Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 6uh8-pdb

Name Class
6uh8-pdb
HEADER    HYDROLASE                               27-SEP-19   6UH8              
TITLE     CRYSTAL STRUCTURE OF DAD2 N242I MUTANT                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DECREASED APICAL DOMINANCE 2;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: DAD2;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PETUNIA HYBRIDA;                                
SOURCE   3 ORGANISM_COMMON: PETUNIA;                                            
SOURCE   4 ORGANISM_TAXID: 4102;                                                
SOURCE   5 GENE: DAD2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA GAMI 2                             
KEYWDS    STRIGOLACTONE RECEPTOR, HYDROLASE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.SHARMA,C.HAMIAUX,K.C.SNOWDEN                                        
REVDAT   1   26-FEB-20 6UH8    0                                                
JRNL        AUTH   H.W.LEE,P.SHARMA,B.J.JANSSEN,R.S.M.DRUMMOND,Z.LUO,C.HAMIAUX, 
JRNL        AUTH 2 T.COLLIER,J.R.ALLISON,R.D.NEWCOMB,K.C.SNOWDEN                
JRNL        TITL   FLEXIBILITY OF THE PETUNIA STRIGOLACTONE RECEPTOR DAD2       
JRNL        TITL 2 PROMOTES ITS INTERACTION WITH SIGNALING PARTNERS             
JRNL        REF    J.BIOL.CHEM.                               2020              
JRNL        REFN                   ESSN 1083-351X                               
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.HAMIAUX,R.S.DRUMMOND,B.J.JANSSEN,S.E.LEDGER,J.M.COONEY,    
REMARK   1  AUTH 2 R.D.NEWCOMB,K.C.SNOWDEN                                      
REMARK   1  TITL   DAD2 IS AN ALPHA/BETA HYDROLASE LIKELY TO BE INVOLVED IN THE 
REMARK   1  TITL 2 PERCEPTION OF THE PLANT BRANCHING HORMONE, STRIGOLACTONE.    
REMARK   1  REF    CURR. BIOL.                   V.  22  2032 2012              
REMARK   1  REFN                   ISSN 1879-0445                               
REMARK   1  PMID   22959345                                                     
REMARK   1  DOI    10.1016/J.CUB.2012.08.007                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.58 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.81                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 128380                         
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) : 0.140                           
REMARK   3   R VALUE            (WORKING SET) : 0.138                           
REMARK   3   FREE R VALUE                     : 0.165                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9970                            
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) : 1.58                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.62                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9482                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 709                          
REMARK   3   BIN FREE R VALUE                    : 0.3020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4142                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 440                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.86                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.48000                                              
REMARK   3    B22 (A**2) : 1.48000                                              
REMARK   3    B33 (A**2) : -4.81000                                             
REMARK   3    B12 (A**2) : 0.74000                                              
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): 0.053         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.052         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.042         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.854         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.978                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.972                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4459 ; 0.013 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  4144 ; 0.002 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6085 ; 1.740 ; 1.629       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9544 ; 1.569 ; 1.570       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   560 ; 5.835 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   247 ;26.711 ;20.324       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   696 ;11.974 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    41 ;21.060 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   555 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5090 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1045 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  8603 ; 3.782 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   313 ;41.638 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  8623 ;25.257 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     2    265       B     2    265    8537 0.100 0.050     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   265                          
REMARK   3    RESIDUE RANGE :   A   301        A   301                          
REMARK   3    ORIGIN FOR THE GROUP (A):   37.605    3.173   -4.278              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0030 T22:   0.0007                                     
REMARK   3      T33:   0.0873 T12:   0.0004                                     
REMARK   3      T13:  -0.0000 T23:   0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0007 L22:   0.0341                                     
REMARK   3      L33:   0.0017 L12:   0.0047                                     
