GenomeNet

Database: PDB
Entry: 2Q6W
LinkDB: 2Q6W
Original site: 2Q6W 
HEADER    IMMUNE SYSTEM                           05-JUN-07   2Q6W              
TITLE     THE STRUCTURE OF HLA-DRA, DRB3*0101 (DR52A) WITH BOUND                
TITLE    2 PLATELET INTEGRIN PEPTIDE ASSOCIATED WITH FETAL AND                  
TITLE    3 NEONATAL ALLOIMMUNE THROMBOCYTOPENIA                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR                
COMPND   3 ALPHA CHAIN;                                                         
COMPND   4 CHAIN: A, D;                                                         
COMPND   5 FRAGMENT: SEQUENCE DATABASE RESIDUES 26-207;                         
COMPND   6 SYNONYM: MHC CLASS II ANTIGEN DRA;                                   
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB3-1            
COMPND  10 BETA CHAIN;                                                          
COMPND  11 CHAIN: B, E;                                                         
COMPND  12 FRAGMENT: SEQUENCE DATABASE RESIDUES 30-219;                         
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: INTEGRIN BETA-3;                                           
COMPND  16 CHAIN: C, F;                                                         
COMPND  17 FRAGMENT: SEQUENCE DATABASE RESIDUES 50-61;                          
COMPND  18 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA, CD61           
COMPND  19 ANTIGEN;                                                             
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 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-DRA;                                                       
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: S2;                                        
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: HLA-DRB3;                                                      
SOURCE  16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  17 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: S2;                                        
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 SYNTHETIC: YES;                                                      
SOURCE  23 OTHER_DETAILS: THE INTEGRIN PEPTIDE IS NATURALLY FOUND               
SOURCE  24 HOMO SAPIENS (HUMAN).                                                
KEYWDS    DRB3, PEPTIDE-CLASS II MHC COMPLEX, FETAL-MATERNAL                    
KEYWDS   2 ALLOIMMUNE THROMBOCYTOPENIA, THROMBOCYTOPENIA PURPURA,               
KEYWDS   3 MYASTHENIA GRAVIS, BETA 11 ARGININE, AUTOIMMUNITY, IMMUNE            
KEYWDS   4 SYSTEM                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.S.PARRY                                                             
REVDAT   2   24-FEB-09 2Q6W    1       VERSN                                    
REVDAT   1   24-JUL-07 2Q6W    0                                                
JRNL        AUTH   C.S.PARRY,J.GORSKI,L.J.STERN                                 
JRNL        TITL   CRYSTALLOGRAPHIC STRUCTURE OF THE HUMAN LEUKOCYTE            
JRNL        TITL 2 ANTIGEN DRA, DRB3*0101: MODELS OF A DIRECTIONAL              
JRNL        TITL 3 ALLOIMMUNE RESPONSE AND AUTOIMMUNITY                         
JRNL        REF    J.MOL.BIOL.                   V. 371   435 2007              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   17583734                                                     
JRNL        DOI    10.1016/J.JMB.2007.05.025                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.05                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 44561                          
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) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3684                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.31                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1757                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 51.29                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 146                          
REMARK   3   BIN FREE R VALUE                    : 0.3770                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6043                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 487                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.82000                                              
REMARK   3    B22 (A**2) : 0.82000                                              
REMARK   3    B33 (A**2) : -1.64000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.295         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.240         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.150         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.910         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6214 ; 0.029 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8463 ; 2.478 ; 1.934       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   751 ; 8.266 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   307 ;34.671 ;23.257       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   945 ;18.375 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;22.268 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   910 ; 0.159 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4857 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4017 ; 0.278 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4312 ; 0.340 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   730 ; 0.235 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    58 ; 0.243 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.267 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3823 ; 1.677 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6107 ; 2.551 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2697 ; 3.834 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2356 ; 5.641 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2Q6W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB043224.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-JAN-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 98                                 
