GenomeNet

Database: PDB
Entry: 4P57
LinkDB: 4P57
Original site: 4P57 
HEADER    IMMUNE SYSTEM                           14-MAR-14   4P57              
TITLE     MHC TCR PEPTIDE COMPLEX                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DP ALPHA 1 CHAIN; 
COMPND   3 CHAIN: A, C;                                                         
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, D;                                                         
COMPND  12 FRAGMENT: UNP RESIDUES 32-218;                                       
COMPND  13 SYNONYM: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN,DP(W2) BETA CHAIN,  
COMPND  14 MHC CLASS II ANTIGEN DPB1;                                           
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HLA-DPA1, HLA-DP1A, HLASB;                                     
SOURCE   6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: HLA-DPB1, HLA-DP1B;                                            
SOURCE  13 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10469                                       
KEYWDS    MHC TCR PEPTIDE BE2+ COMPLEX, BERYLLIOSIS, IMMUNE SYSTEM              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.M.CLAYTON,F.CRAWFORD,J.W.KAPPLER                                    
REVDAT   3   29-JUL-20 4P57    1       COMPND SOURCE REMARK SEQADV              
REVDAT   3 2                   1       HETNAM LINK   SITE                       
REVDAT   2   07-JAN-15 4P57    1       DBREF                                    
REVDAT   1   16-JUL-14 4P57    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.    2.60 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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 77.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 37601                          
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)  : 0.210                          
REMARK   3   R VALUE            (WORKING SET)  : 0.208                          
REMARK   3   FREE R VALUE                      : 0.245                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.030                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1891                           
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               : 19                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.60                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.67                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 95.82                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2844                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2596                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2692                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2572                   
REMARK   3   BIN FREE R VALUE                        : 0.2993                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.34                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 152                      
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            : 6022                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 78                                      
REMARK   3   SOLVENT ATOMS            : 273                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 60.87                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.02350                                              
REMARK   3    B22 (A**2) : 6.02350                                              
REMARK   3    B33 (A**2) : -12.04710                                            
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) : 0.345               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.429               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.269               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.400               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.266               
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      : 0.913                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.894                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6284   ; 1.500  ; HARMONIC            
REMARK   3    BOND ANGLES               : 8578   ; 1.500  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2072   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 181    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 913    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6284   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 1      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 806    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 6689   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.35                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.81                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.89                    
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 4P57 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000200695.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-MAR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 273                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 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   : 37601                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 90.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
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: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CA ACETATE, TRIS, PEG300, VAPOR          
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      117.16500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       51.19600            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       51.19600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       58.58250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       51.19600            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       51.19600            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      175.74750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       51.19600            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       51.19600            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       58.58250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       51.19600            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       51.19600            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      175.74750            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      117.16500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     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     SER B     3                                                      
