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Database: PDB
Entry: 5HGD
LinkDB: 5HGD
Original site: 5HGD 
HEADER    IMMUNE SYSTEM                           08-JAN-16   5HGD              
TITLE     HLA*A2402 COMPLEXED WITH HIV NEF138 Y2F MUTANT 10MER EPITOPE          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-24 ALPHA CHAIN;  
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 25-298;                                       
COMPND   5 SYNONYM: AW-24,HLA CLASS I HISTOCOMPATIBILITY ANTIGEN,A-9 ALPHA      
COMPND   6 CHAIN,MHC CLASS I ANTIGEN A*24;                                      
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: BETA-2-MICROGLOBULIN;                                      
COMPND  10 CHAIN: B, E;                                                         
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: PROTEIN NEF;                                               
COMPND  14 CHAIN: C, F;                                                         
COMPND  15 FRAGMENT: UNP RESIDUES 135-144;                                      
COMPND  16 SYNONYM: 3'ORF,NEGATIVE FACTOR,F-PROTEIN;                            
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HLA-A, HLAA;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 866768;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: B2M, CDABP0092, HDCMA22P;                                      
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 866768;                                     
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1;            
SOURCE  18 ORGANISM_COMMON: HIV-1;                                              
SOURCE  19 ORGANISM_TAXID: 11676                                                
KEYWDS    HLA, ANTIGEN PRESENTATION, HIV, IMMUNE SYSTEM                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.SHI,J.QI,G.F.GAO                                                    
REVDAT   2   18-DEC-19 5HGD    1       JRNL   REMARK                            
REVDAT   1   08-JUN-16 5HGD    0                                                
JRNL        AUTH   X.SUN,Y.SHI,T.AKAHOSHI,M.FUJIWARA,H.GATANAGA,C.SCHONBACH,    
JRNL        AUTH 2 N.KUSE,V.APPAY,G.F.GAO,S.OKA,M.TAKIGUCHI                     
JRNL        TITL   EFFECTS OF A SINGLE ESCAPE MUTATION ON T CELL AND HIV-1      
JRNL        TITL 2 CO-ADAPTATION.                                               
JRNL        REF    CELL REP                      V.  15  2279 2016              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   27239036                                                     
JRNL        DOI    10.1016/J.CELREP.2016.05.017                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.07 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.5_2                                         
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.07                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.09                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.070                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 61282                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3092                            
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 20.0946 -  5.5633    0.95     2893   146  0.1812 0.1978        
REMARK   3     2  5.5633 -  4.4313    0.98     3010   165  0.1534 0.1865        
REMARK   3     3  4.4313 -  3.8757    0.90     2726   141  0.1477 0.1605        
REMARK   3     4  3.8757 -  3.5235    0.71     2150   129  0.1634 0.1674        
REMARK   3     5  3.5235 -  3.2721    0.94     2866   151  0.1780 0.2388        
REMARK   3     6  3.2721 -  3.0799    0.96     2983   147  0.1792 0.2160        
REMARK   3     7  3.0799 -  2.9261    0.95     2939   118  0.1920 0.2592        
REMARK   3     8  2.9261 -  2.7991    0.94     2814   166  0.1892 0.2316        
REMARK   3     9  2.7991 -  2.6916    0.93     2871   168  0.1873 0.2874        
REMARK   3    10  2.6916 -  2.5989    0.93     2850   149  0.1894 0.2512        
REMARK   3    11  2.5989 -  2.5178    0.92     2765   160  0.1983 0.2525        
REMARK   3    12  2.5178 -  2.4460    0.91     2815   130  0.1912 0.2682        
REMARK   3    13  2.4460 -  2.3817    0.90     2783   165  0.1955 0.2757        
REMARK   3    14  2.3817 -  2.3236    0.90     2708   136  0.1969 0.2181        
REMARK   3    15  2.3236 -  2.2709    0.82     2546   130  0.1976 0.2267        
REMARK   3    16  2.2709 -  2.2226    0.34     1050    58  0.2421 0.2855        
REMARK   3    17  2.2226 -  2.1782    0.83     2510   125  0.2011 0.2556        
REMARK   3    18  2.1782 -  2.1372    0.87     2663   143  0.1781 0.2322        
REMARK   3    19  2.1372 -  2.0990    0.87     2630   168  0.1887 0.2397        
REMARK   3    20  2.0990 -  2.0635    0.86     2613   124  0.2089 0.2728        
REMARK   3    21  2.0635 -  2.0302    0.82     2460   144  0.1984 0.2457        
REMARK   3    22  2.0302 -  1.9990    0.81     2545   129  0.1940 0.2357        
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              : 0.38                                          
REMARK   3   B_SOL              : 40.02                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.430           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.73780                                             
