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Database: PDB
Entry: 5WMN
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Original site: 5WMN 
HEADER    IMMUNE SYSTEM                           30-JUL-17   5WMN              
TITLE     CRYSTAL STRUCTURE OF HLA-B7 IN COMPLEX WITH SPI, AN INFLUENZA PEPTIDE 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, B-7 ALPHA CHAIN;   
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: MHC CLASS I ANTIGEN B*7;                                    
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: BETA-2-MICROGLOBULIN;                                      
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: SPI PEPTIDE FROM INFLUENZA A VIRUS;                        
COMPND  12 CHAIN: E, F;                                                         
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HLA-B, HLAB;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
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: PET30;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: B2M, CDABP0092, HDCMA22P;                                      
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET30;                                    
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 SYNTHETIC: YES;                                                      
SOURCE  23 ORGANISM_SCIENTIFIC: UNIDENTIFIED INFLUENZA VIRUS;                   
SOURCE  24 ORGANISM_TAXID: 11309                                                
KEYWDS    HLA, VIRAL PEPTIDE, IAV, EBV, CMV, CROSSREACTIVITY, TCR, T CELL,      
KEYWDS   2 HETEROLOGOUS IMMUNITY, IMMUNE SYSTEM                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.GRAS,J.ROSSJOHN                                                     
REVDAT   2   13-JUN-18 5WMN    1       JRNL                                     
REVDAT   1   06-JUN-18 5WMN    0                                                
JRNL        AUTH   L.C.ROWNTREE,T.H.O.NGUYEN,H.HALIM,A.W.PURCELL,J.ROSSJOHN,    
JRNL        AUTH 2 S.GRAS,T.C.KOTSIMBOS,N.A.MIFSUD                              
JRNL        TITL   INABILITY TO DETECT CROSS-REACTIVE MEMORY T CELLS CHALLENGES 
JRNL        TITL 2 THE FREQUENCY OF HETEROLOGOUS IMMUNITY AMONG COMMON VIRUSES. 
JRNL        REF    J. IMMUNOL.                   V. 200  3993 2018              
JRNL        REFN                   ESSN 1550-6606                               
JRNL        PMID   29735483                                                     
JRNL        DOI    10.4049/JIMMUNOL.1800010                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.82 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER                                               
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.81                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 77437                          
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)  : 0.186                          
REMARK   3   R VALUE            (WORKING SET)  : 0.184                          
REMARK   3   FREE R VALUE                      : 0.222                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.010                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3878                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.82                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.87                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.27                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 5585                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2222                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 5284                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2209                   
REMARK   3   BIN FREE R VALUE                        : 0.2452                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.39                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 301                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6306                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 689                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.36                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.13760                                              
REMARK   3    B22 (A**2) : -7.49760                                             
REMARK   3    B33 (A**2) : 1.36000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.68250                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.209               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.132               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.124               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.128               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.122               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6640   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 9058   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2332   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 198    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 989    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6640   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 823    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7885   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.06                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.59                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.38                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5WMN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229298.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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) : 0.954                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.3.11                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 77499                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.820                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.610                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.73100                            