REMARK 465     LYS B   104                                                      
REMARK 465     GLY B   105                                                      
REMARK 465     PRO B   106                                                      
REMARK 465     LEU B   107                                                      
REMARK 465     GLN B   108                                                      
REMARK 465     HIS B   109                                                      
REMARK 465     ILE C     1                                                      
REMARK 465     GLU C   182                                                      
REMARK 465     PRO C   183                                                      
REMARK 465     VAL D    -9                                                      
REMARK 465     PRO D    -8                                                      
REMARK 465     ARG D    -7                                                      
REMARK 465     GLY D    -6                                                      
REMARK 465     SER D    -5                                                      
REMARK 465     GLY D    -4                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D     3                                                      
REMARK 465     LYS D   104                                                      
REMARK 465     GLY D   105                                                      
REMARK 465     PRO D   106                                                      
REMARK 465     LEU D   107                                                      
REMARK 465     GLN D   108                                                      
REMARK 465     HIS D   109                                                      
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 B -25    CG   CD   OE1  NE2                                  
REMARK 470     LEU B -10    CG   CD1  CD2                                       
REMARK 470     VAL B  -9    CG1  CG2                                            
REMARK 470     ARG B  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  63    CG   CD   CE   NZ                                   
REMARK 470     ARG B  75    CG   CD   NE   CZ   NH1  NH2                        
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     HIS B 110    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG B 128    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 134    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 164    CG   CD   OE1  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   2    CG   CD   CE   NZ                                   
REMARK 470     LYS C  38    CG   CD   CE   NZ                                   
REMARK 470     GLU C  98    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 172    CG   CD   OE1  NE2                                  
REMARK 470     GLN C 181    CG   CD   OE1  NE2                                  
REMARK 470     GLN D -25    CG   CD   OE1  NE2                                  
REMARK 470     LYS D  63    CG   CD   CE   NZ                                   
REMARK 470     ARG D  75    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU D  89    CG   CD1  CD2                                       
REMARK 470     GLN D  90    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 103    CG   CD   CE   NZ                                   
REMARK 470     HIS D 110    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN D 126    CG   CD   OE1  NE2                                  
REMARK 470     GLN D 134    CG   CD   OE1  NE2                                  
REMARK 470     GLN D 165    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 187    CG   CD   CE   NZ                                   
REMARK 470     GLN D 189    CG   CD   OE1  NE2                                  
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 B  31     -106.66     64.27                                   
REMARK 500    ARG B  75      -93.62    -84.54                                   
REMARK 500    THR B  88      -76.56   -112.18                                   
REMARK 500    ASN D  31     -111.39     66.42                                   
REMARK 500    ARG D  75      -91.93   -111.03                                   
REMARK 500    THR D  88      -80.24   -116.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 347        DISTANCE =  5.92 ANGSTROMS                       
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                              CA D 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A  57   OE1                                                    
REMARK 620 2 GLU D -17   OE1  68.3                                              
REMARK 620 3 GLU D -17   OE2  67.7   1.0                                        
REMARK 620 4 GLU D  68   OE2  67.6   1.9   2.5                                  
REMARK 620 5 HOH D 304   O    66.9   1.8   2.0   1.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B -17   OE1                                                    
REMARK 620 2 GLU B -17   OE2  48.0                                              
REMARK 620 3 GLU B  68   OE2  84.7  89.8                                        
REMARK 620 4 HOH B 310   O   106.4 154.2  91.1                                  
REMARK 620 5 GLN C  57   OE1  15.3  58.4  72.1  97.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4P4K   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P4R   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P5M   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P5K   RELATED DB: PDB                                   
DBREF  4P57 A    1   183  UNP    P20036   DPA1_HUMAN      32    214             
DBREF  4P57 B  -25   -15  PDB    4P57     4P57           -25    -15             
DBREF  4P57 B    3   189  UNP    Q5EP54   Q5EP54_HUMAN    32    218             
DBREF  4P57 C    1   183  UNP    P20036   DPA1_HUMAN      32    214             
DBREF  4P57 D  -25   -15  PDB    4P57     4P57           -25    -15             
DBREF  4P57 D    3   189  UNP    Q5EP54   Q5EP54_HUMAN    32    218             
