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LongText Report for: 5trz-pdb

Name Class
5trz-pdb
HEADER    IMMUNE SYSTEM                           27-OCT-16   5TRZ              
TITLE     CRYSTAL STRUCTURE OF MHC-I H2-KD COMPLEXED WITH PEPTIDES OF           
TITLE    2 MYCOBACTERIAL TUBERCULOSIS (YQSGLSIVM)                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, K-D ALPHA CHAIN;   
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 23-297;                                       
COMPND   5 SYNONYM: H-2K(D);                                                    
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: BETA-2-MICROGLOBULIN;                                      
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 21-119;                                       
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: PEPTIDE (P9) OF MTB85B (MYCOBACTERIUM TUBERCULOSIS)        
COMPND  14 YQSGLSIVM;                                                           
COMPND  15 CHAIN: P, Q;                                                         
COMPND  16 FRAGMENT: UNP RESIDUES 102-110;                                      
COMPND  17 SYNONYM: DGAT,30 KDA EXTRACELLULAR PROTEIN,ACYL-COA:DIACYLGLYCEROL   
COMPND  18 ACYLTRANSFERASE,ANTIGEN 85 COMPLEX B,AG85B,EXTRACELLULAR ALPHA-      
COMPND  19 ANTIGEN,FIBRONECTIN-BINDING PROTEIN B,FBPS B;                        
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: H2-K1, H2-K;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21-B;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: B2M, CDABP0092, HDCMA22P;                                      
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET3A;                                    
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 SYNTHETIC: YES;                                                      
SOURCE  23 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE  24 ORGANISM_TAXID: 83332                                                
KEYWDS    MAJOR HISTOMPATIBILITY COMPLEX CLASS I, MHC-I, H2-KD, H-2KD,          
KEYWDS   2 MYCOBACTERIAL TUBERCULOSIS, TB PEPTIDE, MTB85B, MTB85A, MKAN85B,     
KEYWDS   3 IMMUNE RESPONSE, IMMUNE SYSTEM                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.JIANG,K.NATARAJAN,D.MARGULIES                                       
REVDAT   2   14-AUG-19 5TRZ    1       JRNL                                     
REVDAT   1   09-MAY-18 5TRZ    0                                                
JRNL        AUTH   S.KOMINE-AIZAWA,J.JIANG,S.MIZUNO,S.HAYAKAWA,K.MATSUO,        
JRNL        AUTH 2 L.F.BOYD,D.H.MARGULIES,M.HONDA                               
JRNL        TITL   MHC-RESTRICTED AG85B-SPECIFIC CD8+T CELLS ARE ENHANCED BY    
JRNL        TITL 2 RECOMBINANT BCG PRIME AND DNA BOOST IMMUNIZATION IN MICE.    
JRNL        REF    EUR.J.IMMUNOL.                             2019              
JRNL        REFN                   ISSN 0014-2980                               
JRNL        PMID   31135967                                                     
JRNL        DOI    10.1002/EJI.201847988                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 41174                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2065                            
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 39.0000 -  5.6178    0.94     2682   142  0.2108 0.2306        
REMARK   3     2  5.6178 -  4.4601    0.95     2632   138  0.1482 0.1746        
REMARK   3     3  4.4601 -  3.8966    0.95     2612   138  0.1333 0.1606        
REMARK   3     4  3.8966 -  3.5405    0.95     2634   138  0.1484 0.1623        
REMARK   3     5  3.5405 -  3.2868    0.95     2612   138  0.1528 0.1876        
REMARK   3     6  3.2868 -  3.0931    0.95     2601   137  0.1673 0.2109        
REMARK   3     7  3.0931 -  2.9382    0.95     2593   136  0.1712 0.2133        
REMARK   3     8  2.9382 -  2.8103    0.95     2645   139  0.1849 0.2274        
REMARK   3     9  2.8103 -  2.7021    0.94     2577   136  0.1860 0.2153        
REMARK   3    10  2.7021 -  2.6089    0.95     2595   137  0.1906 0.2453        
REMARK   3    11  2.6089 -  2.5273    0.95     2602   137  0.2019 0.2270        
REMARK   3    12  2.5273 -  2.4551    0.95     2562   134  0.2025 0.2834        
REMARK   3    13  2.4551 -  2.3905    0.94     2615   138  0.2207 0.2195        
