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Entry: 2GIT
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HEADER    IMMUNE SYSTEM                           29-MAR-06   2GIT              
TITLE     HUMAN CLASS I MHC HLA-A2 IN COMPLEX WITH THE MODIFIED HTLV-1 TAX (Y5K-
TITLE    2 4-[3-INDOLYL]-BUTYRIC ACID) PEPTIDE                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN;   
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 FRAGMENT: HUMAN CLASS I MAJOR HISTOCOMPATIBILITY COMPLEX HEAVY CHAIN;
COMPND   5 SYNONYM: MHC CLASS I ANTIGEN A*2;                                    
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: BETA-2-MICROGLOBULIN;                                      
COMPND   9 CHAIN: B, E;                                                         
COMPND  10 FRAGMENT: BETA-2-MICROGLOBULIN;                                      
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: TRANSCRIPTIONAL ACTIVATOR TAX;                             
COMPND  14 CHAIN: C, F;                                                         
COMPND  15 FRAGMENT: HTLV-1 TAX PEPTIDE;                                        
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 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;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHN1;                                     
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;                                                           
SOURCE  16 MOL_ID: 3;                                                           
SOURCE  17 SYNTHETIC: YES;                                                      
SOURCE  18 OTHER_DETAILS: COMMERCIAL SYNTHESIS FOR THE PEPTIDE                  
KEYWDS    HTLV-1 TAX PEPTIDE, HAPTENATED PEPTIDE, LYSINE-4-(3-INDOLYL)-BUTYRIC  
KEYWDS   2 ACID, MHC CLASS I, HLA-A2, IMMUNE SYSTEM                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.Y.BORBULEVYCH,B.M.BAKER                                             
REVDAT   4   30-AUG-23 2GIT    1       REMARK SEQADV LINK                       
REVDAT   3   13-JUL-11 2GIT    1       VERSN                                    
REVDAT   2   24-FEB-09 2GIT    1       VERSN                                    
REVDAT   1   03-OCT-06 2GIT    0                                                
JRNL        AUTH   S.J.GAGNON,O.Y.BORBULEVYCH,R.L.DAVIS-HARRISON,R.V.TURNER,    
JRNL        AUTH 2 M.DAMIRJIAN,A.WOJNAROWICZ,W.E.BIDDISON,B.M.BAKER             
JRNL        TITL   T CELL RECEPTOR RECOGNITION VIA COOPERATIVE CONFORMATIONAL   
JRNL        TITL 2 PLASTICITY.                                                  
JRNL        REF    J.MOL.BIOL.                   V. 363   228 2006              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   16962135                                                     
JRNL        DOI    10.1016/J.JMB.2006.08.045                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 82640                          
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; 5% OF THE DATA SET      
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4395                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4214                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 62.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 215                          
REMARK   3   BIN FREE R VALUE                    : 0.2800                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6313                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 64                                      
REMARK   3   SOLVENT ATOMS            : 788                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 18.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.51                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.93000                                              
REMARK   3    B22 (A**2) : -1.11000                                             
REMARK   3    B33 (A**2) : -1.46000                                             
REMARK   3    B12 (A**2) : 0.47000                                              
REMARK   3    B13 (A**2) : 0.66000                                              
REMARK   3    B23 (A**2) : 0.47000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.117         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.115         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.081         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.822         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6579 ; 0.016 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8906 ; 1.729 ; 1.929       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   762 ; 6.356 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   351 ;31.237 ;23.105       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1069 ;14.733 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    57 ;19.120 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   907 ; 0.142 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5133 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2800 ; 0.155 ; 0.080       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4400 ; 0.311 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1133 ; 0.205 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.123 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    41 ; 0.109 ; 0.080       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    52 ; 0.181 ; 0.500       
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):  3852 ; 0.947 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6196 ; 1.664 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2880 ; 2.771 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2710 ; 4.333 ; 4.500       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    183       A     275      4                      
REMARK   3           1     D    183       D     275      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    749 ;  0.26 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    749 ;  1.17 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B E                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      0       B      99      4                      
REMARK   3           1     E      0       E      99      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    B    (A):    831 ;  0.27 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    B (A**2):    831 ;  0.92 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   182                          
REMARK   3    RESIDUE RANGE :   C     1        C     9                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.6378  14.0647   6.8388              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0900 T22:  -0.0677                                     
REMARK   3      T33:  -0.0548 T12:   0.0012                                     
REMARK   3      T13:  -0.0034 T23:  -0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0881 L22:   1.4963                                     
REMARK   3      L33:   2.2172 L12:   0.1291                                     
REMARK   3      L13:   0.0414 L23:  -0.3048                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0446 S12:  -0.0265 S13:   0.1421                       
REMARK   3      S21:   0.0548 S22:  -0.0073 S23:   0.0141                       
REMARK   3      S31:  -0.1543 S32:   0.0444 S33:   0.0519                       
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 :   A   183        A   275                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5994 -19.4809  -6.4668              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0402 T22:  -0.0580                                     
REMARK   3      T33:  -0.0832 T12:  -0.0011                                     
REMARK   3      T13:  -0.0013 T23:  -0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5189 L22:   3.5636                                     
REMARK   3      L33:   2.6527 L12:  -1.3713                                     
REMARK   3      L13:  -1.1394 L23:   1.6638                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0358 S12:   0.1195 S13:  -0.0911                       
REMARK   3      S21:  -0.2482 S22:  -0.0098 S23:   0.0199                       
REMARK   3      S31:   0.1838 S32:   0.0587 S33:  -0.0261                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
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): -10.9662  -4.9426  -7.0060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1060 T22:  -0.0467                                     
REMARK   3      T33:  -0.0486 T12:  -0.0005                                     
REMARK   3      T13:   0.0050 T23:   0.0165                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6738 L22:   3.5846                                     
REMARK   3      L33:   1.4110 L12:   1.4780                                     
REMARK   3      L13:  -0.2258 L23:  -0.4646                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0406 S12:   0.0893 S13:   0.0130                       
REMARK   3      S21:  -0.2047 S22:   0.0789 S23:   0.2733                       
REMARK   3      S31:   0.0888 S32:  -0.1006 S33:  -0.0384                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   182                          
REMARK   3    RESIDUE RANGE :   F     1        F     9                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.9421 -13.2305  26.1622              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0673 T22:  -0.0462                                     
REMARK   3      T33:  -0.0576 T12:  -0.0091                                     
REMARK   3      T13:   0.0105 T23:   0.0166                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9011 L22:   2.0574                                     
REMARK   3      L33:   1.8147 L12:  -0.2371                                     
REMARK   3      L13:   0.0059 L23:   0.4390                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0670 S12:   0.0235 S13:   0.0969                       
REMARK   3      S21:   0.0183 S22:   0.0262 S23:  -0.0990                       
REMARK   3      S31:  -0.1779 S32:   0.0531 S33:   0.0408                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   183        D   275                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.9766 -42.3493  39.1365              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1604 T22:  -0.0570                                     
REMARK   3      T33:  -0.0639 T12:   0.0001                                     
REMARK   3      T13:   0.0116 T23:   0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7964 L22:   2.1628                                     
REMARK   3      L33:   3.0960 L12:   1.2878                                     
REMARK   3      L13:  -2.6481 L23:  -0.8013                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0594 S12:   0.0427 S13:  -0.1154                       
REMARK   3      S21:  -0.0321 S22:  -0.0619 S23:  -0.0271                       
REMARK   3      S31:   0.0485 S32:  -0.1633 S33:   0.0025                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     0        E    99                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7344 -36.1067  39.7756              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1745 T22:  -0.0491                                     
REMARK   3      T33:  -0.0730 T12:  -0.0116                                     
REMARK   3      T13:   0.0297 T23:  -0.0152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8367 L22:   3.9438                                     
REMARK   3      L33:   2.0501 L12:  -0.4249                                     
REMARK   3      L13:   0.2631 L23:   0.1678                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0045 S12:  -0.0262 S13:  -0.0614                       
REMARK   3      S21:   0.1151 S22:   0.0211 S23:  -0.1510                       
REMARK   3      S31:   0.0893 S32:  -0.0209 S33:  -0.0166                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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: THE SIDE CHAIN OF LYI (RES 5 CHAIN C,F)   
REMARK   3  IS DISORDERED AND WAS NOT MODELED.                                  
REMARK   4                                                                      
REMARK   4 2GIT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000037171.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-NOV-05                          
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               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : BLU-ICE (GM/CA)                    
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 87035                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.8                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 66.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.130                              
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: PDB ENTRY 2AV1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350 24%, MES 0.025M, HCOOH 0.1M,     
REMARK 280  PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K             
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: 5670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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: 6300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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 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     LYS C   5    CE   NZ                                             
REMARK 470     LYS F   5    NZ                                                  
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    VAL E  85   CB  -  CA  -  C   ANGL. DEV. = -13.5 DEGREES          
REMARK 500    VAL E  85   CG1 -  CB  -  CG2 ANGL. DEV. =  11.2 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     -127.54     49.96                                   
REMARK 500    SER A 195     -153.68   -138.92                                   
REMARK 500    TRP B  60       -6.52     79.86                                   
REMARK 500    ARG B  97       53.32    -67.50                                   
REMARK 500    ASP B  98        2.28   -168.27                                   
REMARK 500    ASP D  29     -126.50     51.28                                   
REMARK 500    HIS D 114      105.31   -160.22                                   
REMARK 500    TRP E  60       -4.09     77.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 3-INDOLYL-BUTYRIC ACID (LIGAND CODE 3IB)                             
REMARK 600 IS COVALENTLY BONDED TO LYS 5 IN CHAIN C                             
REMARK 600 AND F. COORDINATES WERE NOT INCLUDED                                 
REMARK 600 BECAUSE THE LIGAND WAS DISORDERED.                                   
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 816  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B  83   OD1                                                    
REMARK 620 2 HIS B  84   O    75.3                                              
REMARK 620 3 LEU B  87   O    88.2  80.0                                        
REMARK 620 4 HOH B 882   O   174.9  99.9  89.2                                  
REMARK 620 5 HOH B 904   O    92.4 167.0 104.3  92.6                            
REMARK 620 6 HOH B 923   O    82.2  76.5 156.2  98.6  97.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 816                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT E 807                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 808                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 809                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 810                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT E 811                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 812                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 813                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 814                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 815                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DUZ   RELATED DB: PDB                                   
REMARK 900 HTLV-1 TAX PEPTIDE BOUND TO HLA-A2                                   
REMARK 900 RELATED ID: 2AV1   RELATED DB: PDB                                   
REMARK 900 HTLV-1 TAX PEPTIDE BOUND TO HLA-A2 (E63Q,K66A)                       
REMARK 900 RELATED ID: 2AV7   RELATED DB: PDB                                   
REMARK 900 HTLV-1 TAX PEPTIDE BOUND TO HLA-A2 (K66A)                            
DBREF  2GIT A    1   275  UNP    Q9TQH5   1A02_HUMAN      25    299             
DBREF  2GIT D    1   275  UNP    Q9TQH5   1A02_HUMAN      25    299             
DBREF  2GIT B    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  2GIT E    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  2GIT C    1     9  PDB    2GIT     2GIT             1      9             
DBREF  2GIT F    1     9  PDB    2GIT     2GIT             1      9             
SEQADV 2GIT MET B    0  UNP  P61769              INITIATING METHIONINE          
SEQADV 2GIT MET E    0  UNP  P61769              INITIATING METHIONINE          
SEQRES   1 A  275  GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER          
SEQRES   2 A  275  ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY          
SEQRES   3 A  275  TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP          
SEQRES   4 A  275  ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE          
SEQRES   5 A  275  GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG          
SEQRES   6 A  275  LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU          
SEQRES   7 A  275  GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY          
SEQRES   8 A  275  SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 A  275  SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA          
SEQRES  10 A  275  TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU          
SEQRES  11 A  275  ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR          
SEQRES  12 A  275  LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN LEU          
SEQRES  13 A  275  ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG          
SEQRES  14 A  275  ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR          
SEQRES  15 A  275  ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER          
SEQRES  16 A  275  ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER PHE          
SEQRES  17 A  275  TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY          
SEQRES  18 A  275  GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG          
SEQRES  19 A  275  PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL          
SEQRES  20 A  275  VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS HIS          
SEQRES  21 A  275  VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG          
SEQRES  22 A  275  TRP GLU                                                      
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    9  LEU LEU PHE GLY LYS PRO VAL TYR VAL                          
SEQRES   1 D  275  GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER          
SEQRES   2 D  275  ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY          
SEQRES   3 D  275  TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP          
SEQRES   4 D  275  ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE          
SEQRES   5 D  275  GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG          
SEQRES   6 D  275  LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU          
SEQRES   7 D  275  GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY          
SEQRES   8 D  275  SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 D  275  SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA          
SEQRES  10 D  275  TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU          
SEQRES  11 D  275  ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR          
SEQRES  12 D  275  LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN LEU          
SEQRES  13 D  275  ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG          
SEQRES  14 D  275  ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR          
SEQRES  15 D  275  ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER          
SEQRES  16 D  275  ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER PHE          
SEQRES  17 D  275  TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY          
SEQRES  18 D  275  GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG          
SEQRES  19 D  275  PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL          
SEQRES  20 D  275  VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS HIS          
SEQRES  21 D  275  VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG          
SEQRES  22 D  275  TRP GLU                                                      
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    9  LEU LEU PHE GLY LYS PRO VAL TYR VAL                          
HET    GOL  A 802       6                                                       
HET     NA  B 816       1                                                       
HET    GOL  B 803       6                                                       
HET    FMT  B 809       3                                                       
HET    FMT  B 810       3                                                       
HET    FMT  C 813       3                                                       
HET    GOL  D 804       6                                                       
HET    GOL  D 805       6                                                       
HET    GOL  D 806       6                                                       
HET    FMT  D 808       3                                                       
HET    FMT  D 812       3                                                       
HET    FMT  D 814       3                                                       
HET    FMT  D 815       3                                                       
HET    GOL  E 801       6                                                       
HET    FMT  E 807       3                                                       
HET    FMT  E 811       3                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM      NA SODIUM ION                                                       
HETNAM     FMT FORMIC ACID                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   7  GOL    6(C3 H8 O3)                                                  
FORMUL   8   NA    NA 1+                                                        
FORMUL  10  FMT    9(C H2 O2)                                                   
FORMUL  23  HOH   *788(H2 O)                                                    
HELIX    1   1 ALA A   49  GLU A   53  5                                   5    
HELIX    2   2 GLY A   56  TYR A   85  1                                  30    
HELIX    3   3 MET A  138  ALA A  150  1                                  13    
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 THR A  225  THR A  228  5                                   4    
HELIX    8   8 GLN A  253  GLN A  255  5                                   3    
HELIX    9   9 ALA D   49  GLU D   53  5                                   5    
HELIX   10  10 GLY D   56  TYR D   85  1                                  30    
HELIX   11  11 ASP D  137  ALA D  150  1                                  14    
HELIX   12  12 HIS D  151  GLY D  162  1                                  12    
HELIX   13  13 GLY D  162  GLY D  175  1                                  14    
HELIX   14  14 GLY D  175  GLN D  180  1                                   6    
HELIX   15  15 THR D  225  THR D  228  5                                   4    
HELIX   16  16 GLN D  253  GLN D  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  ARG A   6   O  TYR A  27           
SHEET    5   A 8 THR A  94  VAL A 103 -1  O  VAL A 103   N  HIS A   3           
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  LEU A 126   N  HIS A 114           
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  ALA A 193  0                                        
SHEET    2   B 4 GLU A 198  PHE A 208 -1  O  THR A 200   N  HIS A 192           
SHEET    3   B 4 PHE A 241  PRO A 250 -1  O  ALA A 245   N  CYS A 203           
SHEET    4   B 4 GLU A 229  LEU A 230 -1  N  GLU A 229   O  ALA A 246           
SHEET    1   C 4 LYS A 186  ALA A 193  0                                        
SHEET    2   C 4 GLU A 198  PHE A 208 -1  O  THR A 200   N  HIS A 192           
SHEET    3   C 4 PHE A 241  PRO A 250 -1  O  ALA A 245   N  CYS A 203           
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  ASP A 223  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  LEU A 272 -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  TYR B  66   N  CYS B  25           
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  TYR B  66   N  CYS B  25           
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 GLU B  36  LYS B  41 -1  N  LYS B  41   O  GLU B  44           
SHEET    3   G 4 TYR B  78  ASN B  83 -1  O  ARG B  81   N  ASP B  38           
SHEET    4   G 4 LYS B  91  LYS B  94 -1  O  LYS B  91   N  VAL B  82           
SHEET    1   H 8 GLU D  46  PRO D  47  0                                        
SHEET    2   H 8 THR D  31  ASP D  37 -1  N  ARG D  35   O  GLU D  46           
SHEET    3   H 8 ARG D  21  VAL D  28 -1  N  GLY D  26   O  PHE D  33           
SHEET    4   H 8 HIS D   3  VAL D  12 -1  N  ARG D   6   O  TYR D  27           
SHEET    5   H 8 THR D  94  VAL D 103 -1  O  VAL D 103   N  HIS D   3           
SHEET    6   H 8 PHE D 109  TYR D 118 -1  O  ARG D 111   N  ASP D 102           
SHEET    7   H 8 LYS D 121  LEU D 126 -1  O  ILE D 124   N  TYR D 116           
SHEET    8   H 8 TRP D 133  ALA D 135 -1  O  THR D 134   N  ALA D 125           
SHEET    1   I 4 LYS D 186  ALA D 193  0                                        
SHEET    2   I 4 GLU D 198  PHE D 208 -1  O  TRP D 204   N  HIS D 188           
SHEET    3   I 4 PHE D 241  PRO D 250 -1  O  ALA D 245   N  CYS D 203           
SHEET    4   I 4 GLU D 229  LEU D 230 -1  N  GLU D 229   O  ALA D 246           
SHEET    1   J 4 LYS D 186  ALA D 193  0                                        
SHEET    2   J 4 GLU D 198  PHE D 208 -1  O  TRP D 204   N  HIS D 188           
SHEET    3   J 4 PHE D 241  PRO D 250 -1  O  ALA D 245   N  CYS D 203           
SHEET    4   J 4 ARG D 234  PRO D 235 -1  N  ARG D 234   O  GLN D 242           
SHEET    1   K 4 GLU D 222  ASP D 223  0                                        
SHEET    2   K 4 THR D 214  ARG D 219 -1  N  ARG D 219   O  GLU D 222           
SHEET    3   K 4 TYR D 257  GLN D 262 -1  O  HIS D 260   N  THR D 216           
SHEET    4   K 4 LEU D 270  ARG D 273 -1  O  LEU D 272   N  CYS D 259           
SHEET    1   L 4 LYS E   6  SER E  11  0                                        
SHEET    2   L 4 ASN E  21  PHE E  30 -1  O  ASN E  24   N  TYR E  10           
SHEET    3   L 4 PHE E  62  PHE E  70 -1  O  THR E  68   N  LEU E  23           
SHEET    4   L 4 GLU E  50  HIS E  51 -1  N  GLU E  50   O  TYR E  67           
SHEET    1   M 4 LYS E   6  SER E  11  0                                        
SHEET    2   M 4 ASN E  21  PHE E  30 -1  O  ASN E  24   N  TYR E  10           
SHEET    3   M 4 PHE E  62  PHE E  70 -1  O  THR E  68   N  LEU E  23           
SHEET    4   M 4 SER E  55  PHE E  56 -1  N  SER E  55   O  TYR E  63           
SHEET    1   N 4 GLU E  44  ARG E  45  0                                        
SHEET    2   N 4 GLU E  36  LYS E  41 -1  N  LYS E  41   O  GLU E  44           
SHEET    3   N 4 TYR E  78  ASN E  83 -1  O  ALA E  79   N  LEU E  40           
SHEET    4   N 4 LYS E  91  LYS E  94 -1  O  VAL E  93   N  CYS E  80           
SSBOND   1 CYS A  101    CYS A  164                          1555   1555  2.13  
SSBOND   2 CYS A  203    CYS A  259                          1555   1555  2.07  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.02  
SSBOND   4 CYS D  101    CYS D  164                          1555   1555  2.11  
SSBOND   5 CYS D  203    CYS D  259                          1555   1555  2.05  
SSBOND   6 CYS E   25    CYS E   80                          1555   1555  1.99  
LINK         OD1 ASN B  83                NA    NA B 816     1555   1555  2.65  
LINK         O   HIS B  84                NA    NA B 816     1555   1555  2.68  
LINK         O   LEU B  87                NA    NA B 816     1555   1555  2.39  
LINK        NA    NA B 816                 O   HOH B 882     1555   1555  2.21  
LINK        NA    NA B 816                 O   HOH B 904     1555   1555  2.33  
LINK        NA    NA B 816                 O   HOH B 923     1555   1555  2.50  
CISPEP   1 TYR A  209    PRO A  210          0        -0.29                     
CISPEP   2 HIS B   31    PRO B   32          0        -5.57                     
CISPEP   3 TYR D  209    PRO D  210          0        -0.01                     
CISPEP   4 HIS E   31    PRO E   32          0        -1.38                     
SITE     1 AC1  6 ASN B  83  HIS B  84  LEU B  87  HOH B 882                    
SITE     2 AC1  6 HOH B 904  HOH B 923                                          
SITE     1 AC2  8 TRP D 204  ARG D 234  GLN D 242  SER E  11                    
SITE     2 AC2  8 PRO E  14  ARG E  97  HOH E 825  HOH E 896                    
SITE     1 AC3  6 TYR A  27  ASP A  29  ASP A  30  HOH A 845                    
SITE     2 AC3  6 HOH A 950  FMT B 810                                          
SITE     1 AC4  7 ARG A 234  GLN A 242  TYR B  10  SER B  11                    
SITE     2 AC4  7 HIS B  13  PRO B  14  HOH B 835                               
SITE     1 AC5  7 THR D  31  GLN D  32  ARG D  48  PRO D  50                    
SITE     2 AC5  7 HOH D1014  HOH D1018  HOH D1071                               
SITE     1 AC6  5 ASP D 223  GLN D 224  THR D 225  GLN D 226                    
SITE     2 AC6  5 ASP D 227                                                     
SITE     1 AC7  4 ARG D 131  GLU D 154  HOH D 889  HOH D 987                    
SITE     1 AC8  3 LYS E   6  ILE E   7  HOH E 933                               
SITE     1 AC9  6 THR D  31  ARG D 181  TYR D 209  GLY D 239                    
SITE     2 AC9  6 HOH D1018  HOH D1068                                          
SITE     1 BC1  3 LYS B  91  ILE B  92  HOH B 928                               
SITE     1 BC2  3 GOL A 802  SER B  57  HOH B 844                               
SITE     1 BC3  2 ASN E  83  HIS E  84                                          
SITE     1 BC4  3 MET D 138  THR D 142  HIS D 191                               
SITE     1 BC5  4 LEU C   2  PHE C   3  GLY C   4  HOH C 452                    
SITE     1 BC6  4 THR B  86  SER B  88  ASP D 220  ARG D 256                    
SITE     1 BC7  3 MET D  98  TYR D 113  GLN D 115                               
CRYST1   50.384   62.709   74.773  82.00  76.22  78.18 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      0.019848 -0.004155 -0.004494        0.00000                         
SCALE2      0.000000  0.016292 -0.001557        0.00000                         
SCALE3      0.000000  0.000000  0.013833        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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