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Database: PDB
Entry: 4HIX
LinkDB: 4HIX
Original site: 4HIX 
HEADER    PROTEIN FIBRIL/IMMUNE SYSTEM            12-OCT-12   4HIX              
TITLE     CRYSTAL STRUCTURE OF A HUMANISED 3D6 FAB BOUND TO AMYLOID BETA PEPTIDE
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HUMANIZED 3D6 FAB HEAVY CHAIN;                             
COMPND   3 CHAIN: H;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HUMANIZED 3D6 FAB LIGHT CHAIN;                             
COMPND   7 CHAIN: L;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: BETA-AMYLOID PROTEIN 40;                                   
COMPND  11 CHAIN: A;                                                            
COMPND  12 SYNONYM: BETA-APP40;                                                 
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, MUS MUSCULUS;                     
SOURCE   3 ORGANISM_COMMON: HUMAN, MOUSE;                                       
SOURCE   4 ORGANISM_TAXID: 9606, 10090;                                         
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS, MUS MUSCULUS;                     
SOURCE   7 ORGANISM_COMMON: HUMAN, MOUSE;                                       
SOURCE   8 ORGANISM_TAXID: 9606, 10090;                                         
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606                                                 
KEYWDS    IMMUNOGLOBULIN, IMMUNOTHERAPY CANDIDATE, AMYLOID BETA PEPTIDE,        
KEYWDS   2 PROTEIN FIBRIL-IMMUNE SYSTEM COMPLEX                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.A.MILES,G.A.N.CRESPI,M.W.PARKER                                     
REVDAT   4   19-MAR-14 4HIX    1       SOURCE                                   
REVDAT   3   02-OCT-13 4HIX    1       SOURCE                                   
REVDAT   2   20-MAR-13 4HIX    1       COMPND                                   
REVDAT   1   13-MAR-13 4HIX    0                                                
JRNL        AUTH   L.A.MILES,G.A.CRESPI,L.DOUGHTY,M.W.PARKER                    
JRNL        TITL   BAPINEUZUMAB CAPTURES THE N-TERMINUS OF THE ALZHEIMER'S      
JRNL        TITL 2 DISEASE AMYLOID-BETA PEPTIDE IN A HELICAL CONFORMATION.      
JRNL        REF    SCI REP                       V.   3  1302 2013              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   23416764                                                     
JRNL        DOI    10.1038/SREP01302                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.28                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.070                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 22096                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.2810 -  5.3090    1.00     1648   164  0.1927 0.2029        
REMARK   3     2  5.3090 -  4.2147    1.00     1562   156  0.1327 0.1650        
REMARK   3     3  4.2147 -  3.6822    0.99     1525   151  0.1466 0.1886        
REMARK   3     4  3.6822 -  3.3456    0.99     1517   151  0.1529 0.1940        
REMARK   3     5  3.3456 -  3.1058    0.99     1493   148  0.1654 0.2119        
REMARK   3     6  3.1058 -  2.9228    0.98     1500   149  0.1747 0.2510        
REMARK   3     7  2.9228 -  2.7764    0.97     1470   147  0.1698 0.2425        
REMARK   3     8  2.7764 -  2.6555    0.97     1467   146  0.1815 0.2337        
REMARK   3     9  2.6555 -  2.5533    0.96     1426   142  0.1802 0.2726        
REMARK   3    10  2.5533 -  2.4652    0.94     1397   140  0.1790 0.2614        
REMARK   3    11  2.4652 -  2.3881    0.93     1406   139  0.1968 0.2742        
REMARK   3    12  2.3881 -  2.3199    0.90     1332   133  0.2022 0.3158        
REMARK   3    13  2.3199 -  2.2588    0.85     1273   126  0.2129 0.2622        
REMARK   3    14  2.2588 -  2.2040    0.74     1080   108  0.2299 0.3125        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.860           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           3460                                  
REMARK   3   ANGLE     :  0.981           4693                                  
REMARK   3   CHIRALITY :  0.065            522                                  
REMARK   3   PLANARITY :  0.004            602                                  
REMARK   3   DIHEDRAL  : 12.822           1244                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4HIX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB075522.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95370                            
REMARK 200  MONOCHROMATOR                  : SYNCHROTRON                        
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23109                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 12.100                             
REMARK 200  R MERGE                    (I) : 0.16300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.78800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE, PEG 3350, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 295K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,-Y,-Z+1/2                                         
REMARK 290       4555   -X+1/2,-Y,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        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       29.67150            
REMARK 290   SMTRY2   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.61200            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       29.67150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       45.61200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, A                               
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH H 376  LIES ON A SPECIAL POSITION.                          