REMARK   3    14  2.3905 -  2.3321    0.95     2536   133  0.2150 0.2486        
REMARK   3    15  2.3321 -  2.2791    0.92     2604   138  0.2290 0.2903        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.38                                          
REMARK   3   B_SOL              : 43.90                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.890           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           6524                                  
REMARK   3   ANGLE     :  0.796           8854                                  
REMARK   3   CHIRALITY :  0.049            899                                  
REMARK   3   PLANARITY :  0.006           1151                                  
REMARK   3   DIHEDRAL  : 19.828           3820                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 5TRZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000224689.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-MAR-16                          
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                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0333                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41174                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.960                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.97200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.300                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 4000, 0.1M MES BUFFER, 5% MPD,   
REMARK 280  PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       44.40800            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13420 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P, C, D, Q                      
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 A  89    CG   CD   CE   NZ                                   
REMARK 470     LEU A 219    CG   CD1  CD2                                       
REMARK 470     GLU A 222    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 223    CG   OD1  OD2                                       
REMARK 470     LEU A 224    CG   CD1  CD2                                       
REMARK 470     ASP A 227    CG   OD1  OD2                                       
REMARK 470     LYS A 275    CG   CD   CE   NZ                                   
REMARK 470     LYS B  48    CG   CD   CE   NZ                                   
REMARK 470     ARG C  83    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  89    CG   CD   CE   NZ                                   
REMARK 470     SER C 105    OG                                                  
REMARK 470     ASN C 220    CG   OD1  ND2                                       
REMARK 470     GLU C 222    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 223    CG   OD1  OD2                                       
REMARK 470     LEU C 224    CB   CG   CD1  CD2                                  
REMARK 470     THR C 225    OG1                                                 
REMARK 470     ASP C 227    CG   OD1  OD2                                       
REMARK 470     GLN C 255    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 275    CG   CD   CE   NZ                                   
REMARK 470     LYS D  48    CG   CD   CE   NZ                                   
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   O    HOH C   402     O    HOH C   474              2.08            
REMARK 500   O    HOH B   205     O    HOH B   232              2.09            
REMARK 500   O    HOH C   427     O    HOH C   438              2.12            
REMARK 500   O    HOH A   452     O    HOH A   490              2.14            
REMARK 500   O    HOH C   421     O    HOH C   461              2.14            
REMARK 500   O    HOH A   430     O    HOH A   492              2.14            
REMARK 500   O    HOH A   443     O    HOH A   492              2.16            
REMARK 500   ND2  ASN D    17     OE1  GLU D    74              2.16            
REMARK 500   O    HOH C   401     O    HOH C   465              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH P   108     O    HOH Q   102     1545     2.19            
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     -123.86     55.19                                   
REMARK 500    TYR A 123      -72.14   -115.91                                   
