Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 3HLK-pdb

Name Class
3HLK-pdb
HEADER    HYDROLASE                               27-MAY-09   3HLK              
TITLE     CRYSTAL STRUCTURE OF HUMAN MITOCHONDRIAL ACYL-COA                     
TITLE    2 THIOESTERASE (ACOT2)                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACYL-COENZYME A THIOESTERASE 2, MITOCHONDRIAL;             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ACYL-COA THIOESTERASE 2, ACYL-COENZYME A THIOESTER          
COMPND   5 HYDROLASE 2A, LONG-CHAIN ACYL-COA THIOESTERASE 2, ZAP128,            
COMPND   6 CTE-IA;                                                              
COMPND   7 EC: 3.1.2.2;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ACOT2, PTE2, PTE2A;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ALPHA/BETA HYDROLASE, ALTERNATIVE SPLICING, HYDROLASE,                
KEYWDS   2 MITOCHONDRION, POLYMORPHISM, SERINE ESTERASE, TRANSIT                
KEYWDS   3 PEPTIDE                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.R.MANDEL,B.TWEEL,L.TONG                                             
REVDAT   1   23-JUN-09 3HLK    0                                                
JRNL        AUTH   C.R.MANDEL,B.TWEEL,L.TONG                                    
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN MITOCHONDRIAL ACYL-COA            
JRNL        TITL 2 THIOESTERASE (ACOT2)                                         
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.                2009              
JRNL        REFN                   ESSN 1090-2104                               
JRNL        PMID   19497300                                                     
JRNL        DOI    10.1016/J.BBRC.2009.05.122                                   
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0003                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 62312                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3310                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4262                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.57                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2030                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 215                          
REMARK   3   BIN FREE R VALUE                    : 0.2420                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6388                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 442                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.50000                                              
REMARK   3    B22 (A**2) : 0.50000                                              
REMARK   3    B33 (A**2) : -0.75000                                             
REMARK   3    B12 (A**2) : 0.25000                                              
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): 0.187         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.170         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.119         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.697         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6557 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8903 ; 1.249 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   815 ; 5.939 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   288 ;31.446 ;22.500       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1065 ;15.743 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    62 ;17.690 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   957 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5066 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2811 ; 0.196 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4344 ; 0.307 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   463 ; 0.144 ; 0.200       
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):    43 ; 0.277 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    22 ; 0.194 ; 0.200       
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):  4219 ; 0.800 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6558 ; 1.318 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2664 ; 1.734 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2345 ; 2.731 ; 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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3HLK COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053282.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-DEC-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67802                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 21.0148                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.799                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHAKE&BAKE THEN SOLVE/RESOLVE                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 300 MM AMMONIUM CITRATE, 22%             
REMARK 280  PEG3350, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE         
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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       43.98333            
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       87.96667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       87.96667            
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       43.98333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 538  LIES ON A SPECIAL POSITION.                          