REMARK   3    B22 (A**2) : 5.59470                                              
REMARK   3    B33 (A**2) : -2.85690                                             
REMARK   3    B12 (A**2) : 0.99890                                              
REMARK   3    B13 (A**2) : -3.49330                                             
REMARK   3    B23 (A**2) : 0.78740                                              
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      :  0.004           6480                                  
REMARK   3   ANGLE     :  0.843           8772                                  
REMARK   3   CHIRALITY :  0.061            886                                  
REMARK   3   PLANARITY :  0.003           1154                                  
REMARK   3   DIHEDRAL  : 18.750           2350                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -24.9916 -15.7381 -40.6074              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1501 T22:   0.1619                                     
REMARK   3      T33:   0.1618 T12:  -0.0085                                     
REMARK   3      T13:   0.0062 T23:  -0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0635 L22:   0.1081                                     
REMARK   3      L33:   0.0860 L12:  -0.0690                                     
REMARK   3      L13:   0.0423 L23:  -0.0339                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0033 S12:   0.0088 S13:   0.0031                       
REMARK   3      S21:  -0.0044 S22:  -0.0044 S23:  -0.0014                       
REMARK   3      S31:   0.0077 S32:   0.0056 S33:  -0.0000                       
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 5HGD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000216991.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-APR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63675                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.070                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.9                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.9230                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.358                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 2BCK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES MONOHYDRATE PH 6.5, 12% W/V    
REMARK 280  POLYETHYLENE GLYCOL 20000, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: 19320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     MET D     0                                                      
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 A  29     -122.41     54.01                                   
REMARK 500    HIS A 114      105.61   -163.72                                   
REMARK 500    TYR A 123      -70.60   -109.59                                   
REMARK 500    SER A 195     -164.07   -160.26                                   
REMARK 500    GLN A 224       43.52    -98.66                                   
REMARK 500    TRP B  60       -9.37     82.33                                   
REMARK 500    ASP B  98       33.34    -90.83                                   
REMARK 500    TRP C   8       47.68    -84.07                                   
REMARK 500    ASP D  29     -125.93     50.56                                   
REMARK 500    LEU D 110      -50.74   -120.56                                   
REMARK 500    HIS D 114      107.08   -161.78                                   
REMARK 500    ASP D 122      130.55    -37.22                                   
REMARK 500    TYR D 123      -71.26   -109.84                                   
REMARK 500    SER D 195     -164.22   -165.13                                   
REMARK 500    GLN D 224       38.93    -99.00                                   
REMARK 500    TRP E  60      -11.50     78.71                                   
REMARK 500    ASP E  98       39.81    -91.49                                   
REMARK 500    TRP F   8       46.32    -85.55                                   
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 A 551        DISTANCE =  6.14 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5HGA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HGB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HGH   RELATED DB: PDB                                   
DBREF  5HGD A    1   274  UNP    P05534   1A24_HUMAN      25    298             
DBREF  5HGD B    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  5HGD C    1    10  UNP    P18801   NEF_HV1ND      135    144             
DBREF  5HGD D    1   274  UNP    P05534   1A24_HUMAN      25    298             
DBREF  5HGD E    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  5HGD F    1    10  UNP    P18801   NEF_HV1ND      135    144             
SEQADV 5HGD MET A    0  UNP  P05534              INITIATING METHIONINE          
SEQADV 5HGD MET B    0  UNP  P61769              INITIATING METHIONINE          
SEQADV 5HGD PHE C    2  UNP  P18801    TYR   136 ENGINEERED MUTATION            
SEQADV 5HGD MET D    0  UNP  P05534              INITIATING METHIONINE          
SEQADV 5HGD MET E    0  UNP  P61769              INITIATING METHIONINE          
SEQADV 5HGD PHE F    2  UNP  P18801    TYR   136 ENGINEERED MUTATION            
SEQRES   1 A  275  MET GLY SER HIS SER MET ARG TYR PHE SER THR SER VAL          
SEQRES   2 A  275  SER ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL          
SEQRES   3 A  275  GLY TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER          
SEQRES   4 A  275  ASP ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP          
SEQRES   5 A  275  ILE GLU GLN GLU GLY PRO GLU TYR TRP ASP GLU GLU THR          
SEQRES   6 A  275  GLY LYS VAL LYS ALA HIS SER GLN THR ASP ARG GLU ASN          
SEQRES   7 A  275  LEU ARG ILE ALA LEU ARG TYR TYR ASN GLN SER GLU ALA          
SEQRES   8 A  275  GLY SER HIS THR LEU GLN MET MET PHE GLY CYS ASP VAL          
SEQRES   9 A  275  GLY SER ASP GLY ARG PHE LEU ARG GLY TYR HIS GLN TYR          
SEQRES  10 A  275  ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP          
SEQRES  11 A  275  LEU ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN ILE          
SEQRES  12 A  275  THR LYS ARG LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN          
SEQRES  13 A  275  GLN ARG ALA TYR LEU GLU GLY THR CYS VAL ASP GLY LEU          
SEQRES  14 A  275  ARG ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG          
SEQRES  15 A  275  THR ASP PRO PRO LYS THR HIS MET THR HIS HIS PRO ILE          
SEQRES  16 A  275  SER ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY          
SEQRES  17 A  275  PHE TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP          
SEQRES  18 A  275  GLY GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR          
SEQRES  19 A  275  ARG PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA          
SEQRES  20 A  275  VAL VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS          
SEQRES  21 A  275  HIS VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU          
SEQRES  22 A  275  ARG TRP                                                      
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   10  ARG PHE PRO LEU THR PHE GLY TRP CYS PHE                      
SEQRES   1 D  275  MET GLY SER HIS SER MET ARG TYR PHE SER THR SER VAL          
SEQRES   2 D  275  SER ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL          
SEQRES   3 D  275  GLY TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER          
SEQRES   4 D  275  ASP ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP          
SEQRES   5 D  275  ILE GLU GLN GLU GLY PRO GLU TYR TRP ASP GLU GLU THR          
SEQRES   6 D  275  GLY LYS VAL LYS ALA HIS SER GLN THR ASP ARG GLU ASN          
SEQRES   7 D  275  LEU ARG ILE ALA LEU ARG TYR TYR ASN GLN SER GLU ALA          
SEQRES   8 D  275  GLY SER HIS THR LEU GLN MET MET PHE GLY CYS ASP VAL          
SEQRES   9 D  275  GLY SER ASP GLY ARG PHE LEU ARG GLY TYR HIS GLN TYR          
SEQRES  10 D  275  ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP          
SEQRES  11 D  275  LEU ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN ILE          
SEQRES  12 D  275  THR LYS ARG LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN          
SEQRES  13 D  275  GLN ARG ALA TYR LEU GLU GLY THR CYS VAL ASP GLY LEU          
SEQRES  14 D  275  ARG ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG          
SEQRES  15 D  275  THR ASP PRO PRO LYS THR HIS MET THR HIS HIS PRO ILE          
SEQRES  16 D  275  SER ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY          
SEQRES  17 D  275  PHE TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP          
SEQRES  18 D  275  GLY GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR          
SEQRES  19 D  275  ARG PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA          
SEQRES  20 D  275  VAL VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS          
SEQRES  21 D  275  HIS VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU          
SEQRES  22 D  275  ARG TRP                                                      
SEQRES   1 E  100  MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG          
SEQRES   2 E  100  HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS          
SEQRES   3 E  100  TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP          
SEQRES   4 E  100  LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS          
SEQRES   5 E  100  SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU          
SEQRES   6 E  100  LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU          
SEQRES   7 E  100  TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO          
SEQRES   8 E  100  LYS ILE VAL LYS TRP ASP ARG ASP MET                          
SEQRES   1 F   10  ARG PHE PRO LEU THR PHE GLY TRP CYS PHE                      
FORMUL   7  HOH   *761(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 HIS A  151  GLY A  162  1                                  12    
HELIX    5 AA5 GLY A  162  GLY A  175  1                                  14    
HELIX    6 AA6 GLY A  175  GLN 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 ALA D   49  GLU D   53  5                                   5    
HELIX   10 AB1 GLY D   56  ASN D   86  1                                  31    
