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LongText Report for: 1YCD-pdb

Name Class
1YCD-pdb
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   22-DEC-04   1YCD              
TITLE     CRYSTAL STRUCTURE OF YEAST FSH1/YHR049W, A MEMBER OF THE              
TITLE    2 SERINE HYDROLASE FAMILY                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYPOTHETICAL 27.3 KDA PROTEIN IN AAP1-SMF2                 
COMPND   3 INTERGENIC REGION;                                                   
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: S. CEREVISIAE YHR049WP;                                    
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: YEAST;                                              
SOURCE   4 GENE: YHR049W;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BACTERIA;                                  
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYSS;                         
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    ESTERASE, LIPASE, SERINE HYDROLASE, S. CEREVISIAE,                    
KEYWDS   2 STRUCTURAL GENOMICS, PARIS-SUD YEAST STRUCTURAL GENOMICS,            
KEYWDS   3 YSG                                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.LEULLIOT,M.GRAILLE,F.COSTE,S.QUEVILLON-CHERUEL,J.JANIN,             
AUTHOR   2 H.VAN TILBEURGH,PARIS-SUD YEAST STRUCTURAL GENOMICS (YSG)            
REVDAT   1   10-MAY-05 1YCD    0                                                
JRNL        AUTH   S.QUEVILLON-CHERUEL,N.LEULLIOT,M.GRAILLE,                    
JRNL        AUTH 2 N.HERVOUET,F.COSTE,C.ZELWER,J.JANIN,H.VAN TILBEURGH          
JRNL        TITL   CRYSTAL STRUCTURE OF YEAST YHR049W/FSH1, A MEMBER            
JRNL        TITL 2 OF THE SERINE HYDROLASE FAMILY.                              
JRNL        REF    PROTEIN SCI.                  V.  14  1350 2005              
JRNL        REFN   ASTM PRCIEI  US ISSN 0961-8368                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.70 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 54126                          
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) : 0.167                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2873                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 1.75                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3622                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.90                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2120                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 167                          
REMARK   3   BIN FREE R VALUE                    : 0.2500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 4732                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.56000                                             
REMARK   3    B22 (A**2) : 0.99000                                              
REMARK   3    B33 (A**2) : -0.47000                                             
REMARK   3    B12 (A**2) : 0.18000                                              
REMARK   3    B13 (A**2) : -0.04000                                             
REMARK   3    B23 (A**2) : -0.39000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.107         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.105         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.067         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.958         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3880 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5242 ; 1.283 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   469 ; 5.071 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   171 ;32.863 ;25.205       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   697 ;12.056 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;17.767 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   574 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2887 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2007 ; 0.221 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2669 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   694 ; 0.136 ; 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):    59 ; 0.152 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    65 ; 0.125 ; 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):  2439 ; 0.797 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3840 ; 1.260 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1623 ; 2.060 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1402 ; 3.358 ; 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 : 0                                 
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 0                                          
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 1YCD COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-2005.                
REMARK 100 THE RCSB ID CODE IS RCSB031371.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-SEP-2003                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57009                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.8                               
REMARK 200  DATA REDUNDANCY                : 1.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04700                            
REMARK 200   FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.16500                            
