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Database: PDB
Entry: 3QHT
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Original site: 3QHT 
HEADER    DE NOVO PROTEIN                         26-JAN-11   3QHT              
TITLE     CRYSTAL STRUCTURE OF THE MONOBODY YSMB-1 BOUND TO YEAST SUMO          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN-LIKE PROTEIN SMT3;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: YEAST SMALL UBIQUITIN-LIKE MODIFIER (SUMO);                 
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: MONOBODY YSMB-1;                                           
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: YEAST;                                              
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: SMT3, YDR510W, D9719.15;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: ARTIFICIAL GENE;                                
SOURCE  10 ORGANISM_TAXID: 32630;                                               
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    FIBRONECTIN TYPE III, YEAST SMALL UBIQUITIN-LIKE MODIFIER, SMT3, DE   
KEYWDS   2 NOVO PROTEIN                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.KOIDE,R.N.GILBRETH                                                  
REVDAT   3   08-NOV-17 3QHT    1       REMARK                                   
REVDAT   2   25-MAY-11 3QHT    1       JRNL                                     
REVDAT   1   11-MAY-11 3QHT    0                                                
JRNL        AUTH   R.N.GILBRETH,K.TRUONG,I.MADU,A.KOIDE,J.B.WOJCIK,N.S.LI,      
JRNL        AUTH 2 J.A.PICCIRILLI,Y.CHEN,S.KOIDE                                
JRNL        TITL   ISOFORM-SPECIFIC MONOBODY INHIBITORS OF SMALL                
JRNL        TITL 2 UBIQUITIN-RELATED MODIFIERS ENGINEERED USING                 
JRNL        TITL 3 STRUCTURE-GUIDED LIBRARY DESIGN.                             
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 108  7751 2011              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   21518904                                                     
JRNL        DOI    10.1073/PNAS.1102294108                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 21341                          
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) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1151                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1450                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.29                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2470                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 81                           
REMARK   3   BIN FREE R VALUE                    : 0.3560                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2666                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 48                                      
REMARK   3   SOLVENT ATOMS            : 85                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.67000                                             
REMARK   3    B22 (A**2) : -0.03000                                             
REMARK   3    B33 (A**2) : 0.70000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.287         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.240         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.171         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.399        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.925                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.896                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2777 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3759 ; 1.864 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   336 ; 7.806 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   121 ;33.575 ;23.636       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   449 ;19.323 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;18.328 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   413 ; 0.160 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2084 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1185 ; 0.232 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1898 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   142 ; 0.158 ; 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):    54 ; 0.270 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.140 ; 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):  1733 ; 1.107 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2752 ; 1.923 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1203 ; 2.568 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1007 ; 3.918 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3QHT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JAN-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000063662.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : C(111)                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22586                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.150                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 1FNA AND 2EKE                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG8000, 16% GLYCEROL, PH 8.0,       