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     SER H   215                                                      
REMARK 465     CYS H   216                                                      
REMARK 465     HIS H   217                                                      
REMARK 465     HIS H   218                                                      
REMARK 465     HIS H   219                                                      
REMARK 465     HIS H   220                                                      
REMARK 465     HIS H   221                                                      
REMARK 465     HIS H   222                                                      
REMARK 465     GLU L     0                                                      
REMARK 465     ASP A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     TYR A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     VAL A    12                                                      
REMARK 465     HIS A    13                                                      
REMARK 465     HIS A    14                                                      
REMARK 465     GLN A    15                                                      
REMARK 465     LYS A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     VAL A    18                                                      
REMARK 465     PHE A    19                                                      
REMARK 465     PHE A    20                                                      
REMARK 465     ALA A    21                                                      
REMARK 465     GLU A    22                                                      
REMARK 465     ASP A    23                                                      
REMARK 465     VAL A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     ASN A    27                                                      
REMARK 465     LYS A    28                                                      
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   O    HOH H   411     O    HOH H   414              1.88            
REMARK 500   O    HOH L   389     O    HOH L   409              1.91            
REMARK 500   O    HOH H   402     O    HOH L   400              2.18            
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    ASP H 101      -77.35   -106.31                                   
REMARK 500    SER H 127     -108.24   -101.17                                   
REMARK 500    ASP H 144       70.04     62.74                                   
REMARK 500    VAL L  51      -51.72     71.81                                   
REMARK 500    PRO L 141     -168.49    -79.15                                   
REMARK 500    ASN L 152       -3.06     70.45                                   
REMARK 500    ARG A   5     -150.91   -109.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3BAE   RELATED DB: PDB                                   
REMARK 900 WO2                                                                  
REMARK 900 RELATED ID: 2IPU   RELATED DB: PDB                                   
REMARK 900 PFA1                                                                 
DBREF  4HIX A    1    28  UNP    P05067   A4_HUMAN       672    699             
DBREF  4HIX H    2   222  PDB    4HIX     4HIX             2    222             
DBREF  4HIX L    0   214  PDB    4HIX     4HIX             0    214             
SEQRES   1 H  227  VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN PRO          
SEQRES   2 H  227  GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY PHE          
SEQRES   3 H  227  THR PHE SER ASN TYR GLY MET SER TRP VAL ARG GLN ALA          
SEQRES   4 H  227  PRO GLY LYS GLY LEU GLU TRP VAL ALA SER ILE ARG SER          
SEQRES   5 H  227  GLY GLY GLY ARG THR TYR TYR SER ASP ASN VAL LYS GLY          
SEQRES   6 H  227  ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER LEU          
SEQRES   7 H  227  TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA          
SEQRES   8 H  227  LEU TYR TYR CYS VAL ARG TYR ASP HIS TYR SER GLY SER          
SEQRES   9 H  227  SER ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER          
