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Database: PDB
Entry: 1YKW
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HEADER    UNKNOWN FUNCTION                        18-JAN-05   1YKW              
TITLE     CRYSTAL STRUCTURE OF A NOVEL RUBISCO-LIKE PROTEIN FROM THE GREEN      
TITLE    2 SULFUR BACTERIUM CHLOROBIUM TEPIDUM                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RUBISCO-LIKE PROTEIN;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CHLOROBACULUM TEPIDUM;                          
SOURCE   3 ORGANISM_TAXID: 1097;                                                
SOURCE   4 GENE: CT1772;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL-21;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-11A                                   
KEYWDS    BETA-ALPHA-BARREL, UNKNOWN FUNCTION                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LI,M.R.SAWAYA,F.R.TABITA,D.EISENBERG                                
REVDAT   3   13-JUL-11 1YKW    1       VERSN                                    
REVDAT   2   24-FEB-09 1YKW    1       VERSN                                    
REVDAT   1   17-MAY-05 1YKW    0                                                
JRNL        AUTH   H.LI,M.R.SAWAYA,F.R.TABITA,D.EISENBERG                       
JRNL        TITL   CRYSTAL STRUCTURE OF A RUBISCO-LIKE PROTEIN FROM THE GREEN   
JRNL        TITL 2 SULFUR BACTERIUM CHLOROBIUM TEPIDUM.                         
JRNL        REF    STRUCTURE                     V.  13   779 2005              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   15893668                                                     
JRNL        DOI    10.1016/J.STR.2005.02.017                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 87.71                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 57608                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2956                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3019                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.37                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 161                          
REMARK   3   BIN FREE R VALUE                    : 0.3060                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6398                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 317                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.18000                                             
REMARK   3    B22 (A**2) : -0.74000                                             
REMARK   3    B33 (A**2) : 3.15000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.67000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.193         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.172         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.125         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.954         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6573 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8916 ; 1.626 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   825 ; 6.703 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   290 ;37.166 ;24.310       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1094 ;17.018 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    33 ;17.645 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   984 ; 0.117 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5009 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2874 ; 0.200 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4451 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   338 ; 0.166 ; 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):    31 ; 0.155 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.151 ; 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):  4224 ; 1.018 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6639 ; 1.598 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2637 ; 2.460 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2277 ; 3.820 ; 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 : 4                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      7       A      40      3                      
REMARK   3           1     B      7       B      40      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    136 ;  0.03 ;  0.05           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    139 ;  0.21 ;  5.00           
REMARK   3   TIGHT THERMAL      1    A (A**2):    136 ;  0.12 ;  0.50           
REMARK   3   LOOSE THERMAL      1    A (A**2):    139 ;  0.85 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     90       A     160      3                      
REMARK   3           1     B     90       B     160      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    A    (A):    280 ;  0.04 ;  0.05           