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: 3VCL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-24%PEG4000, 0.2 NH4 ACETATE, 0.1M     
REMARK 280  NA-CACODYLATE PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE    
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       42.13100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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: 19230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E                               
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: 4510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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     MET B     0                                                      
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     ARG A 181    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 226    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  75    CG   CD   CE   NZ                                   
REMARK 470     ARG C 108    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 226    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A   2      -46.22   -145.56                                   
REMARK 500    ASP A  29     -127.42     53.71                                   
REMARK 500    TRP B  60       -6.23     77.54                                   
REMARK 500    SER C   2      -46.67    160.84                                   
REMARK 500    ASP C  29     -125.85     57.15                                   
REMARK 500    ASP C 114       90.03   -162.79                                   
REMARK 500    LYS C 176     -115.93     49.42                                   
REMARK 500    GLN C 224       42.02   -104.36                                   
REMARK 500    ASN D  21     -155.87   -145.85                                   
REMARK 500    TRP D  60       -6.99     77.70                                   
REMARK 500    SER F   6     -157.16    -75.82                                   
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 C 519        DISTANCE =  7.98 ANGSTROMS                       
DBREF  5WMN A    1   276  UNP    P01889   1B07_HUMAN      25    300             
DBREF  5WMN B    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  5WMN C    1   276  UNP    P01889   1B07_HUMAN      25    300             
DBREF  5WMN D    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  5WMN E    1     9  PDB    5WMN     5WMN             1      9             
DBREF  5WMN F    1     9  PDB    5WMN     5WMN             1      9             
SEQADV 5WMN MET B    0  UNP  P61769              INITIATING METHIONINE          
SEQADV 5WMN MET D    0  UNP  P61769              INITIATING METHIONINE          
SEQRES   1 A  276  GLY SER HIS SER MET ARG TYR PHE TYR THR SER VAL SER          
SEQRES   2 A  276  ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE SER VAL GLY          
SEQRES   3 A  276  TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP          
SEQRES   4 A  276  ALA ALA SER PRO ARG GLU GLU PRO ARG ALA PRO TRP ILE          
SEQRES   5 A  276  GLU GLN GLU GLY PRO GLU TYR TRP ASP ARG ASN THR GLN          
SEQRES   6 A  276  ILE TYR LYS ALA GLN ALA GLN THR ASP ARG GLU SER LEU          
SEQRES   7 A  276  ARG ASN LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY          
SEQRES   8 A  276  SER HIS THR LEU GLN SER MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 A  276  PRO ASP GLY ARG LEU LEU ARG GLY HIS ASP GLN TYR ALA          
SEQRES  10 A  276  TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU          
SEQRES  11 A  276  ARG SER TRP THR ALA ALA ASP THR ALA ALA GLN ILE THR          
SEQRES  12 A  276  GLN ARG LYS TRP GLU ALA ALA ARG GLU ALA GLU GLN ARG          
SEQRES  13 A  276  ARG ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU ARG          
SEQRES  14 A  276  ARG TYR LEU GLU ASN GLY LYS ASP LYS LEU GLU ARG ALA          
SEQRES  15 A  276  ASP PRO PRO LYS THR HIS VAL THR HIS HIS PRO ILE SER          
SEQRES  16 A  276  ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY PHE          
SEQRES  17 A  276  TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY          
SEQRES  18 A  276  GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG          
SEQRES  19 A  276  PRO ALA GLY ASP ARG THR PHE GLN LYS TRP ALA ALA VAL          
SEQRES  20 A  276  VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS          
SEQRES  21 A  276  VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG          
SEQRES  22 A  276  TRP GLU PRO                                                  
SEQRES   1 B  100  MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG          
SEQRES   2 B  100  HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS          
