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Database: PDB
Entry: 1N3Y
LinkDB: 1N3Y
Original site: 1N3Y 
HEADER    CELL ADHESION                           30-OCT-02   1N3Y              
TITLE     CRYSTAL STRUCTURE OF THE ALPHA-X BETA2 INTEGRIN I DOMAIN              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-X;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: I DOMAIN;                                                  
COMPND   5 SYNONYM: LEUKOCYTE ADHESION GLYCOPROTEIN P150,95 ALPHA CHAIN;        
COMPND   6 LEUKOCYTE ADHESION RECEPTOR P150,95; CD11C; LEU M5;                  
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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: ITGAX OR CD11C;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    ALPHA/BETA ROSSMANN FOLD, CELL ADHESION                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.VORUP-JENSEN,C.OSTERMEIER,M.SHIMAOKA,U.HOMMEL,T.A.SPRINGER          
REVDAT   4   27-OCT-21 1N3Y    1       SEQADV                                   
REVDAT   3   24-FEB-09 1N3Y    1       VERSN                                    
REVDAT   2   15-FEB-05 1N3Y    1       JRNL                                     
REVDAT   1   18-FEB-03 1N3Y    0                                                
JRNL        AUTH   T.VORUP-JENSEN,C.OSTERMEIER,M.SHIMAOKA,U.HOMMEL,T.A.SPRINGER 
JRNL        TITL   STRUCTURE AND ALLOSTERIC REGULATION OF THE ALPHA X BETA 2    
JRNL        TITL 2 INTEGRIN I DOMAIN.                                           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 100  1873 2003              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   12554829                                                     
JRNL        DOI    10.1073/PNAS.0237387100                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.72                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 32311                          
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) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1601                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 32357                
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5055                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690                       
REMARK   3   BIN FREE R VALUE                    : 0.2980                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 283                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.018                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1512                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 291                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.05000                                             
REMARK   3    B22 (A**2) : -2.05000                                             
REMARK   3    B33 (A**2) : 4.10000                                              
REMARK   3    B12 (A**2) : -0.74000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.19                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.11                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.21                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.11                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.200                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.720                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.240 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.980 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.230 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.450 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.41                                                 
REMARK   3   BSOL        : 61.54                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1N3Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-02.                  
REMARK 100 THE DEPOSITION ID IS D_1000017488.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : ENRAF-NONIUS                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : OSMIC MIRRORS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32357                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22900                            
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: CNS                                                   
REMARK 200 STARTING MODEL: IN-HOUSE STRUCTURE OF A MAC1 I DOMAIN                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, GLYCEROL, SODIUM       
REMARK 280  ACETATE, EDTA, PH 5.0, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       21.92533            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       43.85067            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       32.88800            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       54.81333            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       10.96267            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     GLY A   122                                                      
REMARK 465     SER A   123                                                      