REMARK   3   LOOSE POSITIONAL   2    A    (A):    259 ;  0.23 ;  5.00           
REMARK   3   TIGHT THERMAL      2    A (A**2):    280 ;  0.17 ;  0.50           
REMARK   3   LOOSE THERMAL      2    A (A**2):    259 ;  0.99 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    225       A     320      3                      
REMARK   3           1     B    225       B     320      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    A    (A):    384 ;  0.04 ;  0.05           
REMARK   3   LOOSE POSITIONAL   3    A    (A):    351 ;  0.32 ;  5.00           
REMARK   3   TIGHT THERMAL      3    A (A**2):    384 ;  0.17 ;  0.50           
REMARK   3   LOOSE THERMAL      3    A (A**2):    351 ;  1.10 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    333       A     375      3                      
REMARK   3           1     B    333       B     375      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    A    (A):    168 ;  0.03 ;  0.05           
REMARK   3   LOOSE POSITIONAL   4    A    (A):    141 ;  0.47 ;  5.00           
REMARK   3   TIGHT THERMAL      4    A (A**2):    168 ;  0.18 ;  0.50           
REMARK   3   LOOSE THERMAL      4    A (A**2):    141 ;  1.38 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     4        A    47                          
REMARK   3    RESIDUE RANGE :   A    59        A   144                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.1884  25.0597  61.1763              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0393 T22:  -0.0026                                     
REMARK   3      T33:   0.0308 T12:   0.0500                                     
REMARK   3      T13:   0.0174 T23:   0.1331                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8163 L22:   0.9839                                     
REMARK   3      L33:   3.5280 L12:   0.1362                                     
REMARK   3      L13:   0.7262 L23:  -0.2174                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0248 S12:   0.4554 S13:   0.4528                       
REMARK   3      S21:  -0.0916 S22:   0.0108 S23:  -0.0258                       
REMARK   3      S31:  -0.2571 S32:  -0.1322 S33:  -0.0357                       
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   145        A   428                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.3272  -3.4221  73.7012              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0497 T22:  -0.0803                                     
REMARK   3      T33:  -0.0369 T12:   0.0182                                     
REMARK   3      T13:  -0.0170 T23:  -0.0481                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9732 L22:   0.5813                                     
REMARK   3      L33:   1.0973 L12:  -0.1111                                     
REMARK   3      L13:  -0.3589 L23:   0.0207                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0479 S12:   0.2262 S13:  -0.3297                       
REMARK   3      S21:  -0.0117 S22:   0.0318 S23:  -0.0434                       
REMARK   3      S31:   0.2217 S32:   0.0961 S33:   0.0161                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     4        B    47                          
REMARK   3    RESIDUE RANGE :   B    59        B   144                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.6991 -11.2262  61.2429              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0389 T22:   0.0282                                     
REMARK   3      T33:   0.0118 T12:   0.0313                                     
REMARK   3      T13:   0.0025 T23:  -0.1425                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5708 L22:   1.2555                                     
REMARK   3      L33:   3.5267 L12:   0.1927                                     
REMARK   3      L13:  -0.8214 L23:   0.0587                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0349 S12:   0.4798 S13:  -0.4892                       
REMARK   3      S21:  -0.1173 S22:   0.0217 S23:  -0.0612                       
REMARK   3      S31:   0.3271 S32:   0.0781 S33:   0.0133                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   145        B   174                          
REMARK   3    RESIDUE RANGE :   B   177        B   428                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.4417  17.2069  73.7040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0558 T22:  -0.0734                                     
REMARK   3      T33:  -0.0269 T12:   0.0197                                     
REMARK   3      T13:   0.0104 T23:   0.0455                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8287 L22:   0.6061                                     
REMARK   3      L33:   1.1205 L12:  -0.2019                                     