SEQRES   3 B  100  TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP          
SEQRES   4 B  100  LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS          
SEQRES   5 B  100  SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU          
SEQRES   6 B  100  LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU          
SEQRES   7 B  100  TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO          
SEQRES   8 B  100  LYS ILE VAL LYS TRP ASP ARG ASP MET                          
SEQRES   1 C  276  GLY SER HIS SER MET ARG TYR PHE TYR THR SER VAL SER          
SEQRES   2 C  276  ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE SER VAL GLY          
SEQRES   3 C  276  TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP          
SEQRES   4 C  276  ALA ALA SER PRO ARG GLU GLU PRO ARG ALA PRO TRP ILE          
SEQRES   5 C  276  GLU GLN GLU GLY PRO GLU TYR TRP ASP ARG ASN THR GLN          
SEQRES   6 C  276  ILE TYR LYS ALA GLN ALA GLN THR ASP ARG GLU SER LEU          
SEQRES   7 C  276  ARG ASN LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY          
SEQRES   8 C  276  SER HIS THR LEU GLN SER MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 C  276  PRO ASP GLY ARG LEU LEU ARG GLY HIS ASP GLN TYR ALA          
SEQRES  10 C  276  TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU          
SEQRES  11 C  276  ARG SER TRP THR ALA ALA ASP THR ALA ALA GLN ILE THR          
SEQRES  12 C  276  GLN ARG LYS TRP GLU ALA ALA ARG GLU ALA GLU GLN ARG          
SEQRES  13 C  276  ARG ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU ARG          
SEQRES  14 C  276  ARG TYR LEU GLU ASN GLY LYS ASP LYS LEU GLU ARG ALA          
SEQRES  15 C  276  ASP PRO PRO LYS THR HIS VAL THR HIS HIS PRO ILE SER          
SEQRES  16 C  276  ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY PHE          
SEQRES  17 C  276  TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY          
SEQRES  18 C  276  GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG          
SEQRES  19 C  276  PRO ALA GLY ASP ARG THR PHE GLN LYS TRP ALA ALA VAL          
SEQRES  20 C  276  VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS          
SEQRES  21 C  276  VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG          
SEQRES  22 C  276  TRP GLU PRO                                                  
SEQRES   1 D  100  MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG          
SEQRES   2 D  100  HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS          
SEQRES   3 D  100  TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP          
SEQRES   4 D  100  LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS          
SEQRES   5 D  100  SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU          
SEQRES   6 D  100  LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU          
SEQRES   7 D  100  TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO          
SEQRES   8 D  100  LYS ILE VAL LYS TRP ASP ARG ASP MET                          
SEQRES   1 E    9  SER PRO ILE VAL PRO SER PHE ASP MET                          
SEQRES   1 F    9  SER PRO ILE VAL PRO SER PHE ASP MET                          
FORMUL   7  HOH   *689(H2 O)                                                    
HELIX    1 AA1 ALA A   49  GLU A   53  5                                   5    
HELIX    2 AA2 GLY A   56  TYR A   85  1                                  30    
HELIX    3 AA3 ASP A  137  ALA A  150  1                                  14    
HELIX    4 AA4 ARG A  151  GLY A  162  1                                  12    
HELIX    5 AA5 GLY A  162  GLY A  175  1                                  14    
HELIX    6 AA6 GLY A  175  GLU A  180  1                                   6    
HELIX    7 AA7 THR A  225  THR A  228  5                                   4    
HELIX    8 AA8 GLU A  253  GLN A  255  5                                   3    
HELIX    9 AA9 ILE C   52  GLU C   55  5                                   4    
HELIX   10 AB1 GLY C   56  TYR C   85  1                                  30    
HELIX   11 AB2 ASP C  137  ALA C  150  1                                  14    
HELIX   12 AB3 ARG C  151  GLY C  162  1                                  12    
HELIX   13 AB4 GLY C  162  LYS C  176  1                                  15    
HELIX   14 AB5 LYS C  176  ARG C  181  1                                   6    
HELIX   15 AB6 THR C  225  THR C  228  5                                   4    
HELIX   16 AB7 GLU C  253  GLN C  255  5                                   3    
SHEET    1 AA1 8 GLU A  46  PRO A  47  0                                        
SHEET    2 AA1 8 THR A  31  ASP A  37 -1  N  ARG A  35   O  GLU A  46           
SHEET    3 AA1 8 ARG A  21  VAL A  28 -1  N  GLY A  26   O  PHE A  33           
SHEET    4 AA1 8 HIS A   3  VAL A  12 -1  N  ARG A   6   O  TYR A  27           
SHEET    5 AA1 8 THR A  94  VAL A 103 -1  O  VAL A 103   N  HIS A   3           
SHEET    6 AA1 8 LEU A 109  TYR A 118 -1  O  LEU A 110   N  ASP A 102           
SHEET    7 AA1 8 LYS A 121  LEU A 126 -1  O  LEU A 126   N  ASP A 114           
SHEET    8 AA1 8 TRP A 133  ALA A 135 -1  O  THR A 134   N  ALA A 125           
SHEET    1 AA2 4 LYS A 186  PRO A 193  0                                        
SHEET    2 AA2 4 GLU A 198  PHE A 208 -1  O  LEU A 206   N  LYS A 186           
SHEET    3 AA2 4 PHE A 241  PRO A 250 -1  O  VAL A 249   N  ALA A 199           
SHEET    4 AA2 4 GLU A 229  LEU A 230 -1  N  GLU A 229   O  ALA A 246           