HELIX   11 AB2 ASP D  137  ALA D  150  1                                  14    
HELIX   12 AB3 HIS D  151  GLY D  162  1                                  12    
HELIX   13 AB4 GLY D  162  GLY D  175  1                                  14    
HELIX   14 AB5 GLY D  175  GLN D  180  1                                   6    
HELIX   15 AB6 GLU D  253  GLN D  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  ALA A  24   O  PHE A  36           
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  PHE A  99   N  TYR A   7           
SHEET    6 AA1 8 PHE A 109  TYR A 118 -1  O  ARG A 111   N  ASP A 102           
SHEET    7 AA1 8 LYS A 121  LEU A 126 -1  O  ILE A 124   N  TYR A 116           
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  THR A 200   N  HIS A 192           
SHEET    3 AA2 4 PHE A 241  PRO A 250 -1  O  ALA A 245   N  CYS A 203           
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  THR A 200   N  HIS A 192           
SHEET    3 AA3 4 PHE A 241  PRO A 250 -1  O  ALA A 245   N  CYS A 203           
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  HIS A 260   N  THR A 216           
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  THR B  68   N  LEU B  23           
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  THR B  68   N  LEU B  23           
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  ASN B  83   N  GLU B  36           
SHEET    4 AA7 4 LYS B  91  LYS B  94 -1  O  LYS B  91   N  VAL B  82           
SHEET    1 AA8 8 GLU D  46  PRO D  47  0                                        
SHEET    2 AA8 8 THR D  31  ASP D  37 -1  N  ARG D  35   O  GLU D  46           
SHEET    3 AA8 8 ARG D  21  VAL D  28 -1  N  ALA D  24   O  PHE D  36           
SHEET    4 AA8 8 HIS D   3  VAL D  12 -1  N  PHE D   8   O  VAL D  25           
SHEET    5 AA8 8 THR D  94  VAL D 103 -1  O  PHE D  99   N  TYR D   7           
SHEET    6 AA8 8 PHE D 109  TYR D 118 -1  O  ALA D 117   N  GLN D  96           
SHEET    7 AA8 8 LYS D 121  LEU D 126 -1  O  ILE D 124   N  TYR D 116           
SHEET    8 AA8 8 TRP D 133  ALA D 135 -1  O  THR D 134   N  ALA D 125           
SHEET    1 AA9 4 LYS D 186  PRO D 193  0                                        
SHEET    2 AA9 4 GLU D 198  PHE D 208 -1  O  THR D 200   N  HIS D 192           
SHEET    3 AA9 4 PHE D 241  PRO D 250 -1  O  ALA D 245   N  CYS D 203           
SHEET    4 AA9 4 THR D 228  LEU D 230 -1  N  GLU D 229   O  ALA D 246           
SHEET    1 AB1 4 LYS D 186  PRO D 193  0                                        
SHEET    2 AB1 4 GLU D 198  PHE D 208 -1  O  THR D 200   N  HIS D 192           
SHEET    3 AB1 4 PHE D 241  PRO D 250 -1  O  ALA D 245   N  CYS D 203           
SHEET    4 AB1 4 ARG D 234  PRO D 235 -1  N  ARG D 234   O  GLN D 242           
SHEET    1 AB2 4 GLU D 222  ASP D 223  0                                        
SHEET    2 AB2 4 THR D 214  ARG D 219 -1  N  ARG D 219   O  GLU D 222           
SHEET    3 AB2 4 TYR D 257  GLN D 262 -1  O  HIS D 260   N  THR D 216           
SHEET    4 AB2 4 LEU D 270  LEU D 272 -1  O  LEU D 272   N  CYS D 259           
SHEET    1 AB3 4 LYS E   6  SER E  11  0                                        
SHEET    2 AB3 4 ASN E  21  PHE E  30 -1  O  ASN E  24   N  TYR E  10           
SHEET    3 AB3 4 PHE E  62  PHE E  70 -1  O  TYR E  66   N  CYS E  25           
SHEET    4 AB3 4 GLU E  50  HIS E  51 -1  N  GLU E  50   O  TYR E  67           
SHEET    1 AB4 4 LYS E   6  SER E  11  0                                        
SHEET    2 AB4 4 ASN E  21  PHE E  30 -1  O  ASN E  24   N  TYR E  10           
SHEET    3 AB4 4 PHE E  62  PHE E  70 -1  O  TYR E  66   N  CYS E  25           
SHEET    4 AB4 4 SER E  55  PHE E  56 -1  N  SER E  55   O  TYR E  63           
SHEET    1 AB5 4 GLU E  44  ARG E  45  0                                        
SHEET    2 AB5 4 GLU E  36  LYS E  41 -1  N  LYS E  41   O  GLU E  44           
SHEET    3 AB5 4 TYR E  78  ASN E  83 -1  O  ALA E  79   N  LEU E  40           
SHEET    4 AB5 4 LYS E  91  LYS E  94 -1  O  LYS E  91   N  VAL E  82           
SSBOND   1 CYS A  101    CYS A  164                          1555   1555  2.06  
SSBOND   2 CYS A  203    CYS A  259                          1555   1555  2.03  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.03  
SSBOND   4 CYS D  101    CYS D  164                          1555   1555  2.06  
SSBOND   5 CYS D  203    CYS D  259                          1555   1555  2.04  
SSBOND   6 CYS E   25    CYS E   80                          1555   1555  2.04  
CISPEP   1 TYR A  209    PRO A  210          0         3.09                     
CISPEP   2 HIS B   31    PRO B   32          0         0.70                     
CISPEP   3 TYR D  209    PRO D  210          0         3.20                     
CISPEP   4 HIS E   31    PRO E   32          0         1.46                     
CRYST1   50.655   65.741   87.519  67.97  89.80  89.89 P 1           2          
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      0.019741 -0.000039 -0.000058        0.00000                         
SCALE2      0.000000  0.015211 -0.006155        0.00000                         
SCALE3      0.000000  0.000000  0.012326        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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