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 292K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       29.81850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       87.73100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.81850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       87.73100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9280 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8990 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     GLN A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     LYS A    11                                                      
REMARK 465     PRO A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     LYS A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     GLU A    17                                                      
REMARK 465     VAL A    18                                                      
REMARK 465     GLY A    98                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     VAL B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     GLN B     8                                                      
REMARK 465     GLU B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     LYS B    11                                                      
REMARK 465     PRO B    12                                                      
REMARK 465     GLU B    13                                                      
REMARK 465     VAL B    14                                                      
REMARK 465     LYS B    15                                                      
REMARK 465     PRO B    16                                                      
REMARK 465     GLU B    17                                                      
REMARK 465     VAL B    18                                                      
REMARK 465     LYS B    19                                                      
REMARK 465     PRO B    20                                                      
REMARK 465     GLU B    21                                                      
REMARK 465     GLN B    95                                                      
REMARK 465     ILE B    96                                                      
REMARK 465     GLY B    97                                                      
REMARK 465     GLY B    98                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     VAL C     1                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     VAL D     1                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ILE A  96    CB   CG1  CG2  CD1                                  
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    VAL D   4   C   -  N   -  CA  ANGL. DEV. =  16.0 DEGREES          
REMARK 500    SER D  28   C   -  N   -  CA  ANGL. DEV. =  17.7 DEGREES          
REMARK 500    SER D  28   N   -  CA  -  CB  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    LEU D  81   CA  -  CB  -  CG  ANGL. DEV. =  17.6 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    ASN A  86       11.81     80.15                                   
REMARK 500    GLU A  94      116.27     77.52                                   
REMARK 500    GLN A  95       94.15     74.57                                   
REMARK 500    ILE A  96     -142.24    -73.03                                   
REMARK 500    HIS B  23      111.24     70.59                                   
REMARK 500    SER B  32      -63.42    -98.90                                   
REMARK 500    GLN B  56        1.87    168.71                                   
REMARK 500    ARG B  93      -88.39    -40.66                                   
REMARK 500    ARG B  93      -88.39    -43.70                                   
REMARK 500    SER C   3      119.22     38.71                                   
REMARK 500    ALA C  24       42.40   -107.79                                   
REMARK 500    ASN C  42       32.16    -63.94                                   
REMARK 500    TYR C  79     -117.97     45.67                                   
REMARK 500    VAL D   4       79.32     90.31                                   
REMARK 500    SER D  28      -63.86    124.66                                   
REMARK 500    SER D  43      151.49    179.43                                   
REMARK 500    TYR D  79     -118.33     52.72                                   
