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Database: PDB
Entry: 3VCL
LinkDB: 3VCL
Original site: 3VCL 
HEADER    IMMUNE SYSTEM                           04-JAN-12   3VCL              
TITLE     CRYSTAL STRUCTURE OF HLA-B7 WITH THE HCMV PP65 PEPTIDE RPHERNGFTVL    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, B-7 ALPHA CHAIN;   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 25-299;                                       
COMPND   5 SYNONYM: MHC CLASS I ANTIGEN B*7;                                    
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: BETA-2-MICROGLOBULIN;                                      
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: BETA-2-MICROGLOBULIN FORM PI 5.3;                           
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: PEPTIDE FROM TEGUMENT PROTEIN PP65;                        
COMPND  14 CHAIN: C;                                                            
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HLA-B;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: B2M;                                                           
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 5;                            
SOURCE  18 ORGANISM_COMMON: HHV-5;                                              
SOURCE  19 ORGANISM_TAXID: 10359;                                               
SOURCE  20 OTHER_DETAILS: SYNTHETIC PEPTIDE                                     
KEYWDS    CLASS I HISTOCOMPATIBILITY ANTIGEN, ANTIGEN PRESENTATION, T-CELL      
KEYWDS   2 RECEPTOR, MEMBRANE, IMMUNE SYSTEM                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.PETERSEN,J.ROSSJOHN                                                 
REVDAT   1   21-NOV-12 3VCL    0                                                
JRNL        AUTH   R.M.BRENNAN,J.PETERSEN,M.A.NELLER,J.J.MILES,J.M.BURROWS,     
JRNL        AUTH 2 C.SMITH,J.MCCLUSKEY,R.KHANNA,J.ROSSJOHN,S.R.BURROWS          
JRNL        TITL   THE IMPACT OF A LARGE AND FREQUENT DELETION IN THE HUMAN TCR 
JRNL        TITL 2 BETA LOCUS ON ANTIVIRAL IMMUNITY                             
JRNL        REF    J.IMMUNOL.                    V. 188  2742 2012              
JRNL        REFN                   ISSN 0022-1767                               
JRNL        PMID   22323539                                                     
JRNL        DOI    10.4049/JIMMUNOL.1102675                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.2_869)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.28                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 56534                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2353                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 25.2840 -  3.6594    0.93     5609   243  0.1875 0.2033        
REMARK   3     2  3.6594 -  2.9060    1.00     5703   242  0.1690 0.2052        
REMARK   3     3  2.9060 -  2.5390    1.00     5644   225  0.1816 0.2225        
REMARK   3     4  2.5390 -  2.3070    1.00     5602   251  0.1833 0.2298        
REMARK   3     5  2.3070 -  2.1418    1.00     5568   221  0.1767 0.2192        
REMARK   3     6  2.1418 -  2.0156    1.00     5535   243  0.1776 0.2235        
REMARK   3     7  2.0156 -  1.9146    1.00     5528   241  0.1848 0.2230        
REMARK   3     8  1.9146 -  1.8313    1.00     5491   246  0.2126 0.2478        
REMARK   3     9  1.8313 -  1.7608    1.00     5497   234  0.2365 0.2931        
REMARK   3    10  1.7608 -  1.7001    1.00     5536   207  0.2646 0.2996        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.73                                          
REMARK   3   K_SOL              : 0.40                                          
REMARK   3   B_SOL              : 60.00                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.430           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.79                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.48                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.018           3393                                  
REMARK   3   ANGLE     :  1.699           4621                                  
REMARK   3   CHIRALITY :  0.138            467                                  
REMARK   3   PLANARITY :  0.008            615                                  
REMARK   3   DIHEDRAL  : 13.454           1287                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (chain A and resid 1:52)                               
REMARK   3    ORIGIN FOR THE GROUP (A):   7.4765 -28.1500 -26.0382              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2733 T22:   0.2447                                     
REMARK   3      T33:   0.1366 T12:   0.0666                                     
REMARK   3      T13:   0.0283 T23:   0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1162 L22:   2.5609                                     
REMARK   3      L33:   1.9184 L12:   0.4658                                     
REMARK   3      L13:  -0.1402 L23:   0.6324                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0804 S12:   0.0420 S13:   0.1362                       
REMARK   3      S21:  -0.0472 S22:  -0.0705 S23:   0.2268                       
REMARK   3      S31:  -0.4686 S32:  -0.3214 S33:  -0.0235                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (chain A and resid 53:85)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  10.1552 -28.3617 -35.9826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3355 T22:   0.3180                                     
REMARK   3      T33:   0.1253 T12:   0.0879                                     
REMARK   3      T13:   0.0385 T23:   0.0336                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2042 L22:   2.4420                                     
REMARK   3      L33:   1.8957 L12:  -0.0247                                     
REMARK   3      L13:  -0.0733 L23:   0.7361                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0300 S12:   0.2613 S13:   0.1123                       
REMARK   3      S21:  -0.2704 S22:   0.0219 S23:   0.0485                       
REMARK   3      S31:  -0.6701 S32:  -0.3465 S33:  -0.0598                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (chain A and resid 86:116)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  20.1061 -32.4434 -27.9574              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2214 T22:   0.2921                                     
REMARK   3      T33:   0.1979 T12:  -0.0271                                     
REMARK   3      T13:   0.0656 T23:  -0.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3302 L22:   2.6544                                     
REMARK   3      L33:   1.7660 L12:   1.2463                                     
REMARK   3      L13:   0.6470 L23:  -0.0868                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0929 S12:   0.0878 S13:  -0.1608                       
REMARK   3      S21:  -0.0914 S22:   0.0145 S23:  -0.5292                       
REMARK   3      S31:  -0.4251 S32:   0.2771 S33:  -0.1417                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (chain A and resid 117:165)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  26.5874 -31.9132 -34.5754              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2527 T22:   0.3222                                     
REMARK   3      T33:   0.2649 T12:  -0.0677                                     
REMARK   3      T13:   0.0934 T23:  -0.0450                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3335 L22:   1.5785                                     
REMARK   3      L33:   2.1263 L12:   0.9796                                     
REMARK   3      L13:  -0.4535 L23:  -0.2440                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0637 S12:   0.2178 S13:  -0.1712                       
REMARK   3      S21:  -0.2572 S22:   0.0474 S23:  -0.5490                       
REMARK   3      S31:  -0.4106 S32:   0.4527 S33:  -0.0711                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (chain A and resid 166:212)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1268 -26.1940  -2.2657              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3328 T22:   0.0925                                     
REMARK   3      T33:   0.1307 T12:  -0.0478                                     
REMARK   3      T13:   0.0251 T23:  -0.0522                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5832 L22:   0.5434                                     
REMARK   3      L33:   2.4135 L12:   0.1364                                     
REMARK   3      L13:  -0.4765 L23:  -0.0222                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1055 S12:   0.0435 S13:   0.1731                       
REMARK   3      S21:  -0.0529 S22:   0.0345 S23:  -0.0093                       
REMARK   3      S31:  -0.4354 S32:   0.0255 S33:  -0.0592                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (chain A and resid 213:275)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  16.5483 -33.8226   6.6115              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2633 T22:   0.2054                                     
REMARK   3      T33:   0.1365 T12:  -0.0655                                     
REMARK   3      T13:   0.0154 T23:  -0.0495                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0313 L22:   1.4660                                     
REMARK   3      L33:   3.3390 L12:  -0.2020                                     
REMARK   3      L13:  -0.5560 L23:  -0.3691                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0219 S12:  -0.0877 S13:  -0.0765                       
REMARK   3      S21:   0.1865 S22:  -0.0113 S23:  -0.1675                       
REMARK   3      S31:  -0.0666 S32:   0.4757 S33:   0.0385                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (chain B and resid 1:43)                               
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2336 -39.5649 -10.2664              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1819 T22:   0.2679                                     
REMARK   3      T33:   0.1460 T12:  -0.0572                                     
REMARK   3      T13:   0.0159 T23:  -0.0402                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7525 L22:   1.6650                                     
REMARK   3      L33:   1.5230 L12:   0.1256                                     
REMARK   3      L13:  -0.0772 L23:  -0.5204                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1713 S12:  -0.2330 S13:   0.1480                       
REMARK   3      S21:   0.3111 S22:  -0.1263 S23:   0.0703                       
REMARK   3      S31:   0.0233 S32:  -0.3907 S33:   0.0075                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (chain B and resid 44:51)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.7530 -38.2217 -14.7017              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2594 T22:   0.5976                                     
REMARK   3      T33:   0.4164 T12:  -0.0287                                     
REMARK   3      T13:   0.0133 T23:   0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1580 L22:   2.7825                                     
REMARK   3      L33:   5.6321 L12:   1.1588                                     
REMARK   3      L13:  -1.1584 L23:  -2.4979                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2547 S12:   0.9897 S13:   0.9269                       
REMARK   3      S21:  -0.5136 S22:   0.7592 S23:   1.4612                       
REMARK   3      S31:   0.1908 S32:  -1.3663 S33:  -0.2635                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (chain B and resid 52:78)                              
REMARK   3    ORIGIN FOR THE GROUP (A):   1.9874 -36.4395 -11.7828              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0350 T22:   0.1339                                     
REMARK   3      T33:  -0.1602 T12:  -0.0458                                     
REMARK   3      T13:  -0.0465 T23:  -0.0992                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9380 L22:   2.3826                                     
REMARK   3      L33:   1.0777 L12:  -0.1210                                     
REMARK   3      L13:   1.0049 L23:  -0.0652                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1100 S12:  -0.4360 S13:   0.0721                       
REMARK   3      S21:   0.4489 S22:  -0.0410 S23:   0.4486                       
REMARK   3      S31:  -0.0321 S32:  -0.4536 S33:   0.2909                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (chain B and resid 79:99)                              
REMARK   3    ORIGIN FOR THE GROUP (A):   1.2511 -46.9014  -7.9351              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2725 T22:   0.2828                                     
REMARK   3      T33:   0.1671 T12:  -0.1088                                     
REMARK   3      T13:  -0.0148 T23:   0.0181                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4885 L22:   2.1426                                     
REMARK   3      L33:   2.5303 L12:   0.2788                                     
REMARK   3      L13:   0.1074 L23:   1.2948                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2090 S12:  -0.2968 S13:  -0.1735                       
REMARK   3      S21:   0.5434 S22:  -0.1360 S23:  -0.0557                       
REMARK   3      S31:   0.3996 S32:  -0.3152 S33:  -0.0403                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (chain C and resid 1:11)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3840 -26.7947 -37.5531              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5542 T22:   0.4005                                     
REMARK   3      T33:   0.2551 T12:   0.0232                                     
REMARK   3      T13:   0.1318 T23:   0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7375 L22:   0.1823                                     
REMARK   3      L33:   0.2307 L12:   0.5625                                     
REMARK   3      L13:   0.6331 L23:   0.2051                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0051 S12:   0.3792 S13:  -0.1080                       
REMARK   3      S21:  -0.1182 S22:   0.2287 S23:  -0.1774                       
REMARK   3      S31:  -0.2995 S32:   0.1310 S33:   0.3860                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3VCL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JAN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB069875.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56534                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.281                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 11.900                             
REMARK 200  R MERGE                    (I) : 0.05500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 37.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2H6P                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG2000-MME, 5-10MM NICL2, 0.1M      
REMARK 280  HEPES, PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.0K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      118.55350            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       32.89300            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       32.89300            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       59.27675            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       32.89300            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       32.89300            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      177.83025            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       32.89300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       32.89300            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       59.27675            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       32.89300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       32.89300            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      177.83025            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      118.55350            
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: 6830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 108    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 131    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 181    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 226    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 268    CG   CD   CE   NZ                                   
REMARK 470     LYS B  58    CG   CD   CE   NZ                                   
REMARK 470     LYS B  75    CG   CD   CE   NZ                                   