REMARK   3      L13:  -0.0010 L23:  -0.0076                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0009 S12:   0.0000 S13:   0.0007                       
REMARK   3      S21:   0.0019 S22:  -0.0003 S23:   0.0077                       
REMARK   3      S31:  -0.0003 S32:   0.0001 S33:  -0.0007                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B   265                          
REMARK   3    RESIDUE RANGE :   B   301        B   301                          
REMARK   3    ORIGIN FOR THE GROUP (A):   53.193   35.660  -10.737              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0000 T22:   0.0010                                     
REMARK   3      T33:   0.0820 T12:  -0.0000                                     
REMARK   3      T13:   0.0003 T23:   0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0545 L22:   0.0147                                     
REMARK   3      L33:   0.0129 L12:  -0.0065                                     
REMARK   3      L13:   0.0096 L23:   0.0072                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0000 S12:   0.0072 S13:   0.0048                       
REMARK   3      S21:   0.0000 S22:  -0.0014 S23:   0.0011                       
REMARK   3      S31:   0.0001 S32:   0.0006 S33:   0.0014                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.70                                          
REMARK   3   SHRINKAGE RADIUS   : 0.70                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 6UH8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000244603.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-17                          
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               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.953736                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.31                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 138411                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.580                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.860                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 19.10                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 20.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 18.90                              
REMARK 200  R MERGE FOR SHELL          (I) : 2.18800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   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 2.7.17                                         
REMARK 200 STARTING MODEL: 4DNP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6.5 1.58-1.72 M MGSO4,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.50933            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       33.25467            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       49.88200            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       16.62733            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       83.13667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     HIS A   266                                                      
REMARK 465     ARG A   267                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     HIS B   266                                                      
REMARK 465     ARG B   267                                                      
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 B   515     O    HOH B   599              2.05            
REMARK 500   OE1  GLN A   258     O    HOH A   401              2.13            
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    GLY A   2   N     GLY A   2   CA      0.100                       
REMARK 500    ARG A 108   CD    ARG A 108   NE     -0.145                       
REMARK 500    GLY B   2   N     GLY B   2   CA      0.143                       
REMARK 500    GLU B 173   CD    GLU B 173   OE2     0.077                       
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  36   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A 108   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG A 108   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 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    SER A  96     -119.70     43.40                                   
REMARK 500    ARG A 124      121.72   -172.03                                   
REMARK 500    ASN A 150       92.32   -160.82                                   
REMARK 500    ARG A 216       87.73   -157.07                                   
REMARK 500    ALA A 252       53.05   -140.50                                   
REMARK 500    SER B  96     -120.39     44.74                                   
REMARK 500    ARG B 124      121.16   -174.70                                   
REMARK 500    ASN B 150       98.49   -167.26                                   
REMARK 500    ALA B 252       57.06   -144.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ARG B 216        -14.98                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 598        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH B 642        DISTANCE =  6.01 ANGSTROMS                       
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                              MG B 304  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B  10   OD1                                                    
REMARK 620 2 HOH B 421   O    94.5                                              
REMARK 620 3 HOH B 473   O    78.7  93.3                                        
REMARK 620 4 HOH B 550   O    87.0 175.9  90.7                                  
REMARK 620 5 HOH B 571   O    94.3  85.7 172.9  90.4                            
