.178  16.827  17.547  1.00 10.28           C  
ATOM    432  CG  LEU B  25       1.716  16.713  17.087  1.00  8.79           C  
ATOM    433  CD1 LEU B  25       0.853  17.825  17.652  1.00 11.54           C  
ATOM    434  CD2 LEU B  25       1.650  16.712  15.562  1.00 12.55           C  
ATOM    435  N   TRP B  26       6.221  15.821  16.568  1.00  9.35           N  
ATOM    436  CA  TRP B  26       7.662  16.052  16.572  1.00  9.73           C  
ATOM    437  C   TRP B  26       7.995  17.091  15.507  1.00  9.86           C  
ATOM    438  O   TRP B  26       7.336  17.146  14.460  1.00 10.81           O  
ATOM    439  CB  TRP B  26       8.416  14.768  16.230  1.00 10.19           C  
ATOM    440  CG  TRP B  26       8.002  13.575  17.010  1.00 11.14           C  
ATOM    441  CD1 TRP B  26       6.816  12.887  16.885  1.00 12.71           C  
ATOM    442  CD2 TRP B  26       8.771  12.871  17.981  1.00 10.81           C  
ATOM    443  NE1 TRP B  26       6.793  11.827  17.759  1.00 11.37           N  
ATOM    444  CE2 TRP B  26       7.971  11.802  18.457  1.00 11.57           C  
ATOM    445  CE3 TRP B  26      10.033  13.071  18.544  1.00 12.02           C  
ATOM    446  CZ2 TRP B  26       8.413  10.906  19.429  1.00 10.41           C  
ATOM    447  CZ3 TRP B  26      10.465  12.190  19.523  1.00 12.07           C  
ATOM    448  CH2 TRP B  26       9.653  11.122  19.964  1.00 11.38           C  
ATOM    449  N   ALA B  27       9.010  17.920  15.756  1.00  9.60           N  
ATOM    450  CA  ALA B  27       9.519  18.816  14.712  1.00  9.62           C  
ATOM    451  C   ALA B  27      10.340  17.991  13.711  1.00  9.66           C  
ATOM    452  O   ALA B  27      11.119  17.119  14.104  1.00  9.51           O  
ATOM    453  CB  ALA B  27      10.364  19.935  15.318  1.00  9.86           C  
ATOM    454  N   PHE B  28      10.160  18.259  12.421  1.00  9.19           N  
ATOM    455  CA  PHE B  28      10.977  17.607  11.403  1.00  9.24           C  
ATOM    456  C   PHE B  28      12.067  18.585  10.996  1.00  9.14           C  
ATOM    457  O   PHE B  28      11.778  19.654  10.443  1.00 10.41           O  
ATOM    458  CB  PHE B  28      10.130  17.142  10.203  1.00  8.92           C  
ATOM    459  CG  PHE B  28      10.867  16.232   9.241  1.00  9.03           C  
ATOM    460  CD1 PHE B  28      11.371  14.989   9.650  1.00  9.78           C  
ATOM    461  CD2 PHE B  28      11.059  16.602   7.919  1.00  9.77           C  
ATOM    462  CE1 PHE B  28      12.036  14.145   8.745  1.00 10.32           C  
ATOM    463  CE2 PHE B  28      11.733  15.767   7.006  1.00 11.37           C  
ATOM    464  CZ  PHE B  28      12.210  14.538   7.430  1.00 10.87           C  
ATOM    465  N   CYS B  29      13.305  18.215  11.311  1.00  9.25           N  
ATOM    466  CA  CYS B  29      14.451  19.128  11.302  1.00  9.71           C  
ATOM    467  C   CYS B  29      15.492  18.688  10.300  1.00  9.34           C  
ATOM    468  O   CYS B  29      15.836  17.515  10.263  1.00  9.50           O  
ATOM    469  CB  CYS B  29      15.109  19.097  12.693  1.00  9.63           C  
ATOM    470  SG  CYS B  29      13.982  19.521  14.037  1.00 10.60           S  
ATOM    471  N   CYS B  30      16.002  19.602   9.485  1.00  9.73           N  
ATOM    472  CA  CYS B  30      17.047  19.210   8.533  1.00 10.91           C  
ATOM    473  C   CYS B  30      18.125  20.240   8.543  1.00 10.83           C  
ATOM    474  O   CYS B  30      17.911  21.397   8.922  1.00 11.05           O  
ATOM    475  CB  CYS B  30      16.522  19.103   7.104  1.00 11.30           C  
ATOM    476  SG  CYS B  30      15.023  18.113   6.879  1.00 14.45           S  
ATOM    477  OXT CYS B  30      19.243  19.901   8.151  1.00 12.11           O  
TER     478      CYS B  30                                                      
HETATM  479 CL    CL A  31       3.136  11.431  -7.051  1.00 73.90          CL  
