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Database: PDB
Entry: 4P4K
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Original site: 4P4K 
HEADER    IMMUNE SYSTEM                           12-MAR-14   4P4K              
TITLE     STRUCTURAL BASIS OF CHRONIC BERYLLIUM DISEASE: BRIDGING THE GAP       
TITLE    2 BETWEEN ALLERGIC HYPERSENSITIVITY AND AUTO IMMUNITY                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DP ALPHA 1 CHAIN; 
COMPND   3 CHAIN: A, E;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 32-214;                                       
COMPND   5 SYNONYM: DP(W3),DP(W4),HLA-SB ALPHA CHAIN,MHC CLASS II DP3-ALPHA,MHC 
COMPND   6 CLASS II DPA1;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: MIM2 PEPTIDE,HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DP   
COMPND  10 BETA 1 CHAIN;                                                        
COMPND  11 CHAIN: B, F;                                                         
COMPND  12 FRAGMENT: UNP RESIDUES 32-218;                                       
COMPND  13 SYNONYM: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN,DP(W4) BETA CHAIN,  
COMPND  14 MHC CLASS II ANTIGEN DPB1;                                           
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: HTCRAV22 ALPHA CHAIN;                                      
COMPND  18 CHAIN: C, G;                                                         
COMPND  19 ENGINEERED: YES;                                                     
COMPND  20 MOL_ID: 4;                                                           
COMPND  21 MOLECULE: HTCRAV22 BETA CHAIN;                                       
COMPND  22 CHAIN: D, H;                                                         
COMPND  23 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HLA-DPA1, HLA-DP1A, HLASB;                                     
SOURCE   6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BTI TN 5B1 4;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: HLA-DPB1, HLA-DP1B;                                            
SOURCE  14 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE  16 MOL_ID: 3;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    BE BOUND COMPLEX, CHRONIC BERYLLIUM DISEASE, TCR-MHC PEPTIDE-BE2+,    
KEYWDS   2 IMMUNE SYSTEM                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.M.CLAYTON,F.CRAWFORD,J.W.KAPPLER                                    
REVDAT   3   29-JUL-20 4P4K    1       COMPND SOURCE REMARK SEQADV              
REVDAT   3 2                   1       HETNAM LINK   SITE                       
REVDAT   2   07-JAN-15 4P4K    1       DBREF                                    
REVDAT   1   16-JUL-14 4P4K    0                                                
JRNL        AUTH   G.M.CLAYTON,Y.WANG,F.CRAWFORD,A.NOVIKOV,B.T.WIMBERLY,        
JRNL        AUTH 2 J.S.KIEFT,M.T.FALTA,N.A.BOWERMAN,P.MARRACK,A.P.FONTENOT,     
JRNL        AUTH 3 S.DAI,J.W.KAPPLER                                            
JRNL        TITL   STRUCTURAL BASIS OF CHRONIC BERYLLIUM DISEASE: LINKING       
JRNL        TITL 2 ALLERGIC HYPERSENSITIVITY AND AUTOIMMUNITY.                  
JRNL        REF    CELL                          V. 158   132 2014              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   24995984                                                     
JRNL        DOI    10.1016/J.CELL.2014.04.048                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.0                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 58168                          
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)  : 0.206                          
REMARK   3   R VALUE            (WORKING SET)  : 0.204                          
REMARK   3   FREE R VALUE                      : 0.252                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.070                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2949                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.80                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.87                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.97                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4227                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2496                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 4006                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2461                   
REMARK   3   BIN FREE R VALUE                        : 0.3123                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.23                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 221                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12872                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 74                                      
REMARK   3   SOLVENT ATOMS            : 330                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 78.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.90830                                             
REMARK   3    B22 (A**2) : 0.81900                                              
REMARK   3    B33 (A**2) : 5.08930                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.364               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.959               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.332               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.336               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.887                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 13314  ; 1.500  ; HARMONIC            
REMARK   3    BOND ANGLES               : 18175  ; 1.500  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 4349   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 354    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1954   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 13314  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 2      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1725   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : 10     ; 1.000  ; HARMONIC            
REMARK   3    UTILITY ANGLES            : 12     ; 1.000  ; HARMONIC            
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 14914  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.39                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.74                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 22.00                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4P4K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000200667.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-AUG-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5-6                              
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X26C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58169                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 14.00                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6700                            
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: NULL                                                  
REMARK 200 STARTING MODEL: 3LQZ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8K, NA CACODYLATE, GLYCEROL, VAPOR    
REMARK 280  DIFFUSION, SITTING 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       39.70000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      106.56500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       68.62000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      106.56500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.70000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       68.62000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12790 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 36580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12650 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 36220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
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     ILE A     1                                                      
REMARK 465     ALA A   180                                                      
REMARK 465     GLN A   181                                                      
REMARK 465     GLU A   182                                                      
REMARK 465     PRO A   183                                                      
REMARK 465     GLY B   -13                                                      
REMARK 465     GLY B   -12                                                      
REMARK 465     SER B   -11                                                      
REMARK 465     LEU B   -10                                                      
REMARK 465     VAL B    -9                                                      
REMARK 465     PRO B    -8                                                      
REMARK 465     ARG B    -7                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     SER B    -5                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     MET C     1                                                      
REMARK 465     PRO C   206                                                      
REMARK 465     GLU C   207                                                      
REMARK 465     SER C   208                                                      
REMARK 465     SER C   209                                                      
REMARK 465     MET D     2                                                      
REMARK 465     GLU E   182                                                      
REMARK 465     PRO E   183                                                      
REMARK 465     GLY F   -13                                                      
REMARK 465     GLY F   -12                                                      
REMARK 465     SER F   -11                                                      
REMARK 465     LEU F   -10                                                      
REMARK 465     VAL F    -9                                                      
REMARK 465     PRO F    -8                                                      
REMARK 465     ARG F    -7                                                      
REMARK 465     GLY F    -6                                                      
REMARK 465     SER F    -5                                                      
REMARK 465     GLY F    -4                                                      
REMARK 465     GLY F    -3                                                      
REMARK 465     GLY F    -2                                                      
REMARK 465     GLY F    -1                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ASN G     2                                                      
REMARK 465     PRO G   206                                                      
REMARK 465     GLU G   207                                                      