REMARK 620 6 HOH B 629   O   174.1  89.9  97.1  88.8  89.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  72   OD2                                                    
REMARK 620 2 HOH A 419   O    89.3                                              
REMARK 620 3 HOH A 431   O    89.8  84.2                                        
REMARK 620 4 HOH A 569   O   174.1  96.0  93.4                                  
REMARK 620 5 HOH B 420   O    89.1 175.0  91.1  85.8                            
REMARK 620 6 HOH B 429   O    88.8  89.6 173.7  88.6  95.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 408   O                                                      
REMARK 620 2 HOH A 413   O    84.9                                              
REMARK 620 3 HOH A 588   O    87.1  93.3                                        
REMARK 620 4 HOH B 613   O    89.0 173.8  85.6                                  
REMARK 620 5 HOH B 415   O    93.4  86.4 179.4  94.7                            
REMARK 620 6 HOH B 408   O   171.3 101.6  98.3  84.5  81.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 472   O                                                      
REMARK 620 2 HOH B 639   O    90.9                                              
REMARK 620 3 HOH B 477   O    93.6 175.5                                        
REMARK 620 4 HOH B 615   O    94.2  95.9  83.5                                  
REMARK 620 5 HOH B 507   O    89.1  90.3  90.1 173.0                            
REMARK 620 6 HOH B 633   O   177.3  86.4  89.1  85.8  91.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 305  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 587   O                                                      
REMARK 620 2 HOH B 642   O   101.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 306  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 515   O                                                      
REMARK 620 2 HOH B 422   O    60.6                                              
REMARK 620 3 HOH B 599   O    44.8  53.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 307  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 450   O                                                      
REMARK 620 2 HOH B 619   O    87.6                                              
REMARK 620 3 HOH B 623   O   165.7  78.9                                        
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 MES A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 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 MES B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 306                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 307                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 311                 
DBREF  6UH8 A   -1   267  UNP    L7MTK5   L7MTK5_PETHY     1    269             
DBREF  6UH8 B   -1   267  UNP    L7MTK5   L7MTK5_PETHY     1    269             
SEQADV 6UH8 GLN A   89  UNP  L7MTK5    CYS    91 ENGINEERED MUTATION            
SEQADV 6UH8 ILE A  242  UNP  L7MTK5    ASN   244 ENGINEERED MUTATION            
SEQADV 6UH8 GLN B   89  UNP  L7MTK5    CYS    91 ENGINEERED MUTATION            
SEQADV 6UH8 ILE B  242  UNP  L7MTK5    ASN   244 ENGINEERED MUTATION            
SEQRES   1 A  269  GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL          
SEQRES   2 A  269  ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA          
SEQRES   3 A  269  HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE          
SEQRES   4 A  269  LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR          
SEQRES   5 A  269  ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE          
SEQRES   6 A  269  ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP          
SEQRES   7 A  269  ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP GLN          
SEQRES   8 A  269  CYS ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY          
SEQRES   9 A  269  ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS          
SEQRES  10 A  269  LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP          
SEQRES  11 A  269  GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU          
SEQRES  12 A  269  LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP          
SEQRES  13 A  269  VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL          
SEQRES  14 A  269  PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN          
SEQRES  15 A  269  MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL          
SEQRES  16 A  269  PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS          
SEQRES  17 A  269  VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER          
SEQRES  18 A  269  VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU          
SEQRES  19 A  269  GLY GLY LYS ASN THR VAL HIS TRP LEU ILE ILE GLU GLY          
SEQRES  20 A  269  HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN          
SEQRES  21 A  269  GLU LEU ARG ARG ALA LEU SER HIS ARG                          
SEQRES   1 B  269  GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL          
SEQRES   2 B  269  ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA          
SEQRES   3 B  269  HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE          
SEQRES   4 B  269  LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR          
SEQRES   5 B  269  ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE          
SEQRES   6 B  269  ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP          
SEQRES   7 B  269  ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP GLN          
SEQRES   8 B  269  CYS ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY          
SEQRES   9 B  269  ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS          