HETATM  480  C1  GOL A  32       1.822   8.986   2.919  1.00 34.60           C  
HETATM  481  O1  GOL A  32       0.718   8.449   3.624  1.00 32.41           O  
HETATM  482  C2  GOL A  32       2.492   7.922   2.068  1.00 35.70           C  
HETATM  483  O2  GOL A  32       1.531   6.950   1.767  1.00 38.16           O  
HETATM  484  C3  GOL A  32       3.138   8.525   0.818  1.00 35.76           C  
HETATM  485  O3  GOL A  32       2.968   7.743  -0.344  1.00 34.52           O  
HETATM  486  C1  GOL B  31       7.503  19.146  19.291  1.00 41.60           C  
HETATM  487  O1  GOL B  31       7.579  19.491  20.655  1.00 44.28           O  
HETATM  488  C2  GOL B  31       6.480  20.084  18.685  1.00 41.42           C  
HETATM  489  O2  GOL B  31       6.998  21.397  18.709  1.00 42.42           O  
HETATM  490  C3  GOL B  31       6.167  19.639  17.264  1.00 41.03           C  
HETATM  491  O3  GOL B  31       4.981  20.239  16.794  1.00 36.09           O  
HETATM  492  O   HOH A  33      11.183  23.707  -0.268  1.00  6.25           O  
HETATM  493  O   HOH A  34       5.479  19.209  -3.192  1.00 12.03           O  
HETATM  494  O   HOH A  35      -2.049   9.926   4.403  1.00 27.07           O  
HETATM  495  O   HOH A  36       9.374  -3.513   0.403  1.00 14.46           O  
HETATM  496  O   HOH A  37       5.120  16.781  -4.895  1.00 15.05           O  
HETATM  497  O   HOH A  38       4.338   1.552   4.211  1.00 22.06           O  
HETATM  498  O   HOH A  39       0.831  14.197  -0.235  1.00 17.02           O  
HETATM  499  O   HOH A  40       4.891  20.978   4.030  1.00 21.74           O  
HETATM  500  O   HOH A  41      13.952  17.096   0.475  1.00 31.00           O  
HETATM  501  O   HOH A  42      15.582  -2.704   5.794  1.00 18.47           O  
HETATM  502  O   HOH A  43       0.235  20.284  -0.122  1.00 15.86           O  
HETATM  503  O   HOH A  44       7.009  -2.373   5.147  1.00 27.77           O  
HETATM  504  O   HOH A  45       3.978  -1.253   8.436  1.00 24.72           O  
HETATM  505  O   HOH A  46       0.282   5.671  10.171  1.00 37.53           O  
HETATM  506  O   HOH A  47       2.550  11.383  -0.555  1.00 20.73           O  
HETATM  507  O   HOH A  48       9.454  -6.676   5.605  1.00 14.96           O  
HETATM  508  O   HOH A  49       0.020   8.458  11.001  1.00 26.72           O  
HETATM  509  O   HOH A  50      -1.265   9.891   7.133  1.00 39.27           O  
HETATM  510  O   HOH A  51      14.518   1.130  13.325  1.00 35.45           O  
HETATM  511  O   HOH A  52       8.259  -1.195  -0.461  1.00 35.92           O  
HETATM  512  O   HOH A  53       2.292   3.692   1.343  1.00 28.92           O  
HETATM  513  O   HOH A  54      13.454  11.072   7.299  1.00 15.54           O  
HETATM  514  O   HOH A  55      14.864   1.686   9.089  1.00 30.27           O  
HETATM  515  O   HOH A  56      15.662   0.153   6.640  1.00 17.29           O  
HETATM  516  O   HOH A  57      -1.086   9.455   2.055  1.00 33.33           O  
HETATM  517  O   HOH A  58       9.311  -7.510   2.404  1.00 28.56           O  
HETATM  518  O   HOH A  59       2.854  16.745  -5.936  1.00 33.63           O  
HETATM  519  O   HOH B  32      -2.356  11.317  20.636  1.00 24.70           O  
HETATM  520  O   HOH B  33      13.772  14.069  19.966  1.00 21.86           O  
HETATM  521  O   HOH B  34      12.512  24.231  15.881  1.00  8.79           O  
HETATM  522  O   HOH B  35       9.015  21.557   3.936  1.00  9.41           O  
HETATM  523  O   HOH B  36      21.967  14.539  15.101  1.00 23.78           O  
HETATM  524  O   HOH B  37      -1.519   9.673  16.033  1.00 26.58           O  
HETATM  525  O   HOH B  38       0.456  14.017  22.064  1.00 30.01           O  
HETATM  526  O   HOH B  39      21.506  21.111   8.767  1.00 19.73           O  
HETATM  527  O   HOH B  40       5.247  14.078  23.176  1.00 24.71           O  
HETATM  528  O   HOH B  41      18.626  23.335   7.124  1.00 15.63           O  