REMARK 200  PH                             : 4.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
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                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48049                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 15.800                             
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 55.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.040                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1DLH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-20% PEG 8000, 0.1M SODIUM             
REMARK 280  ACETATE, 10% (V/V) GLYCEROL, 0.01M CD2+, PH 4.4, VAPOR              
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 297.0K                         
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      124.27750            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       46.08450            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       46.08450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       62.13875            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       46.08450            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       46.08450            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      186.41625            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       46.08450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.08450            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       62.13875            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       46.08450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.08450            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      186.41625            
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      124.27750            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ILE A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     SER C    35                                                      
REMARK 465     ILE D     1                                                      
REMARK 465     LYS D     2                                                      
REMARK 465     GLY E     1                                                      
REMARK 465     ASP E     2                                                      
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     GLU A  46    CD   OE1  OE2                                       
REMARK 470     GLU A  47    CD   OE1  OE2                                       
REMARK 470     ARG A  50    CZ   NH1  NH2                                       
REMARK 470     PHE A  51    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A  55    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  57    OE1  NE2                                            
REMARK 470     LYS A 126    NZ                                                  
REMARK 470     GLU A 141    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 166    CD   OE1  OE2                                       
REMARK 470     ASP A 171    CG   OD1  OD2                                       
REMARK 470     ALA A 182    N    CA   C    O    CB                              
REMARK 470     GLY B  20    O                                                   
REMARK 470     GLU B  35    CG   CD   OE1  OE2                                  
REMARK 470     LEU B  53    CG   CD1  CD2                                       
REMARK 470     ARG B  55    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  59    CD   OE1  OE2                                       
REMARK 470     SER B  63    OG                                                  
REMARK 470     LYS B  65    CG   CD   CE   NZ                                   
REMARK 470     ASP B  66    CG   OD1  OD2                                       
REMARK 470     GLU B  69    O                                                   
REMARK 470     ARG B  94    NE   CZ   NH1  NH2                                  
REMARK 470     HIS B  96    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN B  98    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 107    CD   OE1  NE2                                       
REMARK 470     GLN B 110    CD   OE1  NE2                                       
REMARK 470     HIS B 111    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU B 128    CD   OE1  OE2                                       
REMARK 470     ARG B 130    NE   CZ   NH1  NH2                                  
REMARK 470     GLU B 176    CD   OE1  OE2                                       
REMARK 470     VAL B 180    CG1  CG2                                            
REMARK 470     ALA B 190    O                                                   
REMARK 470     ILE D   7    CD1                                                 
REMARK 470     GLU D  46    C    O                                              