REMARK 500    ASN A 220     -107.18     57.13                                   
REMARK 500    GLU A 222       34.25    -91.22                                   
REMARK 500    LEU A 224     -173.60    -62.17                                   
REMARK 500    TRP B  60       -1.19     84.47                                   
REMARK 500    LEU P   5      -97.44   -104.21                                   
REMARK 500    ASP C  29     -123.80     55.62                                   
REMARK 500    TYR C 123      -72.92   -116.52                                   
REMARK 500    GLN C 218      100.25     33.34                                   
REMARK 500    ASN C 220       11.10     53.05                                   
REMARK 500    ASP C 223      -40.48     60.58                                   
REMARK 500    SER D  57     -167.21    -78.91                                   
REMARK 500    TRP D  60       -0.39     85.80                                   
REMARK 500    LEU Q   5      -95.45   -104.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 101                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5TS1   RELATED DB: PDB                                   
DBREF  5TRZ A    2   276  UNP    P01902   HA1D_MOUSE      23    297             
DBREF  5TRZ B    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  5TRZ P    1     9  UNP    P9WQP1   A85B_MYCTU     102    110             
DBREF  5TRZ C    2   276  UNP    P01902   HA1D_MOUSE      23    297             
DBREF  5TRZ D    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  5TRZ Q    1     9  UNP    P9WQP1   A85B_MYCTU     102    110             
SEQADV 5TRZ HIS A  114  UNP  P01902    GLN   135 CONFLICT                       
SEQADV 5TRZ PRO A  276  UNP  P01902    LEU   297 CONFLICT                       
SEQADV 5TRZ MET B    0  UNP  P61769              INITIATING METHIONINE          
SEQADV 5TRZ HIS C  114  UNP  P01902    GLN   135 CONFLICT                       
SEQADV 5TRZ PRO C  276  UNP  P01902    LEU   297 CONFLICT                       
SEQADV 5TRZ MET D    0  UNP  P61769              INITIATING METHIONINE          
SEQRES   1 A  275  PRO HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER ARG          
SEQRES   2 A  275  PRO GLY LEU GLY GLU PRO ARG PHE ILE ALA VAL GLY TYR          
SEQRES   3 A  275  VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP ALA          
SEQRES   4 A  275  ASP ASN PRO ARG PHE GLU PRO ARG ALA PRO TRP MET GLU          
SEQRES   5 A  275  GLN GLU GLY PRO GLU TYR TRP GLU GLU GLN THR GLN ARG          
SEQRES   6 A  275  ALA LYS SER ASP GLU GLN TRP PHE ARG VAL SER LEU ARG          
SEQRES   7 A  275  THR ALA GLN ARG TYR TYR ASN GLN SER LYS GLY GLY SER          
SEQRES   8 A  275  HIS THR PHE GLN ARG MET PHE GLY CYS ASP VAL GLY SER          
SEQRES   9 A  275  ASP TRP ARG LEU LEU ARG GLY TYR HIS GLN PHE ALA TYR          
SEQRES  10 A  275  ASP GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU LYS          
SEQRES  11 A  275  THR TRP THR ALA ALA ASP THR ALA ALA LEU ILE THR ARG          
SEQRES  12 A  275  ARG LYS TRP GLU GLN ALA GLY ASP ALA GLU TYR TYR ARG          
SEQRES  13 A  275  ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU ARG ARG          
SEQRES  14 A  275  TYR LEU GLU LEU GLY ASN GLU THR LEU LEU ARG THR ASP          
SEQRES  15 A  275  SER PRO LYS ALA HIS VAL THR TYR HIS PRO ARG SER GLN          
SEQRES  16 A  275  VAL ASP VAL THR LEU ARG CYS TRP ALA LEU GLY PHE TYR          
SEQRES  17 A  275  PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY GLU          
SEQRES  18 A  275  ASP LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG PRO          
SEQRES  19 A  275  ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL VAL          
SEQRES  20 A  275  VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS HIS VAL          
SEQRES  21 A  275  HIS HIS LYS GLY LEU PRO GLU PRO LEU THR LEU ARG TRP          
SEQRES  22 A  275  LYS PRO                                                      
SEQRES   1 B  100  MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG          
SEQRES   2 B  100  HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS          
SEQRES   3 B  100  TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP          
SEQRES   4 B  100  LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS          
SEQRES   5 B  100  SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU          