HETATM  529  O   HOH B  42       9.711  26.473  10.565  1.00 29.30           O  
HETATM  530  O   HOH B  43      20.313  17.326  10.807  1.00 23.75           O  
HETATM  531  O   HOH B  44      17.170  25.596  14.785  1.00 20.82           O  
HETATM  532  O   HOH B  45       2.719   4.768  16.266  1.00 23.12           O  
HETATM  533  O   HOH B  46      14.244  10.668  10.031  1.00 19.68           O  
HETATM  534  O   HOH B  47      12.118   9.146  18.071  1.00 29.21           O  
HETATM  535  O   HOH B  48       4.870  16.194  21.255  1.00 29.69           O  
HETATM  536  O   HOH B  49       6.457  22.872  10.424  1.00 28.64           O  
HETATM  537  O   HOH B  50      13.549  10.878  12.511  1.00 19.33           O  
HETATM  538  O   HOH B  51      17.268  26.647   5.373  1.00 17.15           O  
HETATM  539  O   HOH B  52      13.124  26.581  11.625  1.00 18.91           O  
HETATM  540  O   HOH B  53      23.054  13.395  10.037  1.00 25.43           O  
HETATM  541  O   HOH B  54       5.890  21.507   6.218  1.00 20.06           O  
HETATM  542  O   HOH B  55       3.782  21.014   9.508  1.00 29.43           O  
HETATM  543  O   HOH B  56      17.376  11.405   6.534  1.00 39.45           O  
HETATM  544  O   HOH B  57       0.656   8.468  15.941  1.00 28.15           O  
HETATM  545  O   HOH B  58       2.539  15.560  21.017  1.00 22.73           O  
HETATM  546  O   HOH B  59       9.830  23.353  16.879  1.00 29.99           O  
HETATM  547  O   HOH B  60       1.464  20.574  10.879  1.00 36.18           O  
HETATM  548  O   HOH B  61      23.044  12.818  13.117  1.00 26.05           O  
HETATM  549  O   HOH B  62      10.962  11.688  23.594  1.00 24.09           O  
HETATM  550  O   HOH B  63       3.085  21.013  18.262  1.00 49.50           O  
HETATM  551  O   HOH B  64      16.563  14.917  18.951  1.00 27.45           O  
CONECT   11  237                                                                
CONECT   29  143                                                                
CONECT   66  231                                                                
CONECT  143   29                                                                
CONECT  231   66                                                                
CONECT  237   11                                                                
CONECT  250  476                                                                
CONECT  268  382                                                                
CONECT  305  470                                                                
CONECT  382  268                                                                
CONECT  470  305                                                                
CONECT  476  250                                                                
CONECT  480  481  482                                                           
CONECT  481  480                                                                
CONECT  482  480  483  484                                                      
CONECT  483  482                                                                
CONECT  484  482  485                                                           
CONECT  485  484                                                                
CONECT  486  487  488                                                           
CONECT  487  486                                                                
CONECT  488  486  489  490                                                      
CONECT  489  488                                                                
CONECT  490  488  491                                                           
CONECT  491  490                                                                
MASTER      323    0    3    0    6    0    4    6  549    2   24    6          
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.