GenomeNet

Database: PDB
Entry: 2GJG
LinkDB: 2GJG
Original site: 2GJG 
HEADER    MOTOR PROTEIN                           30-MAR-06   2GJG              
TITLE     CRYSTAL STRUCTURE OF A PILZ-CONTAINING PROTEIN (PP4397) FROM          
TITLE    2 PSEUDOMONAS PUTIDA KT2440 AT 2.25 A RESOLUTION                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYPOTHETICAL PROTEIN PP4397;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;                             
SOURCE   3 ORGANISM_TAXID: 160488;                                              
SOURCE   4 STRAIN: KT2440;                                                      
SOURCE   5 GENE: NP_746511.1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HK100;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: SPEEDET                                   
KEYWDS    PILZ-CONTAINING PROTEIN, STRUCTURAL GENOMICS, JOINT CENTER FOR        
KEYWDS   2 STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-2,      
KEYWDS   3 MOTOR PROTEIN                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                           
REVDAT   5   13-JUL-11 2GJG    1       VERSN                                    
REVDAT   4   28-JUL-10 2GJG    1       HEADER TITLE  KEYWDS                     
REVDAT   3   24-FEB-09 2GJG    1       VERSN                                    
REVDAT   2   31-OCT-06 2GJG    1       JRNL   KEYWDS SOURCE TITLE               
REVDAT   2 2                   1       REMARK                                   
REVDAT   1   25-APR-06 2GJG    0                                                
JRNL        AUTH   JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                  
JRNL        TITL   CRYSTAL STRUCTURE OF HYPOTHETICAL PROTEIN (NP_746511.1) FROM 
JRNL        TITL 2 PSEUDOMONAS PUTIDA KT2440 AT 2.25 A RESOLUTION               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 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 WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.69                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 11212                          
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) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 564                             
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) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.31                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 775                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4110                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 38                           
REMARK   3   BIN FREE R VALUE                    : 0.5560                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1948                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 137                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 33.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.03000                                             
REMARK   3    B22 (A**2) : 0.52000                                              
REMARK   3    B33 (A**2) : -0.39000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.85000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.416         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.274         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.229         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.634        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.890                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2022 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1810 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2729 ; 1.501 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4182 ; 0.823 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   252 ; 5.905 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   105 ;33.900 ;23.333       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   335 ;15.254 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;20.654 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   290 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2300 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   437 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   364 ; 0.196 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1784 ; 0.175 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   933 ; 0.176 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1288 ; 0.085 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    98 ; 0.177 ; 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):    28 ; 0.207 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    74 ; 0.254 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    16 ; 0.178 ; 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):  1284 ; 0.710 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   508 ; 0.129 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1984 ; 1.051 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   829 ; 1.580 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   743 ; 2.447 ; 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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   130                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.8838  38.6396  15.6758              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1361 T22:  -0.1578                                     
REMARK   3      T33:  -0.1192 T12:   0.0316                                     
REMARK   3      T13:  -0.0224 T23:   0.0334                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7451 L22:   1.8194                                     
REMARK   3      L33:   2.2138 L12:  -0.7583                                     
REMARK   3      L13:  -1.0808 L23:   0.6241                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0193 S12:   0.2036 S13:  -0.0462                       
REMARK   3      S21:  -0.0149 S22:  -0.0374 S23:   0.2130                       
REMARK   3      S31:  -0.0025 S32:  -0.1799 S33:   0.0567                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   131        A   247                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.1146  34.0825 -13.1528              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1196 T22:  -0.0893                                     
REMARK   3      T33:  -0.1223 T12:  -0.0441                                     
REMARK   3      T13:  -0.0400 T23:  -0.0143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7601 L22:   2.2906                                     
REMARK   3      L33:   2.9950 L12:   0.3279                                     
REMARK   3      L13:  -1.6785 L23:  -0.5162                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0335 S12:   0.2707 S13:   0.1262                       
REMARK   3      S21:  -0.0515 S22:   0.0739 S23:   0.1930                       
REMARK   3      S31:  -0.0787 S32:  -0.3162 S33:  -0.1074                       
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:                                           
REMARK   3  1.HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                 
REMARK   3  2.A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE           
REMARK   3  INCORPORATION                                                       
REMARK   3  DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE 
REMARK   3  RESIDUES WAS REDUCED TO 0.75 TO ACCOUNT FOR THE REDUCED SCATTERING  
REMARK   3  POWER DUE TO PARTIAL S-MET INCORPORATION.                           