REMARK 200   FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% PEG 4K, 0.1M MES, PH 5.6, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 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 BIOMOLECULE: 2                                                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     GLU A   240                                                      
REMARK 465     ALA A   241                                                      
REMARK 465     SER A   242                                                      
REMARK 465     GLU A   243                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     SER B   242                                                      
REMARK 465     GLU B   243                                                      
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),F6.3)                  
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LEU A 109   C     SER A 110   N      0.156                        
REMARK 500    SER A 110   C     GLN A 111   N      0.317                        
REMARK 500    LEU B 109   C     SER B 110   N      0.217                        
REMARK 500    SER B 110   C     GLN B 111   N      0.289                        
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: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    SER A 110   C   -  N   -  CA  ANGL. DEV. =  8.5 DEGREES           
REMARK 500    SER A 110   O   -  C   -  N   ANGL. DEV. = -8.9 DEGREES           
REMARK 500    SER B 110   O   -  C   -  N   ANGL. DEV. =-10.1 DEGREES           
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  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 110     -106.68     50.75                                   
REMARK 500    SER B 110     -111.96     51.75                                   
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED            
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE                 
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL                 
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE          
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH   431        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH   542        DISTANCE =  6.38 ANGSTROMS                       
REMARK 525    HOH   784        DISTANCE =  8.33 ANGSTROMS                       
REMARK 525    HOH   806        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH   815        DISTANCE =  6.91 ANGSTROMS                       
REMARK 525    HOH   831        DISTANCE =  6.40 ANGSTROMS                       
REMARK 525    HOH   879        DISTANCE =  5.74 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 THE AUTHOR STATES THAT THE LI5 RESIDUE                               
REMARK 600 IN MOLECULE B DOES NOT CONTAIN C32 ATOM                              
REMARK 600 BECAUSE THIS ATOM WAS NOT DETECTED IN THE                            
REMARK 600 ELECTRON DENSITY FOR MOLECULE B BUT WAS                              
REMARK 600 DETECTED IN MOLECULE A.                                              
DBREF  1YCD A    1   243  SWS    P38777   YHK9_YEAST       1    243             
DBREF  1YCD B    1   243  SWS    P38777   YHK9_YEAST       1    243             
SEQADV 1YCD LEU A  109  SWS  P38777    PHE   109 ENGINEERED                     
SEQADV 1YCD LEU B  109  SWS  P38777    PHE   109 ENGINEERED                     
SEQRES   1 A  243  MET THR VAL GLN ILE PRO LYS LEU LEU PHE LEU HIS GLY          
SEQRES   2 A  243  PHE LEU GLN ASN GLY LYS VAL PHE SER GLU LYS SER SER          
SEQRES   3 A  243  GLY ILE ARG LYS LEU LEU LYS LYS ALA ASN VAL GLN CYS          
SEQRES   4 A  243  ASP TYR ILE ASP ALA PRO VAL LEU LEU GLU LYS LYS ASP          
SEQRES   5 A  243  LEU PRO PHE GLU MET ASP ASP GLU LYS TRP GLN ALA THR          
SEQRES   6 A  243  LEU ASP ALA ASP VAL ASN ARG ALA TRP PHE TYR HIS SER          
SEQRES   7 A  243  GLU ILE SER HIS GLU LEU ASP ILE SER GLU GLY LEU LYS          
SEQRES   8 A  243  SER VAL VAL ASP HIS ILE LYS ALA ASN GLY PRO TYR ASP          
SEQRES   9 A  243  GLY ILE VAL GLY LEU SER GLN GLY ALA ALA LEU SER SER          
SEQRES  10 A  243  ILE ILE THR ASN LYS ILE SER GLU LEU VAL PRO ASP HIS          
SEQRES  11 A  243  PRO GLN PHE LYS VAL SER VAL VAL ILE SER GLY TYR SER          
SEQRES  12 A  243  PHE THR GLU PRO ASP PRO GLU HIS PRO GLY GLU LEU ARG          
SEQRES  13 A  243  ILE THR GLU LYS PHE ARG ASP SER PHE ALA VAL LYS PRO          
SEQRES  14 A  243  ASP MET LYS THR LYS MET ILE PHE ILE TYR GLY ALA SER          
SEQRES  15 A  243  ASP GLN ALA VAL PRO SER VAL ARG SER LYS TYR LEU TYR          
SEQRES  16 A  243  ASP ILE TYR LEU LYS ALA GLN ASN GLY ASN LYS GLU LYS          
SEQRES  17 A  243  VAL LEU ALA TYR GLU HIS PRO GLY GLY HIS MET VAL PRO          
SEQRES  18 A  243  ASN LYS LYS ASP ILE ILE ARG PRO ILE VAL GLU GLN ILE          
SEQRES  19 A  243  THR SER SER LEU GLN GLU ALA SER GLU                          
SEQRES   1 B  243  MET THR VAL GLN ILE PRO LYS LEU LEU PHE LEU HIS GLY          
SEQRES   2 B  243  PHE LEU GLN ASN GLY LYS VAL PHE SER GLU LYS SER SER          
SEQRES   3 B  243  GLY ILE ARG LYS LEU LEU LYS LYS ALA ASN VAL GLN CYS          
SEQRES   4 B  243  ASP TYR ILE ASP ALA PRO VAL LEU LEU GLU LYS LYS ASP          
SEQRES   5 B  243  LEU PRO PHE GLU MET ASP ASP GLU LYS TRP GLN ALA THR          
SEQRES   6 B  243  LEU ASP ALA ASP VAL ASN ARG ALA TRP PHE TYR HIS SER          
SEQRES   7 B  243  GLU ILE SER HIS GLU LEU ASP ILE SER GLU GLY LEU LYS          
SEQRES   8 B  243  SER VAL VAL ASP HIS ILE LYS ALA ASN GLY PRO TYR ASP          
SEQRES   9 B  243  GLY ILE VAL GLY LEU SER GLN GLY ALA ALA LEU SER SER          