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    46                                                      
REMARK 465     SER A    47                                                      
REMARK 465     PRO A    48                                                      
REMARK 465     GLN A    49                                                      
REMARK 465     LEU A    50                                                      
REMARK 465     ARG A    51                                                      
REMARK 465     GLN A    52                                                      
REMARK 465     VAL A    53                                                      
REMARK 465     GLY A    54                                                      
REMARK 465     GLN A    55                                                      
REMARK 465     ILE A    56                                                      
REMARK 465     ILE A    57                                                      
REMARK 465     LEU A   436                                                      
REMARK 465     HIS A   437                                                      
REMARK 465     ALA A   438                                                      
REMARK 465     LEU A   439                                                      
REMARK 465     VAL A   440                                                      
REMARK 465     GLY A   441                                                      
REMARK 465     SER A   442                                                      
REMARK 465     GLY A   473                                                      
REMARK 465     GLY A   474                                                      
REMARK 465     HIS A   475                                                      
REMARK 465     GLU A   476                                                      
REMARK 465     GLY A   477                                                      
REMARK 465     THR A   478                                                      
REMARK 465     ILE A   479                                                      
REMARK 465     PRO A   480                                                      
REMARK 465     SER A   481                                                      
REMARK 465     LYS A   482                                                      
REMARK 465     VAL A   483                                                      
REMARK 465     LEU A   484                                                      
REMARK 465     GLU A   485                                                      
REMARK 465     HIS A   486                                                      
REMARK 465     HIS A   487                                                      
REMARK 465     HIS A   488                                                      
REMARK 465     HIS A   489                                                      
REMARK 465     HIS A   490                                                      
REMARK 465     HIS A   491                                                      
REMARK 465     GLY B    46                                                      
REMARK 465     SER B    47                                                      
REMARK 465     PRO B    48                                                      
REMARK 465     GLN B    49                                                      
REMARK 465     LEU B    50                                                      
REMARK 465     ARG B    51                                                      
REMARK 465     GLN B    52                                                      
REMARK 465     VAL B    53                                                      
REMARK 465     GLY B    54                                                      
REMARK 465     GLN B    55                                                      
REMARK 465     ILE B    56                                                      