SEQADV 4P57 GLY B  -14  UNP  Q5EP54              LINKER                         
SEQADV 4P57 GLY B  -13  UNP  Q5EP54              LINKER                         
SEQADV 4P57 GLY B  -12  UNP  Q5EP54              LINKER                         
SEQADV 4P57 SER B  -11  UNP  Q5EP54              LINKER                         
SEQADV 4P57 LEU B  -10  UNP  Q5EP54              LINKER                         
SEQADV 4P57 VAL B   -9  UNP  Q5EP54              LINKER                         
SEQADV 4P57 PRO B   -8  UNP  Q5EP54              LINKER                         
SEQADV 4P57 ARG B   -7  UNP  Q5EP54              LINKER                         
SEQADV 4P57 GLY B   -6  UNP  Q5EP54              LINKER                         
SEQADV 4P57 SER B   -5  UNP  Q5EP54              LINKER                         
SEQADV 4P57 GLY B   -4  UNP  Q5EP54              LINKER                         
SEQADV 4P57 GLY B   -3  UNP  Q5EP54              LINKER                         
SEQADV 4P57 GLY B   -2  UNP  Q5EP54              LINKER                         
SEQADV 4P57 GLY B   -1  UNP  Q5EP54              LINKER                         
SEQADV 4P57 SER B    3  UNP  Q5EP54    THR    32 VARIANT                        
SEQADV 4P57 LYS B   69  UNP  Q5EP54    GLU    98 ENGINEERED MUTATION            
SEQADV 4P57 GLY D  -14  UNP  Q5EP54              LINKER                         
SEQADV 4P57 GLY D  -13  UNP  Q5EP54              LINKER                         
SEQADV 4P57 GLY D  -12  UNP  Q5EP54              LINKER                         
SEQADV 4P57 SER D  -11  UNP  Q5EP54              LINKER                         
SEQADV 4P57 LEU D  -10  UNP  Q5EP54              LINKER                         
SEQADV 4P57 VAL D   -9  UNP  Q5EP54              LINKER                         
SEQADV 4P57 PRO D   -8  UNP  Q5EP54              LINKER                         
SEQADV 4P57 ARG D   -7  UNP  Q5EP54              LINKER                         
SEQADV 4P57 GLY D   -6  UNP  Q5EP54              LINKER                         
SEQADV 4P57 SER D   -5  UNP  Q5EP54              LINKER                         
SEQADV 4P57 GLY D   -4  UNP  Q5EP54              LINKER                         
SEQADV 4P57 GLY D   -3  UNP  Q5EP54              LINKER                         
SEQADV 4P57 GLY D   -2  UNP  Q5EP54              LINKER                         
SEQADV 4P57 GLY D   -1  UNP  Q5EP54              LINKER                         
SEQADV 4P57 SER D    3  UNP  Q5EP54    THR    32 VARIANT                        
SEQADV 4P57 LYS B   69  UNP  Q5EP54    GLU    98 ENGINEERED MUTATION            
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  LYS 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  183  ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL          
SEQRES   2 C  183  GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE          
SEQRES   3 C  183  ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS          
SEQRES   4 C  183  GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE          
SEQRES   5 C  183  SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE          
SEQRES   6 C  183  LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN          
SEQRES   7 C  183  HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL          
SEQRES   8 C  183  PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR          
SEQRES   9 C  183  LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU          
SEQRES  10 C  183  ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU          
SEQRES  11 C  183  GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR          
SEQRES  12 C  183  SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER          
SEQRES  13 C  183  ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 C  183  LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN GLU          
SEQRES  15 C  183  PRO                                                          
SEQRES   1 D  212  GLN ALA PHE TRP ILE ASP LEU PHE GLU THR ILE GLY GLY          
SEQRES   2 D  212  GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER          
SEQRES   3 D  212  PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR          
SEQRES   4 D  212  ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE          
SEQRES   5 D  212  TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL          
SEQRES   6 D  212  GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP          
SEQRES   7 D  212  GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU          
SEQRES   8 D  212  LYS ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR          
SEQRES   9 D  212  GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN          
SEQRES  10 D  212  PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU          
SEQRES  11 D  212  GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE          
SEQRES  12 D  212  TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY          
SEQRES  13 D  212  GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE          
SEQRES  14 D  212  ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU          
SEQRES  15 D  212  GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN          
SEQRES  16 D  212  VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU          
SEQRES  17 D  212  TRP LYS ALA GLN                                              
HET    NAG  A 201      14                                                       
HET    NAG  A 202      14                                                       
HET    GOL  A 203       6                                                       
HET    NAG  B 201      14                                                       
HET     CA  B 202       1                                                       
HET    NAG  C 201      14                                                       
HET    NAG  C 202      14                                                       
HET     CA  D 201       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     GOL GLYCEROL                                                         
HETNAM      CA CALCIUM ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  NAG    5(C8 H15 N O6)                                               
FORMUL   7  GOL    C3 H8 O3                                                     
FORMUL   9   CA    2(CA 2+)                                                     