SEQRES  10 B  269  LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP          
SEQRES  11 B  269  GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU          
SEQRES  12 B  269  LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP          
SEQRES  13 B  269  VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL          
SEQRES  14 B  269  PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN          
SEQRES  15 B  269  MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL          
SEQRES  16 B  269  PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS          
SEQRES  17 B  269  VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER          
SEQRES  18 B  269  VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU          
SEQRES  19 B  269  GLY GLY LYS ASN THR VAL HIS TRP LEU ILE ILE GLU GLY          
SEQRES  20 B  269  HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN          
SEQRES  21 B  269  GLU LEU ARG ARG ALA LEU SER HIS ARG                          
HET    MES  A 301      12                                                       
HET     MG  A 302       1                                                       
HET    GOL  A 303       6                                                       
HET    MES  B 301      12                                                       
HET     MG  B 302       1                                                       
HET     MG  B 303       1                                                       
HET     MG  B 304       1                                                       
HET     MG  B 305       1                                                       
HET     MG  B 306       1                                                       
HET     MG  B 307       1                                                       
HET    SO4  B 308       5                                                       
HET    SO4  B 309       5                                                       
HET    SO4  B 310       5                                                       
HET    GOL  B 311       6                                                       
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  MES    2(C6 H13 N O4 S)                                             
FORMUL   4   MG    7(MG 2+)                                                     
FORMUL   5  GOL    2(C3 H8 O3)                                                  
FORMUL  13  SO4    3(O4 S 2-)                                                   
FORMUL  17  HOH   *440(H2 O)                                                    
HELIX    1 AA1 GLY A    2  LEU A    9  1                                   8    
HELIX    2 AA2 ASP A   30  ASN A   35  5                                   6    
HELIX    3 AA3 ILE A   37  LEU A   42  5                                   6    
HELIX    4 AA4 ASN A   59  PHE A   63  5                                   5    
HELIX    5 AA5 LEU A   71  LEU A   85  1                                  15    
HELIX    6 AA6 SER A   96  ARG A  109  1                                  14    
HELIX    7 AA7 GLU A  136  ASN A  150  1                                  15    
HELIX    8 AA8 ASN A  150  GLY A  164  1                                  15    
HELIX    9 AA9 VAL A  167  MET A  181  1                                  15    
HELIX   10 AB1 ARG A  182  ASN A  195  1                                  14    
HELIX   11 AB2 MET A  198  VAL A  205  5                                   8    
HELIX   12 AB3 PRO A  221  LEU A  232  1                                  12    
HELIX   13 AB4 LEU A  247  ALA A  252  1                                   6    
HELIX   14 AB5 ALA A  252  SER A  265  1                                  14    
HELIX   15 AB6 GLN B    3  LEU B    9  1                                   7    
HELIX   16 AB7 ASP B   30  ASN B   35  5                                   6    
HELIX   17 AB8 ILE B   37  PHE B   41  5                                   5    
HELIX   18 AB9 ASN B   59  PHE B   63  5                                   5    
HELIX   19 AC1 LEU B   71  LEU B   85  1                                  15    
HELIX   20 AC2 SER B   96  ARG B  109  1                                  14    
HELIX   21 AC3 GLU B  136  ASN B  150  1                                  15    
HELIX   22 AC4 ASN B  150  GLY B  164  1                                  15    
HELIX   23 AC5 VAL B  167  MET B  181  1                                  15    
HELIX   24 AC6 ARG B  182  ASN B  195  1                                  14    
HELIX   25 AC7 MET B  198  VAL B  205  5                                   8    
HELIX   26 AC8 PRO B  221  LEU B  232  1                                  12    
HELIX   27 AC9 LEU B  247  ALA B  252  1                                   6    
HELIX   28 AD1 ALA B  252  SER B  265  1                                  14    
SHEET    1 AA1 7 ARG A  12  VAL A  14  0                                        
SHEET    2 AA1 7 TYR A  45  TYR A  50 -1  O  VAL A  47   N  VAL A  14           
SHEET    3 AA1 7 ARG A  19  ALA A  24  1  N  LEU A  21   O  VAL A  48           
SHEET    4 AA1 7 CYS A  90  HIS A  95  1  O  VAL A  93   N  ALA A  24           
SHEET    5 AA1 7 PHE A 113  ILE A 119  1  O  ILE A 117   N  TYR A  92           
SHEET    6 AA1 7 CYS A 209  ARG A 216  1  O  PHE A 212   N  LEU A 118           
SHEET    7 AA1 7 ASN A 236  GLU A 244  1  O  HIS A 239   N  ILE A 211           
SHEET    1 AA2 7 ARG B  12  VAL B  14  0                                        
SHEET    2 AA2 7 TYR B  45  TYR B  50 -1  O  VAL B  47   N  VAL B  14           
SHEET    3 AA2 7 ARG B  19  ALA B  24  1  N  LEU B  21   O  VAL B  48           
SHEET    4 AA2 7 CYS B  90  HIS B  95  1  O  VAL B  93   N  ALA B  24           