REMARK 465     HIS B   437                                                      
REMARK 465     ALA B   438                                                      
REMARK 465     LEU B   439                                                      
REMARK 465     VAL B   440                                                      
REMARK 465     GLY B   441                                                      
REMARK 465     GLY B   473                                                      
REMARK 465     GLY B   474                                                      
REMARK 465     HIS B   475                                                      
REMARK 465     GLU B   476                                                      
REMARK 465     GLY B   477                                                      
REMARK 465     THR B   478                                                      
REMARK 465     ILE B   479                                                      
REMARK 465     PRO B   480                                                      
REMARK 465     SER B   481                                                      
REMARK 465     LYS B   482                                                      
REMARK 465     VAL B   483                                                      
REMARK 465     LEU B   484                                                      
REMARK 465     GLU B   485                                                      
REMARK 465     HIS B   486                                                      
REMARK 465     HIS B   487                                                      
REMARK 465     HIS B   488                                                      
REMARK 465     HIS B   489                                                      
REMARK 465     HIS B   490                                                      
REMARK 465     HIS B   491                                                      
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    ALA A   376     O    HOH A   685              2.11            
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    ASP A 353   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 356   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    LEU B 100   CA  -  CB  -  CG  ANGL. DEV. =  14.9 DEGREES          
REMARK 500    ASP B 353   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP B 366   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B 459   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 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    GLU A  91       19.89     59.24                                   
REMARK 500    LEU A 152       -5.07     85.37                                   
REMARK 500    GLU A 256     -127.77     46.89                                   
REMARK 500    SER A 294     -130.06     56.19                                   
REMARK 500    LYS A 330     -120.89     46.54                                   
REMARK 500    THR A 347      147.76   -170.59                                   
REMARK 500    ASP A 349     -151.25   -118.21                                   
REMARK 500    TYR A 428       -2.68     67.82                                   
REMARK 500    ARG B  74      109.67    -58.48                                   
REMARK 500    TYR B 252       -8.18   -150.30                                   
REMARK 500    GLU B 256     -130.72     56.60                                   
REMARK 500    SER B 294     -136.39     68.79                                   
REMARK 500    LYS B 330     -118.27     50.00                                   
REMARK 500    THR B 347      143.89   -174.09                                   
REMARK 500    PRO B 372       67.55    -69.08                                   
REMARK 500    TYR B 428       -2.28     77.63                                   
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 649        DISTANCE =  5.46 ANGSTROMS                       
REMARK 525    HOH B 660        DISTANCE = 11.77 ANGSTROMS                       