REMARK   3      L13:   0.3141 L23:  -0.0959                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0379 S12:   0.2228 S13:   0.3409                       
REMARK   3      S21:   0.0339 S22:   0.0330 S23:   0.0464                       
REMARK   3      S31:  -0.2073 S32:  -0.0925 S33:   0.0050                       
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1YKW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB031632.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-NOV-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1271                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60951                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 90.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.39700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: EPMR                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 5RUB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MAGNESIUM FORMATE , PH 5.9,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.0K                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       39.22550            
REMARK 290   SMTRY3   2  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A    48                                                      
REMARK 465     GLN A    49                                                      
REMARK 465     TRP A    50                                                      
REMARK 465     LYS A    51                                                      
REMARK 465     ARG A    52                                                      
REMARK 465     VAL A    53                                                      
REMARK 465     GLY A    54                                                      
REMARK 465     VAL A    55                                                      
REMARK 465     ASP A    56                                                      
REMARK 465     GLU A    57                                                      
REMARK 465     ASP A    58                                                      
REMARK 465     SER A   429                                                      
REMARK 465     LEU A   430                                                      
REMARK 465     LEU A   431                                                      
REMARK 465     LYS A   432                                                      
REMARK 465     LYS A   433                                                      
REMARK 465     GLN A   434                                                      
REMARK 465     ASP A   435                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ALA B    48                                                      
REMARK 465     GLN B    49                                                      
REMARK 465     TRP B    50                                                      
REMARK 465     LYS B    51                                                      
REMARK 465     ARG B    52                                                      
REMARK 465     VAL B    53                                                      
REMARK 465     GLY B    54                                                      
REMARK 465     VAL B    55                                                      
REMARK 465     ASP B    56                                                      
REMARK 465     GLU B    57                                                      
REMARK 465     ASP B    58                                                      
REMARK 465     ILE B   175                                                      
REMARK 465     GLY B   176                                                      
REMARK 465     SER B   429                                                      
REMARK 465     LEU B   430                                                      
REMARK 465     LEU B   431                                                      
REMARK 465     LYS B   432                                                      
REMARK 465     LYS B   433                                                      
REMARK 465     GLN B   434                                                      
REMARK 465     ASP B   435                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  46     -104.03   -151.69                                   
REMARK 500    CYS A 117       46.54   -145.57                                   
REMARK 500    ASN A 160       51.91     38.69                                   
REMARK 500    ALA A 204     -126.55   -104.84                                   
REMARK 500    SER A 209       78.77   -151.50                                   
REMARK 500    PHE A 290      -33.09     91.68                                   
REMARK 500    MET A 329       33.95    -80.36                                   