REMARK 465     SER G   208                                                      
REMARK 465     SER G   209                                                      
REMARK 465     MET H     2                                                      
REMARK 465     ALA H   242                                                      
REMARK 465     ASP H   243                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   2    CG   CD   CE   NZ                                   
REMARK 470     LEU A  99    CG   CD1  CD2                                       
REMARK 470     GLN A 172    CG   CD   OE1  NE2                                  
REMARK 470     GLN B -25    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  63    CG   CD   CE   NZ                                   
REMARK 470     LEU B  89    CG   CD1  CD2                                       
REMARK 470     GLN B  90    CG   CD   OE1  NE2                                  
REMARK 470     ARG B  96    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 103    CG   CD   CE   NZ                                   
REMARK 470     LYS B 104    CG   CD   CE   NZ                                   
REMARK 470     LEU B 107    CG   CD1  CD2                                       
REMARK 470     HIS B 109    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN B 165    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 187    CG   CD   CE   NZ                                   
REMARK 470     GLN B 189    CG   CD   OE1  NE2                                  
REMARK 470     LYS C  68    CG   CD   CE   NZ                                   
REMARK 470     LYS C 107    CG   CD   CE   NZ                                   
REMARK 470     ARG C 128    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 146    CG   CD   OE1  NE2                                  
REMARK 470     ASN C 148    CG   OD1  ND2                                       
REMARK 470     GLN C 151    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 153    CG   CD   CE   NZ                                   
REMARK 470     ASP C 156    CG   OD1  OD2                                       
REMARK 470     LYS C 162    CG   CD   CE   NZ                                   
REMARK 470     ARG C 168    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN C 193    CG   OD1  ND2                                       
REMARK 470     ASN C 194    CG   OD1  ND2                                       
REMARK 470     GLU C 199    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 200    CG   OD1  OD2                                       
REMARK 470     SER C 205    OG                                                  
REMARK 470     ARG D   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 117    CG   CD   CE   NZ                                   
REMARK 470     GLU D 131    CG   CD   OE1  OE2                                  
REMARK 470     ILE D 134    CG1  CG2  CD1                                       
REMARK 470     SER D 135    OG                                                  
REMARK 470     LYS D 163    CG   CD   CE   NZ                                   
REMARK 470     GLN D 174    CG   CD   OE1  NE2                                  
REMARK 470     LEU D 182    CG   CD1  CD2                                       
REMARK 470     GLN D 201    CG   CD   OE1  NE2                                  
REMARK 470     ASN D 219    CG   OD1  ND2                                       
REMARK 470     GLU D 221    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 243    CG   OD1  OD2                                       
REMARK 470     LYS E   2    CG   CD   CE   NZ                                   
REMARK 470     GLU E 158    CG   CD   OE1  OE2                                  
REMARK 470     GLN E 181    CG   CD   OE1  NE2                                  
REMARK 470     GLN F -25    CG   CD   OE1  NE2                                  
REMARK 470     LYS F  63    CG   CD   CE   NZ                                   
REMARK 470     LYS F 103    CG   CD   CE   NZ                                   
REMARK 470     LYS F 104    CG   CD   CE   NZ                                   
REMARK 470     LEU F 107    CG   CD1  CD2                                       
REMARK 470     GLN F 189    CG   CD   OE1  NE2                                  
REMARK 470     TYR G  30    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS G  60    CG   CD   CE   NZ                                   
REMARK 470     LYS G  68    CG   CD   CE   NZ                                   
REMARK 470     LYS G 107    CG   CD   CE   NZ                                   
REMARK 470     GLN G 118    CG   CD   OE1  NE2                                  
REMARK 470     LYS G 131    CG   CD   CE   NZ                                   
REMARK 470     ASP G 134    CG   OD1  OD2                                       
REMARK 470     LYS G 135    CG   CD   CE   NZ                                   
REMARK 470     GLN G 146    CG   CD   OE1  NE2                                  
REMARK 470     GLN G 151    CG   CD   OE1  NE2                                  
REMARK 470     LYS G 153    CG   CD   CE   NZ                                   
REMARK 470     ASP G 156    CG   OD1  OD2                                       
REMARK 470     LYS G 162    CG   CD   CE   NZ                                   
REMARK 470     ARG G 168    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN G 182    CG   OD1  ND2                                       
REMARK 470     LYS G 183    CG   CD   CE   NZ                                   
REMARK 470     SER G 184    OG                                                  
REMARK 470     ASN G 194    CG   OD1  ND2                                       
REMARK 470     GLU G 199    CG   CD   OE1  OE2                                  
REMARK 470     ARG H   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG H  67    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS H 117    CG   CD   CE   NZ                                   
REMARK 470     GLU H 131    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 163    CG   CD   CE   NZ                                   
REMARK 470     GLN H 174    CG   CD   OE1  NE2                                  
REMARK 470     LYS H 177    CG   CD   CE   NZ                                   
REMARK 470     ARG H 204    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU H 218    CG   CD   OE1  OE2                                  
REMARK 470     GLN H 224    CG   CD   OE1  NE2                                  
REMARK 470     ASP H 225    CG   OD1  OD2                                       
REMARK 470     ARG H 241    CG   CD   NE   CZ   NH1  NH2                        
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   ND2  ASN B     6     O    HOH B   339              2.14            
REMARK 500   OE1  GLU F   -17     OE2  GLU F    69              2.15            
REMARK 500   O    ALA B    47     O    HOH B   327              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  28       -4.16     67.97                                   
REMARK 500    GLU A 158       43.22    -98.12                                   
REMARK 500    ASN B  31     -104.14     59.72                                   
REMARK 500    ARG B  75      -94.80    -97.32                                   
REMARK 500    THR B  88      -52.28   -123.42                                   
REMARK 500    GLN B 108      -39.59   -157.45                                   
REMARK 500    HIS B 109     -173.54    -68.97                                   
REMARK 500    ASN B 144      161.88     70.56                                   
REMARK 500    ALA B 188      -33.80    -37.36                                   
REMARK 500    ASP C  54       -9.76     86.58                                   
REMARK 500    ASN C  59      143.89   -170.90                                   
REMARK 500    PHE C  73       58.52   -140.18                                   
REMARK 500    ALA C  86     -174.81   -174.60                                   
REMARK 500    ASN C 119       76.44   -119.58                                   
REMARK 500    LYS C 131      -73.43    -87.79                                   
REMARK 500    SER C 155      -70.13    -59.95                                   
REMARK 500    MET C 167       37.12    -86.86                                   
REMARK 500    ARG C 168      -54.69      2.92                                   
REMARK 500    ASN C 182       42.00    -76.30                                   
REMARK 500    LYS C 183     -167.27     55.22                                   
REMARK 500    ALA C 191      -59.61    -29.06                                   
REMARK 500    PHE C 192       56.71   -108.55                                   
REMARK 500    LEU D  46      -63.88    -97.97                                   
REMARK 500    GLU D  52      -22.26     69.88                                   
REMARK 500    ASN D  59       77.69   -107.45                                   
REMARK 500    SER D  72       -6.63     78.68                                   
REMARK 500    ALA D  87     -177.65   -171.79                                   
REMARK 500    ASP D 152       48.36    -82.13                                   
REMARK 500    LEU D 182      122.68   -179.45                                   
REMARK 500    GLU E  28       -5.73     69.48                                   
REMARK 500    GLU E 158       40.92    -94.55                                   
REMARK 500    ASN F  31     -104.97     61.90                                   
REMARK 500    ARG F  75      -94.46    -97.68                                   
REMARK 500    THR F  88      -53.21   -122.43                                   
REMARK 500    LYS F 104       45.72    -97.24                                   
REMARK 500    PRO F 106     -137.23    -87.46                                   
REMARK 500    GLN F 108      -14.63     65.74                                   
REMARK 500    ASN F 144      161.88     69.84                                   
REMARK 500    MET G   7      115.50    -36.34                                   
REMARK 500    PRO G  40      -82.26    -10.14                                   
REMARK 500    ASP G  54       -9.41     85.95                                   
REMARK 500    ASN G  59      145.13   -172.19                                   
REMARK 500    ALA G  86     -174.69   -174.27                                   
REMARK 500    ASN G 119       56.83     72.40                                   
REMARK 500    LYS G 131      -71.80    -88.61                                   
REMARK 500    ASP G 142       16.08     55.27                                   
REMARK 500    SER G 155      -70.36    -59.98                                   
REMARK 500    MET G 167       36.41    -86.93                                   
REMARK 500    ARG G 168      -54.32      2.67                                   
REMARK 500    ALA G 191      -73.09    -35.96                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      58 RAMACHANDRAN OUTLIERS.                        
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                              NA B 202  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B -20   OD1                                                    
REMARK 620 2 ASP B -20   OD2  44.0                                              
REMARK 620 3 GLU B -17   OE1 104.3 148.2                                        
REMARK 620 4 GLU B  68   OE2 137.3  97.2 111.1                                  
REMARK 620 5 GLU B  69   OE1  54.6  76.8  85.7 148.5                            
REMARK 620 6 GLU B  69   OE2  96.2 120.6  54.3 123.6  45.4                      
REMARK 620 7 HOH B 344   O   102.0  93.1  91.5  55.2 154.4 144.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             0BE B 203  BE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B -20   OD1                                                    
REMARK 620 2 GLU B  26   OE1 114.1                                              
REMARK 620 3 GLU B  69   OE1 111.8 113.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA F 201  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F -20   OD2                                                    
REMARK 620 2 GLU F -17   OE1 135.1                                              
REMARK 620 3 GLU F  68   OE2 111.5 103.9                                        
REMARK 620 4 GLU F  69   OE1  72.8  78.4 167.7                                  
REMARK 620 5 GLU F  69   OE2 115.4  50.3 130.0  42.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             0BE F 202  BE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F -20   OD1                                                    
REMARK 620 2 GLU F  26   OE1 101.7                                              
REMARK 620 3 GLU F  69   OE1 103.5 108.7                                        
REMARK 620 N                    1     2                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4P4R   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P57   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P5M   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P5K   RELATED DB: PDB                                   
DBREF  4P4K A    1   183  UNP    P20036   DPA1_HUMAN      32    214             
DBREF  4P4K B  -25   -15  PDB    4P4K     4P4K           -25    -15             
DBREF  4P4K B    3   189  UNP    P04440   DPB1_HUMAN      32    218             
DBREF  4P4K C    1   209  PDB    4P4K     4P4K             1    209             
DBREF  4P4K D    2   243  PDB    4P4K     4P4K             2    243             
DBREF  4P4K E    1   183  UNP    P20036   DPA1_HUMAN      32    214             
DBREF  4P4K F  -25   -15  PDB    4P4K     4P4K           -25    -15             
DBREF  4P4K F    3   189  UNP    P04440   DPB1_HUMAN      32    218             
DBREF  4P4K G    1   209  PDB    4P4K     4P4K             1    209             
DBREF  4P4K H    2   243  PDB    4P4K     4P4K             2    243             
SEQADV 4P4K GLY B  -14  UNP  P04440              LINKER                         
SEQADV 4P4K GLY B  -13  UNP  P04440              LINKER                         
SEQADV 4P4K GLY B  -12  UNP  P04440              LINKER                         
SEQADV 4P4K SER B  -11  UNP  P04440              LINKER                         
SEQADV 4P4K LEU B  -10  UNP  P04440              LINKER                         
SEQADV 4P4K VAL B   -9  UNP  P04440              LINKER                         
SEQADV 4P4K PRO B   -8  UNP  P04440              LINKER                         
SEQADV 4P4K ARG B   -7  UNP  P04440              LINKER                         
SEQADV 4P4K GLY B   -6  UNP  P04440              LINKER                         
SEQADV 4P4K SER B   -5  UNP  P04440              LINKER                         
SEQADV 4P4K GLY B   -4  UNP  P04440              LINKER                         
SEQADV 4P4K GLY B   -3  UNP  P04440              LINKER                         
SEQADV 4P4K GLY B   -2  UNP  P04440              LINKER                         
SEQADV 4P4K GLY B   -1  UNP  P04440              LINKER                         
SEQADV 4P4K SER B    3  UNP  P04440    THR    32 VARIANT                        
SEQADV 4P4K VAL B   36  UNP  P04440    ALA    65 VARIANT                        
SEQADV 4P4K ASP B   55  UNP  P04440    ALA    84 VARIANT                        
SEQADV 4P4K GLU B   56  UNP  P04440    ALA    85 VARIANT                        
SEQADV 4P4K GLU B   69  UNP  P04440    LYS    98 VARIANT                        
SEQADV 4P4K GLY F  -14  UNP  P04440              LINKER                         
SEQADV 4P4K GLY F  -13  UNP  P04440              LINKER                         
SEQADV 4P4K GLY F  -12  UNP  P04440              LINKER                         
SEQADV 4P4K SER F  -11  UNP  P04440              LINKER                         
SEQADV 4P4K LEU F  -10  UNP  P04440              LINKER                         
SEQADV 4P4K VAL F   -9  UNP  P04440              LINKER                         
SEQADV 4P4K PRO F   -8  UNP  P04440              LINKER                         
SEQADV 4P4K ARG F   -7  UNP  P04440              LINKER                         
SEQADV 4P4K GLY F   -6  UNP  P04440              LINKER                         
SEQADV 4P4K SER F   -5  UNP  P04440              LINKER                         
SEQADV 4P4K GLY F   -4  UNP  P04440              LINKER                         
SEQADV 4P4K GLY F   -3  UNP  P04440              LINKER                         
SEQADV 4P4K GLY F   -2  UNP  P04440              LINKER                         
SEQADV 4P4K GLY F   -1  UNP  P04440              LINKER                         
SEQADV 4P4K SER F    3  UNP  P04440    THR    32 VARIANT                        
SEQADV 4P4K VAL F   36  UNP  P04440    ALA    65 VARIANT                        
SEQADV 4P4K ASP F   55  UNP  P04440    ALA    84 VARIANT                        
SEQADV 4P4K GLU F   56  UNP  P04440    ALA    85 VARIANT                        
SEQADV 4P4K GLU F   69  UNP  P04440    LYS    98 VARIANT                        
SEQRES   1 A  183  ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL          
SEQRES   2 A  183  GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE          
SEQRES   3 A  183  ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS          
SEQRES   4 A  183  GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE          
SEQRES   5 A  183  SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE          
SEQRES   6 A  183  LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN          
SEQRES   7 A  183  HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL          
SEQRES   8 A  183  PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR          
SEQRES   9 A  183  LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU          
SEQRES  10 A  183  ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU          
SEQRES  11 A  183  GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR          
SEQRES  12 A  183  SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER          
SEQRES  13 A  183  ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 A  183  LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN GLU          
SEQRES  15 A  183  PRO                                                          
SEQRES   1 B  212  GLN ALA PHE TRP ILE ASP LEU PHE GLU THR ILE GLY GLY          
SEQRES   2 B  212  GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER          
SEQRES   3 B  212  PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR          
SEQRES   4 B  212  ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE          
SEQRES   5 B  212  TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL          
SEQRES   6 B  212  GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP          
SEQRES   7 B  212  GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU          
SEQRES   8 B  212  GLU ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR          
SEQRES   9 B  212  GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN          
SEQRES  10 B  212  PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU          
SEQRES  11 B  212  GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE          
SEQRES  12 B  212  TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY          
SEQRES  13 B  212  GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE          
SEQRES  14 B  212  ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU          
SEQRES  15 B  212  GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN          
SEQRES  16 B  212  VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU          
SEQRES  17 B  212  TRP LYS ALA GLN                                              
SEQRES   1 C  209  MET ASN SER VAL THR GLN MET GLU GLY PRO VAL THR LEU          
SEQRES   2 C  209  SER GLU GLU ALA PHE LEU THR ILE ASN CYS THR TYR THR          
SEQRES   3 C  209  ALA THR GLY TYR PRO SER LEU PHE TRP TYR VAL GLN TYR          
SEQRES   4 C  209  PRO GLY GLU GLY LEU GLN LEU LEU LEU LYS ALA THR LYS          
SEQRES   5 C  209  ALA ASP ASP LYS GLY SER ASN LYS GLY PHE GLU ALA THR          
SEQRES   6 C  209  TYR ARG LYS GLU THR THR SER PHE HIS LEU GLU LYS GLY          
SEQRES   7 C  209  SER VAL GLN VAL SER ASP SER ALA VAL TYR PHE CYS ALA          
SEQRES   8 C  209  LEU SER LEU TYR SER GLY ALA GLY SER TYR GLN LEU THR          
SEQRES   9 C  209  PHE GLY LYS GLY THR LYS LEU SER VAL ILE PRO ASN ILE          
SEQRES  10 C  209  GLN ASN PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP SER          
SEQRES  11 C  209  LYS SER SER ASP LYS SER VAL CYS LEU PHE THR ASP PHE          
SEQRES  12 C  209  ASP SER GLN THR ASN VAL SER GLN SER LYS ASP SER ASP          
SEQRES  13 C  209  VAL TYR ILE THR ASP LYS CYS VAL LEU ASP MET ARG SER          
SEQRES  14 C  209  MET ASP PHE LYS SER ASN SER ALA VAL ALA TRP SER ASN          
SEQRES  15 C  209  LYS SER ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN SER          
SEQRES  16 C  209  ILE ILE PRO GLU ASP THR PHE PHE PRO SER PRO GLU SER          
SEQRES  17 C  209  SER                                                          
SEQRES   1 D  242  MET GLY VAL THR GLN THR PRO ARG TYR LEU ILE LYS THR          
SEQRES   2 D  242  ARG GLY GLN GLN VAL THR LEU SER CYS SER PRO ILE SER          
SEQRES   3 D  242  GLY HIS ARG SER VAL SER TRP TYR GLN GLN THR PRO GLY          
SEQRES   4 D  242  GLN GLY LEU GLN PHE LEU PHE GLU TYR PHE SER GLU THR          
SEQRES   5 D  242  GLN ARG ASN LYS GLY ASN PHE PRO GLY ARG PHE SER GLY          
SEQRES   6 D  242  ARG GLN PHE SER ASN SER ARG SER GLU MET ASN VAL SER          
SEQRES   7 D  242  THR LEU GLU LEU GLY ASP SER ALA LEU TYR LEU CYS ALA          
SEQRES   8 D  242  SER SER LEU ALA GLN GLY GLY GLU THR GLN TYR PHE GLY          
SEQRES   9 D  242  PRO GLY THR ARG LEU LEU VAL LEU GLU ASP LEU LYS ASN          
SEQRES  10 D  242  VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO SER GLU          
SEQRES  11 D  242  ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU VAL CYS          
SEQRES  12 D  242  LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU LEU SER          
SEQRES  13 D  242  TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY VAL CYS          
SEQRES  14 D  242  THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU ASN          
SEQRES  15 D  242  ASP SER ARG TYR SER LEU SER SER ARG LEU ARG VAL SER          
SEQRES  16 D  242  ALA THR PHE TRP GLN ASN PRO ARG ASN HIS PHE ARG CYS          
SEQRES  17 D  242  GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP GLU TRP          
SEQRES  18 D  242  THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE VAL SER          
SEQRES  19 D  242  ALA GLU ALA TRP GLY ARG ALA ASP                              
SEQRES   1 E  183  ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL          
SEQRES   2 E  183  GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE          
SEQRES   3 E  183  ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS          
SEQRES   4 E  183  GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE          
SEQRES   5 E  183  SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE          
SEQRES   6 E  183  LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN          
SEQRES   7 E  183  HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL          
SEQRES   8 E  183  PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR          
SEQRES   9 E  183  LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU          
SEQRES  10 E  183  ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU          
SEQRES  11 E  183  GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR          
SEQRES  12 E  183  SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER          
