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Database: PDB
Entry: 1KXG
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Original site: 1KXG 
HEADER    CYTOKINE                                31-JAN-02   1KXG              
TITLE     THE 2.0 ANG RESOLUTION STRUCTURE OF BLYS, B LYMPHOCYTE                
TITLE    2 STIMULATOR.                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: B LYMPHOCYTE STIMULATOR;                                   
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: SOLUBLE PORTION (RESIDUES 134-285);                        
COMPND   5 SYNONYM: BLYS, TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY              
COMPND   6 MEMBER 13B;                                                          
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PA2                                        
KEYWDS    BAFF, TALL-1, THANK, ZTNF4, CYTOKINE, TNF SUPERFAMILY,                
KEYWDS   2 JELLYROLL, BETA-SANDWICH                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.A.OREN,Y.LI,Y.VOLOVIK,T.S.MORRIS,C.DHARIA,K.DAS,                    
AUTHOR   2 O.GALPERINA,R.GENTZ,E.ARNOLD                                         
REVDAT   3   24-FEB-09 1KXG    1       VERSN                                    
REVDAT   2   03-APR-02 1KXG    1       JRNL                                     
REVDAT   1   20-MAR-02 1KXG    0                                                
JRNL        AUTH   D.A.OREN,Y.LI,Y.VOLOVIK,T.S.MORRIS,C.DHARIA,K.DAS,           
JRNL        AUTH 2 O.GALPERINA,R.GENTZ,E.ARNOLD                                 
JRNL        TITL   STRUCTURAL BASIS OF BLYS RECEPTOR RECOGNITION.               
JRNL        REF    NAT.STRUCT.BIOL.              V.   9   288 2002              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   11862220                                                     
JRNL        DOI    10.1038/NSB769                                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3298001.290                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 93180                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1849                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 14664                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2230                       
REMARK   3   BIN FREE R VALUE                    : 0.2430                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 1.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 282                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.014                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6858                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 153                                     
REMARK   3   SOLVENT ATOMS            : 462                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.22                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.17                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.25                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.19                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.72                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.570 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.520 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.270 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.520 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 46.31                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : CIT+DIO.PARAM                                  
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : CIT+DIO.TOP                                    
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUES 204-206 IN ALL SIX CHAINS        
REMARK   3  HAVE VERY POOR ELECTRON DENSITY.                                    
REMARK   4                                                                      
REMARK   4 1KXG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB015436.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JUL-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 108.0                              
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.942                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 93234                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -1.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 20.800                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.38400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
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: 1D0G                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% DIOXANE, 25 MM MGCL2, PH 6.0,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 279.0K                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      107.48667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       53.74333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       80.61500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       26.87167            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      134.35833            
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 300 REMARK: THE BIOLOGICALLY ACTIVE FORM IS A TRIMER AND TWO             