SHEET    5 AA2 7 PHE B 113  ILE B 119  1  O  ILE B 117   N  TYR B  92           
SHEET    6 AA2 7 CYS B 209  THR B 214  1  O  PHE B 212   N  LEU B 118           
SHEET    7 AA2 7 ASN B 236  LEU B 241  1  O  HIS B 239   N  ILE B 211           
LINK         OD1 ASN B  10                MG    MG B 304     1555   1555  2.06  
LINK         OD2 ASP B  72                MG    MG B 303     1555   1555  2.08  
LINK        MG    MG A 302                 O   HOH A 408     1555   1555  2.32  
LINK        MG    MG A 302                 O   HOH A 413     1555   1555  1.92  
LINK        MG    MG A 302                 O   HOH A 588     1555   1555  1.89  
LINK        MG    MG A 302                 O   HOH B 613     1555   1555  1.97  
LINK        MG    MG A 302                 O   HOH B 415     1555   1555  2.08  
LINK        MG    MG A 302                 O   HOH B 408     1555   1555  2.26  
LINK        MG    MG B 302                 O   HOH B 472     1555   1555  2.11  
LINK        MG    MG B 302                 O   HOH B 639     1555   1555  2.00  
LINK        MG    MG B 302                 O   HOH B 477     1555   1555  2.01  
LINK        MG    MG B 302                 O   HOH B 615     1555   1555  2.06  
LINK        MG    MG B 302                 O   HOH B 507     1555   1555  2.10  
LINK        MG    MG B 302                 O   HOH B 633     1555   1555  2.17  
LINK        MG    MG B 303                 O   HOH A 419     1555   1555  2.23  
LINK        MG    MG B 303                 O   HOH A 431     1555   1555  2.11  
LINK        MG    MG B 303                 O   HOH A 569     1555   1555  2.07  
LINK        MG    MG B 303                 O   HOH B 420     1555   1555  2.22  
LINK        MG    MG B 303                 O   HOH B 429     1555   1555  2.05  
LINK        MG    MG B 304                 O   HOH B 421     1555   1555  2.10  
LINK        MG    MG B 304                 O   HOH B 473     1555   1555  2.21  
LINK        MG    MG B 304                 O   HOH B 550     1555   1555  2.17  
LINK        MG    MG B 304                 O   HOH B 571     1555   1555  2.00  
LINK        MG    MG B 304                 O   HOH B 629     1555   1555  2.15  
LINK        MG    MG B 305                 O   HOH B 587     1555   1555  2.11  
LINK        MG    MG B 305                 O   HOH B 642     1555   1555  2.35  
LINK        MG    MG B 306                 O   HOH B 515     1555   1555  2.91  
LINK        MG    MG B 306                 O   HOH B 422     1555   1555  2.75  
LINK        MG    MG B 306                 O   HOH B 599     1555   1555  2.04  
LINK        MG    MG B 307                 O   HOH B 450     1555   1555  2.25  
LINK        MG    MG B 307                 O   HOH B 619     1555   1555  2.34  
LINK        MG    MG B 307                 O   HOH B 623     1555   1555  1.99  
SITE     1 AC1 11 SER A  96  PHE A 125  PHE A 135  PHE A 158                    
SITE     2 AC1 11 VAL A 193  PHE A 194  SER A 219  HIS A 246                    
SITE     3 AC1 11 HOH A 433  HOH A 445  HOH A 531                               
SITE     1 AC2  6 HOH A 408  HOH A 413  HOH A 588  HOH B 408                    
SITE     2 AC2  6 HOH B 415  HOH B 613                                          
SITE     1 AC3  6 TYR A 131  HIS A 132  SER A 223  VAL A 224                    
SITE     2 AC3  6 TYR A 227  HOH A 493                                          
SITE     1 AC4 10 SER B  96  PHE B 125  PHE B 135  PHE B 158                    
SITE     2 AC4 10 PHE B 194  SER B 219  HIS B 246  HOH B 406                    
SITE     3 AC4 10 HOH B 460  HOH B 509                                          
SITE     1 AC5  6 HOH B 472  HOH B 477  HOH B 507  HOH B 615                    
SITE     2 AC5  6 HOH B 633  HOH B 639                                          
SITE     1 AC6  6 HOH A 419  HOH A 431  HOH A 569  ASP B  72                    
SITE     2 AC6  6 HOH B 420  HOH B 429                                          
SITE     1 AC7  6 ASN B  10  HOH B 421  HOH B 473  HOH B 550                    
SITE     2 AC7  6 HOH B 571  HOH B 629                                          
SITE     1 AC8  2 HOH B 587  HOH B 642                                          
SITE     1 AC9  3 HOH B 422  HOH B 515  HOH B 599                               
SITE     1 AD1  4 HIS B 231  HOH B 450  HOH B 619  HOH B 623                    
SITE     1 AD2  7 PRO B 221  ALA B 222  SER B 223  HOH B 477                    
SITE     2 AD2  7 HOH B 507  HOH B 516  HOH B 521                               
SITE     1 AD3  4 HOH A 417  ARG B 108  ARG B 109  HOH B 537                    
SITE     1 AD4  6 ARG B  36  ALA B 252  PRO B 253  THR B 254                    
SITE     2 AD4  6 HOH B 404  HOH B 481                                          
SITE     1 AD5  5 GLU B  18  TYR B 131  HIS B 132  SER B 223                    
SITE     2 AD5  5 VAL B 224                                                     
CRYST1  133.736  133.736   99.764  90.00  90.00 120.00 P 65         12          
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      0.007477  0.004317  0.000000        0.00000                         
SCALE2      0.000000  0.008634  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010024        0.00000                         
TER    2176      SER A 265                                                      
TER    4296      SER B 265                                                      
MASTER      564    0   14   28   14    0   26    6 4640    2   94   42          
END                                                                             

Send your questions or comments to :
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
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer