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Database: PDB
Entry: 1ZMK
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Original site: 1ZMK 
HEADER    ANTIMICROBIAL PROTEIN                   10-MAY-05   1ZMK              
TITLE     CRYSTAL STRUCTURE OF HUMAN ALPHA-DEFENSIN-2 (VARIANT GLY16-> D-ALA), P
TITLE    2 42 21 2 SPACE GROUP                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUTROPHIL DEFENSIN 2;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DEFA3, DEF3;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ALPHA-DEFENSIN, ANTIMICROBIAL, D-AMINO ACID SUBSTITUTIONS,            
KEYWDS   2 ANTIMICROBIAL PROTEIN                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LUBKOWSKI,A.PRAHL,W.LU                                              
REVDAT   7   23-AUG-23 1ZMK    1       REMARK                                   
REVDAT   6   20-OCT-21 1ZMK    1       REMARK SEQADV LINK                       
REVDAT   5   11-OCT-17 1ZMK    1       REMARK                                   
REVDAT   4   13-JUL-11 1ZMK    1       VERSN                                    
REVDAT   3   24-FEB-09 1ZMK    1       VERSN                                    
REVDAT   2   20-DEC-05 1ZMK    1       JRNL                                     
REVDAT   1   16-AUG-05 1ZMK    0                                                
JRNL        AUTH   C.XIE,A.PRAHL,B.ERICKSEN,Z.WU,P.ZENG,X.LI,W.Y.LU,            
JRNL        AUTH 2 J.LUBKOWSKI,W.LU                                             
JRNL        TITL   RECONSTRUCTION OF THE CONSERVED BETA-BULGE IN MAMMALIAN      
JRNL        TITL 2 DEFENSINS USING D-AMINO ACIDS.                               
JRNL        REF    J.BIOL.CHEM.                  V. 280 32921 2005              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15894545                                                     
JRNL        DOI    10.1074/JBC.M503084200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.47                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 13688                          
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) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.177                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 734                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.37                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1921                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.50                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 105                          
REMARK   3   BIN FREE R VALUE                    : 0.2010                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 468                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 75                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.03000                                              
REMARK   3    B22 (A**2) : 0.03000                                              
REMARK   3    B33 (A**2) : -0.06000                                             
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): 0.054         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.047         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.025         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.270         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.966                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   498 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):   447 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):   673 ; 1.721 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  1020 ; 3.881 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):    56 ; 8.149 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    22 ;19.488 ;18.182       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):    73 ;10.723 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;10.136 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):    65 ; 0.183 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   540 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   130 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):    71 ; 0.288 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):   422 ; 0.235 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   213 ; 0.197 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   342 ; 0.119 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    65 ; 0.245 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     4 ; 0.258 ; 0.500       
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):     8 ; 0.306 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    62 ; 0.279 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    25 ; 0.424 ; 0.500       
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):   369 ; 2.553 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   122 ; 1.012 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   458 ; 3.102 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   304 ; 3.017 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   215 ; 3.380 ; 3.000       
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):  1307 ; 1.636 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    77 ; 9.842 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):   929 ; 3.526 ; 3.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 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    29                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.4999  28.4337  42.5799              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0011 T22:  -0.0016                                     
REMARK   3      T33:  -0.0322 T12:   0.0204                                     
REMARK   3      T13:   0.0031 T23:  -0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8732 L22:   0.4419                                     
REMARK   3      L33:   0.5575 L12:   0.3533                                     
REMARK   3      L13:   0.4303 L23:  -0.0208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0949 S12:  -0.2616 S13:   0.0880                       
REMARK   3      S21:   0.0919 S22:   0.0528 S23:   0.0421                       
REMARK   3      S31:   0.0255 S32:   0.0022 S33:   0.0421                       
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    29                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.1823  34.1961  32.6357              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0230 T22:  -0.0105                                     
REMARK   3      T33:  -0.0096 T12:   0.0066                                     
REMARK   3      T13:   0.0002 T23:  -0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3516 L22:   2.9878                                     
REMARK   3      L33:   1.3046 L12:   0.6794                                     
REMARK   3      L13:   0.1297 L23:   0.9094                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0052 S12:  -0.0091 S13:   0.0399                       
REMARK   3      S21:   0.0054 S22:  -0.0363 S23:   0.0902                       
