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LongText Report for: 3QH4-pdb

Name Class
3QH4-pdb
HEADER    HYDROLASE                               25-JAN-11   3QH4              
TITLE     CRYSTAL STRUCTURE OF ESTERASE LIPW FROM MYCOBACTERIUM MARINUM         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ESTERASE LIPW;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM MARINUM;                          
SOURCE   3 ORGANISM_TAXID: 216594;                                              
SOURCE   4 STRAIN: ATCC BAA-535 / M;                                            
SOURCE   5 GENE: LIPW, MMAR_0404;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: AVA0421                                   
KEYWDS    STRUCTURAL GENOMICS, SSGCID, SEATTLE STRUCTURAL GENOMICS CENTER FOR   
KEYWDS   2 INFECTIOUS DISEASE, MYCOBACTERIUM, TUBERCULOSIS, MARINUM, ORTHOLOG,  
KEYWDS   3 LIPW, ESTERASE, HEROIN ESTERASE, MULTIDRUG RESISTANCE, TB, HYDROLASE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   1   09-FEB-11 3QH4    0                                                
JRNL        AUTH   T.E.EDWARDS,J.ABENDROTH,                                     
JRNL        AUTH 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE    
JRNL        AUTH 3 (SSGCID)                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF ESTERASE LIPW FROM MYCOBACTERIUM        
JRNL        TITL 2 MARINUM                                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 30076                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.147                           
REMARK   3   R VALUE            (WORKING SET) : 0.144                           
REMARK   3   FREE R VALUE                     : 0.188                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1515                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.79                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1967                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1650                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 122                          
REMARK   3   BIN FREE R VALUE                    : 0.2090                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2336                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 419                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.91                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.17000                                             
REMARK   3    B22 (A**2) : 0.45000                                              
REMARK   3    B33 (A**2) : -0.28000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.105         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.057         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.834         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2417 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3317 ; 1.400 ; 1.961       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   323 ; 5.577 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;32.432 ;22.212       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   336 ;11.076 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;18.718 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   380 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1908 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1585 ; 0.733 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2534 ; 1.287 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   832 ; 2.101 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   778 ; 3.308 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   -10        A  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  61.8631  13.3035  36.1235              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0143 T22:   0.0077                                     
REMARK   3      T33:   0.0074 T12:   0.0059                                     
REMARK   3      T13:   0.0018 T23:  -0.0027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3364 L22:   0.1920                                     
REMARK   3      L33:   0.2835 L12:  -0.1242                                     
REMARK   3      L13:  -0.0166 L23:   0.0868                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0048 S12:   0.0211 S13:  -0.0036                       
REMARK   3      S21:  -0.0027 S22:  -0.0213 S23:  -0.0021                       
REMARK   3      S31:  -0.0426 S32:  -0.0292 S33:   0.0165                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : RESIDUAL ONLY                                  
REMARK   4                                                                      
REMARK   4 3QH4 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063637.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JAN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30172                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.03800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 21.7600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.07300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 9.130                              
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: PDB ENTRY 1LZK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 55.6 MG/ML, 0.2 M MGCL2,      
REMARK 280  0.1 M TRIS, 20 % PEG 6000, CRYO-PROTECTED WITH 25 % ETHYLENE        
REMARK 280  GLYCOL, PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289 K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.63500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.49500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.63500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.49500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     GLY A    -1                                                      
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     MET A   1    CG   SD   CE                                        
REMARK 470     GLU A  28    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  42    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  43    CG   CD   OE1  OE2                                  