REMARK 300 COMPLETE TRIMERS ARE FOUND IN THE ASYMMETRIC UNIT.                   
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 27.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 7.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A   134                                                      
REMARK 465     VAL A   135                                                      
REMARK 465     GLN A   136                                                      
REMARK 465     GLY A   137                                                      
REMARK 465     PRO A   138                                                      
REMARK 465     GLU A   139                                                      
REMARK 465     GLU A   140                                                      
REMARK 465     THR A   141                                                      
REMARK 465     ALA B   134                                                      
REMARK 465     VAL B   135                                                      
REMARK 465     GLN B   136                                                      
REMARK 465     GLY B   137                                                      
REMARK 465     PRO B   138                                                      
REMARK 465     GLU B   139                                                      
REMARK 465     GLU B   140                                                      
REMARK 465     THR B   141                                                      
REMARK 465     ALA C   134                                                      
REMARK 465     VAL C   135                                                      
REMARK 465     GLN C   136                                                      
REMARK 465     GLY C   137                                                      
REMARK 465     PRO C   138                                                      
REMARK 465     GLU C   139                                                      
REMARK 465     GLU C   140                                                      
REMARK 465     THR C   141                                                      
REMARK 465     ALA D   134                                                      
REMARK 465     VAL D   135                                                      
REMARK 465     GLN D   136                                                      
REMARK 465     GLY D   137                                                      
REMARK 465     PRO D   138                                                      
REMARK 465     GLU D   139                                                      
REMARK 465     GLU D   140                                                      
REMARK 465     THR D   141                                                      
REMARK 465     ALA E   134                                                      
REMARK 465     VAL E   135                                                      
REMARK 465     GLN E   136                                                      
REMARK 465     GLY E   137                                                      
REMARK 465     PRO E   138                                                      
REMARK 465     GLU E   139                                                      
REMARK 465     GLU E   140                                                      
REMARK 465     THR E   141                                                      
REMARK 465     ALA F   134                                                      
REMARK 465     VAL F   135                                                      
REMARK 465     GLN F   136                                                      
REMARK 465     GLY F   137                                                      
REMARK 465     PRO F   138                                                      
REMARK 465     GLU F   139                                                      
REMARK 465     GLU F   140                                                      
REMARK 465     THR F   141                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 242       78.89   -169.91                                   
REMARK 500    PRO A 264       61.39    -67.82                                   
REMARK 500    ARG A 265      142.43   -170.18                                   
REMARK 500    THR B 205      -18.34     67.04                                   
REMARK 500    ALA B 207      134.20    -28.19                                   
REMARK 500    ASN B 242       79.06   -162.93                                   
REMARK 500    PRO B 264       60.06    -67.05                                   
REMARK 500    THR C 205      178.18    -54.85                                   
REMARK 500    ASN C 242       79.70   -161.57                                   
REMARK 500    PRO C 264       54.32    -68.34                                   
REMARK 500    THR D 205      -18.94     37.87                                   
REMARK 500    ASN D 242       79.50   -167.08                                   
REMARK 500    PRO D 264       48.78    -66.65                                   
REMARK 500    THR E 205       -7.23     56.49                                   