REMARK 470     GLU C   4    CG   CD   OE1  OE2                                  
REMARK 470     ASN C   6    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N    ILE B     1     O    HOH B   300              1.91            
REMARK 500   OD1  ASP B    34     O    HOH B   288              1.99            
REMARK 500   OE1  GLU A   229     O    HOH A   554              2.08            
REMARK 500   NE2  HIS A   188     O    HOH A   696              2.09            
REMARK 500   OE1  GLN A   224     O    HOH A   654              2.14            
REMARK 500   O    HOH A   643     O    HOH A   650              2.15            
REMARK 500   O1   GOL A   303     O    HOH A   632              2.16            
REMARK 500   O    HOH B   214     O    HOH B   313              2.17            
REMARK 500   O    HOH A   416     O    HOH A   605              2.18            
REMARK 500   O    HOH B   303     O    HOH B   316              2.19            
REMARK 500   O    HOH B   226     O    HOH B   288              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE A 208   CZ    PHE A 208   CE2     0.117                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ARG A 157   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 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    ARG A  14       68.38   -151.61                                   
REMARK 500    ASP A  29     -129.66     55.65                                   
REMARK 500    ASP A 114      100.13   -160.55                                   
REMARK 500    GLN A 224       53.19   -111.95                                   
REMARK 500    ARG A 239       -4.94     86.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              NI A 301  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 180   OE1                                                    
REMARK 620 2 HIS A   3   NE2  80.6                                              
REMARK 620 3 GLY A   1   N   176.4 103.0                                        
REMARK 620 4 HOH A 598   O    91.9  94.5  87.5                                  
REMARK 620 5 HOH A 548   O    85.1  88.5  95.3 175.4                            
REMARK 620 6 HOH A 547   O    80.6 160.2  95.9  92.1  83.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 102  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  51   NE2                                                    
REMARK 620 2 HOH B 307   O    72.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI A 302  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 275   O                                                      
REMARK 620 2 HOH A 696   O   122.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 101  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 300   O                                                      
REMARK 620 2 HOH B 348   O    91.8                                              
REMARK 620 3 HOH B 349   O    80.2 168.9                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 106                 
DBREF  3VCL A    1   275  UNP    P01889   1B07_HUMAN      25    299             
DBREF  3VCL B    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  3VCL C    1    11  UNP    F5HB26   F5HB26_HCMV    265    275             
SEQRES   1 A  275  GLY SER HIS SER MET ARG TYR PHE TYR THR SER VAL SER          
SEQRES   2 A  275  ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE SER 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 PRO ARG GLU GLU PRO ARG ALA PRO TRP ILE          
SEQRES   5 A  275  GLU GLN GLU GLY PRO GLU TYR TRP ASP ARG ASN THR GLN          
SEQRES   6 A  275  ILE TYR LYS ALA GLN ALA GLN THR ASP ARG GLU SER LEU          
SEQRES   7 A  275  ARG ASN LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY          
SEQRES   8 A  275  SER HIS THR LEU GLN SER MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 A  275  PRO ASP GLY ARG LEU LEU ARG GLY HIS ASP GLN TYR ALA          
SEQRES  10 A  275  TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU          
SEQRES  11 A  275  ARG SER TRP THR ALA ALA ASP THR ALA ALA GLN ILE THR          
SEQRES  12 A  275  GLN ARG LYS TRP GLU ALA ALA ARG GLU ALA GLU GLN ARG          
SEQRES  13 A  275  ARG ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU ARG          
SEQRES  14 A  275  ARG TYR LEU GLU ASN GLY LYS ASP LYS LEU GLU ARG ALA          
SEQRES  15 A  275  ASP PRO PRO LYS THR HIS VAL THR HIS HIS PRO ILE SER          
SEQRES  16 A  275  ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY 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 ARG THR PHE GLN LYS TRP ALA ALA VAL          
SEQRES  20 A  275  VAL VAL PRO SER GLY GLU 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   99  ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS          
SEQRES   2 B   99  PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR          
SEQRES   3 B   99  VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU          
SEQRES   4 B   99  LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER          
SEQRES   5 B   99  ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU          
SEQRES   6 B   99  TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR          
SEQRES   7 B   99  ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS          
SEQRES   8 B   99  ILE VAL LYS TRP ASP ARG ASP MET                              
SEQRES   1 C   11  ARG PRO HIS GLU ARG ASN GLY PHE THR VAL LEU                  
HET     NI  A 301       1                                                       
HET     NI  A 302       1                                                       
HET    GOL  A 303       6                                                       