REMARK   3  3.ELECTRON DENSITY MAP SUPPORTS THE CONFIGURATION OF RESIDUE 194    
REMARK   3  WITH                                                                
REMARK   3  RAMACHANDRAN OUTLIER IN THIS MODEL.                                 
REMARK   3  4.ETHYLENE GLYCOL MOLECULES FROM CRYSTALIZATION CONDITION ARE BULIT 
REMARK   3  IN THIS                                                             
REMARK   3  MODEL.                                                              
REMARK   3  5.ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY                      
REMARK   4                                                                      
REMARK   4 2GJG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB037193.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-FEB-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97941, 0.97879, 0.91162          
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : FLAT COLLIMATING MIRROR, DOUBLE    
REMARK 200                                   CRYSTAL MONOCHROMATOR, TOROID      
REMARK 200                                   FOCUSING MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11812                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.690                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : 0.06100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.30000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 35.0% 2-PROPANOL, 5.0% PEG-1000, 0.1M    
REMARK 280  CITRATE PH 5.5 , VAPOR DIFFUSION,SITTING DROP,NANODROP,             
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       44.61200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.40950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       44.61200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.40950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
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   BIOMT1   2 -1.000000  0.000000  0.000000       89.22400            
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     GLY A     0                                                      
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     ASN A   3    CB   CG   OD1                                       
REMARK 470     GLN A   9    OE1  NE2                                            
REMARK 470     LEU A  18    CD1  CD2                                            
REMARK 470     ILE A  35    CD1                                                 
REMARK 470     THR A  37    CG2                                                 
REMARK 470     GLU A  55    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  67    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A  99    NZ                                                  
REMARK 470     GLU A 102    OE1  OE2                                            
REMARK 470     GLN A 223    CD   OE1  NE2                                       
REMARK 470     LYS A 227    CE   NZ                                             
REMARK 470     GLU A 229    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 234    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 237    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 238    CD   OE1  OE2                                       
REMARK 470     ARG A 240    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 241    CZ   NH1  NH2                                       
REMARK 470     LYS A 244    CE   NZ                                             
REMARK 470     ASP A 246    CB   CG   OD1  OD2                                  
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    ASP A 194      103.66    -19.11                                   
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 EDO A 248                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 249                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 250                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 360827   RELATED DB: TARGETDB                            
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION                      
REMARK 999 TAG MGSDKIHHHHHHENLYFQG.  THE TAG WAS REMOVED WITH TEV               
REMARK 999 PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE                  
REMARK 999 TARGET SEQUENCE.                                                     
DBREF  2GJG A    1   247  UNP    Q88EQ6   Q88EQ6_PSEPK     1    247             
SEQADV 2GJG GLY A    0  UNP  Q88EQ6              LEADER SEQUENCE                
SEQADV 2GJG MSE A    1  UNP  Q88EQ6    MET     1 MODIFIED RESIDUE               
SEQADV 2GJG MSE A   64  UNP  Q88EQ6    MET    64 MODIFIED RESIDUE               
SEQADV 2GJG MSE A  151  UNP  Q88EQ6    MET   151 MODIFIED RESIDUE               
SEQADV 2GJG MSE A  196  UNP  Q88EQ6    MET   196 MODIFIED RESIDUE               
SEQRES   1 A  248  GLY MSE PHE ASN GLU SER ASP ALA PRO GLN PRO PRO LYS          
SEQRES   2 A  248  VAL LEU SER THR PRO LEU GLU ILE ALA ALA ASN LEU ARG          
SEQRES   3 A  248  GLN LEU GLN GLU SER HIS ASP PRO LEU ILE ILE THR PHE          
SEQRES   4 A  248  HIS ASP ARG SER HIS ARG PHE GLN SER TYR VAL VAL HIS          
SEQRES   5 A  248  VAL ASP ARG GLU SER ASN THR LEU ALA LEU ASP GLU MSE          
SEQRES   6 A  248  ILE PRO ARG ASP GLY GLU LYS PHE ILE GLU ASN GLY GLU          
SEQRES   7 A  248  HIS PHE ARG VAL GLU GLY PHE HIS ASP GLY VAL ARG ILE          
SEQRES   8 A  248  ALA TRP GLU CYS ASP HIS ALA LEU LYS ILE SER GLU VAL          
SEQRES   9 A  248  ASP GLY HIS ARG CYS TYR SER GLY PRO LEU PRO GLN GLU          
SEQRES  10 A  248  VAL THR TYR HIS GLN ARG ARG ASN ALA PHE ARG ALA ALA          
SEQRES  11 A  248  LEU LYS LEU SER GLN LEU VAL ASP ILE ILE LEU ASP GLY          
SEQRES  12 A  248  ALA HIS LEU LYS GLY ASN GLY ALA MSE ARG GLY LYS LEU          
SEQRES  13 A  248  LEU ASP ILE SER ALA THR GLY CYS LYS LEU ARG PHE GLU          
SEQRES  14 A  248  GLY ASN VAL GLU ASP ARG LEU GLN LEU GLY GLN VAL TYR          
SEQRES  15 A  248  GLU ARG PHE LYS ALA GLY ASN PRO LEU GLY LEU VAL ASP          
SEQRES  16 A  248  THR MSE VAL GLU LEU ARG HIS LEU HIS TYR GLU GLU ARG          
SEQRES  17 A  248  ILE ASN THR THR PHE ALA GLY VAL ARG PHE HIS ASN LEU          
SEQRES  18 A  248  SER GLY GLN ALA GLN ARG LYS ILE GLU SER PHE VAL TYR          
SEQRES  19 A  248  GLN LEU GLN ARG GLU ALA ARG ARG PHE ASP LYS ASP ASP          
SEQRES  20 A  248  TYR                                                          
MODRES 2GJG MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 2GJG MSE A   64  MET  SELENOMETHIONINE                                   
MODRES 2GJG MSE A  151  MET  SELENOMETHIONINE                                   
MODRES 2GJG MSE A  196  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  64       8                                                       
HET    MSE  A 151       8                                                       
HET    MSE  A 196       8                                                       
HET    EDO  A 248       4                                                       
HET    EDO  A 249       4                                                       
HET    EDO  A 250       4                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  MSE    4(C5 H11 N O2 SE)                                            
FORMUL   2  EDO    3(C2 H6 O2)                                                  
FORMUL   5  HOH   *137(H2 O)                                                    
HELIX    1   1 THR A   16  SER A   30  1                                  15    
HELIX    2   2 PRO A   66  ASP A   68  5                                   3    
HELIX    3   3 GLY A   69  ASN A   75  1                                   7    
HELIX    4   4 ARG A  122  LEU A  130  1                                   9    
HELIX    5   5 VAL A  171  LEU A  175  5                                   5    
HELIX    6   6 GLU A  206  ILE A  208  5                                   3    
HELIX    7   7 SER A  221  LYS A  244  1                                  24    
SHEET    1   A 6 LYS A  12  LEU A  14  0                                        
SHEET    2   A 6 VAL A 117  HIS A 120 -1  O  VAL A 117   N  LEU A  14           
SHEET    3   A 6 VAL A  88  CYS A  94 -1  N  ALA A  91   O  THR A 118           
SHEET    4   A 6 PHE A  79  HIS A  85 -1  N  PHE A  79   O  CYS A  94           
SHEET    5   A 6 LEU A  34  PHE A  38 -1  N  THR A  37   O  ARG A  80           
SHEET    6   A 6 PHE A  45  SER A  47 -1  O  PHE A  45   N  ILE A  36           
SHEET    1   B 4 VAL A  49  ASP A  53  0                                        
SHEET    2   B 4 THR A  58  ASP A  62 -1  O  THR A  58   N  ASP A  53           
SHEET    3   B 4 HIS A 106  GLY A 111 -1  O  GLY A 111   N  LEU A  59           
SHEET    4   B 4 LYS A  99  VAL A 103 -1  N  LYS A  99   O  SER A 110           
SHEET    1   C 7 ASP A 137  ASP A 141  0                                        
SHEET    2   C 7 MSE A 151  ILE A 158 -1  O  MSE A 151   N  LEU A 140           
SHEET    3   C 7 GLY A 162  GLU A 168 -1  O  LYS A 164   N  LEU A 156           
SHEET    4   C 7 THR A 210  HIS A 218 -1  O  VAL A 215   N  CYS A 163           
SHEET    5   C 7 LEU A 192  GLU A 205 -1  N  HIS A 203   O  PHE A 212           
SHEET    6   C 7 VAL A 180  ALA A 186 -1  N  PHE A 184   O  THR A 195           
SHEET    7   C 7 ASP A 137  ASP A 141 -1  N  ASP A 141   O  ARG A 183           
LINK         C   MSE A   1                 N   PHE A   2     1555   1555  1.33  
LINK         C   GLU A  63                 N   MSE A  64     1555   1555  1.33  
LINK         C   MSE A  64                 N   ILE A  65     1555   1555  1.33  
LINK         C   ALA A 150                 N   MSE A 151     1555   1555  1.33  
LINK         C   MSE A 151                 N   ARG A 152     1555   1555  1.33  
LINK         C   THR A 195                 N   MSE A 196     1555   1555  1.33  
LINK         C   MSE A 196                 N   VAL A 197     1555   1555  1.32  
CISPEP   1 ILE A   65    PRO A   66          0        -1.51                     
CISPEP   2 ASN A  188    PRO A  189          0         4.73                     
SITE     1 AC1  6 LEU A  59  LEU A  61  TRP A  92  LEU A  98                    
SITE     2 AC1  6 HOH A 273  HOH A 278                                          
SITE     1 AC2  6 GLU A 116  HIS A 203  TYR A 204  GLU A 205                    
SITE     2 AC2  6 GLU A 206  HOH A 269                                          
SITE     1 AC3  6 PRO A   8  GLN A   9  HIS A 120  GLN A 121                    
SITE     2 AC3  6 ARG A 122  ALA A 125                                          
CRYST1   89.224   48.819   57.476  90.00  93.41  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011210  0.000000  0.000670        0.00000                         
SCALE2      0.000000  0.020480  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017430        0.00000                         
HETATM    1  N   MSE A   1      17.737  28.461 -13.987  1.00 39.67           N  
HETATM    2  CA  MSE A   1      17.224  27.056 -14.064  1.00 39.65           C  
HETATM    3  C   MSE A   1      17.841  26.183 -12.977  1.00 39.27           C  
HETATM    4  O   MSE A   1      17.230  25.219 -12.519  1.00 39.26           O  
HETATM    5  CB  MSE A   1      17.523  26.448 -15.428  1.00 39.95           C  
HETATM    6  CG  MSE A   1      16.917  27.202 -16.599  1.00 40.86           C  
HETATM    7 SE   MSE A   1      14.970  27.335 -16.582  0.75 43.39          SE  
HETATM    8  CE  MSE A   1      14.705  28.960 -15.442  1.00 42.11           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system