REMARK 500    ALA E 207      132.11    -29.24                                   
REMARK 500    ASN E 242       75.07   -164.85                                   
REMARK 500    PRO E 264       58.35    -68.90                                   
REMARK 500    LYS F 204     -162.67   -104.70                                   
REMARK 500    THR F 205      -18.76     54.52                                   
REMARK 500    ALA F 207      133.81    -28.55                                   
REMARK 500    ASN F 242       73.88   -166.73                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 701  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN B 234   OE1                                                    
REMARK 620 2 HOH B1019   O   111.2                                              
REMARK 620 3 HOH C1017   O    80.2  78.5                                        
REMARK 620 4 GLN A 234   OE1  88.9  86.4 156.6                                  
REMARK 620 5 GLN C 234   OE1  91.4 157.0 110.7  90.1                            
REMARK 620 6 HOH A 504   O   152.4  83.0  79.7 116.3  78.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 901  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CIT A 889   O4                                                     
REMARK 620 2 HOH F 395   O    88.0                                              
REMARK 620 3 CIT F 888   O4  173.5  94.6                                        
REMARK 620 4 CIT A 889   O7   63.1  91.7 110.8                                  
REMARK 620 5 CIT F 888   O7  115.4 106.1  58.1  54.0                            
REMARK 620 6 HOH A  10   O    88.1 164.5  90.9  99.9  89.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 903  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CIT F 888   O1                                                     
REMARK 620 2 CIT F 888   O7   70.3                                              
REMARK 620 3 ARG A 214   NH2  92.7 128.8                                        
REMARK 620 4 HOH A  10   O   153.4  89.2 113.6                                  
REMARK 620 5 LYS A 252   O    70.3 131.1  80.6 116.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 702  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C1018   O                                                      
REMARK 620 2 HOH C1017   O    88.9                                              
REMARK 620 3 HOH B1020   O    90.5  92.4                                        
REMARK 620 4 HOH A 504   O    90.4  88.2 178.9                                  
REMARK 620 5 HOH A 507   O    86.6 175.3  89.1  90.5                            
REMARK 620 6 HOH B1019   O   177.9  89.5  90.8  88.2  95.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 801  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH E1020   O                                                      
REMARK 620 2 HOH F 603   O    85.5                                              
REMARK 620 3 HOH D1013   O    84.7  85.1                                        
REMARK 620 4 HOH D1014   O    93.2 176.5  91.6                                  
REMARK 620 5 HOH E1021   O    91.1  92.0 175.0  91.2                            
REMARK 620 6 HOH F 608   O   175.7  90.4  93.5  90.8  90.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 802  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN E 234   OE1                                                    
REMARK 620 2 HOH E1020   O   115.2                                              
REMARK 620 3 HOH F 603   O    83.5  79.8                                        
REMARK 620 4 GLN F 234   OE1  89.5 153.1 115.2                                  
REMARK 620 5 HOH D1013   O   156.8  79.8  81.9  80.5                            
REMARK 620 6 GLN D 234   OE1  91.2  82.1 156.9  87.2 109.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 902  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH F 395   O                                                      
REMARK 620 2 CIT A 889   O7   93.6                                              
REMARK 620 3 CIT F 888   O5  117.5  52.9                                        
REMARK 620 4 ARG F 214   NH2 119.5 119.5  66.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 701                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 702                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 801                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 802                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 901                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 902                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 903                  
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT F 888                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 889                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A 1001                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A 1002                
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO C 1003                
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A 1004                
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO B 1005                
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO C 1006                
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO C 1007                
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO C 1008                
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO D 1009                
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO E 1010                
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO E 1011                
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO D 1012                
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO F 1013                
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO C 1014                
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A 1015                
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO C 1016                
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A 1017                
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO B 1018                
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO E 1019                
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO F 1020                
DBREF  1KXG A  134   285  UNP    Q9Y275   TN13B_HUMAN    134    285             
DBREF  1KXG B  134   285  UNP    Q9Y275   TN13B_HUMAN    134    285             
DBREF  1KXG C  134   285  UNP    Q9Y275   TN13B_HUMAN    134    285             
DBREF  1KXG D  134   285  UNP    Q9Y275   TN13B_HUMAN    134    285             
DBREF  1KXG E  134   285  UNP    Q9Y275   TN13B_HUMAN    134    285             
DBREF  1KXG F  134   285  UNP    Q9Y275   TN13B_HUMAN    134    285             
SEQRES   1 A  152  ALA VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS          
SEQRES   2 A  152  LEU GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN          
SEQRES   3 A  152  LYS GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE          
SEQRES   4 A  152  LYS ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE          
SEQRES   5 A  152  LEU VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN          
SEQRES   6 A  152  VAL LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU          
SEQRES   7 A  152  ILE GLN ARG LYS LYS VAL HIS VAL PHE GLY ASP GLU LEU          
SEQRES   8 A  152  SER LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO          
SEQRES   9 A  152  GLU THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE          
SEQRES  10 A  152  ALA LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE          
SEQRES  11 A  152  PRO ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL          
SEQRES  12 A  152  THR PHE PHE GLY ALA LEU LYS LEU LEU                          
SEQRES   1 B  152  ALA VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS          
SEQRES   2 B  152  LEU GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN          
SEQRES   3 B  152  LYS GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE          
SEQRES   4 B  152  LYS ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE          
SEQRES   5 B  152  LEU VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN          
SEQRES   6 B  152  VAL LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU          
SEQRES   7 B  152  ILE GLN ARG LYS LYS VAL HIS VAL PHE GLY ASP GLU LEU          
SEQRES   8 B  152  SER LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO          
SEQRES   9 B  152  GLU THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE          
SEQRES  10 B  152  ALA LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE          
SEQRES  11 B  152  PRO ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL          
SEQRES  12 B  152  THR PHE PHE GLY ALA LEU LYS LEU LEU                          
SEQRES   1 C  152  ALA VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS          
SEQRES   2 C  152  LEU GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN          
SEQRES   3 C  152  LYS GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE          
SEQRES   4 C  152  LYS ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE          
SEQRES   5 C  152  LEU VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN          
SEQRES   6 C  152  VAL LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU          
SEQRES   7 C  152  ILE GLN ARG LYS LYS VAL HIS VAL PHE GLY ASP GLU LEU          
SEQRES   8 C  152  SER LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO          
SEQRES   9 C  152  GLU THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE          
SEQRES  10 C  152  ALA LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE          
SEQRES  11 C  152  PRO ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL          
SEQRES  12 C  152  THR PHE PHE GLY ALA LEU LYS LEU LEU                          
SEQRES   1 D  152  ALA VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS          
SEQRES   2 D  152  LEU GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN          
SEQRES   3 D  152  LYS GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE          
SEQRES   4 D  152  LYS ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE          
SEQRES   5 D  152  LEU VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN          
SEQRES   6 D  152  VAL LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU          
SEQRES   7 D  152  ILE GLN ARG LYS LYS VAL HIS VAL PHE GLY ASP GLU LEU          
SEQRES   8 D  152  SER LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO          
SEQRES   9 D  152  GLU THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE          
SEQRES  10 D  152  ALA LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE          
SEQRES  11 D  152  PRO ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL          
SEQRES  12 D  152  THR PHE PHE GLY ALA LEU LYS LEU LEU                          
SEQRES   1 E  152  ALA VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS          
SEQRES   2 E  152  LEU GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN          
SEQRES   3 E  152  LYS GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE          
SEQRES   4 E  152  LYS ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE          
SEQRES   5 E  152  LEU VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN          
SEQRES   6 E  152  VAL LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU          
SEQRES   7 E  152  ILE GLN ARG LYS LYS VAL HIS VAL PHE GLY ASP GLU LEU          
SEQRES   8 E  152  SER LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO          
SEQRES   9 E  152  GLU THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE          
SEQRES  10 E  152  ALA LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE          
SEQRES  11 E  152  PRO ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL          
SEQRES  12 E  152  THR PHE PHE GLY ALA LEU LYS LEU LEU                          
SEQRES   1 F  152  ALA VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS          
SEQRES   2 F  152  LEU GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN          
SEQRES   3 F  152  LYS GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE          
SEQRES   4 F  152  LYS ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE          
SEQRES   5 F  152  LEU VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN          
SEQRES   6 F  152  VAL LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU          
SEQRES   7 F  152  ILE GLN ARG LYS LYS VAL HIS VAL PHE GLY ASP GLU LEU          
SEQRES   8 F  152  SER LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO          
SEQRES   9 F  152  GLU THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE          
SEQRES  10 F  152  ALA LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE          
SEQRES  11 F  152  PRO ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL          
SEQRES  12 F  152  THR PHE PHE GLY ALA LEU LYS LEU LEU                          
HET     MG  A 701       1                                                       
HET     MG  B 702       1                                                       
HET     MG  D 801       1                                                       
HET     MG  D 802       1                                                       
HET     MG  A 901       1                                                       
HET     MG  F 902       1                                                       
HET     MG  A 903       1                                                       
HET    CIT  F 888      13                                                       
HET    CIT  A 889      13                                                       
HET    DIO  A1001       6                                                       
HET    DIO  A1002       6                                                       
HET    DIO  C1003       6                                                       
HET    DIO  A1004       6                                                       
HET    DIO  B1005       6                                                       
HET    DIO  C1006       6                                                       
HET    DIO  C1007       6                                                       
HET    DIO  C1008       6                                                       
HET    DIO  D1009       6                                                       
HET    DIO  E1010       6                                                       
HET    DIO  E1011       6                                                       
HET    DIO  D1012       6                                                       
HET    DIO  F1013       6                                                       
HET    DIO  C1014       6                                                       
HET    DIO  A1015       6                                                       
HET    DIO  C1016       6                                                       
HET    DIO  A1017       6                                                       
HET    DIO  B1018       6                                                       
HET    DIO  E1019       6                                                       
HET    DIO  F1020       6                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     CIT CITRIC ACID                                                      
HETNAM     DIO 1,4-DIETHYLENE DIOXIDE                                           
FORMUL   7   MG    7(MG 2+)                                                     
FORMUL  14  CIT    2(C6 H8 O7)                                                  
FORMUL  16  DIO    20(C4 H8 O2)                                                 
FORMUL  36  HOH   *462(H2 O)                                                    
SHEET    1   A 3 ASN A 243  LEU A 253  0                                        
SHEET    2   A 3 GLY A 191  TYR A 201 -1  N  ILE A 195   O  GLY A 249           
SHEET    3   A 3 ILE A 270  SER A 271 -1  O  SER A 271   N  LEU A 200           
SHEET    1   B 5 ASN A 243  LEU A 253  0                                        
SHEET    2   B 5 GLY A 191  TYR A 201 -1  N  ILE A 195   O  GLY A 249           
SHEET    3   B 5 PHE A 278  LYS A 283 -1  O  LEU A 282   N  PHE A 194           
SHEET    4   B 5 CYS A 146  ALA A 151 -1  N  LEU A 149   O  PHE A 279           
SHEET    5   B 5 TRP A 168  ARG A 174 -1  O  ARG A 174   N  CYS A 146           
SHEET    1   C 5 LEU A 226  ASN A 235  0                                        
SHEET    2   C 5 ALA A 207  LYS A 215 -1  N  ARG A 214   O  VAL A 227           
SHEET    3   C 5 GLU A 258  ILE A 263 -1  O  GLU A 258   N  LYS A 215           
SHEET    4   C 5 TYR A 163  PHE A 165 -1  N  THR A 164   O  ILE A 263           
SHEET    5   C 5 ILE A 158  LYS A 160 -1  N  ILE A 158   O  PHE A 165           
SHEET    1   D 5 LEU A 226  ASN A 235  0                                        
SHEET    2   D 5 ALA A 207  LYS A 215 -1  N  ARG A 214   O  VAL A 227           
SHEET    3   D 5 GLU A 258  ILE A 263 -1  O  GLU A 258   N  LYS A 215           
SHEET    4   D 5 LYS A 184  VAL A 187 -1  N  ILE A 185   O  LEU A 259           
SHEET    5   D 5 LEU A 178  LYS A 181 -1  N  GLU A 179   O  LEU A 186           
SHEET    1   E 5 TRP B 168  ARG B 174  0                                        
SHEET    2   E 5 CYS B 146  ALA B 151 -1  N  CYS B 146   O  ARG B 174           
SHEET    3   E 5 PHE B 278  LYS B 283 -1  O  PHE B 279   N  LEU B 149           
SHEET    4   E 5 GLY B 191  TYR B 201 -1  N  TYR B 196   O  GLY B 280           
SHEET    5   E 5 ASN B 243  LEU B 253 -1  O  GLY B 249   N  ILE B 195           
SHEET    1   F 5 LEU B 226  GLN B 234  0                                        
SHEET    2   F 5 MET B 208  LYS B 215 -1  N  MET B 208   O  GLN B 234           
SHEET    3   F 5 GLU B 258  ILE B 263 -1  O  GLU B 258   N  LYS B 215           
SHEET    4   F 5 TYR B 163  PHE B 165 -1  N  THR B 164   O  ILE B 263           
SHEET    5   F 5 ILE B 158  LYS B 160 -1  N  ILE B 158   O  PHE B 165           
SHEET    1   G 5 LEU B 226  GLN B 234  0                                        
SHEET    2   G 5 MET B 208  LYS B 215 -1  N  MET B 208   O  GLN B 234           
SHEET    3   G 5 GLU B 258  ILE B 263 -1  O  GLU B 258   N  LYS B 215           
SHEET    4   G 5 LYS B 184  VAL B 187 -1  N  ILE B 185   O  LEU B 259           
SHEET    5   G 5 LEU B 178  LYS B 181 -1  N  GLU B 179   O  LEU B 186           
SHEET    1   H 5 TRP C 168  ARG C 174  0                                        
SHEET    2   H 5 CYS C 146  ALA C 151 -1  N  CYS C 146   O  ARG C 174           
SHEET    3   H 5 PHE C 278  LYS C 283 -1  O  PHE C 279   N  LEU C 149           
SHEET    4   H 5 GLY C 191  TYR C 201 -1  N  PHE C 194   O  LEU C 282           
SHEET    5   H 5 ASN C 243  LEU C 253 -1  O  GLY C 249   N  ILE C 195           
SHEET    1   I 5 LEU C 226  ASN C 235  0                                        
SHEET    2   I 5 ALA C 207  LYS C 215 -1  N  ARG C 214   O  VAL C 227           
SHEET    3   I 5 GLU C 258  ILE C 263 -1  O  ALA C 262   N  LEU C 211           
SHEET    4   I 5 TYR C 163  PHE C 165 -1  N  THR C 164   O  ILE C 263           
SHEET    5   I 5 ILE C 158  LYS C 160 -1  N  ILE C 158   O  PHE C 165           
SHEET    1   J 5 LEU C 226  ASN C 235  0                                        
SHEET    2   J 5 ALA C 207  LYS C 215 -1  N  ARG C 214   O  VAL C 227           
SHEET    3   J 5 GLU C 258  ILE C 263 -1  O  ALA C 262   N  LEU C 211           
SHEET    4   J 5 LYS C 184  VAL C 187 -1  N  ILE C 185   O  LEU C 259           
SHEET    5   J 5 LEU C 178  LYS C 181 -1  N  GLU C 179   O  LEU C 186           
SHEET    1   K 5 TRP D 168  ARG D 174  0                                        
SHEET    2   K 5 CYS D 146  ALA D 151 -1  N  CYS D 146   O  ARG D 174           
SHEET    3   K 5 PHE D 278  LYS D 283 -1  O  PHE D 279   N  LEU D 149           
SHEET    4   K 5 GLY D 191  TYR D 201 -1  N  PHE D 194   O  LEU D 282           
SHEET    5   K 5 ASN D 243  LEU D 253 -1  O  GLY D 249   N  ILE D 195           
SHEET    1   L 5 LEU D 226  GLN D 234  0                                        
SHEET    2   L 5 MET D 208  LYS D 215 -1  N  ARG D 214   O  VAL D 227           
SHEET    3   L 5 GLU D 258  ILE D 263 -1  O  GLU D 258   N  LYS D 215           
SHEET    4   L 5 TYR D 163  PHE D 165 -1  N  THR D 164   O  ILE D 263           
SHEET    5   L 5 ILE D 158  LYS D 160 -1  N  ILE D 158   O  PHE D 165           
SHEET    1   M 5 LEU D 226  GLN D 234  0                                        
SHEET    2   M 5 MET D 208  LYS D 215 -1  N  ARG D 214   O  VAL D 227           
SHEET    3   M 5 GLU D 258  ILE D 263 -1  O  GLU D 258   N  LYS D 215           
SHEET    4   M 5 LYS D 184  VAL D 187 -1  N  ILE D 185   O  LEU D 259           
SHEET    5   M 5 LEU D 178  LYS D 181 -1  N  GLU D 179   O  LEU D 186           
SHEET    1   N 3 ASN E 243  LEU E 253  0                                        
SHEET    2   N 3 GLY E 191  TYR E 201 -1  N  ILE E 195   O  GLY E 249           
SHEET    3   N 3 ILE E 270  SER E 271 -1  O  SER E 271   N  LEU E 200           
SHEET    1   O 5 ASN E 243  LEU E 253  0                                        
SHEET    2   O 5 GLY E 191  TYR E 201 -1  N  ILE E 195   O  GLY E 249           
SHEET    3   O 5 PHE E 278  LYS E 283 -1  O  LEU E 282   N  PHE E 194           
SHEET    4   O 5 CYS E 146  ALA E 151 -1  N  LEU E 149   O  PHE E 279           
SHEET    5   O 5 TRP E 168  ARG E 174 -1  O  ARG E 174   N  CYS E 146           
SHEET    1   P 5 LEU E 226  GLN E 234  0                                        
SHEET    2   P 5 MET E 208  LYS E 215 -1  N  ARG E 214   O  VAL E 227           
SHEET    3   P 5 GLU E 258  ILE E 263 -1  O  ALA E 262   N  LEU E 211           
SHEET    4   P 5 TYR E 163  PHE E 165 -1  N  THR E 164   O  ILE E 263           
SHEET    5   P 5 ILE E 158  LYS E 160 -1  N  ILE E 158   O  PHE E 165           
SHEET    1   Q 5 LEU E 226  GLN E 234  0                                        
SHEET    2   Q 5 MET E 208  LYS E 215 -1  N  ARG E 214   O  VAL E 227           
SHEET    3   Q 5 GLU E 258  ILE E 263 -1  O  ALA E 262   N  LEU E 211           
SHEET    4   Q 5 LYS E 184  VAL E 187 -1  N  ILE E 185   O  LEU E 259           
SHEET    5   Q 5 LEU E 178  LYS E 181 -1  N  GLU E 179   O  LEU E 186           
SHEET    1   R 3 ASN F 243  LEU F 253  0                                        
SHEET    2   R 3 GLY F 191  TYR F 201 -1  N  ILE F 195   O  GLY F 249           
SHEET    3   R 3 ILE F 270  SER F 271 -1  O  SER F 271   N  LEU F 200           
SHEET    1   S 5 ASN F 243  LEU F 253  0                                        
SHEET    2   S 5 GLY F 191  TYR F 201 -1  N  ILE F 195   O  GLY F 249           
SHEET    3   S 5 PHE F 278  LYS F 283 -1  O  PHE F 278   N  GLN F 198           
SHEET    4   S 5 CYS F 146  ALA F 151 -1  N  LEU F 149   O  PHE F 279           
SHEET    5   S 5 TRP F 168  ARG F 174 -1  O  ARG F 174   N  CYS F 146           
SHEET    1   T 5 LEU F 226  GLN F 234  0                                        
SHEET    2   T 5 MET F 208  LYS F 215 -1  N  ARG F 214   O  VAL F 227           
SHEET    3   T 5 GLU F 258  ILE F 263 -1  O  ALA F 262   N  LEU F 211           
SHEET    4   T 5 TYR F 163  PHE F 165 -1  N  THR F 164   O  ILE F 263           
SHEET    5   T 5 ILE F 158  LYS F 160 -1  N  ILE F 158   O  PHE F 165           
SHEET    1   U 5 LEU F 226  GLN F 234  0                                        
SHEET    2   U 5 MET F 208  LYS F 215 -1  N  ARG F 214   O  VAL F 227           
SHEET    3   U 5 GLU F 258  ILE F 263 -1  O  ALA F 262   N  LEU F 211           
SHEET    4   U 5 LYS F 184  VAL F 187 -1  N  ILE F 185   O  LEU F 259           
SHEET    5   U 5 LEU F 178  LYS F 181 -1  N  GLU F 179   O  LEU F 186           
SSBOND   1 CYS A  232    CYS A  245                          1555   1555  2.03  
SSBOND   2 CYS B  232    CYS B  245                          1555   1555  2.04  
SSBOND   3 CYS C  232    CYS C  245                          1555   1555  2.03  
SSBOND   4 CYS D  232    CYS D  245                          1555   1555  2.03  
SSBOND   5 CYS E  232    CYS E  245                          1555   1555  2.03  
SSBOND   6 CYS F  232    CYS F  245                          1555   1555  2.03  
LINK        MG    MG A 701                 OE1 GLN B 234     1555   1555  2.49  
LINK        MG    MG A 701                 O   HOH B1019     1555   1555  2.54  
LINK        MG    MG A 701                 O   HOH C1017     1555   1555  2.71  
LINK        MG    MG A 701                 OE1 GLN A 234     1555   1555  2.34  
LINK        MG    MG A 701                 OE1 GLN C 234     1555   1555  2.45  
LINK        MG    MG A 701                 O   HOH A 504     1555   1555  2.61  
LINK        MG    MG A 901                 O4  CIT A 889     1555   1555  2.45  
LINK        MG    MG A 901                 O   HOH F 395     1555   1555  2.76  
LINK        MG    MG A 901                 O4  CIT F 888     1555   1555  2.37  
LINK        MG    MG A 901                 O7  CIT A 889     1555   1555  2.95  
LINK        MG    MG A 901                 O7  CIT F 888     1555   1555  2.83  
LINK        MG    MG A 901                 O   HOH A  10     1555   1555  2.85  
LINK        MG    MG A 903                 O1  CIT F 888     1555   1555  2.83  
LINK        MG    MG A 903                 O7  CIT F 888     1555   1555  2.93  
LINK        MG    MG A 903                 NH2 ARG A 214     1555   1555  2.95  
LINK        MG    MG A 903                 O   HOH A  10     1555   1555  2.75  
LINK        MG    MG A 903                 O   LYS A 252     1555   1555  3.07  
LINK        MG    MG B 702                 O   HOH C1018     1555   1555  2.52  
LINK        MG    MG B 702                 O   HOH C1017     1555   1555  2.36  
LINK        MG    MG B 702                 O   HOH B1020     1555   1555  2.62  
LINK        MG    MG B 702                 O   HOH A 504     1555   1555  2.54  
LINK        MG    MG B 702                 O   HOH A 507     1555   1555  2.46  
LINK        MG    MG B 702                 O   HOH B1019     1555   1555  2.36  
LINK        MG    MG D 801                 O   HOH E1020     1555   1555  2.43  
LINK        MG    MG D 801                 O   HOH F 603     1555   1555  2.43  
LINK        MG    MG D 801                 O   HOH D1013     1555   1555  2.50  
LINK        MG    MG D 801                 O   HOH D1014     1555   1555  2.47  
LINK        MG    MG D 801                 O   HOH E1021     1555   1555  2.36  
LINK        MG    MG D 801                 O   HOH F 608     1555   1555  2.53  
LINK        MG    MG D 802                 OE1 GLN E 234     1555   1555  2.34  
LINK        MG    MG D 802                 O   HOH E1020     1555   1555  2.61  
LINK        MG    MG D 802                 O   HOH F 603     1555   1555  2.53  
LINK        MG    MG D 802                 OE1 GLN F 234     1555   1555  2.46  
LINK        MG    MG D 802                 O   HOH D1013     1555   1555  2.56  
LINK        MG    MG D 802                 OE1 GLN D 234     1555   1555  2.42  
LINK        MG    MG F 902                 O   HOH F 395     1555   1555  2.69  
LINK        MG    MG F 902                 O7  CIT A 889     1555   1555  2.93  
LINK        MG    MG F 902                 O5  CIT F 888     1555   1555  3.15  
LINK        MG    MG F 902                 NH2 ARG F 214     1555   1555  2.86  
SITE     1 AC1  7 GLN A 234  HOH A 504  GLN B 234   MG B 702                    
SITE     2 AC1  7 HOH B1019  GLN C 234  HOH C1017                               
SITE     1 AC2  7 HOH A 504  HOH A 507   MG A 701  HOH B1019                    
SITE     2 AC2  7 HOH B1020  HOH C1017  HOH C1018                               
SITE     1 AC3  7  MG D 802  HOH D1013  HOH D1014  HOH E1020                    
SITE     2 AC3  7 HOH E1021  HOH F 603  HOH F 608                               
SITE     1 AC4  7 GLN D 234   MG D 801  HOH D1013  GLN E 234                    
SITE     2 AC4  7 HOH E1020  GLN F 234  HOH F 603                               
SITE     1 AC5  4 HOH A  10  CIT A 889  HOH F 395  CIT F 888                    
SITE     1 AC6  5 CIT A 889  ARG F 214  LYS F 252  HOH F 395                    
SITE     2 AC6  5 CIT F 888                                                     
SITE     1 AC7  5 HOH A  10  ARG A 214  LYS A 252  CIT A 889                    
SITE     2 AC7  5 CIT F 888                                                     
SITE     1 AC8 15 HOH A   4  HOH A  44  ARG A 214  LYS A 252                    
SITE     2 AC8 15 CIT A 889   MG A 901   MG A 903  ARG F 214                    
SITE     3 AC8 15 LYS F 216  HIS F 218  PHE F 220  GLU F 223                    
SITE     4 AC8 15 GLU F 254  HOH F 344   MG F 902                               
SITE     1 AC9 15 HOH A   2  ARG A 214  LYS A 216  HIS A 218                    
SITE     2 AC9 15 PHE A 220  GLU A 223  GLU A 254  HOH A 389                    
SITE     3 AC9 15  MG A 901   MG A 903  ARG F 214  LYS F 252                    
SITE     4 AC9 15 HOH F 349  CIT F 888   MG F 902                               
SITE     1 BC1  4 LYS A 160  PHE A 165  ASN A 183  GLN A 260                    
SITE     1 BC2  6 GLN A 234  SER A 244  TYR A 246  SER B 244                    
SITE     2 BC2  6 TYR B 246  TYR C 246                                          
SITE     1 BC3  4 LEU A 282  PHE B 194  PHE C 194  LEU C 282                    
SITE     1 BC4  4 HOH A 509  HOH A 510  HOH A 511  HOH C1020                    
SITE     1 BC5  3 ILE B 158  PHE B 165  ASN B 183                               
SITE     1 BC6  5 GLY C 209  LEU C 211  ARG C 231  CYS C 232                    
SITE     2 BC6  5 PRO C 264                                                     
SITE     1 BC7  4 PHE C 165  ASN C 183  LYS C 184  GLN C 260                    
SITE     1 BC8  4 TYR C 192  LYS C 252  HOH C1022  HIS E 218                    
SITE     1 BC9  3 PHE D 165  ASN D 183  GLN D 260                               
SITE     1 CC1  4 PHE D 194  PHE E 194  LEU E 282  LEU F 282                    
SITE     1 CC2  4 PHE E 165  ASN E 183  LYS E 184  GLN E 260                    
SITE     1 CC3  4 TYR D 246  SER E 244  TYR E 246  TYR F 246                    
SITE     1 CC4  3 PHE F 165  ASN F 183  LYS F 184                               
SITE     1 CC5  3 ALA C 268  GLN C 269  ILE C 270                               
SITE     1 CC6  4 THR A 157  ALA A 268  GLN A 269  ILE A 270                    
SITE     1 CC7  4 HIS C 218  TYR E 192  LYS E 252  HOH F 371                    
SITE     1 CC8  5 LYS A 215  LYS A 216  VAL A 217  GLY A 256                    
SITE     2 CC8  5 GLU A 258                                                     
SITE     1 CC9  3 GLY B 209  ARG B 231  PRO B 264                               
SITE     1 DC1  4 THR E 157  ALA E 268  GLN E 269  ILE E 270                    
SITE     1 DC2  5 PRO D 237  HOH D1015  HOH E1023  HOH F 423                    
SITE     2 DC2  5 HOH F 609                                                     
CRYST1  123.580  123.580  161.230  90.00  90.00 120.00 P 65         36          
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      0.008092  0.004672  0.000000        0.00000                         
SCALE2      0.000000  0.009344  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006202        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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