SHEET    1 AA3 4 LYS A 186  PRO A 193  0                                        
SHEET    2 AA3 4 GLU A 198  PHE A 208 -1  O  LEU A 206   N  LYS A 186           
SHEET    3 AA3 4 PHE A 241  PRO A 250 -1  O  VAL A 249   N  ALA A 199           
SHEET    4 AA3 4 ARG A 234  PRO A 235 -1  N  ARG A 234   O  GLN A 242           
SHEET    1 AA4 4 GLU A 222  ASP A 223  0                                        
SHEET    2 AA4 4 THR A 214  ARG A 219 -1  N  ARG A 219   O  GLU A 222           
SHEET    3 AA4 4 TYR A 257  GLN A 262 -1  O  THR A 258   N  GLN A 218           
SHEET    4 AA4 4 LEU A 270  LEU A 272 -1  O  LEU A 272   N  CYS A 259           
SHEET    1 AA5 4 LYS B   6  SER B  11  0                                        
SHEET    2 AA5 4 ASN B  21  PHE B  30 -1  O  ASN B  24   N  TYR B  10           
SHEET    3 AA5 4 PHE B  62  PHE B  70 -1  O  PHE B  62   N  PHE B  30           
SHEET    4 AA5 4 GLU B  50  HIS B  51 -1  N  GLU B  50   O  TYR B  67           
SHEET    1 AA6 4 LYS B   6  SER B  11  0                                        
SHEET    2 AA6 4 ASN B  21  PHE B  30 -1  O  ASN B  24   N  TYR B  10           
SHEET    3 AA6 4 PHE B  62  PHE B  70 -1  O  PHE B  62   N  PHE B  30           
SHEET    4 AA6 4 SER B  55  PHE B  56 -1  N  SER B  55   O  TYR B  63           
SHEET    1 AA7 4 GLU B  44  ARG B  45  0                                        
SHEET    2 AA7 4 GLU B  36  LYS B  41 -1  N  LYS B  41   O  GLU B  44           
SHEET    3 AA7 4 TYR B  78  ASN B  83 -1  O  ARG B  81   N  ASP B  38           
SHEET    4 AA7 4 LYS B  91  LYS B  94 -1  O  LYS B  91   N  VAL B  82           
SHEET    1 AA8 8 GLU C  46  PRO C  47  0                                        
SHEET    2 AA8 8 THR C  31  ASP C  37 -1  N  ARG C  35   O  GLU C  46           
SHEET    3 AA8 8 ARG C  21  VAL C  28 -1  N  VAL C  28   O  THR C  31           
SHEET    4 AA8 8 HIS C   3  VAL C  12 -1  N  THR C  10   O  ILE C  23           
SHEET    5 AA8 8 THR C  94  VAL C 103 -1  O  VAL C 103   N  HIS C   3           
SHEET    6 AA8 8 LEU C 109  TYR C 118 -1  O  LEU C 110   N  ASP C 102           
SHEET    7 AA8 8 LYS C 121  LEU C 126 -1  O  LEU C 126   N  ASP C 114           
SHEET    8 AA8 8 TRP C 133  ALA C 135 -1  O  THR C 134   N  ALA C 125           
SHEET    1 AA9 4 LYS C 186  PRO C 193  0                                        
SHEET    2 AA9 4 GLU C 198  PHE C 208 -1  O  LEU C 206   N  LYS C 186           
SHEET    3 AA9 4 PHE C 241  PRO C 250 -1  O  ALA C 245   N  CYS C 203           
SHEET    4 AA9 4 GLU C 229  LEU C 230 -1  N  GLU C 229   O  ALA C 246           
SHEET    1 AB1 4 LYS C 186  PRO C 193  0                                        
SHEET    2 AB1 4 GLU C 198  PHE C 208 -1  O  LEU C 206   N  LYS C 186           
SHEET    3 AB1 4 PHE C 241  PRO C 250 -1  O  ALA C 245   N  CYS C 203           
SHEET    4 AB1 4 ARG C 234  PRO C 235 -1  N  ARG C 234   O  GLN C 242           
SHEET    1 AB2 4 GLU C 222  ASP C 223  0                                        
SHEET    2 AB2 4 THR C 214  ARG C 219 -1  N  ARG C 219   O  GLU C 222           
SHEET    3 AB2 4 TYR C 257  GLN C 262 -1  O  HIS C 260   N  THR C 216           
SHEET    4 AB2 4 LEU C 270  LEU C 272 -1  O  LEU C 272   N  CYS C 259           
SHEET    1 AB3 4 LYS D   6  SER D  11  0                                        
SHEET    2 AB3 4 ASN D  21  PHE D  30 -1  O  ASN D  24   N  TYR D  10           
SHEET    3 AB3 4 PHE D  62  PHE D  70 -1  O  TYR D  66   N  CYS D  25           
SHEET    4 AB3 4 GLU D  50  HIS D  51 -1  N  GLU D  50   O  TYR D  67           
SHEET    1 AB4 4 LYS D   6  SER D  11  0                                        
SHEET    2 AB4 4 ASN D  21  PHE D  30 -1  O  ASN D  24   N  TYR D  10           
SHEET    3 AB4 4 PHE D  62  PHE D  70 -1  O  TYR D  66   N  CYS D  25           
SHEET    4 AB4 4 SER D  55  PHE D  56 -1  N  SER D  55   O  TYR D  63           
SHEET    1 AB5 4 GLU D  44  ARG D  45  0                                        
SHEET    2 AB5 4 GLU D  36  LYS D  41 -1  N  LYS D  41   O  GLU D  44           
SHEET    3 AB5 4 TYR D  78  ASN D  83 -1  O  ARG D  81   N  ASP D  38           
SHEET    4 AB5 4 LYS D  91  LYS D  94 -1  O  LYS D  91   N  VAL D  82           
SSBOND   1 CYS A  101    CYS A  164                          1555   1555  2.05  
SSBOND   2 CYS A  203    CYS A  259                          1555   1555  2.02  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.03  
SSBOND   4 CYS C  101    CYS C  164                          1555   1555  2.06  
SSBOND   5 CYS C  203    CYS C  259                          1555   1555  2.03  
SSBOND   6 CYS D   25    CYS D   80                          1555   1555  2.05  
CISPEP   1 GLY A    1    SER A    2          0        -1.69                     
CISPEP   2 TYR A  209    PRO A  210          0         0.23                     
CISPEP   3 HIS B   31    PRO B   32          0         1.83                     
CISPEP   4 TYR C  209    PRO C  210          0        -1.54                     
CISPEP   5 HIS D   31    PRO D   32          0        -3.09                     
CRYST1   69.396   84.262   77.945  90.00 104.00  90.00 P 1 21 1      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      0.014410  0.000000  0.003593        0.00000                         
SCALE2      0.000000  0.011868  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013222        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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