REMARK   3      S31:  -0.0180 S32:  -0.0328 S33:   0.0415                       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1ZMK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000032895.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUN-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9200                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24405                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 10.20                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.42900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: BASED ON MONOMER OF HNP-3 (PDB ID CODE 1DFN)         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRI-SODIUM CITRATE DIHYDRATE,            
REMARK 280  TRIS/HCL, PEG 8000, PH 8.5, VAPOR DIFFUSION, HANGING DROP,          
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 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   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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  0.000000 -1.000000  0.000000       23.57400            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       23.57400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       25.32150            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       23.57400            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       23.57400            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       25.32150            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       23.57400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       23.57400            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       25.32150            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       23.57400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       23.57400            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       25.32150            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 4120 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -154.0 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       47.14800            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       47.14800            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000       50.64300            
REMARK 350   BIOMT1   4  0.000000 -1.000000  0.000000       47.14800            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000       47.14800            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000       50.64300            
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 CL    CL B 102  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 135  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N    CYS A     1    CL     CL A   101              2.01            
REMARK 500   N    CYS B     1    CL     CL A   101              2.05            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   124     O    HOH B   227     5546     1.56            
REMARK 500   O    HOH A   138     O    HOH B   235     2665     1.96            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS B  29   CB    CYS B  29   SG     -0.110                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    CYS B  29   CA  -  CB  -  SG  ANGL. DEV. =   9.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DFN   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RELATED ALPHA-DEFENSIN                          
REMARK 900 RELATED ID: 1ZMI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1ZMM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1ZMP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1ZMQ   RELATED DB: PDB                                   
DBREF  1ZMK A    1    29  UNP    P59666   DEF3_HUMAN      66     94             
DBREF  1ZMK B    1    29  UNP    P59666   DEF3_HUMAN      66     94             
SEQADV 1ZMK DAL A   16  UNP  P59666    GLY    81 ENGINEERED MUTATION            
SEQADV 1ZMK DAL B   16  UNP  P59666    GLY    81 ENGINEERED MUTATION            
SEQRES   1 A   29  CYS TYR CYS ARG ILE PRO ALA CYS ILE ALA GLY GLU ARG          
SEQRES   2 A   29  ARG TYR DAL THR CYS ILE TYR GLN GLY ARG LEU TRP ALA          
SEQRES   3 A   29  PHE CYS CYS                                                  
SEQRES   1 B   29  CYS TYR CYS ARG ILE PRO ALA CYS ILE ALA GLY GLU ARG          
SEQRES   2 B   29  ARG TYR DAL THR CYS ILE TYR GLN GLY ARG LEU TRP ALA          
SEQRES   3 B   29  PHE CYS CYS                                                  
MODRES 1ZMK DAL A   16  ALA  D-ALANINE                                          
MODRES 1ZMK DAL B   16  ALA  D-ALANINE                                          
HET    DAL  A  16       5                                                       
HET    DAL  B  16       5                                                       
HET     CL  A 101       1                                                       
HET     CL  B 102       1                                                       
HET    GOL  B 201      12                                                       
HETNAM     DAL D-ALANINE                                                        
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  DAL    2(C3 H7 N O2)                                                
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   5  GOL    C3 H8 O3                                                     
FORMUL   6  HOH   *75(H2 O)                                                     
SHEET    1   A 6 TYR A   2  ARG A   4  0                                        
SHEET    2   A 6 ARG A  23  CYS A  29 -1  O  CYS A  28   N  TYR A   2           
SHEET    3   A 6 ARG A  13  TYR A  20 -1  N  TYR A  15   O  PHE A  27           
SHEET    4   A 6 ARG B  13  TYR B  20 -1  O  ILE B  19   N  THR A  17           
SHEET    5   A 6 ARG B  23  CYS B  29 -1  O  PHE B  27   N  TYR B  15           
SHEET    6   A 6 TYR B   2  ARG B   4 -1  N  TYR B   2   O  CYS B  28           
SSBOND   1 CYS A    1    CYS A   29                          1555   1555  2.05  
SSBOND   2 CYS A    3    CYS A   18                          1555   1555  2.05  
SSBOND   3 CYS A    8    CYS A   28                          1555   1555  2.05  
SSBOND   4 CYS B    1    CYS B   29                          1555   1555  2.21  
SSBOND   5 CYS B    3    CYS B   18                          1555   1555  2.03  
SSBOND   6 CYS B    8    CYS B   28                          1555   1555  2.06  
LINK         C   TYR A  15                 N   DAL A  16     1555   1555  1.33  
LINK         C   DAL A  16                 N   THR A  17     1555   1555  1.33  
LINK         C   TYR B  15                 N   DAL B  16     1555   1555  1.30  
LINK         C   DAL B  16                 N   THR B  17     1555   1555  1.33  
CISPEP   1 ILE A    5    PRO A    6          0         1.37                     
CISPEP   2 ILE B    5    PRO B    6          0         7.43                     
SITE     1 AC1  3 CYS A   1  CYS B   1  HOH B 223                               
SITE     1 AC2  1 HOH B 218                                                     
SITE     1 AC3  7 ARG B  14  THR B  17  ARG B  23  LEU B  24                    
SITE     2 AC3  7 TRP B  25  ALA B  26  HOH B 231                               
CRYST1   47.148   47.148   50.643  90.00  90.00  90.00 P 42 21 2    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      0.021210  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.021210  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019746        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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