SEQRES  10 B  243  ILE ILE THR ASN LYS ILE SER GLU LEU VAL PRO ASP HIS          
SEQRES  11 B  243  PRO GLN PHE LYS VAL SER VAL VAL ILE SER GLY TYR SER          
SEQRES  12 B  243  PHE THR GLU PRO ASP PRO GLU HIS PRO GLY GLU LEU ARG          
SEQRES  13 B  243  ILE THR GLU LYS PHE ARG ASP SER PHE ALA VAL LYS PRO          
SEQRES  14 B  243  ASP MET LYS THR LYS MET ILE PHE ILE TYR GLY ALA SER          
SEQRES  15 B  243  ASP GLN ALA VAL PRO SER VAL ARG SER LYS TYR LEU TYR          
SEQRES  16 B  243  ASP ILE TYR LEU LYS ALA GLN ASN GLY ASN LYS GLU LYS          
SEQRES  17 B  243  VAL LEU ALA TYR GLU HIS PRO GLY GLY HIS MET VAL PRO          
SEQRES  18 B  243  ASN LYS LYS ASP ILE ILE ARG PRO ILE VAL GLU GLN ILE          
SEQRES  19 B  243  THR SER SER LEU GLN GLU ALA SER GLU                          
HET    LI5  A 800      14                                                       
HET    LI5  B 800      13                                                       
HETNAM     LI5 2-HYDROXY-4,5-DIOXOHEPTYL HYDROGEN PHOSPHONATE                   
FORMUL   3  LI5    2(C7 H12 O6 P1)                                              
FORMUL   5  HOH   *936(H2 O1)                                                   
HELIX    1   1 ASN A   17  SER A   25  1                                   9    
HELIX    2   2 SER A   25  ALA A   35  1                                  11    
HELIX    3   3 GLU A   49  LEU A   53  5                                   5    
HELIX    4   4 ASP A   58  ALA A   68  1                                  11    
HELIX    5   5 ILE A   80  LEU A   84  5                                   5    
HELIX    6   6 ILE A   86  GLY A  101  1                                  16    
HELIX    7   7 SER A  110  VAL A  127  1                                  18    
HELIX    8   8 GLU A  159  ARG A  162  5                                   4    
HELIX    9   9 PRO A  187  GLN A  202  1                                  16    
HELIX   10  10 LYS A  223  GLN A  239  1                                  17    
HELIX   11  11 ASN B   17  SER B   25  1                                   9    
HELIX   12  12 SER B   25  ALA B   35  1                                  11    
HELIX   13  13 GLU B   49  LEU B   53  5                                   5    
HELIX   14  14 ASP B   58  ALA B   68  1                                  11    
HELIX   15  15 ILE B   80  LEU B   84  5                                   5    
HELIX   16  16 ILE B   86  GLY B  101  1                                  16    
HELIX   17  17 SER B  110  VAL B  127  1                                  18    
HELIX   18  18 GLU B  159  ARG B  162  5                                   4    
HELIX   19  19 PRO B  187  GLN B  202  1                                  16    
HELIX   20  20 LYS B  223  GLN B  239  1                                  17    
SHEET    1   A 6 GLN A  38  ILE A  42  0                                        
SHEET    2   A 6 LYS A   7  LEU A  11  1  N  LEU A   8   O  GLN A  38           
SHEET    3   A 6 GLY A 105  LEU A 109  1  O  VAL A 107   N  LEU A  11           
SHEET    4   A 6 VAL A 135  ILE A 139  1  O  VAL A 137   N  ILE A 106           
SHEET    5   A 6 LYS A 174  GLY A 180  1  O  ILE A 176   N  SER A 136           
SHEET    6   A 6 VAL A 209  HIS A 214  1  O  LEU A 210   N  PHE A 177           
SHEET    1   B 2 VAL A  46  LEU A  47  0                                        
SHEET    2   B 2 ARG A  72  ALA A  73 -1  O  ALA A  73   N  VAL A  46           
SHEET    1   C 2 THR A 145  PRO A 147  0                                        
SHEET    2   C 2 LEU A 155  ILE A 157 -1  O  ARG A 156   N  GLU A 146           
SHEET    1   D 6 GLN B  38  ILE B  42  0                                        
SHEET    2   D 6 LYS B   7  LEU B  11  1  N  PHE B  10   O  ASP B  40           
SHEET    3   D 6 GLY B 105  LEU B 109  1  O  VAL B 107   N  LEU B  11           
SHEET    4   D 6 VAL B 135  ILE B 139  1  O  VAL B 137   N  ILE B 106           
SHEET    5   D 6 LYS B 174  GLY B 180  1  O  ILE B 176   N  VAL B 138           
SHEET    6   D 6 VAL B 209  HIS B 214  1  O  LEU B 210   N  MET B 175           
SHEET    1   E 2 VAL B  46  LEU B  47  0                                        
SHEET    2   E 2 ARG B  72  ALA B  73 -1  O  ALA B  73   N  VAL B  46           
SHEET    1   F 2 THR B 145  PRO B 147  0                                        
SHEET    2   F 2 LEU B 155  ILE B 157 -1  O  ARG B 156   N  GLU B 146           
LINK         OG  SER A 110                 P   LI5 A 800                        
LINK         OG  SER B 110                 P   LI5 B 800                        
CISPEP   1 VAL A    3    GLN A    4          0        -0.39                     
CISPEP   2 GLY A  101    PRO A  102          0         3.85                     
CISPEP   3 GLY B  101    PRO B  102          0         0.19                     
CRYST1   46.133   53.329   64.271 102.85  90.04 112.47 P 1           2          
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      0.021676  0.008966  0.002239        0.00000                         
SCALE2      0.000000  0.020292  0.005036        0.00000                         
SCALE3      0.000000  0.000000  0.016031        0.00000                         
TER    1882      GLN A 239                                                      
TER    3771      ALA B 241                                                      
MASTER      309    0    2   20   20    0    0    6 4732    2   29   38          
END                                                                             

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