SEQRES   6 B  100  LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU          
SEQRES   7 B  100  TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO          
SEQRES   8 B  100  LYS ILE VAL LYS TRP ASP ARG ASP MET                          
SEQRES   1 P    9  TYR GLN SER GLY LEU SER ILE VAL MET                          
SEQRES   1 C  275  PRO HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER ARG          
SEQRES   2 C  275  PRO GLY LEU GLY GLU PRO ARG PHE ILE ALA VAL GLY TYR          
SEQRES   3 C  275  VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP ALA          
SEQRES   4 C  275  ASP ASN PRO ARG PHE GLU PRO ARG ALA PRO TRP MET GLU          
SEQRES   5 C  275  GLN GLU GLY PRO GLU TYR TRP GLU GLU GLN THR GLN ARG          
SEQRES   6 C  275  ALA LYS SER ASP GLU GLN TRP PHE ARG VAL SER LEU ARG          
SEQRES   7 C  275  THR ALA GLN ARG TYR TYR ASN GLN SER LYS GLY GLY SER          
SEQRES   8 C  275  HIS THR PHE GLN ARG MET PHE GLY CYS ASP VAL GLY SER          
SEQRES   9 C  275  ASP TRP ARG LEU LEU ARG GLY TYR HIS GLN PHE ALA TYR          
SEQRES  10 C  275  ASP GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU LYS          
SEQRES  11 C  275  THR TRP THR ALA ALA ASP THR ALA ALA LEU ILE THR ARG          
SEQRES  12 C  275  ARG LYS TRP GLU GLN ALA GLY ASP ALA GLU TYR TYR ARG          
SEQRES  13 C  275  ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU ARG ARG          
SEQRES  14 C  275  TYR LEU GLU LEU GLY ASN GLU THR LEU LEU ARG THR ASP          
SEQRES  15 C  275  SER PRO LYS ALA HIS VAL THR TYR HIS PRO ARG SER GLN          
SEQRES  16 C  275  VAL ASP VAL THR LEU ARG CYS TRP ALA LEU GLY PHE TYR          
SEQRES  17 C  275  PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY GLU          
SEQRES  18 C  275  ASP LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG PRO          
SEQRES  19 C  275  ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL VAL          
SEQRES  20 C  275  VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS HIS VAL          
SEQRES  21 C  275  HIS HIS LYS GLY LEU PRO GLU PRO LEU THR LEU ARG TRP          
SEQRES  22 C  275  LYS PRO                                                      
SEQRES   1 D  100  MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG          
SEQRES   2 D  100  HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS          
SEQRES   3 D  100  TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP          
SEQRES   4 D  100  LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS          
SEQRES   5 D  100  SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU          
SEQRES   6 D  100  LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU          
SEQRES   7 D  100  TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO          
SEQRES   8 D  100  LYS ILE VAL LYS TRP ASP ARG ASP MET                          
SEQRES   1 Q    9  TYR GLN SER GLY LEU SER ILE VAL MET                          
HET    GOL  A 301       6                                                       
HET    EDO  A 302       4                                                       
HET    EDO  A 303       4                                                       
HET    GOL  B 101       6                                                       
HET    GOL  C 301       6                                                       
HET    EDO  C 302       4                                                       
HET    EDO  C 303       4                                                       
HET    EDO  C 304       4                                                       
HET    EDO  C 305       4                                                       
HET    EDO  C 306       4                                                       
HET    EDO  D 101       4                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   7  GOL    3(C3 H8 O3)                                                  
FORMUL   8  EDO    8(C2 H6 O2)                                                  
FORMUL  18  HOH   *276(H2 O)                                                    
HELIX    1 AA1 ALA A   49  GLU A   53  5                                   5    
HELIX    2 AA2 GLY A   56  TYR A   85  1                                  30    
HELIX    3 AA3 ASP A  137  GLY A  151  1                                  15    