FORMUL  13  HOH   *273(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 LEU C   45  PHE C   52  1                                   8    
HELIX    8 AA8 ALA C   56  SER C   77  1                                  22    
HELIX    9 AA9 THR D   49  LEU D   51  5                                   3    
HELIX   10 AB1 GLY D   52  SER D   61  1                                  10    
HELIX   11 AB2 GLN D   62  ALA D   71  1                                  10    
HELIX   12 AB3 ARG D   75  GLY D   84  1                                  10    
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  ALA A  10   O  MET A  23           
SHEET    5 AA1 8 LEU B   8  PHE B  18 -1  O  CYS B  15   N  SER A   7           
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  ALA B  47 -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  HIS A 108   N  THR A  90           
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  HIS A 108   N  THR A  90           
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  LEU A 127  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  ASP A 162   N  LEU A 122           
SHEET    4 AA4 4 LEU A 174  TRP A 178 -1  O  LYS A 176   N  CYS A 163           
SHEET    1 AA5 4 ARG B  96  PRO B 101  0                                        
SHEET    2 AA5 4 ASN B 111  PHE B 120 -1  O  HIS B 116   N  ASN B  98           
SHEET    3 AA5 4 PHE B 153  MET B 161 -1  O  MET B 161   N  ASN B 111           
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  HIS B 116   N  ASN B  98           
SHEET    3 AA6 4 PHE B 153  MET B 161 -1  O  MET B 161   N  ASN B 111           
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 8 GLU C  40  TRP C  43  0                                        
SHEET    2 AA8 8 ASP C  29  ASP C  35 -1  N  TYR C  33   O  VAL C  42           
SHEET    3 AA8 8 GLY C  20  PHE C  26 -1  N  PHE C  24   O  PHE C  32           
SHEET    4 AA8 8 HIS C   5  GLN C  14 -1  N  ALA C  10   O  MET C  23           
SHEET    5 AA8 8 LEU D   8  PHE D  18 -1  O  CYS D  15   N  SER C   7           
SHEET    6 AA8 8 THR D  21  TYR D  30 -1  O  ILE D  29   N  GLN D  10           
SHEET    7 AA8 8 GLU D  33  ASP D  39 -1  O  GLU D  33   N  TYR D  30           
SHEET    8 AA8 8 PHE D  45  ALA D  47 -1  O  ARG D  46   N  ARG D  37           
SHEET    1 AA9 4 GLU C  88  PRO C  93  0                                        
SHEET    2 AA9 4 ASN C 103  PHE C 112 -1  O  HIS C 108   N  THR C  90           
SHEET    3 AA9 4 PHE C 145  PHE C 153 -1  O  PHE C 153   N  ASN C 103           
SHEET    4 AA9 4 VAL C 132  GLU C 134 -1  N  ALA C 133   O  TYR C 150           
SHEET    1 AB1 4 GLU C  88  PRO C  93  0                                        
SHEET    2 AB1 4 ASN C 103  PHE C 112 -1  O  HIS C 108   N  THR C  90           
SHEET    3 AB1 4 PHE C 145  PHE C 153 -1  O  PHE C 153   N  ASN C 103           
SHEET    4 AB1 4 LEU C 138  PRO C 139 -1  N  LEU C 138   O  HIS C 146           
SHEET    1 AB2 4 GLU C 126  VAL C 128  0                                        
SHEET    2 AB2 4 ASN C 118  CYS C 123 -1  N  CYS C 123   O  GLU C 126           
SHEET    3 AB2 4 PHE C 160  GLU C 166 -1  O  ASP C 162   N  LEU C 122           
SHEET    4 AB2 4 LEU C 174  GLU C 179 -1  O  TRP C 178   N  TYR C 161           
SHEET    1 AB3 4 ARG D  96  PRO D 101  0                                        
SHEET    2 AB3 4 ASN D 111  PHE D 120 -1  O  THR D 118   N  ARG D  96           
SHEET    3 AB3 4 PHE D 153  MET D 161 -1  O  MET D 161   N  ASN D 111           
SHEET    4 AB3 4 VAL D 140  SER D 142 -1  N  VAL D 141   O  MET D 158           
SHEET    1 AB4 4 ARG D  96  PRO D 101  0                                        
SHEET    2 AB4 4 ASN D 111  PHE D 120 -1  O  THR D 118   N  ARG D  96           
SHEET    3 AB4 4 PHE D 153  MET D 161 -1  O  MET D 161   N  ASN D 111           
SHEET    4 AB4 4 ILE D 146  ARG D 147 -1  N  ILE D 146   O  GLN D 154           
SHEET    1 AB5 4 GLN D 134  GLU D 136  0                                        
SHEET    2 AB5 4 GLN D 126  LEU D 131 -1  N  LEU D 131   O  GLN D 134           
SHEET    3 AB5 4 VAL D 168  GLU D 174 -1  O  GLN D 172   N  ARG D 128           
SHEET    4 AB5 4 VAL D 182  LYS D 187 -1  O  TRP D 186   N  TYR D 169           
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.04  
SSBOND   2 CYS B   15    CYS B   77                          1555   1555  2.05  
SSBOND   3 CYS B  115    CYS B  171                          1555   1555  2.03  
SSBOND   4 CYS C  107    CYS C  163                          1555   1555  2.03  
SSBOND   5 CYS D   15    CYS D   77                          1555   1555  2.05  
SSBOND   6 CYS D  115    CYS D  171                          1555   1555  2.03  
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 C  78                 C1  NAG C 201     1555   1555  1.44  
LINK         ND2 ASN C 118                 C1  NAG C 202     1555   1555  1.43  
LINK         OE1 GLN A  57                CA    CA D 201     1555   6544  2.48  
LINK         OE1 GLU B -17                CA    CA B 202     1555   1555  2.42  
LINK         OE2 GLU B -17                CA    CA B 202     1555   1555  2.88  
LINK         OE2 GLU B  68                CA    CA B 202     1555   1555  2.96  
LINK        CA    CA B 202                 O   HOH B 310     1555   1555  2.49  
LINK        CA    CA B 202                 OE1 GLN C  57     6444   1555  2.39  
LINK         OE1 GLU D -17                CA    CA D 201     1555   1555  2.29  
LINK         OE2 GLU D -17                CA    CA D 201     1555   1555  2.63  
LINK         OE2 GLU D  68                CA    CA D 201     1555   1555  2.27  
LINK        CA    CA D 201                 O   HOH D 304     1555   1555  2.43  
CISPEP   1 ARG A   17    PRO A   18          0        -3.48                     
CISPEP   2 PHE A  113    PRO A  114          0        -0.14                     
CISPEP   3 TYR B  121    PRO B  122          0        -1.23                     
CISPEP   4 ARG C   17    PRO C   18          0        -2.15                     
CISPEP   5 PHE C  113    PRO C  114          0        -0.18                     
CISPEP   6 TYR D  121    PRO D  122          0        -1.37                     
CRYST1  102.392  102.392  234.330  90.00  90.00  90.00 P 41 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009766  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009766  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004267        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system