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Database: PDB
Entry: 2NWD
LinkDB: 2NWD
Original site: 2NWD 
HEADER    HYDROLASE                               14-NOV-06   2NWD              
TITLE     STRUCTURE OF CHEMICALLY SYNTHESIZED HUMAN LYSOZYME AT 1 ANGSTROM      
TITLE    2 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSOZYME C;                                                
COMPND   3 CHAIN: X;                                                            
COMPND   4 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C;                              
COMPND   5 EC: 3.2.1.17;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 OTHER_DETAILS: CHEMICAL PROTEIN SYNTHESIS                            
KEYWDS    NATIVE CHEMICAL LIGATION, CHEMICAL PROTEIN SYNTHESIS, CONVERGENT      
KEYWDS   2 SYNTHESIS, HYDROLASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.DUREK,V.Y.TORBEEV,S.B.H.KENT                                        
REVDAT   4   30-AUG-23 2NWD    1       REMARK                                   
REVDAT   3   24-FEB-09 2NWD    1       VERSN                                    
REVDAT   2   03-APR-07 2NWD    1       JRNL                                     
REVDAT   1   19-DEC-06 2NWD    0                                                
JRNL        AUTH   T.DUREK,V.Y.TORBEEV,S.B.KENT                                 
JRNL        TITL   CONVERGENT CHEMICAL SYNTHESIS AND HIGH-RESOLUTION X-RAY      
JRNL        TITL 2 STRUCTURE OF HUMAN LYSOZYME.                                 
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 104  4846 2007              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   17360367                                                     
JRNL        DOI    10.1073/PNAS.0610630104                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.04 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 50848                          
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) : 0.134                           
REMARK   3   R VALUE            (WORKING SET) : 0.133                           
REMARK   3   FREE R VALUE                     : 0.152                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2721                            
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) : 1.04                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.07                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3566                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.17                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2050                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 172                          
REMARK   3   BIN FREE R VALUE                    : 0.2500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1029                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 210                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 8.17                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.37000                                             
REMARK   3    B22 (A**2) : 0.22000                                              
REMARK   3    B33 (A**2) : 0.15000                                              
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): 0.025         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.026         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.015         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.651         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.976                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.974                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1065 ; 0.017 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):   751 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1443 ; 1.716 ; 1.915       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  1777 ; 1.111 ; 3.009       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   129 ; 6.625 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    56 ;35.339 ;22.143       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   177 ;11.198 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;15.693 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   149 ; 0.113 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1214 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   248 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   216 ; 0.230 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):   853 ; 0.209 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   530 ; 0.184 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   540 ; 0.087 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    94 ; 0.221 ; 0.200       
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):    12 ; 0.089 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    47 ; 0.365 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    23 ; 0.183 ; 0.200       
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):   822 ; 2.853 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   271 ; 1.556 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1025 ; 3.288 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   510 ; 3.946 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   418 ; 4.847 ; 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):  2327 ; 2.076 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   210 ;14.635 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  1792 ; 6.034 ; 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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 2NWD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-NOV-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000040383.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53675                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CCP4                                                  
REMARK 200 STARTING MODEL: 1JSF, SEE REF. K. HARADA, Y. ABE, M. MURAKI,         
REMARK 200  PROTEINS, 1998, 30, 232.                                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: C 6 MG/ML, 60 MM LICL, 1.25 MM HEPES,    
REMARK 280  15 MM SODIUM PHOSPHATE, 1.25 M NACL , PH 4.9, VAPOR DIFFUSION,      
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       28.13050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       16.42550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.56650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       16.42550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.13050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.56650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X                                     
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 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   OE1  GLN X   126     O    HOH X   324              1.97            
REMARK 500   O    HOH X   274     O    HOH X   282              2.16            
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    GLU X   7   CG    GLU X   7   CD      0.122                       
REMARK 500    ARG X  21   CG    ARG X  21   CD     -0.179                       
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    GLU X   7   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.2 DEGREES          
REMARK 500    GLU X   7   CG  -  CD  -  OE1 ANGL. DEV. =  14.3 DEGREES          
REMARK 500    ARG X  21   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    ARG X  21   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG X 119   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2NWD X    1   130  UNP    P61626   LYSC_HUMAN      19    148             
SEQRES   1 X  130  LYS VAL PHE GLU ARG CYS GLU LEU ALA ARG THR LEU LYS          
SEQRES   2 X  130  ARG LEU GLY MET ASP GLY TYR ARG GLY ILE SER LEU ALA          
SEQRES   3 X  130  ASN TRP MET CYS LEU ALA LYS TRP GLU SER GLY TYR ASN          
SEQRES   4 X  130  THR ARG ALA THR ASN TYR ASN ALA GLY ASP ARG SER THR          
SEQRES   5 X  130  ASP TYR GLY ILE PHE GLN ILE ASN SER ARG TYR TRP CYS          
SEQRES   6 X  130  ASN ASP GLY LYS THR PRO GLY ALA VAL ASN ALA CYS HIS          
SEQRES   7 X  130  LEU SER CYS SER ALA LEU LEU GLN ASP ASN ILE ALA ASP          
SEQRES   8 X  130  ALA VAL ALA CYS ALA LYS ARG VAL VAL ARG ASP PRO GLN          
SEQRES   9 X  130  GLY ILE ARG ALA TRP VAL ALA TRP ARG ASN ARG CYS GLN          
SEQRES  10 X  130  ASN ARG ASP VAL ARG GLN TYR VAL GLN GLY CYS GLY VAL          
FORMUL   2  HOH   *210(H2 O)                                                    
HELIX    1   1 GLU X    4  LEU X   15  1                                  12    
HELIX    2   2 GLY X   19  ILE X   23  5                                   5    
HELIX    3   3 SER X   24  GLY X   37  1                                  14    
HELIX    4   4 SER X   80  GLN X   86  5                                   7    
HELIX    5   5 ILE X   89  ASP X  102  1                                  14    
HELIX    6   6 GLN X  104  ALA X  108  5                                   5    
HELIX    7   7 TRP X  109  CYS X  116  1                                   8    
HELIX    8   8 VAL X  121  VAL X  125  5                                   5    
SHEET    1   A 3 THR X  43  TYR X  45  0                                        
SHEET    2   A 3 THR X  52  TYR X  54 -1  O  ASP X  53   N  ASN X  44           
SHEET    3   A 3 ILE X  59  ASN X  60 -1  O  ILE X  59   N  TYR X  54           
SSBOND   1 CYS X    6    CYS X  128                          1555   1555  2.08  
SSBOND   2 CYS X   30    CYS X  116                          1555   1555  2.07  
SSBOND   3 CYS X   65    CYS X   81                          1555   1555  2.06  
SSBOND   4 CYS X   77    CYS X   95                          1555   1555  2.05  
CRYST1   56.261   61.133   32.851  90.00  90.00  90.00 P 21 21 21    4          
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      0.017774  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016358  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.030440        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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