HELIX    4 AA4 GLY A  151  GLY A  162  1                                  12    
HELIX    5 AA5 GLY A  162  GLY A  175  1                                  14    
HELIX    6 AA6 GLY A  175  LEU A  180  1                                   6    
HELIX    7 AA7 LYS A  253  GLN A  255  5                                   3    
HELIX    8 AA8 ALA C   49  GLU C   55  5                                   7    
HELIX    9 AA9 GLY C   56  TYR C   85  1                                  30    
HELIX   10 AB1 ASP C  137  GLY C  151  1                                  15    
HELIX   11 AB2 GLY C  151  GLY C  162  1                                  12    
HELIX   12 AB3 GLY C  162  GLY C  175  1                                  14    
HELIX   13 AB4 GLY C  175  LEU C  180  1                                   6    
HELIX   14 AB5 LYS C  253  TYR C  257  5                                   5    
SHEET    1 AA1 8 GLU A  46  PRO A  47  0                                        
SHEET    2 AA1 8 THR A  31  ASP A  37 -1  N  ARG A  35   O  GLU A  46           
SHEET    3 AA1 8 GLY A  18  VAL A  28 -1  N  VAL A  28   O  THR A  31           
SHEET    4 AA1 8 HIS A   3  ARG A  14 -1  N  THR A  10   O  ILE A  23           
SHEET    5 AA1 8 THR A  94  VAL A 103 -1  O  PHE A  95   N  ALA A  11           
SHEET    6 AA1 8 LEU A 109  TYR A 118 -1  O  LEU A 110   N  ASP A 102           
SHEET    7 AA1 8 ARG A 121  LEU A 126 -1  O  ILE A 124   N  PHE A 116           
SHEET    8 AA1 8 TRP A 133  ALA A 135 -1  O  THR A 134   N  ALA A 125           
SHEET    1 AA2 4 LYS A 186  HIS A 192  0                                        
SHEET    2 AA2 4 ASP A 198  PHE A 208 -1  O  THR A 200   N  HIS A 192           
SHEET    3 AA2 4 PHE A 241  PRO A 250 -1  O  ALA A 245   N  CYS A 203           
SHEET    4 AA2 4 GLU A 229  LEU A 230 -1  N  GLU A 229   O  ALA A 246           
SHEET    1 AA3 4 LYS A 186  HIS A 192  0                                        
SHEET    2 AA3 4 ASP A 198  PHE A 208 -1  O  THR A 200   N  HIS A 192           
SHEET    3 AA3 4 PHE A 241  PRO A 250 -1  O  ALA A 245   N  CYS A 203           
SHEET    4 AA3 4 ARG A 234  PRO A 235 -1  N  ARG A 234   O  GLN A 242           
SHEET    1 AA4 3 THR A 214  LEU A 219  0                                        
SHEET    2 AA4 3 TYR A 257  HIS A 262 -1  O  THR A 258   N  GLN A 218           
SHEET    3 AA4 3 LEU A 270  ARG A 273 -1  O  LEU A 272   N  CYS A 259           
SHEET    1 AA5 4 LYS B   6  SER B  11  0                                        
SHEET    2 AA5 4 ASN B  21  PHE B  30 -1  O  ASN B  24   N  TYR B  10           
SHEET    3 AA5 4 PHE B  62  PHE B  70 -1  O  PHE B  70   N  ASN B  21           
SHEET    4 AA5 4 GLU B  50  HIS B  51 -1  N  GLU B  50   O  TYR B  67           
SHEET    1 AA6 4 LYS B   6  SER B  11  0                                        
SHEET    2 AA6 4 ASN B  21  PHE B  30 -1  O  ASN B  24   N  TYR B  10           
SHEET    3 AA6 4 PHE B  62  PHE B  70 -1  O  PHE B  70   N  ASN B  21           
SHEET    4 AA6 4 SER B  55  PHE B  56 -1  N  SER B  55   O  TYR B  63           
SHEET    1 AA7 4 GLU B  44  ARG B  45  0                                        
SHEET    2 AA7 4 ILE B  35  LYS B  41 -1  N  LYS B  41   O  GLU B  44           
SHEET    3 AA7 4 TYR B  78  HIS B  84 -1  O  ALA B  79   N  LEU B  40           
SHEET    4 AA7 4 LYS B  91  LYS B  94 -1  O  VAL B  93   N  CYS B  80           
SHEET    1 AA8 8 GLU C  46  PRO C  47  0                                        
SHEET    2 AA8 8 THR C  31  ASP C  37 -1  N  ARG C  35   O  GLU C  46           
SHEET    3 AA8 8 GLY C  18  VAL C  28 -1  N  VAL C  28   O  THR C  31           
SHEET    4 AA8 8 HIS C   3  ARG C  14 -1  N  ARG C   6   O  TYR C  27           
SHEET    5 AA8 8 THR C  94  VAL C 103 -1  O  ARG C  97   N  VAL C   9           
SHEET    6 AA8 8 LEU C 109  TYR C 118 -1  O  LEU C 110   N  ASP C 102           
SHEET    7 AA8 8 ARG C 121  LEU C 126 -1  O  LEU C 126   N  HIS C 114           
SHEET    8 AA8 8 TRP C 133  ALA C 135 -1  O  THR C 134   N  ALA C 125           
SHEET    1 AA9 4 LYS C 186  HIS C 192  0                                        
SHEET    2 AA9 4 ASP C 198  PHE C 208 -1  O  TRP C 204   N  HIS C 188           
SHEET    3 AA9 4 PHE C 241  PRO C 250 -1  O  ALA C 245   N  CYS C 203           
SHEET    4 AA9 4 MET C 228  LEU C 230 -1  N  GLU C 229   O  ALA C 246           
SHEET    1 AB1 4 LYS C 186  HIS C 192  0                                        