REMARK 500    SER D  86       74.41     41.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO A   20     GLU A   21                   61.36                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 99                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 100                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 95                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 96                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 97                  
DBREF  3QHT A    2    98  UNP    Q12306   SMT3_YEAST       2     98             
DBREF  3QHT B    2    98  UNP    Q12306   SMT3_YEAST       2     98             
DBREF  3QHT C   -2    94  PDB    3QHT     3QHT             1     97             
DBREF  3QHT D   -2    94  PDB    3QHT     3QHT             1     97             
SEQADV 3QHT GLY A    1  UNP  Q12306              EXPRESSION TAG                 
SEQADV 3QHT GLY B    1  UNP  Q12306              EXPRESSION TAG                 
SEQRES   1 A   98  GLY SER ASP SER GLU VAL ASN GLN GLU ALA LYS PRO GLU          
SEQRES   2 A   98  VAL LYS PRO GLU VAL LYS PRO GLU THR HIS ILE ASN LEU          
SEQRES   3 A   98  LYS VAL SER ASP GLY SER SER GLU ILE PHE PHE LYS ILE          
SEQRES   4 A   98  LYS LYS THR THR PRO LEU ARG ARG LEU MET GLU ALA PHE          
SEQRES   5 A   98  ALA LYS ARG GLN GLY LYS GLU MET ASP SER LEU ARG PHE          
SEQRES   6 A   98  LEU TYR ASP GLY ILE ARG ILE GLN ALA ASP GLN THR PRO          
SEQRES   7 A   98  GLU ASP LEU ASP MET GLU ASP ASN ASP ILE ILE GLU ALA          
SEQRES   8 A   98  HIS ARG GLU GLN ILE GLY GLY                                  
SEQRES   1 B   98  GLY SER ASP SER GLU VAL ASN GLN GLU ALA LYS PRO GLU          
SEQRES   2 B   98  VAL LYS PRO GLU VAL LYS PRO GLU THR HIS ILE ASN LEU          
SEQRES   3 B   98  LYS VAL SER ASP GLY SER SER GLU ILE PHE PHE LYS ILE          
SEQRES   4 B   98  LYS LYS THR THR PRO LEU ARG ARG LEU MET GLU ALA PHE          
SEQRES   5 B   98  ALA LYS ARG GLN GLY LYS GLU MET ASP SER LEU ARG PHE          
SEQRES   6 B   98  LEU TYR ASP GLY ILE ARG ILE GLN ALA ASP GLN THR PRO          
SEQRES   7 B   98  GLU ASP LEU ASP MET GLU ASP ASN ASP ILE ILE GLU ALA          
SEQRES   8 B   98  HIS ARG GLU GLN ILE GLY GLY                                  
SEQRES   1 C   97  GLY SER SER VAL SER SER VAL PRO THR LYS LEU GLU VAL          
SEQRES   2 C   97  VAL ALA ALA THR PRO THR SER LEU LEU ILE SER TRP ASP          
SEQRES   3 C   97  ALA SER SER SER SER VAL SER TYR TYR ARG ILE THR TYR          
SEQRES   4 C   97  GLY GLU THR GLY GLY ASN SER PRO VAL GLN GLU PHE THR          
SEQRES   5 C   97  VAL PRO GLY SER SER SER THR ALA THR ILE SER GLY LEU          
SEQRES   6 C   97  SER PRO GLY VAL ASP TYR THR ILE THR VAL TYR ALA TYR          
SEQRES   7 C   97  TYR SER TYR TYR ASP LEU TYR TYR SER TYR SER PRO SER          
SEQRES   8 C   97  SER ILE ASN TYR ARG THR                                      
SEQRES   1 D   97  GLY SER SER VAL SER SER VAL PRO THR LYS LEU GLU VAL          
SEQRES   2 D   97  VAL ALA ALA THR PRO THR SER LEU LEU ILE SER TRP ASP          
SEQRES   3 D   97  ALA SER SER SER SER VAL SER TYR TYR ARG ILE THR TYR          
SEQRES   4 D   97  GLY GLU THR GLY GLY ASN SER PRO VAL GLN GLU PHE THR          
SEQRES   5 D   97  VAL PRO GLY SER SER SER THR ALA THR ILE SER GLY LEU          
SEQRES   6 D   97  SER PRO GLY VAL ASP TYR THR ILE THR VAL TYR ALA TYR          
SEQRES   7 D   97  TYR SER TYR TYR ASP LEU TYR TYR SER TYR SER PRO SER          
SEQRES   8 D   97  SER ILE ASN TYR ARG THR                                      
HET    GOL  A  99       6                                                       
HET    GOL  A 100       6                                                       
HET    GOL  A 101       6                                                       
HET    GOL  A 102       6                                                       
HET    GOL  A 103       6                                                       
HET    GOL  C  95       6                                                       
HET    GOL  C  96       6                                                       
HET    GOL  C  97       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  GOL    8(C3 H8 O3)                                                  
FORMUL  13  HOH   *85(H2 O)                                                     
HELIX    1   1 LEU A   45  GLN A   56  1                                  12    
HELIX    2   2 GLU A   59  ASP A   61  5                                   3    
HELIX    3   3 LEU B   45  ARG B   55  1                                  11    
HELIX    4   4 GLU B   59  LEU B   63  5                                   5    
SHEET    1   A 9 ILE A  70  ARG A  71  0                                        
SHEET    2   A 9 LEU A  63  TYR A  67 -1  N  TYR A  67   O  ILE A  70           
SHEET    3   A 9 ASP A  87  ARG A  93 -1  O  GLU A  90   N  LEU A  66           
SHEET    4   A 9 HIS A  23  SER A  29  1  N  SER A  29   O  ALA A  91           