REMARK 470     ILE D  82    CG2                                                 
REMARK 470     ASN D  94    CG   OD1  ND2                                       
REMARK 470     GLU D  98    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 100    CZ   NH1  NH2                                       
REMARK 470     ILE D 106    CD1                                                 
REMARK 470     LYS D 111    NZ                                                  
REMARK 470     ALA D 182    O                                                   
REMARK 470     ASN E  19    CB   CG   OD1  ND2                                  
REMARK 470     GLU E  22    CG   CD   OE1  OE2                                  
REMARK 470     ARG E  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E  52    CG   CD   OE1  OE2                                  
REMARK 470     GLU E  59    CG   CD   OE1  OE2                                  
REMARK 470     SER E  60    CB   OG                                             
REMARK 470     ASP E  66    CG   OD1  OD2                                       
REMARK 470     LEU E  67    CG   CD1  CD2                                       
REMARK 470     GLU E  69    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 128    CG   CD   OE1  OE2                                  
REMARK 470     ARG E 133    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASN E 134    CG   OD1  ND2                                       
REMARK 470     GLN E 136    CB   CG   CD   OE1  NE2                             
REMARK 470     GLU E 138    CD   OE1  OE2                                       
REMARK 470     LYS E 139    CB   CG   CD   CE   NZ                              
REMARK 470     ALA E 140    CB                                                  
REMARK 470     ARG E 166    CD   NE   CZ   NH1  NH2                             
REMARK 470     SER E 167    CB   OG                                             
REMARK 470     VAL E 170    CB   CG1  CG2                                       
REMARK 470     ALA E 190    O                                                   
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     MET D   36   CG    SD    CE                                      
REMARK 480     SER F   35   CB    OG                                            
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   SD   MET D    36     O    HOH D   293              1.00            
REMARK 500   CE   MET D    36     O    HOH D   301              1.11            
REMARK 500   SD   MET D    36     O    HOH D   301              1.20            
REMARK 500   CE   MET D    36     O    HOH D   293              1.38            
REMARK 500   N    GLY E   125     O    HOH E   278              1.38            
REMARK 500   CG   MET D    36     O    HOH D   293              1.42            
REMARK 500   O    HOH D   293     O    HOH D   301              1.51            
REMARK 500   CA   GLY E   125     O    HOH E   278              1.57            
REMARK 500   O    MET D    36     O    HOH D   253              1.74            
REMARK 500   C    GLY E   125     O    HOH E   278              1.76            
REMARK 500   N    SER E   126     O    HOH E   278              1.77            
REMARK 500   CG2  THR E     3     O    HOH E   279              1.87            
REMARK 500   CB   LEU B    53     O    HOH B   304              1.87            
REMARK 500   CD2  LEU D    92     CE1  PHE D   108              1.92            
REMARK 500   C    PRO E   124     O    HOH E   278              1.93            
REMARK 500   ND2  ASN D   118     O    HOH D   295              1.95            
REMARK 500   C    MET D    36     O    HOH D   253              1.95            
REMARK 500   OH   TYR E    26     OD2  ASP F    28              1.96            
REMARK 500   O    HOH B   290     O    HOH B   313              2.03            
REMARK 500   N    GLU D    47     O    HOH D   294              2.07            
REMARK 500   CE3  TRP F    25     O    HOH D   303              2.10            
REMARK 500   OD2  ASP E    43     O    HOH E   267              2.11            
REMARK 500   O    LEU E   109     O    HOH E   261              2.13            
REMARK 500   CD2  TRP F    25     O    HOH E   280              2.15            
REMARK 500   OE1  GLU A    21     O    HOH A   283              2.16            
REMARK 500   O    HOH A   224     O    HOH A   294              2.16            
REMARK 500   O    HOH B   256     O    HOH B   311              2.17            
REMARK 500   CE2  TRP F    25     O    HOH E   280              2.17            
REMARK 500   O    HOH B   246     O    HOH B   300              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 163   CB    CYS A 163   SG     -0.114                       
REMARK 500    SER B  13   CB    SER B  13   OG     -0.088                       
REMARK 500    GLU B  52   CG    GLU B  52   CD      0.105                       
REMARK 500    GLN B  70   C     GLN B  70   O       0.116                       
REMARK 500    TYR B  78   CZ    TYR B  78   CE2    -0.093                       
REMARK 500    GLU B  87   CB    GLU B  87   CG     -0.124                       
REMARK 500    TYR D 150   CE2   TYR D 150   CD2    -0.107                       
REMARK 500    SER F  35   CA    SER F  35   CB      0.176                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  44   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 123   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    LYS A 176   CD  -  CE  -  NZ  ANGL. DEV. = -16.1 DEGREES          