REMARK 465     HIS A   124                                                      
REMARK 465     MET A   125                                                      
REMARK 465     ALA A   126                                                      
REMARK 465     SER A   127                                                      
REMARK 465     ARG A   128                                                      
REMARK 465     GLU A   318                                                      
REMARK 465     GLY A   319                                                      
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    SER A 175     -114.51   -150.92                                   
REMARK 500    ASN A 192       75.68   -151.86                                   
REMARK 500    SER A 199       49.00   -108.49                                   
REMARK 500    GLN A 204      174.32     73.05                                   
REMARK 500    ARG A 219      -57.62   -144.80                                   
REMARK 500    ASN A 275     -145.74    -87.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1N3Y A  128   319  UNP    P20702   ITAX_HUMAN     147    338             
SEQADV 1N3Y GLY A  122  UNP  P20702              CLONING ARTIFACT               
SEQADV 1N3Y SER A  123  UNP  P20702              CLONING ARTIFACT               
SEQADV 1N3Y HIS A  124  UNP  P20702              CLONING ARTIFACT               
SEQADV 1N3Y MET A  125  UNP  P20702              CLONING ARTIFACT               
SEQADV 1N3Y ALA A  126  UNP  P20702              CLONING ARTIFACT               
SEQADV 1N3Y SER A  127  UNP  P20702              CLONING ARTIFACT               
SEQADV 1N3Y SER A  190  UNP  P20702    THR   209 ENGINEERED MUTATION            
SEQADV 1N3Y ALA A  232  UNP  P20702    THR   251 ENGINEERED MUTATION            
SEQRES   1 A  198  GLY SER HIS MET ALA SER ARG GLN GLU GLN ASP ILE VAL          
SEQRES   2 A  198  PHE LEU ILE ASP GLY SER GLY SER ILE SER SER ARG ASN          
SEQRES   3 A  198  PHE ALA THR MET MET ASN PHE VAL ARG ALA VAL ILE SER          
SEQRES   4 A  198  GLN PHE GLN ARG PRO SER THR GLN PHE SER LEU MET GLN          
SEQRES   5 A  198  PHE SER ASN LYS PHE GLN THR HIS PHE THR PHE GLU GLU          
SEQRES   6 A  198  PHE ARG ARG SER SER ASN PRO LEU SER LEU LEU ALA SER          
SEQRES   7 A  198  VAL HIS GLN LEU GLN GLY PHE THR TYR THR ALA THR ALA          
SEQRES   8 A  198  ILE GLN ASN VAL VAL HIS ARG LEU PHE HIS ALA SER TYR          
SEQRES   9 A  198  GLY ALA ARG ARG ASP ALA ALA LYS ILE LEU ILE VAL ILE          
SEQRES  10 A  198  THR ASP GLY LYS LYS GLU GLY ASP SER LEU ASP TYR LYS          
SEQRES  11 A  198  ASP VAL ILE PRO MET ALA ASP ALA ALA GLY ILE ILE ARG          
SEQRES  12 A  198  TYR ALA ILE GLY VAL GLY LEU ALA PHE GLN ASN ARG ASN          
SEQRES  13 A  198  SER TRP LYS GLU LEU ASN ASP ILE ALA SER LYS PRO SER          
SEQRES  14 A  198  GLN GLU HIS ILE PHE LYS VAL GLU ASP PHE ASP ALA LEU          
SEQRES  15 A  198  LYS ASP ILE GLN ASN GLN LEU LYS GLU LYS ILE PHE ALA          
SEQRES  16 A  198  ILE GLU GLY                                                  
FORMUL   2  HOH   *291(H2 O)                                                    
HELIX    1   1 SER A  144  SER A  160  1                                  17    
HELIX    2   2 THR A  183  SER A  190  1                                   8    
HELIX    3   3 ASN A  192  ALA A  198  5                                   7    
HELIX    4   4 TYR A  208  HIS A  218  1                                  11    
HELIX    5   5 HIS A  222  GLY A  226  5                                   5    
HELIX    6   6 ASP A  249  ALA A  260  1                                  12    
HELIX    7   7 LEU A  271  ASN A  275  5                                   5    
HELIX    8   8 SER A  278  ALA A  286  1                                   9    
HELIX    9   9 SER A  290  GLU A  292  5                                   3    
HELIX   10  10 ASP A  299  ASP A  305  5                                   7    
HELIX   11  11 ILE A  306  ALA A  316  1                                  11    
SHEET    1   A 6 PHE A 178  PHE A 182  0                                        
SHEET    2   A 6 THR A 167  PHE A 174 -1  N  GLN A 173   O  GLN A 179           
SHEET    3   A 6 GLN A 131  ASP A 138  1  N  ILE A 133   O  GLN A 168           
SHEET    4   A 6 ALA A 232  THR A 239  1  O  ILE A 236   N  LEU A 136           
SHEET    5   A 6 ILE A 263  VAL A 269  1  O  ILE A 263   N  LEU A 235           
SHEET    6   A 6 ILE A 294  VAL A 297  1  O  PHE A 295   N  GLY A 268           
CISPEP   1 ARG A  164    PRO A  165          0        -0.17                     
CISPEP   2 LYS A  288    PRO A  289          0         0.11                     
CRYST1   84.694   84.694   65.776  90.00  90.00 120.00 P 61          6          
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      0.011807  0.006817  0.000000        0.00000                         
SCALE2      0.000000  0.013634  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015203        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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