REMARK 470     THR A  62    OG1  CG2                                            
REMARK 470     ARG A  67    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 154    CG   CD   NE   CZ   NH1  NH2                        
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    PHE A  92       -8.66     68.85                                   
REMARK 500    ASN A  96     -161.18   -167.32                                   
REMARK 500    PRO A 129       30.19    -99.87                                   
REMARK 500    SER A 162     -128.64     60.20                                   
REMARK 500    GLN A 190       54.79     34.23                                   
REMARK 500    PHE A 204       46.29   -100.40                                   
REMARK 500    ALA A 206       26.48   -148.29                                   
REMARK 500    ALA A 209      -54.82     75.65                                   
REMARK 500    ILE A 253       68.06   -101.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: MYMAA.00277.C   RELATED DB: TARGETDB                     
DBREF  3QH4 A    3   313  UNP    B2HLX2   B2HLX2_MYCMM     2    312             
SEQADV 3QH4 GLY A   -3  UNP  B2HLX2              EXPRESSION TAG                 
SEQADV 3QH4 PRO A   -2  UNP  B2HLX2              EXPRESSION TAG                 
SEQADV 3QH4 GLY A   -1  UNP  B2HLX2              EXPRESSION TAG                 
SEQADV 3QH4 SER A    0  UNP  B2HLX2              EXPRESSION TAG                 
SEQADV 3QH4 MET A    1  UNP  B2HLX2              EXPRESSION TAG                 
SEQADV 3QH4 VAL A    2  UNP  B2HLX2              EXPRESSION TAG                 
SEQRES   1 A  317  GLY PRO GLY SER MET VAL THR GLN PRO GLU ALA VAL ASP          
SEQRES   2 A  317  ARG LEU ASP PRO LEU LEU ARG ALA VAL ALA THR ALA ARG          
SEQRES   3 A  317  ILE ASP PHE THR ALA GLU SER ILE LEU THR ILE ARG GLU          
SEQRES   4 A  317  SER MET ASN GLN ARG ARG ARG GLU ALA ALA ALA THR GLU          
SEQRES   5 A  317  THR ALA ALA ALA GLY VAL ALA VAL ALA ASP ASP VAL VAL          
SEQRES   6 A  317  THR GLY GLU ALA GLY ARG PRO VAL PRO VAL ARG ILE TYR          
SEQRES   7 A  317  ARG ALA ALA PRO THR PRO ALA PRO VAL VAL VAL TYR CYS          
SEQRES   8 A  317  HIS ALA GLY GLY PHE ALA LEU GLY ASN LEU ASP THR ASP          
SEQRES   9 A  317  HIS ARG GLN CYS LEU GLU LEU ALA ARG ARG ALA ARG CYS          
SEQRES  10 A  317  ALA VAL VAL SER VAL ASP TYR ARG LEU ALA PRO GLU HIS          
SEQRES  11 A  317  PRO TYR PRO ALA ALA LEU HIS ASP ALA ILE GLU VAL LEU          
SEQRES  12 A  317  THR TRP VAL VAL GLY ASN ALA THR ARG LEU GLY PHE ASP          
SEQRES  13 A  317  ALA ARG ARG LEU ALA VAL ALA GLY SER SER ALA GLY ALA          
SEQRES  14 A  317  THR LEU ALA ALA GLY LEU ALA HIS GLY ALA ALA ASP GLY          
SEQRES  15 A  317  SER LEU PRO PRO VAL ILE PHE GLN LEU LEU HIS GLN PRO          
SEQRES  16 A  317  VAL LEU ASP ASP ARG PRO THR ALA SER ARG SER GLU PHE          
SEQRES  17 A  317  ARG ALA THR PRO ALA PHE ASP GLY GLU ALA ALA SER LEU          
SEQRES  18 A  317  MET TRP ARG HIS TYR LEU ALA GLY GLN THR PRO SER PRO          
SEQRES  19 A  317  GLU SER VAL PRO GLY ARG ARG GLY GLN LEU ALA GLY LEU          
SEQRES  20 A  317  PRO ALA THR LEU ILE THR CYS GLY GLU ILE ASP PRO PHE          
SEQRES  21 A  317  ARG ASP GLU VAL LEU ASP TYR ALA GLN ARG LEU LEU GLY          
SEQRES  22 A  317  ALA GLY VAL SER THR GLU LEU HIS ILE PHE PRO ARG ALA          
SEQRES  23 A  317  CYS HIS GLY PHE ASP SER LEU LEU PRO GLU TRP THR THR          
SEQRES  24 A  317  SER GLN ARG LEU PHE ALA MET GLN GLY HIS ALA LEU ALA          
SEQRES  25 A  317  ASP ALA PHE TYR PRO                                          
FORMUL   2  HOH   *419(H2 O)                                                    
HELIX    1   1 ALA A    7  LEU A   11  5                                   5    
HELIX    2   2 ASP A   12  ALA A   17  1                                   6    
HELIX    3   3 THR A   26  GLY A   53  1                                  28    
HELIX    4   4 ASP A  100  ARG A  112  1                                  13    
HELIX    5   5 PRO A  129  ASN A  145  1                                  17    
HELIX    6   6 ASN A  145  GLY A  150  1                                   6    
HELIX    7   7 SER A  162  ASP A  177  1                                  16    
HELIX    8   8 THR A  198  PHE A  204  1                                   7    
HELIX    9   9 ASP A  211  ALA A  224  1                                  14    
HELIX   10  10 VAL A  233  ARG A  237  5                                   5    
HELIX   11  11 PHE A  256  ALA A  270  1                                  15    
HELIX   12  12 GLY A  285  LEU A  290  1                                   6    
HELIX   13  13 TRP A  293  TYR A  312  1                                  20    
SHEET    1   A 8 ALA A  55  THR A  62  0                                        
SHEET    2   A 8 PRO A  68  ARG A  75 -1  O  VAL A  69   N  VAL A  61           
SHEET    3   A 8 ALA A 114  VAL A 118 -1  O  VAL A 115   N  TYR A  74           
SHEET    4   A 8 ALA A  81  CYS A  87  1  N  VAL A  84   O  VAL A 116           
SHEET    5   A 8 PHE A 151  SER A 161  1  O  ASP A 152   N  ALA A  81           
SHEET    6   A 8 PHE A 185  HIS A 189  1  O  HIS A 189   N  GLY A 160           
SHEET    7   A 8 THR A 246  ILE A 253  1  O  LEU A 247   N  LEU A 188           
SHEET    8   A 8 THR A 274  CYS A 283  1  O  GLU A 275   N  ILE A 248           
CISPEP   1 THR A   79    PRO A   80          0        -8.56                     
CISPEP   2 ALA A  123    PRO A  124          0        -0.34                     
CISPEP   3 TYR A  128    PRO A  129          0         3.38                     
CRYST1   73.270   86.990   46.190  90.00  90.00  90.00 P 21 21 2     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      0.013648  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011496  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021650        0.00000                         
TER    2357      PRO A 313                                                      
MASTER      301    0    0   13    8    0    0    6 2755    1    0   25          
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.
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