SHEET    2 AB1 4 ASP C 198  PHE C 208 -1  O  TRP C 204   N  HIS C 188           
SHEET    3 AB1 4 PHE C 241  PRO C 250 -1  O  ALA C 245   N  CYS C 203           
SHEET    4 AB1 4 ARG C 234  PRO C 235 -1  N  ARG C 234   O  GLN C 242           
SHEET    1 AB2 3 ILE C 213  THR C 216  0                                        
SHEET    2 AB2 3 CYS C 259  HIS C 263 -1  O  HIS C 260   N  THR C 216           
SHEET    3 AB2 3 LEU C 270  LEU C 272 -1  O  LEU C 272   N  CYS C 259           
SHEET    1 AB3 4 LYS D   6  SER D  11  0                                        
SHEET    2 AB3 4 ASN D  21  PHE D  30 -1  O  ASN D  24   N  TYR D  10           
SHEET    3 AB3 4 PHE D  62  PHE D  70 -1  O  THR D  68   N  LEU D  23           
SHEET    4 AB3 4 GLU D  50  HIS D  51 -1  N  GLU D  50   O  TYR D  67           
SHEET    1 AB4 4 LYS D   6  SER D  11  0                                        
SHEET    2 AB4 4 ASN D  21  PHE D  30 -1  O  ASN D  24   N  TYR D  10           
SHEET    3 AB4 4 PHE D  62  PHE D  70 -1  O  THR D  68   N  LEU D  23           
SHEET    4 AB4 4 SER D  55  PHE D  56 -1  N  SER D  55   O  TYR D  63           
SHEET    1 AB5 4 GLU D  44  ARG D  45  0                                        
SHEET    2 AB5 4 GLU D  36  LYS D  41 -1  N  LYS D  41   O  GLU D  44           
SHEET    3 AB5 4 TYR D  78  ASN D  83 -1  O  ARG D  81   N  ASP D  38           
SHEET    4 AB5 4 LYS D  91  LYS D  94 -1  O  LYS D  91   N  VAL D  82           
SSBOND   1 CYS A  101    CYS A  164                          1555   1555  2.04  
SSBOND   2 CYS A  203    CYS A  259                          1555   1555  2.02  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.03  
SSBOND   4 CYS C  101    CYS C  164                          1555   1555  2.04  
SSBOND   5 CYS C  203    CYS C  259                          1555   1555  2.02  
SSBOND   6 CYS D   25    CYS D   80                          1555   1555  2.03  
CISPEP   1 TYR A  209    PRO A  210          0         3.83                     
CISPEP   2 HIS B   31    PRO B   32          0         1.53                     
CISPEP   3 TYR C  209    PRO C  210          0         4.09                     
CISPEP   4 HIS D   31    PRO D   32          0         1.25                     
SITE     1 AC1  5 ASP A  29  ASP A  30  HOH A 405  TYR B  63                    
SITE     2 AC1  5 GOL B 101                                                     
SITE     1 AC2  3 VAL A 231  GLU A 232  GLN B   8                               
SITE     1 AC3  3 TYR A 118  ARG A 121  ASP A 137                               
SITE     1 AC4  3 GOL A 301  LYS B  58  HOH B 211                               
SITE     1 AC5  4 THR C  31  THR C 178  TYR C 209  GLY C 239                    
SITE     1 AC6  6 ARG A 273  GLU C 173  LEU C 174  ASN C 176                    
SITE     2 AC6  6 GLU C 177  HOH C 429                                          
SITE     1 AC7  4 HIS C 262  HIS C 263  LEU C 266  PRO C 269                    
SITE     1 AC8  4 ALA A 150  ALA C 150  GLY C 151  LEU Q   5                    
SITE     1 AC9  2 ARG C 202  ASP D  96                                          
SITE     1 AD1  4 GLY C 252  LYS C 253  GLU C 254  GLN C 255                    
SITE     1 AD2  5 ARG C 234  GLN D   8  VAL D   9  MET D  99                    
SITE     2 AD2  5 HOH D 202                                                     
CRYST1   46.635   88.816  110.754  90.00  89.99  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021443  0.000000 -0.000005        0.00000                         
SCALE2      0.000000  0.011259  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009029        0.00000                         
TER    2252      PRO A 276                                                      
TER    3086      MET B  99                                                      
TER    3156      MET P   9                                                      
TER    5395      PRO C 276                                                      
TER    6229      MET D  99                                                      
TER    6299      MET Q   9                                                      
MASTER      341    0   11   14   62    0   14    6 6619    6   62   62          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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