REMARK 500    GLY B  20   CA  -  C   -  N   ANGL. DEV. = -17.2 DEGREES          
REMARK 500    ARG B  23   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    GLU B  69   CA  -  C   -  N   ANGL. DEV. = -18.6 DEGREES          
REMARK 500    LEU B 158   CB  -  CG  -  CD2 ANGL. DEV. = -12.4 DEGREES          
REMARK 500    CYS B 173   CA  -  CB  -  SG  ANGL. DEV. = -10.9 DEGREES          
REMARK 500    MET D  36   CA  -  CB  -  CG  ANGL. DEV. = -17.7 DEGREES          
REMARK 500    LEU D  92   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    ARG D 146   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG E  29   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG E  29   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG E  93   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    SER E 126   N   -  CA  -  CB  ANGL. DEV. = -12.0 DEGREES          
REMARK 500    SER F  35   N   -  CA  -  CB  ANGL. DEV. =  13.0 DEGREES          
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    MET A  36      -74.28    -60.52                                   
REMARK 500    ALA A  37      123.75    -34.13                                   
REMARK 500    LYS A  38      -16.28     89.80                                   
REMARK 500    HIS A 143       -7.71     80.07                                   
REMARK 500    SER A 156      139.00   -172.46                                   
REMARK 500    ASN B  19       65.00     63.05                                   
REMARK 500    ASN B  33     -128.81     58.03                                   
REMARK 500    TYR B  78      -61.27   -136.37                                   
REMARK 500    THR B  90      -74.43   -122.83                                   
REMARK 500    GLN B 110      -14.73     84.94                                   
REMARK 500    ASN B 134       54.54     32.96                                   
REMARK 500    TRP B 153       31.88     70.53                                   
REMARK 500    SER B 167      129.91    -35.07                                   
REMARK 500    LYS D  39       53.06     36.00                                   
REMARK 500    ARG D 100        7.33     82.30                                   
REMARK 500    HIS D 143       -3.67     66.31                                   
REMARK 500    ARG E   4      142.06    -34.88                                   
REMARK 500    ASN E  33     -114.42     56.51                                   
REMARK 500    ALA E  58      -73.88    -40.62                                   
REMARK 500    ASN E  62        2.29    -58.83                                   
REMARK 500    TYR E  78      -65.65   -138.69                                   
REMARK 500    THR E  90      -79.22   -123.40                                   
REMARK 500    GLN E 110      -14.25     76.86                                   
REMARK 500    SER E 126      118.90    -37.66                                   
REMARK 500    ASN E 134       71.48   -150.42                                   
REMARK 500    TRP E 153       32.13     70.04                                   
REMARK 500    SER E 182     -147.33    -77.91                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO A   87     GLU A   88                  148.10                    
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 E 250        DISTANCE =  5.70 ANGSTROMS                       
DBREF  2Q6W A    1   182  UNP    P01903   2DRA_HUMAN      26    207             
DBREF  2Q6W B    1   190  UNP    P79483   2B31_HUMAN      30    219             
DBREF  2Q6W C   24    35  UNP    P05106   ITB3_HUMAN      50     61             
DBREF  2Q6W D    1   182  UNP    P01903   2DRA_HUMAN      26    207             
DBREF  2Q6W E    1   190  UNP    P79483   2B31_HUMAN      30    219             
DBREF  2Q6W F   24    35  UNP    P05106   ITB3_HUMAN      50     61             
SEQADV 2Q6W ARG C   26  UNP  P05106    CYS    52 ENGINEERED                     
SEQADV 2Q6W ARG F   26  UNP  P05106    CYS    52 ENGINEERED                     
SEQRES   1 A  182  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR          
SEQRES   2 A  182  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE          
SEQRES   3 A  182  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS          
SEQRES   4 A  182  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA          
SEQRES   5 A  182  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL          
SEQRES   6 A  182  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN          
SEQRES   7 A  182  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL          
SEQRES   8 A  182  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL          
SEQRES   9 A  182  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL          
SEQRES  10 A  182  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR          
SEQRES  11 A  182  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS          
SEQRES  12 A  182  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER          
SEQRES  13 A  182  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 A  182  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA          
SEQRES   1 B  190  GLY ASP THR ARG PRO ARG PHE LEU GLU LEU ARG LYS SER          
SEQRES   2 B  190  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG TYR          
SEQRES   3 B  190  LEU ASP ARG TYR PHE HIS ASN GLN GLU GLU PHE LEU ARG          
SEQRES   4 B  190  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU          