SHEET    5   A 9 GLU A  34  LYS A  40 -1  O  ILE A  39   N  ILE A  24           
SHEET    6   A 9 LEU C  81  SER C  84 -1  O  TYR C  82   N  LYS A  38           
SHEET    7   A 9 ASP C  67  TYR C  78 -1  N  TYR C  76   O  TYR C  83           
SHEET    8   A 9 TYR C  31  GLU C  38 -1  N  TYR C  31   O  TYR C  75           
SHEET    9   A 9 GLN C  46  PRO C  51 -1  O  PHE C  48   N  ILE C  34           
SHEET    1   B 8 ILE A  70  ARG A  71  0                                        
SHEET    2   B 8 LEU A  63  TYR A  67 -1  N  TYR A  67   O  ILE A  70           
SHEET    3   B 8 ASP A  87  ARG A  93 -1  O  GLU A  90   N  LEU A  66           
SHEET    4   B 8 HIS A  23  SER A  29  1  N  SER A  29   O  ALA A  91           
SHEET    5   B 8 GLU A  34  LYS A  40 -1  O  ILE A  39   N  ILE A  24           
SHEET    6   B 8 LEU C  81  SER C  84 -1  O  TYR C  82   N  LYS A  38           
SHEET    7   B 8 ASP C  67  TYR C  78 -1  N  TYR C  76   O  TYR C  83           
SHEET    8   B 8 SER C  88  ARG C  93 -1  O  ILE C  90   N  ILE C  70           
SHEET    1   C 9 ILE B  70  ARG B  71  0                                        
SHEET    2   C 9 ARG B  64  TYR B  67 -1  N  TYR B  67   O  ILE B  70           
SHEET    3   C 9 ASP B  87  HIS B  92 -1  O  HIS B  92   N  ARG B  64           
SHEET    4   C 9 ILE B  24  SER B  29  1  N  SER B  29   O  ALA B  91           
SHEET    5   C 9 GLU B  34  ILE B  39 -1  O  PHE B  37   N  LEU B  26           
SHEET    6   C 9 LEU D  81  TYR D  85 -1  O  SER D  84   N  PHE B  36           
SHEET    7   C 9 ASP D  67  TYR D  78 -1  N  TYR D  76   O  TYR D  83           
SHEET    8   C 9 TYR D  31  GLU D  38 -1  N  TYR D  31   O  TYR D  75           
SHEET    9   C 9 GLN D  46  PRO D  51 -1  O  VAL D  50   N  TYR D  32           
SHEET    1   D 8 ILE B  70  ARG B  71  0                                        
SHEET    2   D 8 ARG B  64  TYR B  67 -1  N  TYR B  67   O  ILE B  70           
SHEET    3   D 8 ASP B  87  HIS B  92 -1  O  HIS B  92   N  ARG B  64           
SHEET    4   D 8 ILE B  24  SER B  29  1  N  SER B  29   O  ALA B  91           
SHEET    5   D 8 GLU B  34  ILE B  39 -1  O  PHE B  37   N  LEU B  26           
SHEET    6   D 8 LEU D  81  TYR D  85 -1  O  SER D  84   N  PHE B  36           
SHEET    7   D 8 ASP D  67  TYR D  78 -1  N  TYR D  76   O  TYR D  83           
SHEET    8   D 8 SER D  88  ARG D  93 -1  O  ILE D  90   N  ILE D  70           
SHEET    1   E 3 GLU C   9  THR C  14  0                                        
SHEET    2   E 3 SER C  17  SER C  21 -1  O  LEU C  19   N  VAL C  11           
SHEET    3   E 3 THR C  56  ILE C  59 -1  O  ILE C  59   N  LEU C  18           
SHEET    1   F 3 GLU D   9  ALA D  13  0                                        
SHEET    2   F 3 LEU D  18  SER D  21 -1  O  LEU D  19   N  VAL D  11           
SHEET    3   F 3 THR D  56  ILE D  59 -1  O  ILE D  59   N  LEU D  18           
CISPEP   1 ILE A   96    GLY A   97          0        -2.74                     
CISPEP   2 VAL C    4    PRO C    5          0        -0.68                     
CISPEP   3 SER D    3    VAL D    4          0        -3.76                     
CISPEP   4 VAL D    4    PRO D    5          0        -0.88                     
CISPEP   5 SER D   27    SER D   28          0         3.77                     
SITE     1 AC1  6 GLU A  21  HIS A  23  ASN A  25  LYS A  38                    
SITE     2 AC1  6 ASP A  85  GLU C  47                                          
SITE     1 AC2  5 SER A  32  SER A  33  GLU A  34  HOH A 107                    
SITE     2 AC2  5 SER C  86                                                     
SITE     1 AC3  6 TYR A  67  ASP A  68  ASP A  87  ILE A  88                    
SITE     2 AC3  6 SER C  25  HOH C 118                                          
SITE     1 AC4  3 ASP A  68  ILE A  70  THR D  49                               
SITE     1 AC5  5 ASP A  75  HOH A 116  HOH A 117  TYR D  78                    
SITE     2 AC5  5 TYR D  79                                                     
SITE     1 AC6  5 ASP B  75  GLY C  41  TYR C  78  TYR C  79                    
SITE     2 AC6  5 HOH C 100                                                     
SITE     1 AC7  9 HOH A 109  PRO C   5  THR C   6  ASP C  23                    
SITE     2 AC7  9 ALA C  24  SER C  25  SER C  26  TYR C  32                    
SITE     3 AC7  9 HOH C 116                                                     
SITE     1 AC8  3 ASN C  91  TYR C  92  ARG C  93                               
CRYST1   59.637  175.462   52.830  90.00  90.00  90.00 P 21 21 2     8          
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      0.016768  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005699  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018929        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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