REMARK 525    HOH B 684        DISTANCE =  9.91 ANGSTROMS                       
DBREF  3HLK A   46   483  UNP    P49753   ACOT2_HUMAN     46    483             
DBREF  3HLK B   46   483  UNP    P49753   ACOT2_HUMAN     46    483             
SEQADV 3HLK LEU A  484  UNP  P49753              EXPRESSION TAG                 
SEQADV 3HLK GLU A  485  UNP  P49753              EXPRESSION TAG                 
SEQADV 3HLK HIS A  486  UNP  P49753              EXPRESSION TAG                 
SEQADV 3HLK HIS A  487  UNP  P49753              EXPRESSION TAG                 
SEQADV 3HLK HIS A  488  UNP  P49753              EXPRESSION TAG                 
SEQADV 3HLK HIS A  489  UNP  P49753              EXPRESSION TAG                 
SEQADV 3HLK HIS A  490  UNP  P49753              EXPRESSION TAG                 
SEQADV 3HLK HIS A  491  UNP  P49753              EXPRESSION TAG                 
SEQADV 3HLK LEU B  484  UNP  P49753              EXPRESSION TAG                 
SEQADV 3HLK GLU B  485  UNP  P49753              EXPRESSION TAG                 
SEQADV 3HLK HIS B  486  UNP  P49753              EXPRESSION TAG                 
SEQADV 3HLK HIS B  487  UNP  P49753              EXPRESSION TAG                 
SEQADV 3HLK HIS B  488  UNP  P49753              EXPRESSION TAG                 
SEQADV 3HLK HIS B  489  UNP  P49753              EXPRESSION TAG                 
SEQADV 3HLK HIS B  490  UNP  P49753              EXPRESSION TAG                 
SEQADV 3HLK HIS B  491  UNP  P49753              EXPRESSION TAG                 
SEQRES   1 A  446  GLY SER PRO GLN LEU ARG GLN VAL GLY GLN ILE ILE ARG          
SEQRES   2 A  446  VAL PRO ALA ARG MSE ALA ALA THR LEU ILE LEU GLU PRO          
SEQRES   3 A  446  ALA GLY ARG CYS CYS TRP ASP GLU PRO VAL ARG ILE ALA          
SEQRES   4 A  446  VAL ARG GLY LEU ALA PRO GLU GLN PRO VAL THR LEU ARG          
SEQRES   5 A  446  ALA SER LEU ARG ASP GLU LYS GLY ALA LEU PHE GLN ALA          
SEQRES   6 A  446  HIS ALA ARG TYR ARG ALA ASP THR LEU GLY GLU LEU ASP          
SEQRES   7 A  446  LEU GLU ARG ALA PRO ALA LEU GLY GLY SER PHE ALA GLY          
SEQRES   8 A  446  LEU GLU PRO MSE GLY LEU LEU TRP ALA LEU GLU PRO GLU          
SEQRES   9 A  446  LYS PRO LEU VAL ARG LEU VAL LYS ARG ASP VAL ARG THR          
SEQRES  10 A  446  PRO LEU ALA VAL GLU LEU GLU VAL LEU ASP GLY HIS ASP          
SEQRES  11 A  446  PRO ASP PRO GLY ARG LEU LEU CYS GLN THR ARG HIS GLU          
SEQRES  12 A  446  ARG TYR PHE LEU PRO PRO GLY VAL ARG ARG GLU PRO VAL          
SEQRES  13 A  446  ARG VAL GLY ARG VAL ARG GLY THR LEU PHE LEU PRO PRO          
SEQRES  14 A  446  GLU PRO GLY PRO PHE PRO GLY ILE VAL ASP MSE PHE GLY          
SEQRES  15 A  446  THR GLY GLY GLY LEU LEU GLU TYR ARG ALA SER LEU LEU          
SEQRES  16 A  446  ALA GLY LYS GLY PHE ALA VAL MSE ALA LEU ALA TYR TYR          
SEQRES  17 A  446  ASN TYR GLU ASP LEU PRO LYS THR MSE GLU THR LEU HIS          
SEQRES  18 A  446  LEU GLU TYR PHE GLU GLU ALA MSE ASN TYR LEU LEU SER          
SEQRES  19 A  446  HIS PRO GLU VAL LYS GLY PRO GLY VAL GLY LEU LEU GLY          
SEQRES  20 A  446  ILE SER LYS GLY GLY GLU LEU CYS LEU SER MSE ALA SER          
SEQRES  21 A  446  PHE LEU LYS GLY ILE THR ALA ALA VAL VAL ILE ASN GLY          
SEQRES  22 A  446  SER VAL ALA ASN VAL GLY GLY THR LEU ARG TYR LYS GLY          
SEQRES  23 A  446  GLU THR LEU PRO PRO VAL GLY VAL ASN ARG ASN ARG ILE          
SEQRES  24 A  446  LYS VAL THR LYS ASP GLY TYR ALA ASP ILE VAL ASP VAL          
SEQRES  25 A  446  LEU ASN SER PRO LEU GLU GLY PRO ASP GLN LYS SER PHE          
SEQRES  26 A  446  ILE PRO VAL GLU ARG ALA GLU SER THR PHE LEU PHE LEU          
SEQRES  27 A  446  VAL GLY GLN ASP ASP HIS ASN TRP LYS SER GLU PHE TYR          
SEQRES  28 A  446  ALA ASN GLU ALA CYS LYS ARG LEU GLN ALA HIS GLY ARG          
SEQRES  29 A  446  ARG LYS PRO GLN ILE ILE CYS TYR PRO GLU THR GLY HIS          
SEQRES  30 A  446  TYR ILE GLU PRO PRO TYR PHE PRO LEU CYS ARG ALA SER          
SEQRES  31 A  446  LEU HIS ALA LEU VAL GLY SER PRO ILE ILE TRP GLY GLY          