SEQRES   5 B  190  LEU GLY ARG PRO VAL ALA GLU SER TRP ASN SER GLN LYS          
SEQRES   6 B  190  ASP LEU LEU GLU GLN LYS ARG GLY ARG VAL ASP ASN TYR          
SEQRES   7 B  190  CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL          
SEQRES   8 B  190  GLN ARG ARG VAL HIS PRO GLN VAL THR VAL TYR PRO ALA          
SEQRES   9 B  190  LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS          
SEQRES  10 B  190  SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG          
SEQRES  11 B  190  TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL          
SEQRES  12 B  190  SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN          
SEQRES  13 B  190  THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU          
SEQRES  14 B  190  VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER          
SEQRES  15 B  190  ALA LEU THR VAL GLU TRP ARG ALA                              
SEQRES   1 C   12  ALA TRP ARG SER ASP GLU ALA LEU PRO LEU GLY SER              
SEQRES   1 D  182  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR          
SEQRES   2 D  182  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE          
SEQRES   3 D  182  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS          
SEQRES   4 D  182  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA          
SEQRES   5 D  182  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL          
SEQRES   6 D  182  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN          
SEQRES   7 D  182  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL          
SEQRES   8 D  182  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL          
SEQRES   9 D  182  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL          
SEQRES  10 D  182  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR          
SEQRES  11 D  182  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS          
SEQRES  12 D  182  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER          
SEQRES  13 D  182  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 D  182  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA          
SEQRES   1 E  190  GLY ASP THR ARG PRO ARG PHE LEU GLU LEU ARG LYS SER          
SEQRES   2 E  190  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG TYR          
SEQRES   3 E  190  LEU ASP ARG TYR PHE HIS ASN GLN GLU GLU PHE LEU ARG          
SEQRES   4 E  190  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU          
SEQRES   5 E  190  LEU GLY ARG PRO VAL ALA GLU SER TRP ASN SER GLN LYS          
SEQRES   6 E  190  ASP LEU LEU GLU GLN LYS ARG GLY ARG VAL ASP ASN TYR          
SEQRES   7 E  190  CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL          
SEQRES   8 E  190  GLN ARG ARG VAL HIS PRO GLN VAL THR VAL TYR PRO ALA          
SEQRES   9 E  190  LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS          
SEQRES  10 E  190  SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG          
SEQRES  11 E  190  TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL          
SEQRES  12 E  190  SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN          
SEQRES  13 E  190  THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU          
SEQRES  14 E  190  VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER          
SEQRES  15 E  190  ALA LEU THR VAL GLU TRP ARG ALA                              
SEQRES   1 F   12  ALA TRP ARG SER ASP GLU ALA LEU PRO LEU GLY SER              
FORMUL   7  HOH   *487(H2 O)                                                    
HELIX    1   1 GLU A   47  ALA A   52  1                                   6    
HELIX    2   2 GLU A   55  SER A   77  1                                  23    
HELIX    3   3 THR B   51  LEU B   53  5                                   3    
HELIX    4   4 GLY B   54  SER B   63  1                                  10    
HELIX    5   5 GLN B   64  ARG B   72  1                                   9    
HELIX    6   6 GLY B   73  TYR B   78  1                                   6    
HELIX    7   7 TYR B   78  GLU B   87  1                                  10    
HELIX    8   8 GLU D   47  PHE D   51  5                                   5    
HELIX    9   9 GLU D   55  SER D   77  1                                  23    
HELIX   10  10 THR E   51  LEU E   53  5                                   3    
HELIX   11  11 GLY E   54  SER E   63  1                                  10    
HELIX   12  12 GLN E   64  GLY E   73  1                                  10    
HELIX   13  13 GLY E   73  TYR E   78  1                                   6    
HELIX   14  14 TYR E   78  GLU E   87  1                                  10    
SHEET    1   A 8 GLU A  40  TRP A  43  0                                        
SHEET    2   A 8 ASP A  29  ASP A  35 -1  N  ASP A  35   O  GLU A  40           
SHEET    3   A 8 SER A  19  PHE A  26 -1  N  PHE A  26   O  ASP A  29           
SHEET    4   A 8 HIS A   5  ASN A  15 -1  N  LEU A  14   O  SER A  19           
SHEET    5   A 8 PHE B   7  PHE B  18 -1  O  PHE B   7   N  ASN A  15           
SHEET    6   A 8 ARG B  23  HIS B  32 -1  O  ARG B  25   N  HIS B  16           
SHEET    7   A 8 GLU B  35  ASP B  41 -1  O  GLU B  35   N  HIS B  32           
SHEET    8   A 8 TYR B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39           
SHEET    1   B 4 GLU A  88  THR A  93  0                                        
SHEET    2   B 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92           
SHEET    3   B 4 PHE A 145  PHE A 153 -1  O  LEU A 151   N  LEU A 105           
SHEET    4   B 4 SER A 133  GLU A 134 -1  N  SER A 133   O  TYR A 150           
SHEET    1   C 4 GLU A  88  THR A  93  0                                        
SHEET    2   C 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92           
SHEET    3   C 4 PHE A 145  PHE A 153 -1  O  LEU A 151   N  LEU A 105           
SHEET    4   C 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  ARG A 146           
SHEET    1   D 4 LYS A 126  VAL A 128  0                                        
SHEET    2   D 4 ASN A 118  ARG A 123 -1  N  ARG A 123   O  LYS A 126           
SHEET    3   D 4 TYR A 161  GLU A 166 -1  O  ARG A 164   N  THR A 120           
SHEET    4   D 4 LEU A 174  TRP A 178 -1  O  LYS A 176   N  CYS A 163           
SHEET    1   E 4 GLN B  98  PRO B 103  0                                        
SHEET    2   E 4 ASN B 113  PHE B 122 -1  O  VAL B 116   N  TYR B 102           
SHEET    3   E 4 PHE B 155  THR B 163 -1  O  THR B 163   N  ASN B 113           
SHEET    4   E 4 VAL B 142  SER B 144 -1  N  VAL B 143   O  MET B 160           
SHEET    1   F 4 GLN B  98  PRO B 103  0                                        
SHEET    2   F 4 ASN B 113  PHE B 122 -1  O  VAL B 116   N  TYR B 102           
SHEET    3   F 4 PHE B 155  THR B 163 -1  O  THR B 163   N  ASN B 113           
SHEET    4   F 4 ILE B 148  GLN B 149 -1  N  ILE B 148   O  GLN B 156           
SHEET    1   G 4 GLN B 136  GLU B 138  0                                        
SHEET    2   G 4 GLU B 128  ARG B 133 -1  N  TRP B 131   O  GLU B 138           
SHEET    3   G 4 VAL B 170  GLU B 176 -1  O  GLU B 176   N  GLU B 128           
SHEET    4   G 4 LEU B 184  ARG B 189 -1  O  LEU B 184   N  VAL B 175           
SHEET    1   H 8 GLU D  40  TRP D  43  0                                        
SHEET    2   H 8 ASP D  29  ASP D  35 -1  N  HIS D  33   O  VAL D  42           
SHEET    3   H 8 SER D  19  PHE D  26 -1  N  PHE D  26   O  ASP D  29           
SHEET    4   H 8 HIS D   5  ASN D  15 -1  N  LEU D  14   O  SER D  19           
SHEET    5   H 8 PHE E   7  PHE E  18 -1  O  PHE E   7   N  ASN D  15           
SHEET    6   H 8 ARG E  23  HIS E  32 -1  O  LEU E  27   N  GLU E  14           
SHEET    7   H 8 GLU E  35  ASP E  41 -1  O  GLU E  35   N  HIS E  32           
SHEET    8   H 8 TYR E  47  ALA E  49 -1  O  ARG E  48   N  ARG E  39           
SHEET    1   I 4 GLU D  88  THR D  93  0                                        
SHEET    2   I 4 ASN D 103  PHE D 112 -1  O  ILE D 106   N  LEU D  92           
SHEET    3   I 4 PHE D 145  PHE D 153 -1  O  LEU D 151   N  LEU D 105           
SHEET    4   I 4 SER D 133  GLU D 134 -1  N  SER D 133   O  TYR D 150           
SHEET    1   J 4 GLU D  88  THR D  93  0                                        
SHEET    2   J 4 ASN D 103  PHE D 112 -1  O  ILE D 106   N  LEU D  92           
SHEET    3   J 4 PHE D 145  PHE D 153 -1  O  LEU D 151   N  LEU D 105           
SHEET    4   J 4 LEU D 138  PRO D 139 -1  N  LEU D 138   O  ARG D 146           
SHEET    1   K 4 LYS D 126  VAL D 128  0                                        
SHEET    2   K 4 ASN D 118  ARG D 123 -1  N  ARG D 123   O  LYS D 126           
SHEET    3   K 4 VAL D 160  GLU D 166 -1  O  ARG D 164   N  THR D 120           
SHEET    4   K 4 LEU D 174  GLU D 179 -1  O  TRP D 178   N  TYR D 161           
SHEET    1   L 4 GLN E  98  PRO E 103  0                                        
SHEET    2   L 4 ASN E 113  PHE E 122 -1  O  SER E 120   N  GLN E  98           
SHEET    3   L 4 PHE E 155  THR E 163 -1  O  VAL E 159   N  CYS E 117           
SHEET    4   L 4 VAL E 142  SER E 144 -1  N  VAL E 143   O  MET E 160           
SHEET    1   M 4 GLN E  98  PRO E 103  0                                        
SHEET    2   M 4 ASN E 113  PHE E 122 -1  O  SER E 120   N  GLN E  98           
SHEET    3   M 4 PHE E 155  THR E 163 -1  O  VAL E 159   N  CYS E 117           
SHEET    4   M 4 ILE E 148  GLN E 149 -1  N  ILE E 148   O  GLN E 156           
SHEET    1   N 4 GLU E 137  GLU E 138  0                                        
SHEET    2   N 4 GLU E 128  PHE E 132 -1  N  TRP E 131   O  GLU E 138           
SHEET    3   N 4 VAL E 170  GLU E 176 -1  O  THR E 172   N  PHE E 132           
SHEET    4   N 4 LEU E 184  ARG E 189 -1  O  VAL E 186   N  CYS E 173           
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.02  
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.20  
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.00  
SSBOND   4 CYS D  107    CYS D  163                          1555   1555  2.10  
SSBOND   5 CYS E   15    CYS E   79                          1555   1555  2.23  
SSBOND   6 CYS E  117    CYS E  173                          1555   1555  2.01  
CISPEP   1 ASN A   15    PRO A   16          0         1.84                     
CISPEP   2 THR A  113    PRO A  114          0        -0.30                     
CISPEP   3 TYR B  123    PRO B  124          0         1.72                     
CISPEP   4 ASN D   15    PRO D   16          0         4.20                     
CISPEP   5 THR D  113    PRO D  114          0        -5.41                     
CISPEP   6 TYR E  123    PRO E  124          0         1.28                     
CRYST1   92.169   92.169  248.555  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      0.010850  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010850  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004023        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system