SEQRES  10 H  227  SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA          
SEQRES  11 H  227  PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU          
SEQRES  12 H  227  GLY CYS LEU VAL LYS ASP TYR PHE PRO GLN PRO VAL THR          
SEQRES  13 H  227  VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS          
SEQRES  14 H  227  THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER          
SEQRES  15 H  227  LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY          
SEQRES  16 H  227  THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER          
SEQRES  17 H  227  ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS          
SEQRES  18 H  227  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 L  220  GLU TYR VAL VAL MET THR GLN SER PRO LEU SER LEU PRO          
SEQRES   2 L  220  VAL THR PRO GLY GLU PRO ALA SER ILE SER CYS LYS SER          
SEQRES   3 L  220  SER GLN SER LEU LEU ASP SER ASP GLY LYS THR TYR LEU          
SEQRES   4 L  220  ASN TRP LEU LEU GLN LYS PRO GLY GLN SER PRO GLN ARG          
SEQRES   5 L  220  LEU ILE TYR LEU VAL SER LYS LEU ASP SER GLY VAL PRO          
SEQRES   6 L  220  ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR          
SEQRES   7 L  220  LEU LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL          
SEQRES   8 L  220  TYR TYR CYS TRP GLN GLY THR HIS PHE PRO ARG THR PHE          
SEQRES   9 L  220  GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA          
SEQRES  10 L  220  ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN          
SEQRES  11 L  220  LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN          
SEQRES  12 L  220  ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL          
SEQRES  13 L  220  ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL          
SEQRES  14 L  220  THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER          
SEQRES  15 L  220  SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS          
SEQRES  16 L  220  LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER          
SEQRES  17 L  220  SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS              
SEQRES   1 A   28  ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS          
SEQRES   2 A   28  HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER          
SEQRES   3 A   28  ASN LYS                                                      
FORMUL   4  HOH   *237(H2 O)                                                    
HELIX    1   1 THR H   28  TYR H   32  5                                   5    
HELIX    2   2 ASP H   61  LYS H   64  5                                   4    
HELIX    3   3 ASN H   73  LYS H   75  5                                   3    
HELIX    4   4 ARG H   83  THR H   87  5                                   5    
HELIX    5   5 SER H  156  ALA H  158  5                                   3    
HELIX    6   6 SER H  187  LEU H  189  5                                   3    
HELIX    7   7 LYS H  201  ASN H  204  5                                   4    
HELIX    8   8 GLU L   79  VAL L   83  5                                   5    
HELIX    9   9 SER L  121  SER L  127  1                                   7    
HELIX   10  10 LYS L  183  GLU L  187  1                                   5    
HELIX   11  11 ASP A    1  ARG A    5  5                                   5    
SHEET    1   A 4 GLN H   3  SER H   7  0                                        
SHEET    2   A 4 LEU H  18  SER H  25 -1  O  SER H  21   N  SER H   7           
SHEET    3   A 4 SER H  77  MET H  82 -1  O  MET H  82   N  LEU H  18           
SHEET    4   A 4 PHE H  67  ASP H  72 -1  N  SER H  70   O  TYR H  79           
SHEET    1   B 6 LEU H  11  VAL H  12  0                                        
SHEET    2   B 6 THR H 107  VAL H 111  1  O  THR H 110   N  VAL H  12           
SHEET    3   B 6 ALA H  88  ASP H  96 -1  N  ALA H  88   O  VAL H 109           
SHEET    4   B 6 GLY H  33  GLN H  39 -1  N  VAL H  37   O  TYR H  91           
SHEET    5   B 6 LEU H  45  ILE H  51 -1  O  GLU H  46   N  ARG H  38           
SHEET    6   B 6 THR H  57  TYR H  59 -1  O  TYR H  58   N  SER H  50           