SEQRES  13 E  183  ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 E  183  LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN GLU          
SEQRES  15 E  183  PRO                                                          
SEQRES   1 F  212  GLN ALA PHE TRP ILE ASP LEU PHE GLU THR ILE GLY GLY          
SEQRES   2 F  212  GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER          
SEQRES   3 F  212  PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR          
SEQRES   4 F  212  ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE          
SEQRES   5 F  212  TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL          
SEQRES   6 F  212  GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP          
SEQRES   7 F  212  GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU          
SEQRES   8 F  212  GLU ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR          
SEQRES   9 F  212  GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN          
SEQRES  10 F  212  PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU          
SEQRES  11 F  212  GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE          
SEQRES  12 F  212  TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY          
SEQRES  13 F  212  GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE          
SEQRES  14 F  212  ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU          
SEQRES  15 F  212  GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN          
SEQRES  16 F  212  VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU          
SEQRES  17 F  212  TRP LYS ALA GLN                                              
SEQRES   1 G  209  MET ASN SER VAL THR GLN MET GLU GLY PRO VAL THR LEU          
SEQRES   2 G  209  SER GLU GLU ALA PHE LEU THR ILE ASN CYS THR TYR THR          
SEQRES   3 G  209  ALA THR GLY TYR PRO SER LEU PHE TRP TYR VAL GLN TYR          
SEQRES   4 G  209  PRO GLY GLU GLY LEU GLN LEU LEU LEU LYS ALA THR LYS          
SEQRES   5 G  209  ALA ASP ASP LYS GLY SER ASN LYS GLY PHE GLU ALA THR          
SEQRES   6 G  209  TYR ARG LYS GLU THR THR SER PHE HIS LEU GLU LYS GLY          
SEQRES   7 G  209  SER VAL GLN VAL SER ASP SER ALA VAL TYR PHE CYS ALA          
SEQRES   8 G  209  LEU SER LEU TYR SER GLY ALA GLY SER TYR GLN LEU THR          
SEQRES   9 G  209  PHE GLY LYS GLY THR LYS LEU SER VAL ILE PRO ASN ILE          
SEQRES  10 G  209  GLN ASN PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP SER          
SEQRES  11 G  209  LYS SER SER ASP LYS SER VAL CYS LEU PHE THR ASP PHE          
SEQRES  12 G  209  ASP SER GLN THR ASN VAL SER GLN SER LYS ASP SER ASP          
SEQRES  13 G  209  VAL TYR ILE THR ASP LYS CYS VAL LEU ASP MET ARG SER          
SEQRES  14 G  209  MET ASP PHE LYS SER ASN SER ALA VAL ALA TRP SER ASN          
SEQRES  15 G  209  LYS SER ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN SER          
SEQRES  16 G  209  ILE ILE PRO GLU ASP THR PHE PHE PRO SER PRO GLU SER          
SEQRES  17 G  209  SER                                                          
SEQRES   1 H  242  MET GLY VAL THR GLN THR PRO ARG TYR LEU ILE LYS THR          
SEQRES   2 H  242  ARG GLY GLN GLN VAL THR LEU SER CYS SER PRO ILE SER          
SEQRES   3 H  242  GLY HIS ARG SER VAL SER TRP TYR GLN GLN THR PRO GLY          
SEQRES   4 H  242  GLN GLY LEU GLN PHE LEU PHE GLU TYR PHE SER GLU THR          
SEQRES   5 H  242  GLN ARG ASN LYS GLY ASN PHE PRO GLY ARG PHE SER GLY          
SEQRES   6 H  242  ARG GLN PHE SER ASN SER ARG SER GLU MET ASN VAL SER          
SEQRES   7 H  242  THR LEU GLU LEU GLY ASP SER ALA LEU TYR LEU CYS ALA          
SEQRES   8 H  242  SER SER LEU ALA GLN GLY GLY GLU THR GLN TYR PHE GLY          
SEQRES   9 H  242  PRO GLY THR ARG LEU LEU VAL LEU GLU ASP LEU LYS ASN          
SEQRES  10 H  242  VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO SER GLU          
SEQRES  11 H  242  ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU VAL CYS          
SEQRES  12 H  242  LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU LEU SER          
SEQRES  13 H  242  TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY VAL CYS          
SEQRES  14 H  242  THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU ASN          
SEQRES  15 H  242  ASP SER ARG TYR SER LEU SER SER ARG LEU ARG VAL SER          
SEQRES  16 H  242  ALA THR PHE TRP GLN ASN PRO ARG ASN HIS PHE ARG CYS          
SEQRES  17 H  242  GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP GLU TRP          
SEQRES  18 H  242  THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE VAL SER          
SEQRES  19 H  242  ALA GLU ALA TRP GLY ARG ALA ASP                              
HET    NAG  A 201      14                                                       
HET    NAG  A 202      14                                                       
HET    NAG  B 201      14                                                       
HET     NA  B 202       1                                                       
HET    0BE  B 203       1                                                       
HET    NAG  E 201      14                                                       
HET    NAG  E 202      14                                                       
HET     NA  F 201       1                                                       
HET    0BE  F 202       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      NA SODIUM ION                                                       
HETNAM     0BE BERYLLIUM                                                        
FORMUL   9  NAG    5(C8 H15 N O6)                                               
FORMUL  12   NA    2(NA 1+)                                                     
FORMUL  13  0BE    2(BE 2+)                                                     
FORMUL  18  HOH   *330(H2 O)                                                    
HELIX    1 AA1 LEU A   45  PHE A   52  1                                   8    
HELIX    2 AA2 ALA A   56  SER A   77  1                                  22    
HELIX    3 AA3 THR B   49  LEU B   51  5                                   3    
HELIX    4 AA4 GLY B   52  SER B   61  1                                  10    
HELIX    5 AA5 GLN B   62  ALA B   71  1                                  10    
HELIX    6 AA6 ARG B   75  GLY B   84  1                                  10    
HELIX    7 AA7 GLN C   81  SER C   85  5                                   5    
HELIX    8 AA8 ARG C  168  ASP C  171  5                                   4    
HELIX    9 AA9 ALA C  187  PHE C  192  1                                   6    
HELIX   10 AB1 GLU D   82  SER D   86  5                                   5    
HELIX   11 AB2 SER D  130  GLN D  138  1                                   9    
HELIX   12 AB3 ALA D  197  GLN D  201  1                                   5    
HELIX   13 AB4 LEU E   45  PHE E   52  1                                   8    
HELIX   14 AB5 ALA E   56  SER E   77  1                                  22    
HELIX   15 AB6 THR F   49  LEU F   51  5                                   3    
HELIX   16 AB7 GLY F   52  SER F   61  1                                  10    
HELIX   17 AB8 GLN F   62  ALA F   71  1                                  10    
HELIX   18 AB9 ARG F   75  GLY F   84  1                                  10    
HELIX   19 AC1 GLN G   81  SER G   85  5                                   5    
HELIX   20 AC2 ARG G  168  ASP G  171  5                                   4    
HELIX   21 AC3 ALA G  187  PHE G  192  1                                   6    
HELIX   22 AC4 GLU H   82  SER H   86  5                                   5    
HELIX   23 AC5 SER H  130  GLN H  138  1                                   9    
HELIX   24 AC6 ALA H  197  ASN H  202  1                                   6    
SHEET    1 AA1 8 GLU A  40  TRP A  43  0                                        
SHEET    2 AA1 8 ASP A  29  ASP A  35 -1  N  TYR A  33   O  VAL A  42           
SHEET    3 AA1 8 GLY A  20  PHE A  26 -1  N  PHE A  24   O  PHE A  32           
SHEET    4 AA1 8 HIS A   5  GLN A  14 -1  N  THR A   8   O  GLU A  25           
SHEET    5 AA1 8 LEU B   8  PHE B  18 -1  O  GLY B  11   N  ALA A  11           
SHEET    6 AA1 8 THR B  21  TYR B  30 -1  O  ILE B  29   N  GLN B  10           
SHEET    7 AA1 8 GLU B  33  ASP B  39 -1  O  GLU B  33   N  TYR B  30           
SHEET    8 AA1 8 PHE B  45  ARG B  46 -1  O  ARG B  46   N  ARG B  37           
SHEET    1 AA2 4 GLU A  88  PRO A  93  0                                        
SHEET    2 AA2 4 ASN A 103  PHE A 112 -1  O  ASP A 110   N  GLU A  88           
SHEET    3 AA2 4 PHE A 145  PHE A 153 -1  O  LEU A 151   N  LEU A 105           
SHEET    4 AA2 4 VAL A 132  GLU A 134 -1  N  ALA A 133   O  TYR A 150           
SHEET    1 AA3 4 GLU A  88  PRO A  93  0                                        
SHEET    2 AA3 4 ASN A 103  PHE A 112 -1  O  ASP A 110   N  GLU A  88           
SHEET    3 AA3 4 PHE A 145  PHE A 153 -1  O  LEU A 151   N  LEU A 105           
SHEET    4 AA3 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  HIS A 146           
SHEET    1 AA4 4 GLU A 126  VAL A 128  0                                        
SHEET    2 AA4 4 ASN A 118  CYS A 123 -1  N  CYS A 123   O  GLU A 126           
SHEET    3 AA4 4 TYR A 161  GLU A 166 -1  O  ARG A 164   N  THR A 120           
SHEET    4 AA4 4 LEU A 174  TRP A 178 -1  O  TRP A 178   N  TYR A 161           
SHEET    1 AA5 4 ARG B  96  PRO B 101  0                                        
SHEET    2 AA5 4 ASN B 111  PHE B 120 -1  O  THR B 118   N  ARG B  96           
SHEET    3 AA5 4 PHE B 153  MET B 161 -1  O  LEU B 159   N  LEU B 113           
SHEET    4 AA5 4 VAL B 140  SER B 142 -1  N  VAL B 141   O  MET B 158           
SHEET    1 AA6 4 ARG B  96  PRO B 101  0                                        
SHEET    2 AA6 4 ASN B 111  PHE B 120 -1  O  THR B 118   N  ARG B  96           
SHEET    3 AA6 4 PHE B 153  MET B 161 -1  O  LEU B 159   N  LEU B 113           
SHEET    4 AA6 4 ILE B 146  ARG B 147 -1  N  ILE B 146   O  GLN B 154           
SHEET    1 AA7 4 GLN B 134  GLU B 136  0                                        
SHEET    2 AA7 4 GLN B 126  LEU B 131 -1  N  LEU B 131   O  GLN B 134           
SHEET    3 AA7 4 VAL B 168  GLU B 174 -1  O  GLN B 172   N  ARG B 128           
SHEET    4 AA7 4 VAL B 182  LYS B 187 -1  O  TRP B 186   N  TYR B 169           
SHEET    1 AA8 2 SER C   3  GLN C   6  0                                        
SHEET    2 AA8 2 CYS C  23  THR C  26 -1  O  THR C  24   N  THR C   5           
SHEET    1 AA9 5 VAL C  11  SER C  14  0                                        
SHEET    2 AA9 5 THR C 109  ILE C 114  1  O  ILE C 114   N  LEU C  13           
SHEET    3 AA9 5 ALA C  86  TYR C  95 -1  N  TYR C  88   O  THR C 109           
SHEET    4 AA9 5 SER C  32  GLN C  38 -1  N  TYR C  36   O  PHE C  89           
SHEET    5 AA9 5 LEU C  44  ALA C  50 -1  O  GLN C  45   N  VAL C  37           
SHEET    1 AB1 4 VAL C  11  SER C  14  0                                        
SHEET    2 AB1 4 THR C 109  ILE C 114  1  O  ILE C 114   N  LEU C  13           
SHEET    3 AB1 4 ALA C  86  TYR C  95 -1  N  TYR C  88   O  THR C 109           
SHEET    4 AB1 4 TYR C 101  PHE C 105 -1  O  GLN C 102   N  LEU C  94           
SHEET    1 AB2 4 LEU C  19  ILE C  21  0                                        
SHEET    2 AB2 4 LEU C  75  LYS C  77 -1  O  LYS C  77   N  LEU C  19           
SHEET    3 AB2 4 PHE C  62  THR C  65 -1  N  GLU C  63   O  GLU C  76           
SHEET    4 AB2 4 LYS C  56  ASN C  59 -1  N  GLY C  57   O  ALA C  64           
SHEET    1 AB3 4 ALA C 123  ARG C 128  0                                        
SHEET    2 AB3 4 SER C 136  THR C 141 -1  O  LEU C 139   N  TYR C 125           
SHEET    3 AB3 4 LYS C 173  SER C 181 -1  O  ALA C 179   N  CYS C 138           
SHEET    4 AB3 4 VAL C 157  ILE C 159 -1  N  TYR C 158   O  TRP C 180           
SHEET    1 AB4 4 ALA C 123  ARG C 128  0                                        
SHEET    2 AB4 4 SER C 136  THR C 141 -1  O  LEU C 139   N  TYR C 125           
SHEET    3 AB4 4 LYS C 173  SER C 181 -1  O  ALA C 179   N  CYS C 138           
SHEET    4 AB4 4 CYS C 163  ASP C 166 -1  N  LEU C 165   O  SER C 174           
SHEET    1 AB5 4 THR D   5  THR D   7  0                                        
SHEET    2 AB5 4 VAL D  19  SER D  24 -1  O  SER D  24   N  THR D   5           
SHEET    3 AB5 4 SER D  74  VAL D  78 -1  O  MET D  76   N  LEU D  21           
SHEET    4 AB5 4 PHE D  64  GLN D  68 -1  N  SER D  65   O  ASN D  77           
SHEET    1 AB6 6 TYR D  10  THR D  14  0                                        
SHEET    2 AB6 6 THR D 108  LEU D 113  1  O  LEU D 113   N  LYS D  13           
SHEET    3 AB6 6 ALA D  87  SER D  94 -1  N  ALA D  87   O  LEU D 110           
SHEET    4 AB6 6 SER D  31  THR D  38 -1  N  SER D  33   O  ALA D  92           
SHEET    5 AB6 6 GLY D  42  PHE D  50 -1  O  LEU D  46   N  TRP D  34           
SHEET    6 AB6 6 THR D  53  LYS D  57 -1  O  ASN D  56   N  GLU D  48           
SHEET    1 AB7 4 TYR D  10  THR D  14  0                                        
SHEET    2 AB7 4 THR D 108  LEU D 113  1  O  LEU D 113   N  LYS D  13           
SHEET    3 AB7 4 ALA D  87  SER D  94 -1  N  ALA D  87   O  LEU D 110           
SHEET    4 AB7 4 TYR D 103  PHE D 104 -1  O  TYR D 103   N  SER D  93           
SHEET    1 AB8 4 GLU D 123  PHE D 127  0                                        
SHEET    2 AB8 4 LYS D 139  PHE D 149 -1  O  VAL D 143   N  PHE D 127           
SHEET    3 AB8 4 TYR D 187  SER D 196 -1  O  VAL D 195   N  ALA D 140           
SHEET    4 AB8 4 VAL D 169  THR D 171 -1  N  CYS D 170   O  ARG D 192           
SHEET    1 AB9 4 GLU D 123  PHE D 127  0                                        
SHEET    2 AB9 4 LYS D 139  PHE D 149 -1  O  VAL D 143   N  PHE D 127           
SHEET    3 AB9 4 TYR D 187  SER D 196 -1  O  VAL D 195   N  ALA D 140           
SHEET    4 AB9 4 LEU D 176  LYS D 177 -1  N  LEU D 176   O  SER D 188           
SHEET    1 AC1 4 LYS D 163  VAL D 165  0                                        
SHEET    2 AC1 4 VAL D 154  VAL D 160 -1  N  VAL D 160   O  LYS D 163           
SHEET    3 AC1 4 HIS D 206  PHE D 213 -1  O  ARG D 208   N  TRP D 159           
SHEET    4 AC1 4 GLN D 232  TRP D 239 -1  O  GLN D 232   N  PHE D 213           
SHEET    1 AC2 8 GLU E  40  TRP E  43  0                                        
SHEET    2 AC2 8 ASP E  29  ASP E  35 -1  N  TYR E  33   O  VAL E  42           
SHEET    3 AC2 8 GLY E  20  PHE E  26 -1  N  PHE E  24   O  PHE E  32           
SHEET    4 AC2 8 HIS E   5  VAL E  13 -1  N  THR E   8   O  GLU E  25           
SHEET    5 AC2 8 PHE F   9  PHE F  18 -1  O  PHE F   9   N  VAL E  13           
SHEET    6 AC2 8 THR F  21  TYR F  30 -1  O  ILE F  29   N  GLN F  10           
SHEET    7 AC2 8 GLU F  33  ASP F  39 -1  O  GLU F  33   N  TYR F  30           
SHEET    8 AC2 8 PHE F  45  ALA F  47 -1  O  ARG F  46   N  ARG F  37           
SHEET    1 AC3 4 GLU E  88  PRO E  93  0                                        
SHEET    2 AC3 4 ASN E 103  PHE E 112 -1  O  HIS E 108   N  THR E  90           
SHEET    3 AC3 4 PHE E 145  PHE E 153 -1  O  LEU E 151   N  LEU E 105           
SHEET    4 AC3 4 VAL E 132  GLU E 134 -1  N  ALA E 133   O  TYR E 150           
SHEET    1 AC4 4 GLU E  88  PRO E  93  0                                        
SHEET    2 AC4 4 ASN E 103  PHE E 112 -1  O  HIS E 108   N  THR E  90           
SHEET    3 AC4 4 PHE E 145  PHE E 153 -1  O  LEU E 151   N  LEU E 105           
SHEET    4 AC4 4 LEU E 138  PRO E 139 -1  N  LEU E 138   O  HIS E 146           
SHEET    1 AC5 4 GLU E 126  VAL E 128  0                                        
SHEET    2 AC5 4 ASN E 118  CYS E 123 -1  N  CYS E 123   O  GLU E 126           
SHEET    3 AC5 4 TYR E 161  GLU E 166 -1  O  ARG E 164   N  THR E 120           
SHEET    4 AC5 4 LEU E 174  TRP E 178 -1  O  TRP E 178   N  TYR E 161           
SHEET    1 AC6 4 ARG F  96  PRO F 101  0                                        
SHEET    2 AC6 4 ASN F 111  PHE F 120 -1  O  THR F 118   N  ARG F  96           
SHEET    3 AC6 4 PHE F 153  MET F 161 -1  O  MET F 161   N  ASN F 111           
SHEET    4 AC6 4 VAL F 140  SER F 142 -1  N  VAL F 141   O  MET F 158           
SHEET    1 AC7 4 ARG F  96  PRO F 101  0                                        
SHEET    2 AC7 4 ASN F 111  PHE F 120 -1  O  THR F 118   N  ARG F  96           
SHEET    3 AC7 4 PHE F 153  MET F 161 -1  O  MET F 161   N  ASN F 111           
SHEET    4 AC7 4 ILE F 146  ARG F 147 -1  N  ILE F 146   O  GLN F 154           
SHEET    1 AC8 4 GLN F 134  GLU F 136  0                                        
SHEET    2 AC8 4 GLN F 126  LEU F 131 -1  N  LEU F 131   O  GLN F 134           
SHEET    3 AC8 4 VAL F 168  GLU F 174 -1  O  GLN F 172   N  ARG F 128           
SHEET    4 AC8 4 VAL F 182  LYS F 187 -1  O  TRP F 186   N  TYR F 169           
SHEET    1 AC9 2 VAL G   4  GLN G   6  0                                        
SHEET    2 AC9 2 CYS G  23  TYR G  25 -1  O  THR G  24   N  THR G   5           
SHEET    1 AD1 5 VAL G  11  SER G  14  0                                        
SHEET    2 AD1 5 THR G 109  ILE G 114  1  O  SER G 112   N  LEU G  13           
SHEET    3 AD1 5 ALA G  86  TYR G  95 -1  N  ALA G  86   O  LEU G 111           
SHEET    4 AD1 5 SER G  32  GLN G  38 -1  N  TYR G  36   O  PHE G  89           
SHEET    5 AD1 5 GLN G  45  ALA G  50 -1  O  GLN G  45   N  VAL G  37           
SHEET    1 AD2 4 VAL G  11  SER G  14  0                                        
SHEET    2 AD2 4 THR G 109  ILE G 114  1  O  SER G 112   N  LEU G  13           
SHEET    3 AD2 4 ALA G  86  TYR G  95 -1  N  ALA G  86   O  LEU G 111           
SHEET    4 AD2 4 TYR G 101  PHE G 105 -1  O  GLN G 102   N  LEU G  94           
SHEET    1 AD3 4 LEU G  19  ILE G  21  0                                        
SHEET    2 AD3 4 LEU G  75  LYS G  77 -1  O  LEU G  75   N  ILE G  21           
SHEET    3 AD3 4 PHE G  62  THR G  65 -1  N  GLU G  63   O  GLU G  76           
SHEET    4 AD3 4 LYS G  56  ASN G  59 -1  N  GLY G  57   O  ALA G  64           
SHEET    1 AD4 4 ALA G 123  ARG G 128  0                                        
SHEET    2 AD4 4 SER G 136  THR G 141 -1  O  LEU G 139   N  TYR G 125           
SHEET    3 AD4 4 LYS G 173  SER G 181 -1  O  ALA G 179   N  CYS G 138           
SHEET    4 AD4 4 VAL G 157  ILE G 159 -1  N  TYR G 158   O  TRP G 180           
SHEET    1 AD5 4 ALA G 123  ARG G 128  0                                        
SHEET    2 AD5 4 SER G 136  THR G 141 -1  O  LEU G 139   N  TYR G 125           
SHEET    3 AD5 4 LYS G 173  SER G 181 -1  O  ALA G 179   N  CYS G 138           
SHEET    4 AD5 4 CYS G 163  ASP G 166 -1  N  LEU G 165   O  SER G 174           
SHEET    1 AD6 4 THR H   5  THR H   7  0                                        
SHEET    2 AD6 4 VAL H  19  SER H  24 -1  O  SER H  22   N  THR H   7           
SHEET    3 AD6 4 SER H  74  VAL H  78 -1  O  MET H  76   N  LEU H  21           
SHEET    4 AD6 4 PHE H  64  GLN H  68 -1  N  SER H  65   O  ASN H  77           
SHEET    1 AD7 6 TYR H  10  THR H  14  0                                        
SHEET    2 AD7 6 THR H 108  LEU H 113  1  O  LEU H 113   N  LYS H  13           
SHEET    3 AD7 6 ALA H  87  SER H  94 -1  N  ALA H  87   O  LEU H 110           
SHEET    4 AD7 6 SER H  31  THR H  38 -1  N  GLN H  37   O  LEU H  88           
SHEET    5 AD7 6 GLY H  42  PHE H  50 -1  O  TYR H  49   N  VAL H  32           
SHEET    6 AD7 6 THR H  53  LYS H  57 -1  O  THR H  53   N  PHE H  50           
SHEET    1 AD8 4 TYR H  10  THR H  14  0                                        
SHEET    2 AD8 4 THR H 108  LEU H 113  1  O  LEU H 113   N  LYS H  13           
SHEET    3 AD8 4 ALA H  87  SER H  94 -1  N  ALA H  87   O  LEU H 110           
SHEET    4 AD8 4 TYR H 103  PHE H 104 -1  O  TYR H 103   N  SER H  93           
SHEET    1 AD9 4 GLU H 123  PHE H 127  0                                        
SHEET    2 AD9 4 LYS H 139  PHE H 149 -1  O  VAL H 143   N  PHE H 127           
SHEET    3 AD9 4 TYR H 187  SER H 196 -1  O  VAL H 195   N  ALA H 140           
SHEET    4 AD9 4 VAL H 169  THR H 171 -1  N  CYS H 170   O  ARG H 192           
SHEET    1 AE1 4 GLU H 123  PHE H 127  0                                        
SHEET    2 AE1 4 LYS H 139  PHE H 149 -1  O  VAL H 143   N  PHE H 127           
SHEET    3 AE1 4 TYR H 187  SER H 196 -1  O  VAL H 195   N  ALA H 140           
SHEET    4 AE1 4 LEU H 176  LYS H 177 -1  N  LEU H 176   O  SER H 188           
SHEET    1 AE2 4 LYS H 163  VAL H 165  0                                        
SHEET    2 AE2 4 VAL H 154  VAL H 160 -1  N  VAL H 160   O  LYS H 163           
SHEET    3 AE2 4 HIS H 206  PHE H 213 -1  O  ARG H 208   N  TRP H 159           
SHEET    4 AE2 4 GLN H 232  TRP H 239 -1  O  GLN H 232   N  PHE H 213           
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.01  
SSBOND   2 CYS B   15    CYS B   77                          1555   1555  2.04  
SSBOND   3 CYS B  115    CYS B  171                          1555   1555  2.03  
SSBOND   4 CYS C   23    CYS C   90                          1555   1555  2.02  
SSBOND   5 CYS C  138    CYS C  188                          1555   1555  2.04  
SSBOND   6 CYS C  163    CYS D  170                          1555   1555  2.03  
SSBOND   7 CYS D   23    CYS D   91                          1555   1555  2.02  
SSBOND   8 CYS D  144    CYS D  209                          1555   1555  2.01  
SSBOND   9 CYS E  107    CYS E  163                          1555   1555  2.03  
SSBOND  10 CYS F   15    CYS F   77                          1555   1555  2.04  
SSBOND  11 CYS F  115    CYS F  171                          1555   1555  2.03  
SSBOND  12 CYS G   23    CYS G   90                          1555   1555  2.03  
SSBOND  13 CYS G  138    CYS G  188                          1555   1555  2.06  
SSBOND  14 CYS G  163    CYS H  170                          1555   1555  2.04  
SSBOND  15 CYS H   23    CYS H   91                          1555   1555  2.01  
SSBOND  16 CYS H  144    CYS H  209                          1555   1555  2.01  
LINK         ND2 ASN A  78                 C1  NAG A 201     1555   1555  1.44  
LINK         ND2 ASN A 118                 C1  NAG A 202     1555   1555  1.43  
LINK         ND2 ASN B  19                 C1  NAG B 201     1555   1555  1.44  
LINK         ND2 ASN E  78                 C1  NAG E 202     1555   1555  1.44  
LINK         ND2 ASN E 118                 C1  NAG E 201     1555   1555  1.43  
LINK         OD1 ASP B -20                NA    NA B 202     1555   1555  2.98  
LINK         OD2 ASP B -20                NA    NA B 202     1555   1555  2.82  
LINK         OD1 ASP B -20                BE   0BE B 203     1555   1555  1.65  
LINK         OE1 GLU B -17                NA    NA B 202     1555   1555  2.06  
LINK         OE1 GLU B  26                BE   0BE B 203     1555   1555  1.67  
LINK         OE2 GLU B  68                NA    NA B 202     1555   1555  2.98  
LINK         OE1 GLU B  69                NA    NA B 202     1555   1555  2.97  
LINK         OE2 GLU B  69                NA    NA B 202     1555   1555  2.67  
LINK         OE1 GLU B  69                BE   0BE B 203     1555   1555  1.65  
LINK        NA    NA B 202                 O   HOH B 344     1555   1555  2.70  
LINK         OD2 ASP F -20                NA    NA F 201     1555   1555  3.13  
LINK         OD1 ASP F -20                BE   0BE F 202     1555   1555  1.82  
LINK         OE1 GLU F -17                NA    NA F 201     1555   1555  2.23  
LINK         OE1 GLU F  26                BE   0BE F 202     1555   1555  1.96  
LINK         OE2 GLU F  68                NA    NA F 201     1555   1555  2.83  
LINK         OE1 GLU F  69                NA    NA F 201     1555   1555  3.17  
LINK         OE2 GLU F  69                NA    NA F 201     1555   1555  2.72  
LINK         OE1 GLU F  69                BE   0BE F 202     1555   1555  1.74  
CISPEP   1 ARG A   17    PRO A   18          0        -0.12                     
CISPEP   2 PHE A  113    PRO A  114          0         1.58                     
CISPEP   3 TYR B  121    PRO B  122          0        -0.37                     
CISPEP   4 LYS C  183    SER C  184          0        -3.44                     
CISPEP   5 THR D    7    PRO D    8          0        -5.30                     
CISPEP   6 SER D   27    GLY D   28          0        -0.94                     
CISPEP   7 TYR D  150    PRO D  151          0         0.46                     
CISPEP   8 ARG E   17    PRO E   18          0         0.03                     
CISPEP   9 PHE E  113    PRO E  114          0         1.22                     
CISPEP  10 TYR F  121    PRO F  122          0        -0.06                     
CISPEP  11 ASN G  193    ASN G  194          0         2.24                     
CISPEP  12 ASN G  194    SER G  195          0         7.65                     
CISPEP  13 THR H    7    PRO H    8          0        -5.41                     
CISPEP  14 SER H   27    GLY H   28          0         0.72                     
CISPEP  15 TYR H  150    PRO H  151          0         0.13                     
CRYST1   79.400  137.240  213.130  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012594  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007287  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004692        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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