SEQRES  32 A  446  GLU PRO ARG ALA HIS ALA MSE ALA GLN VAL ASP ALA TRP          
SEQRES  33 A  446  LYS GLN LEU GLN THR PHE PHE HIS LYS HIS LEU GLY GLY          
SEQRES  34 A  446  HIS GLU GLY THR ILE PRO SER LYS VAL LEU GLU HIS HIS          
SEQRES  35 A  446  HIS HIS HIS HIS                                              
SEQRES   1 B  446  GLY SER PRO GLN LEU ARG GLN VAL GLY GLN ILE ILE ARG          
SEQRES   2 B  446  VAL PRO ALA ARG MSE ALA ALA THR LEU ILE LEU GLU PRO          
SEQRES   3 B  446  ALA GLY ARG CYS CYS TRP ASP GLU PRO VAL ARG ILE ALA          
SEQRES   4 B  446  VAL ARG GLY LEU ALA PRO GLU GLN PRO VAL THR LEU ARG          
SEQRES   5 B  446  ALA SER LEU ARG ASP GLU LYS GLY ALA LEU PHE GLN ALA          
SEQRES   6 B  446  HIS ALA ARG TYR ARG ALA ASP THR LEU GLY GLU LEU ASP          
SEQRES   7 B  446  LEU GLU ARG ALA PRO ALA LEU GLY GLY SER PHE ALA GLY          
SEQRES   8 B  446  LEU GLU PRO MSE GLY LEU LEU TRP ALA LEU GLU PRO GLU          
SEQRES   9 B  446  LYS PRO LEU VAL ARG LEU VAL LYS ARG ASP VAL ARG THR          
SEQRES  10 B  446  PRO LEU ALA VAL GLU LEU GLU VAL LEU ASP GLY HIS ASP          
SEQRES  11 B  446  PRO ASP PRO GLY ARG LEU LEU CYS GLN THR ARG HIS GLU          
SEQRES  12 B  446  ARG TYR PHE LEU PRO PRO GLY VAL ARG ARG GLU PRO VAL          
SEQRES  13 B  446  ARG VAL GLY ARG VAL ARG GLY THR LEU PHE LEU PRO PRO          
SEQRES  14 B  446  GLU PRO GLY PRO PHE PRO GLY ILE VAL ASP MSE PHE GLY          
SEQRES  15 B  446  THR GLY GLY GLY LEU LEU GLU TYR ARG ALA SER LEU LEU          
SEQRES  16 B  446  ALA GLY LYS GLY PHE ALA VAL MSE ALA LEU ALA TYR TYR          
SEQRES  17 B  446  ASN TYR GLU ASP LEU PRO LYS THR MSE GLU THR LEU HIS          
SEQRES  18 B  446  LEU GLU TYR PHE GLU GLU ALA MSE ASN TYR LEU LEU SER          
SEQRES  19 B  446  HIS PRO GLU VAL LYS GLY PRO GLY VAL GLY LEU LEU GLY          
SEQRES  20 B  446  ILE SER LYS GLY GLY GLU LEU CYS LEU SER MSE ALA SER          
SEQRES  21 B  446  PHE LEU LYS GLY ILE THR ALA ALA VAL VAL ILE ASN GLY          
SEQRES  22 B  446  SER VAL ALA ASN VAL GLY GLY THR LEU ARG TYR LYS GLY          
SEQRES  23 B  446  GLU THR LEU PRO PRO VAL GLY VAL ASN ARG ASN ARG ILE          
SEQRES  24 B  446  LYS VAL THR LYS ASP GLY TYR ALA ASP ILE VAL ASP VAL          
SEQRES  25 B  446  LEU ASN SER PRO LEU GLU GLY PRO ASP GLN LYS SER PHE          
SEQRES  26 B  446  ILE PRO VAL GLU ARG ALA GLU SER THR PHE LEU PHE LEU          
SEQRES  27 B  446  VAL GLY GLN ASP ASP HIS ASN TRP LYS SER GLU PHE TYR          
SEQRES  28 B  446  ALA ASN GLU ALA CYS LYS ARG LEU GLN ALA HIS GLY ARG          
SEQRES  29 B  446  ARG LYS PRO GLN ILE ILE CYS TYR PRO GLU THR GLY HIS          
SEQRES  30 B  446  TYR ILE GLU PRO PRO TYR PHE PRO LEU CYS ARG ALA SER          
SEQRES  31 B  446  LEU HIS ALA LEU VAL GLY SER PRO ILE ILE TRP GLY GLY          
SEQRES  32 B  446  GLU PRO ARG ALA HIS ALA MSE ALA GLN VAL ASP ALA TRP          
SEQRES  33 B  446  LYS GLN LEU GLN THR PHE PHE HIS LYS HIS LEU GLY GLY          
SEQRES  34 B  446  HIS GLU GLY THR ILE PRO SER LYS VAL LEU GLU HIS HIS          
SEQRES  35 B  446  HIS HIS HIS HIS                                              
MODRES 3HLK MSE A   63  MET  SELENOMETHIONINE                                   
MODRES 3HLK MSE A  140  MET  SELENOMETHIONINE                                   
MODRES 3HLK MSE A  225  MET  SELENOMETHIONINE                                   
MODRES 3HLK MSE A  248  MET  SELENOMETHIONINE                                   
MODRES 3HLK MSE A  262  MET  SELENOMETHIONINE                                   
MODRES 3HLK MSE A  274  MET  SELENOMETHIONINE                                   
MODRES 3HLK MSE A  303  MET  SELENOMETHIONINE                                   
MODRES 3HLK MSE A  455  MET  SELENOMETHIONINE                                   
MODRES 3HLK MSE B   63  MET  SELENOMETHIONINE                                   
MODRES 3HLK MSE B  140  MET  SELENOMETHIONINE                                   
MODRES 3HLK MSE B  225  MET  SELENOMETHIONINE                                   
MODRES 3HLK MSE B  248  MET  SELENOMETHIONINE                                   
MODRES 3HLK MSE B  262  MET  SELENOMETHIONINE                                   
MODRES 3HLK MSE B  274  MET  SELENOMETHIONINE                                   
MODRES 3HLK MSE B  303  MET  SELENOMETHIONINE                                   
MODRES 3HLK MSE B  455  MET  SELENOMETHIONINE                                   
HET    MSE  A  63       8                                                       
HET    MSE  A 140       8                                                       
HET    MSE  A 225       8                                                       
HET    MSE  A 248       8                                                       
HET    MSE  A 262       8                                                       
HET    MSE  A 274       8                                                       
HET    MSE  A 303       8                                                       
HET    MSE  A 455       8                                                       
HET    MSE  B  63       8                                                       
HET    MSE  B 140       8                                                       
HET    MSE  B 225       8                                                       
HET    MSE  B 248       8                                                       
HET    MSE  B 262       8                                                       
HET    MSE  B 274       8                                                       
HET    MSE  B 303       8                                                       
HET    MSE  B 455       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    16(C5 H11 N O2 SE)                                           
FORMUL   3  HOH   *441(H2 O)                                                    
HELIX    1   1 MSE A  140  ALA A  145  1                                   6    
HELIX    2   2 GLU A  234  GLY A  242  1                                   9    
HELIX    3   3 LEU A  267  SER A  279  1                                  13    
HELIX    4   4 SER A  294  LEU A  307  1                                  14    
HELIX    5   5 ASN A  340  ILE A  344  5                                   5    
HELIX    6   6 GLU A  363  PHE A  370  5                                   8    
HELIX    7   7 PRO A  372  ALA A  376  5                                   5    
HELIX    8   8 LYS A  392  HIS A  407  1                                  16    
HELIX    9   9 GLU A  449  LEU A  472  1                                  24    
HELIX   10  10 MSE B  140  ALA B  145  1                                   6    
HELIX   11  11 GLU B  234  GLY B  242  1                                   9    
HELIX   12  12 LEU B  267  HIS B  280  1                                  14    
HELIX   13  13 SER B  294  LEU B  307  1                                  14    
HELIX   14  14 ASN B  340  ILE B  344  5                                   5    
HELIX   15  15 GLU B  363  PHE B  370  5                                   8    
HELIX   16  16 PRO B  372  ALA B  376  5                                   5    
HELIX   17  17 LYS B  392  ALA B  406  1                                  15    
HELIX   18  18 GLU B  449  LEU B  472  1                                  24    
SHEET    1   A 3 THR A  66  GLU A  70  0                                        
SHEET    2   A 3 ARG A  82  ARG A  86 -1  O  ARG A  82   N  GLU A  70           
SHEET    3   A 3 LEU A 122  ASP A 123 -1  O  LEU A 122   N  VAL A  85           
SHEET    1   B 6 CYS A  75  CYS A  76  0                                        
SHEET    2   B 6 LEU A 181  TYR A 190  1  O  TYR A 190   N  CYS A  75           
SHEET    3   B 6 LEU A 164  ASP A 172 -1  N  VAL A 170   O  LEU A 182           
SHEET    4   B 6 PRO A  93  ARG A 101 -1  N  THR A  95   O  LEU A 171           
SHEET    5   B 6 LEU A 107  ARG A 115 -1  O  PHE A 108   N  LEU A 100           
SHEET    6   B 6 GLY A 131  GLY A 132 -1  O  GLY A 131   N  ARG A 113           
SHEET    1   C 6 CYS A  75  CYS A  76  0                                        
SHEET    2   C 6 LEU A 181  TYR A 190  1  O  TYR A 190   N  CYS A  75           
SHEET    3   C 6 LEU A 164  ASP A 172 -1  N  VAL A 170   O  LEU A 182           
SHEET    4   C 6 PRO A  93  ARG A 101 -1  N  THR A  95   O  LEU A 171           
SHEET    5   C 6 LEU A 107  ARG A 115 -1  O  PHE A 108   N  LEU A 100           
SHEET    6   C 6 GLU A 147  PRO A 148 -1  O  GLU A 147   N  GLN A 109           
SHEET    1   D 8 ARG A 197  VAL A 203  0                                        
SHEET    2   D 8 VAL A 206  LEU A 212 -1  O  GLY A 208   N  VAL A 201           
SHEET    3   D 8 ALA A 246  LEU A 250 -1  O  ALA A 249   N  THR A 209           
SHEET    4   D 8 GLY A 221  MSE A 225  1  N  ASP A 224   O  MSE A 248           
SHEET    5   D 8 VAL A 288  ILE A 293  1  O  LEU A 291   N  VAL A 223           
SHEET    6   D 8 ILE A 310  ILE A 316  1  O  ILE A 316   N  GLY A 292           
SHEET    7   D 8 THR A 379  GLY A 385  1  O  LEU A 383   N  VAL A 315           
SHEET    8   D 8 GLN A 413  TYR A 417  1  O  ILE A 415   N  PHE A 382           
SHEET    1   E 3 THR A 264  HIS A 266  0                                        
SHEET    2   E 3 THR A 326  TYR A 329  1  O  THR A 326   N  LEU A 265           
SHEET    3   E 3 GLU A 332  LEU A 334 -1  O  GLU A 332   N  TYR A 329           
SHEET    1   F 2 LYS A 345  VAL A 346  0                                        
SHEET    2   F 2 ALA A 352  ASP A 353 -1  O  ASP A 353   N  LYS A 345           
SHEET    1   G 3 THR B  66  GLU B  70  0                                        
SHEET    2   G 3 ARG B  82  ARG B  86 -1  O  ARG B  82   N  GLU B  70           
SHEET    3   G 3 LEU B 122  ASP B 123 -1  O  LEU B 122   N  VAL B  85           
SHEET    1   H 7 CYS B  75  CYS B  76  0                                        
SHEET    2   H 7 LEU B 181  TYR B 190  1  O  TYR B 190   N  CYS B  75           
SHEET    3   H 7 LEU B 164  ASP B 172 -1  N  VAL B 166   O  HIS B 187           
SHEET    4   H 7 PRO B  93  ARG B 101 -1  N  THR B  95   O  LEU B 171           
SHEET    5   H 7 LEU B 107  ARG B 115 -1  O  PHE B 108   N  LEU B 100           
SHEET    6   H 7 ALA B 129  GLY B 132 -1  O  LEU B 130   N  ARG B 113           
SHEET    7   H 7 ALA B 135  GLY B 136 -1  O  GLY B 136   N  ALA B 129           
SHEET    1   I 6 CYS B  75  CYS B  76  0                                        
SHEET    2   I 6 LEU B 181  TYR B 190  1  O  TYR B 190   N  CYS B  75           
SHEET    3   I 6 LEU B 164  ASP B 172 -1  N  VAL B 166   O  HIS B 187           
SHEET    4   I 6 PRO B  93  ARG B 101 -1  N  THR B  95   O  LEU B 171           
SHEET    5   I 6 LEU B 107  ARG B 115 -1  O  PHE B 108   N  LEU B 100           
SHEET    6   I 6 GLU B 147  PRO B 148 -1  O  GLU B 147   N  GLN B 109           
SHEET    1   J 8 ARG B 197  VAL B 203  0                                        
SHEET    2   J 8 VAL B 206  LEU B 212 -1  O  LEU B 212   N  ARG B 197           
SHEET    3   J 8 ALA B 246  LEU B 250 -1  O  VAL B 247   N  PHE B 211           
SHEET    4   J 8 GLY B 221  MSE B 225  1  N  ASP B 224   O  LEU B 250           
SHEET    5   J 8 VAL B 288  ILE B 293  1  O  LEU B 291   N  VAL B 223           
SHEET    6   J 8 ILE B 310  ILE B 316  1  O  ILE B 316   N  GLY B 292           
SHEET    7   J 8 THR B 379  GLY B 385  1  O  LEU B 381   N  VAL B 315           
SHEET    8   J 8 GLN B 413  TYR B 417  1  O  TYR B 417   N  VAL B 384           
SHEET    1   K 3 THR B 264  HIS B 266  0                                        
SHEET    2   K 3 THR B 326  TYR B 329  1  O  THR B 326   N  LEU B 265           
SHEET    3   K 3 GLU B 332  LEU B 334 -1  O  GLU B 332   N  TYR B 329           
SHEET    1   L 2 LYS B 345  VAL B 346  0                                        
SHEET    2   L 2 ALA B 352  ASP B 353 -1  O  ASP B 353   N  LYS B 345           
SHEET    1   M 2 ALA B 434  SER B 435  0                                        
SHEET    2   M 2 ILE B 444  ILE B 445 -1  O  ILE B 444   N  SER B 435           
LINK         C   ARG A  62                 N   MSE A  63     1555   1555  1.33  
LINK         C   MSE A  63                 N   ALA A  64     1555   1555  1.33  
LINK         C   PRO A 139                 N   MSE A 140     1555   1555  1.34  
LINK         C   MSE A 140                 N   GLY A 141     1555   1555  1.33  
LINK         C   ASP A 224                 N   MSE A 225     1555   1555  1.33  
LINK         C   MSE A 225                 N   PHE A 226     1555   1555  1.33  
LINK         C   VAL A 247                 N   MSE A 248     1555   1555  1.33  
LINK         C   MSE A 248                 N   ALA A 249     1555   1555  1.33  
LINK         C   THR A 261                 N   MSE A 262     1555   1555  1.33  
LINK         C   MSE A 262                 N   GLU A 263     1555   1555  1.34  
LINK         C   ALA A 273                 N   MSE A 274     1555   1555  1.33  
LINK         C   MSE A 274                 N   ASN A 275     1555   1555  1.33  
LINK         C   SER A 302                 N   MSE A 303     1555   1555  1.34  
LINK         C   MSE A 303                 N   ALA A 304     1555   1555  1.33  
LINK         C   ALA A 454                 N   MSE A 455     1555   1555  1.33  
LINK         C   MSE A 455                 N   ALA A 456     1555   1555  1.34  
LINK         C   ARG B  62                 N   MSE B  63     1555   1555  1.33  
LINK         C   MSE B  63                 N   ALA B  64     1555   1555  1.33  
LINK         C   PRO B 139                 N   MSE B 140     1555   1555  1.34  
LINK         C   MSE B 140                 N   GLY B 141     1555   1555  1.32  
LINK         C   ASP B 224                 N   MSE B 225     1555   1555  1.33  
LINK         C   MSE B 225                 N   PHE B 226     1555   1555  1.32  
LINK         C   VAL B 247                 N   MSE B 248     1555   1555  1.33  
LINK         C   MSE B 248                 N   ALA B 249     1555   1555  1.33  
LINK         C   THR B 261                 N   MSE B 262     1555   1555  1.33  
LINK         C   MSE B 262                 N   GLU B 263     1555   1555  1.33  
LINK         C   ALA B 273                 N   MSE B 274     1555   1555  1.32  
LINK         C   MSE B 274                 N   ASN B 275     1555   1555  1.33  
LINK         C   SER B 302                 N   MSE B 303     1555   1555  1.33  
LINK         C   MSE B 303                 N   ALA B 304     1555   1555  1.33  
LINK         C   ALA B 454                 N   MSE B 455     1555   1555  1.34  
LINK         C   MSE B 455                 N   ALA B 456     1555   1555  1.33  
CISPEP   1 GLU A   70    PRO A   71          0        -3.17                     
CISPEP   2 GLU A  215    PRO A  216          0         2.89                     
CISPEP   3 GLY A  217    PRO A  218          0         0.88                     
CISPEP   4 GLY A  285    PRO A  286          0         9.22                     
CISPEP   5 THR A  347    LYS A  348          0       -12.17                     
CISPEP   6 GLU B   70    PRO B   71          0        -6.27                     
CISPEP   7 GLU B  215    PRO B  216          0         8.79                     
CISPEP   8 GLY B  217    PRO B  218          0        -3.67                     
CISPEP   9 GLY B  285    PRO B  286          0         0.40                     
CISPEP  10 THR B  347    LYS B  348          0       -11.98                     
CRYST1  124.557  124.557  131.950  90.00  90.00 120.00 P 31 2 1     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      0.008028  0.004635  0.000000        0.00000                         
SCALE2      0.000000  0.009270  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007579        0.00000                         
TER    3184      LEU A 472                                                      
TER    6390      LEU B 472                                                      
MASTER      419    0   16   18   59    0    0    6 6829    2  160   70          
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