SHEET    1   C 4 LEU H  11  VAL H  12  0                                        
SHEET    2   C 4 THR H 107  VAL H 111  1  O  THR H 110   N  VAL H  12           
SHEET    3   C 4 ALA H  88  ASP H  96 -1  N  ALA H  88   O  VAL H 109           
SHEET    4   C 4 SER H 100A TRP H 103 -1  O  TYR H 102   N  ARG H  94           
SHEET    1   D 4 SER H 120  LEU H 124  0                                        
SHEET    2   D 4 THR H 135  TYR H 145 -1  O  LEU H 141   N  PHE H 122           
SHEET    3   D 4 TYR H 176  PRO H 185 -1  O  TYR H 176   N  TYR H 145           
SHEET    4   D 4 VAL H 163  THR H 165 -1  N  HIS H 164   O  VAL H 181           
SHEET    1   E 4 SER H 120  LEU H 124  0                                        
SHEET    2   E 4 THR H 135  TYR H 145 -1  O  LEU H 141   N  PHE H 122           
SHEET    3   E 4 TYR H 176  PRO H 185 -1  O  TYR H 176   N  TYR H 145           
SHEET    4   E 4 VAL H 169  LEU H 170 -1  N  VAL H 169   O  SER H 177           
SHEET    1   F 3 THR H 151  TRP H 154  0                                        
SHEET    2   F 3 ILE H 195  HIS H 200 -1  O  ASN H 197   N  SER H 153           
SHEET    3   F 3 THR H 205  LYS H 210 -1  O  VAL H 207   N  VAL H 198           
SHEET    1   G 4 MET L   4  SER L   7  0                                        
SHEET    2   G 4 ALA L  19  SER L  25 -1  O  SER L  22   N  SER L   7           
SHEET    3   G 4 ASP L  70  ILE L  75 -1  O  PHE L  71   N  CYS L  23           
SHEET    4   G 4 PHE L  62  SER L  67 -1  N  SER L  63   O  LYS L  74           
SHEET    1   H 6 SER L  10  VAL L  13  0                                        
SHEET    2   H 6 THR L 102  ILE L 106  1  O  LYS L 103   N  LEU L  11           
SHEET    3   H 6 GLY L  84  GLN L  90 -1  N  GLY L  84   O  VAL L 104           
SHEET    4   H 6 LEU L  33  GLN L  38 -1  N  LEU L  36   O  TYR L  87           
SHEET    5   H 6 GLN L  45  TYR L  49 -1  O  LEU L  47   N  TRP L  35           
SHEET    6   H 6 LYS L  53  LEU L  54 -1  O  LYS L  53   N  TYR L  49           
SHEET    1   I 4 SER L  10  VAL L  13  0                                        
SHEET    2   I 4 THR L 102  ILE L 106  1  O  LYS L 103   N  LEU L  11           
SHEET    3   I 4 GLY L  84  GLN L  90 -1  N  GLY L  84   O  VAL L 104           
SHEET    4   I 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1   J 4 SER L 114  PHE L 118  0                                        
SHEET    2   J 4 THR L 129  PHE L 139 -1  O  LEU L 135   N  PHE L 116           
SHEET    3   J 4 TYR L 173  SER L 182 -1  O  LEU L 175   N  LEU L 136           
SHEET    4   J 4 SER L 159  VAL L 163 -1  N  GLN L 160   O  THR L 178           
SHEET    1   K 4 ALA L 153  LEU L 154  0                                        
SHEET    2   K 4 LYS L 145  VAL L 150 -1  N  VAL L 150   O  ALA L 153           
SHEET    3   K 4 VAL L 191  THR L 197 -1  O  ALA L 193   N  LYS L 149           
SHEET    4   K 4 VAL L 205  ASN L 210 -1  O  VAL L 205   N  VAL L 196           
SSBOND   1 CYS H   22    CYS H   92                          1555   1555  2.05  
SSBOND   2 CYS H  140    CYS H  196                          1555   1555  2.03  
SSBOND   3 CYS L   23    CYS L   88                          1555   1555  2.05  
SSBOND   4 CYS L  134    CYS L  194                          1555   1555  2.03  
CISPEP   1 SER H  128    LYS H  129          0        -2.21                     
CISPEP   2 LYS H  129    SER H  130          0        -3.03                     
CISPEP   3 PHE H  146    PRO H  147          0        -2.14                     
CISPEP   4 GLN H  148    PRO H  149          0         2.48                     
CISPEP   5 SER L    7    PRO L    8          0        -1.66                     
CISPEP   6 PHE L   94    PRO L   95          0         4.40                     
CISPEP   7 TYR L  140    PRO L  141          0         3.23                     
CRYST1   59.343   83.039   91.224  90.00  90.00  90.00 P 21 2 21     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016851  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012043  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010962        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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