HET    GOL  A 304       6                                                       
HET    GOL  A 305       6                                                       
HET    GOL  A 306       6                                                       
HET     NI  B 101       1                                                       
HET     NI  B 102       1                                                       
HET    GOL  B 103       6                                                       
HET    GOL  B 104       6                                                       
HET    GOL  B 105       6                                                       
HET    GOL  B 106       6                                                       
HETNAM      NI NICKEL (II) ION                                                  
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   4   NI    4(NI 2+)                                                     
FORMUL   6  GOL    8(C3 H8 O3)                                                  
FORMUL  16  HOH   *458(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 ASP A  137  ALA A  150  1                                  14    
HELIX    4   4 ARG A  151  GLY A  162  1                                  12    
HELIX    5   5 GLY A  162  GLY A  175  1                                  14    
HELIX    6   6 GLY A  175  GLU 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  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 LEU 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  TYR A 123   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  ALA A 245   N  CYS A 203           
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  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  PHE B  70   N  ASN B  21           
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  PHE B  70   N  ASN B  21           
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           
SSBOND   1 CYS A  101    CYS A  164                          1555   1555  2.10  
SSBOND   2 CYS A  203    CYS A  259                          1555   1555  2.08  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.03  
LINK         OE1 GLU A 180                NI    NI A 301     1555   1555  1.93  
LINK         NE2 HIS A   3                NI    NI A 301     1555   1555  2.15  
LINK         N   GLY A   1                NI    NI A 301     1555   1555  2.33  
LINK         NE2 HIS B  51                NI    NI B 102     1555   1555  2.46  
LINK         O   GLU A 275                NI    NI A 302     1555   1555  2.63  
LINK        NI    NI B 101                 O   HOH B 300     1555   1555  2.24  
LINK        NI    NI A 301                 O   HOH A 598     1555   1555  2.29  
LINK        NI    NI A 301                 O   HOH A 548     1555   1555  2.31  
LINK        NI    NI A 301                 O   HOH A 547     1555   1555  2.34  
LINK        NI    NI A 302                 O   HOH A 696     1555   1555  2.36  
LINK        NI    NI B 101                 O   HOH B 348     1555   1555  2.46  
LINK        NI    NI B 102                 O   HOH B 307     1555   1555  2.47  
LINK        NI    NI B 101                 O   HOH B 349     1555   1555  2.66  
CISPEP   1 TYR A  209    PRO A  210          0         1.89                     
CISPEP   2 HIS B   31    PRO B   32          0        -0.80                     
CISPEP   3 ARG C    5    ASN C    6          0        15.65                     
SITE     1 AC1  6 GLY A   1  HIS A   3  GLU A 180  HOH A 547                    
SITE     2 AC1  6 HOH A 548  HOH A 598                                          
SITE     1 AC2  5 HIS A 188  VAL A 189  GLU A 275  HOH A 648                    
SITE     2 AC2  5 HOH A 696                                                     
SITE     1 AC3  7 THR A  31  LYS A 178  TYR A 209  ARG A 239                    
SITE     2 AC3  7 HOH A 432  HOH A 471  HOH A 632                               
SITE     1 AC4  6 ARG A  44  GLU A  45  TRP A  60  ARG A 157                    
SITE     2 AC4  6 GLU A 161  HOH A 693                                          
SITE     1 AC5 10 PHE A   8  TYR A  27  ASP A  29  ASP A  30                    
SITE     2 AC5 10 HOH A 534  HOH A 544  HOH A 617  HOH A 635                    
SITE     3 AC5 10 TYR B  63  HOH B 232                                          
SITE     1 AC6  6 GLU A 264  GLY A 265  LEU A 266  PRO A 267                    
SITE     2 AC6  6 HOH A 588  ASN B  42                                          
SITE     1 AC7  5 HIS A 197  HOH B 286  HOH B 300  HOH B 348                    
SITE     2 AC7  5 HOH B 349                                                     
SITE     1 AC8  3 HIS B  51  HOH B 307  HOH B 342                               
SITE     1 AC9  6 PRO B   5  LYS B   6  ILE B   7  LYS B  91                    
SITE     2 AC9  6 HOH B 277  HOH B 285                                          
SITE     1 BC1  7 HOH A 556  ASP B  34  GLU B  36  ASN B  83                    
SITE     2 BC1  7 HIS B  84  VAL B  85  HOH B 316                               
SITE     1 BC2  7 ASP B  76  GLU B  77  TRP B  95  ASP B  96                    
SITE     2 BC2  7 ARG B  97  HOH B 212  HOH B 242                               
SITE     1 BC3  8 VAL A 231  ARG A 234  GLN B   8  VAL B   9                    
SITE     2 BC3  8 VAL B  93  MET B  99  HOH B 204  HOH B 302                    
CRYST1   65.786   65.786  237.107  90.00  90.00  90.00 P 41 21 2     8          
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      0.015201  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015201  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004218        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system