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Database: PDB
Entry: 3WLB
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Original site: 3WLB 
HEADER    IMMUNE SYSTEM                           08-NOV-13   3WLB              
TITLE     HLA-A24 IN COMPLEX WITH HIV-1 NEF126-10(8T10F)                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-24 ALPHA CHAIN;  
COMPND   3 CHAIN: A;                                                            
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;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 21-119;                                       
COMPND  12 SYNONYM: BETA-2-MICROGLOBULIN FORM PI 5.3;                           
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: PROTEIN NEF;                                               
COMPND  16 CHAIN: C;                                                            
COMPND  17 FRAGMENT: UNP RESIDUES 126-135;                                      
COMPND  18 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-A, HLAA;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21D(+);                                
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: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET21A(+);                                
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 SYNTHETIC: YES;                                                      
SOURCE  23 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE  24 ORGANISM_TAXID: 11676;                                               
SOURCE  25 OTHER_DETAILS: SYNTHETIC PEPTIDE                                     
KEYWDS    HIV-1, NEF, HLA-A24, MHC CLASS I, IMMUNOGLOBURIN DOMAIN, IMMUNE       
KEYWDS   2 RESPONSE, IMMUNE SYSTEM, TCR, T CELL RECEPTOR                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.SHIMIZU,S.FUKAI,A.YAMAGATA,A.IWAMOTO,C.HAN                          
REVDAT   2   22-NOV-17 3WLB    1       REMARK                                   
REVDAT   1   11-JUN-14 3WLB    0                                                
JRNL        AUTH   C.HAN,A.KAWANA-TACHIKAWA,A.SHIMIZU,D.ZHU,H.NAKAMURA,         
JRNL        AUTH 2 E.ADACHI,T.KIKUCHI,M.KOGA,T.KOIBUCHI,G.F.GAO,Y.SATO,         
JRNL        AUTH 3 A.YAMAGATA,E.MARTIN,S.FUKAI,Z.L.BRUMME,A.IWAMOTO             
JRNL        TITL   SWITCHING AND EMERGENCE OF CTL EPITOPES IN HIV-1 INFECTION   
JRNL        REF    RETROVIROLOGY                 V.  11    38 2014              
JRNL        REFN                   ESSN 1742-4690                               
JRNL        PMID   24886641                                                     
JRNL        DOI    10.1186/1742-4690-11-38                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 29606                          
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) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1559                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1990                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 107                          
REMARK   3   BIN FREE R VALUE                    : 0.2720                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3138                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 279                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.66                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.84000                                              
REMARK   3    B22 (A**2) : -0.18000                                             
REMARK   3    B33 (A**2) : -0.67000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.170         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.112         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.884         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3227 ; 0.008 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4376 ; 1.205 ; 1.932       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   381 ; 5.931 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   174 ;32.187 ;23.276       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   528 ;16.259 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;21.693 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   442 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2553 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  3227 ; 5.284 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    78 ;19.616 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  3339 ; 8.536 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   274                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.6735   6.2760   4.4118              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0054 T22:   0.0169                                     
REMARK   3      T33:   0.0082 T12:   0.0015                                     
REMARK   3      T13:   0.0027 T23:  -0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0920 L22:   0.2045                                     
REMARK   3      L33:   0.0879 L12:   0.1326                                     
REMARK   3      L13:   0.0274 L23:   0.0077                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0122 S12:  -0.0108 S13:   0.0054                       
REMARK   3      S21:   0.0124 S22:  -0.0177 S23:   0.0046                       
REMARK   3      S31:   0.0172 S32:  -0.0054 S33:   0.0055                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     0        B    99                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.3934  17.6538 -10.7264              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0141 T22:   0.0217                                     
REMARK   3      T33:   0.0035 T12:  -0.0142                                     
REMARK   3      T13:   0.0032 T23:  -0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2823 L22:   0.3912                                     
REMARK   3      L33:   0.3570 L12:   0.2358                                     
REMARK   3      L13:  -0.0277 L23:   0.0056                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0256 S12:   0.0055 S13:   0.0058                       
REMARK   3      S21:  -0.0204 S22:   0.0366 S23:   0.0259                       
REMARK   3      S31:  -0.0354 S32:   0.0500 S33:  -0.0110                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 3WLB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-NOV-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000096478.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31585                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31800                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: 3I6L                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%(W/V) PEG3350, 200 MM SODIUM          
REMARK 280  PHOSPHATE DIBASIC, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE       
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       33.54200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.54850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.86250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       43.54850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.54200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.86250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS B  80   CA  -  CB  -  SG  ANGL. DEV. =   8.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  29     -122.49     46.68                                   
REMARK 500    HIS A 114       98.84   -166.72                                   
REMARK 500    ASP A 227       24.83     81.14                                   
REMARK 500    LYS B  48       51.40    -94.51                                   
REMARK 500    TRP B  60       -1.88     77.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3WL9   RELATED DB: PDB                                   
DBREF  3WLB A    1   274  UNP    P05534   1A24_HUMAN      25    298             
DBREF  3WLB B    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  3WLB C    1    10  UNP    Q9WPV9   Q9WPV9_9HIV1   126    135             
SEQADV 3WLB MET A    0  UNP  P05534              EXPRESSION TAG                 
SEQADV 3WLB MET B    0  UNP  P61769              EXPRESSION TAG                 
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  ASN TYR THR PRO GLY PRO GLY THR ARG PHE                      
FORMUL   4  HOH   *279(H2 O)                                                    
HELIX    1   1 ALA A   49  GLU A   53  5                                   5    
HELIX    2   2 GLY A   56  ASN A   86  1                                  31    
HELIX    3   3 ASP A  137  ALA A  150  1                                  14    
HELIX    4   4 HIS A  151  GLY A  162  1                                  12    
HELIX    5   5 GLY A  162  GLY A  175  1                                  14    
HELIX    6   6 GLY A  175  GLN A  180  1                                   6    
HELIX    7   7 GLU A  253  GLN A  255  5                                   3    
SHEET    1   A 8 GLU A  46  PRO A  47  0                                        
SHEET    2   A 8 THR A  31  ASP A  37 -1  N  ARG A  35   O  GLU A  46           
SHEET    3   A 8 ARG A  21  VAL A  28 -1  N  GLY A  26   O  PHE A  33           
SHEET    4   A 8 HIS A   3  VAL A  12 -1  N  THR A  10   O  ILE A  23           
SHEET    5   A 8 THR A  94  VAL A 103 -1  O  LEU A  95   N  SER A  11           
SHEET    6   A 8 PHE A 109  TYR A 118 -1  O  LEU A 110   N  ASP A 102           
SHEET    7   A 8 LYS A 121  LEU A 126 -1  O  ILE A 124   N  TYR A 116           
SHEET    8   A 8 TRP A 133  ALA A 135 -1  O  THR A 134   N  ALA A 125           
SHEET    1   B 4 LYS A 186  PRO A 193  0                                        
SHEET    2   B 4 GLU A 198  PHE A 208 -1  O  TRP A 204   N  HIS A 188           
SHEET    3   B 4 PHE A 241  PRO A 250 -1  O  VAL A 249   N  ALA A 199           
SHEET    4   B 4 THR A 228  LEU A 230 -1  N  GLU A 229   O  ALA A 246           
SHEET    1   C 4 LYS A 186  PRO A 193  0                                        
SHEET    2   C 4 GLU A 198  PHE A 208 -1  O  TRP A 204   N  HIS A 188           
SHEET    3   C 4 PHE A 241  PRO A 250 -1  O  VAL A 249   N  ALA A 199           
SHEET    4   C 4 ARG A 234  PRO A 235 -1  N  ARG A 234   O  GLN A 242           
SHEET    1   D 4 GLU A 222  GLN A 224  0                                        
SHEET    2   D 4 THR A 214  ARG A 219 -1  N  ARG A 219   O  GLU A 222           
SHEET    3   D 4 TYR A 257  GLN A 262 -1  O  HIS A 260   N  THR A 216           
SHEET    4   D 4 LEU A 270  ARG A 273 -1  O  LEU A 272   N  CYS A 259           
SHEET    1   E 4 LYS B   6  SER B  11  0                                        
SHEET    2   E 4 ASN B  21  PHE B  30 -1  O  ASN B  24   N  TYR B  10           
SHEET    3   E 4 PHE B  62  PHE B  70 -1  O  THR B  68   N  LEU B  23           
SHEET    4   E 4 GLU B  50  HIS B  51 -1  N  GLU B  50   O  TYR B  67           
SHEET    1   F 4 LYS B   6  SER B  11  0                                        
SHEET    2   F 4 ASN B  21  PHE B  30 -1  O  ASN B  24   N  TYR B  10           
SHEET    3   F 4 PHE B  62  PHE B  70 -1  O  THR B  68   N  LEU B  23           
SHEET    4   F 4 SER B  55  PHE B  56 -1  N  SER B  55   O  TYR B  63           
SHEET    1   G 4 GLU B  44  ARG B  45  0                                        
SHEET    2   G 4 ILE B  35  LYS B  41 -1  N  LYS B  41   O  GLU B  44           
SHEET    3   G 4 TYR B  78  HIS B  84 -1  O  ALA B  79   N  LEU B  40           
SHEET    4   G 4 LYS B  91  LYS B  94 -1  O  LYS B  91   N  VAL B  82           
SSBOND   1 CYS A  164    CYS A  101                          1555   1555  2.08  
SSBOND   2 CYS A  259    CYS A  203                          1555   1555  2.04  
SSBOND   3 CYS B   80    CYS B   25                          1555   1555  2.13  
CISPEP   1 TYR A  209    PRO A  210          0        -0.68                     
CISPEP   2 HIS B   31    PRO B   32          0         0.84                     
CISPEP   3 GLY C    5    PRO C    6          0        -0.78                     
CRYST1   67.084   77.725   87.097  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014907  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012866  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011481        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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