REMARK 500    SER B  46     -110.11   -141.12                                   
REMARK 500    ASP B  69      149.01   -176.22                                   
REMARK 500    CYS B 117       53.04   -143.38                                   
REMARK 500    PRO B 179      -37.25    -36.17                                   
REMARK 500    ALA B 204     -119.15   -114.25                                   
REMARK 500    SER B 209       75.86   -151.52                                   
REMARK 500    PHE B 290      -35.35     86.80                                   
REMARK 500    MET B 329       32.72    -94.14                                   
REMARK 500    VAL B 385      -66.49    -96.81                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR                                         
DBREF  1YKW A    1   435  UNP    Q8KBL4   Q8KBL4_CHLTE     1    435             
DBREF  1YKW B    1   435  UNP    Q8KBL4   Q8KBL4_CHLTE     1    435             
SEQADV 1YKW VAL A  328  UNP  Q8KBL4    MET   328 ENGINEERED                     
SEQADV 1YKW VAL B  328  UNP  Q8KBL4    MET   328 ENGINEERED                     
SEQRES   1 A  435  MET ASN ALA GLU ASP VAL LYS GLY PHE PHE ALA SER ARG          
SEQRES   2 A  435  GLU SER LEU ASP MET GLU GLN TYR LEU VAL LEU ASP TYR          
SEQRES   3 A  435  TYR LEU GLU SER VAL GLY ASP ILE GLU THR ALA LEU ALA          
SEQRES   4 A  435  HIS PHE CYS SER GLU GLN SER THR ALA GLN TRP LYS ARG          
SEQRES   5 A  435  VAL GLY VAL ASP GLU ASP PHE ARG LEU VAL HIS ALA ALA          
SEQRES   6 A  435  LYS VAL ILE ASP TYR GLU VAL ILE GLU GLU LEU GLU GLN          
SEQRES   7 A  435  LEU SER TYR PRO VAL LYS HIS SER GLU THR GLY LYS ILE          
SEQRES   8 A  435  HIS ALA CYS ARG VAL THR ILE ALA HIS PRO HIS CYS ASN          
SEQRES   9 A  435  PHE GLY PRO LYS ILE PRO ASN LEU LEU THR ALA VAL CYS          
SEQRES  10 A  435  GLY GLU GLY THR TYR PHE THR PRO GLY VAL PRO VAL VAL          
SEQRES  11 A  435  LYS LEU MET ASP ILE HIS PHE PRO ASP THR TYR LEU ALA          
SEQRES  12 A  435  ASP PHE GLU GLY PRO LYS PHE GLY ILE GLU GLY LEU ARG          
SEQRES  13 A  435  ASP ILE LEU ASN ALA HIS GLY ARG PRO ILE PHE PHE GLY          
SEQRES  14 A  435  VAL VAL LYS PRO ASN ILE GLY LEU SER PRO GLY GLU PHE          
SEQRES  15 A  435  ALA GLU ILE ALA TYR GLN SER TRP LEU GLY GLY LEU ASP          
SEQRES  16 A  435  ILE ALA LYS ASP ASP GLU MET LEU ALA ASP VAL THR TRP          
SEQRES  17 A  435  SER SER ILE GLU GLU ARG ALA ALA HIS LEU GLY LYS ALA          
SEQRES  18 A  435  ARG ARG LYS ALA GLU ALA GLU THR GLY GLU PRO LYS ILE          
SEQRES  19 A  435  TYR LEU ALA ASN ILE THR ASP GLU VAL ASP SER LEU MET          
SEQRES  20 A  435  GLU LYS HIS ASP VAL ALA VAL ARG ASN GLY ALA ASN ALA          
SEQRES  21 A  435  LEU LEU ILE ASN ALA LEU PRO VAL GLY LEU SER ALA VAL          
SEQRES  22 A  435  ARG MET LEU SER ASN TYR THR GLN VAL PRO LEU ILE GLY          
SEQRES  23 A  435  HIS PHE PRO PHE ILE ALA SER PHE SER ARG MET GLU LYS          
SEQRES  24 A  435  TYR GLY ILE HIS SER LYS VAL MET THR LYS LEU GLN ARG          
SEQRES  25 A  435  LEU ALA GLY LEU ASP ALA VAL ILE MET PRO GLY PHE GLY          
SEQRES  26 A  435  ASP ARG VAL MET THR PRO GLU GLU GLU VAL LEU GLU ASN          
SEQRES  27 A  435  VAL ILE GLU CYS THR LYS PRO MET GLY ARG ILE LYS PRO          
SEQRES  28 A  435  CYS LEU PRO VAL PRO GLY GLY SER ASP SER ALA LEU THR          
SEQRES  29 A  435  LEU GLN THR VAL TYR GLU LYS VAL GLY ASN VAL ASP PHE          
SEQRES  30 A  435  GLY PHE VAL PRO GLY ARG GLY VAL PHE GLY HIS PRO MET          
SEQRES  31 A  435  GLY PRO LYS ALA GLY ALA LYS SER ILE ARG GLN ALA TRP          
SEQRES  32 A  435  GLU ALA ILE GLU GLN GLY ILE SER ILE GLU THR TRP ALA          
SEQRES  33 A  435  GLU THR HIS PRO GLU LEU GLN ALA MET VAL ASP GLN SER          
SEQRES  34 A  435  LEU LEU LYS LYS GLN ASP                                      
SEQRES   1 B  435  MET ASN ALA GLU ASP VAL LYS GLY PHE PHE ALA SER ARG          
SEQRES   2 B  435  GLU SER LEU ASP MET GLU GLN TYR LEU VAL LEU ASP TYR          
SEQRES   3 B  435  TYR LEU GLU SER VAL GLY ASP ILE GLU THR ALA LEU ALA          
SEQRES   4 B  435  HIS PHE CYS SER GLU GLN SER THR ALA GLN TRP LYS ARG          
SEQRES   5 B  435  VAL GLY VAL ASP GLU ASP PHE ARG LEU VAL HIS ALA ALA          
SEQRES   6 B  435  LYS VAL ILE ASP TYR GLU VAL ILE GLU GLU LEU GLU GLN          
SEQRES   7 B  435  LEU SER TYR PRO VAL LYS HIS SER GLU THR GLY LYS ILE          
SEQRES   8 B  435  HIS ALA CYS ARG VAL THR ILE ALA HIS PRO HIS CYS ASN          
SEQRES   9 B  435  PHE GLY PRO LYS ILE PRO ASN LEU LEU THR ALA VAL CYS          
SEQRES  10 B  435  GLY GLU GLY THR TYR PHE THR PRO GLY VAL PRO VAL VAL          
SEQRES  11 B  435  LYS LEU MET ASP ILE HIS PHE PRO ASP THR TYR LEU ALA          
SEQRES  12 B  435  ASP PHE GLU GLY PRO LYS PHE GLY ILE GLU GLY LEU ARG          
SEQRES  13 B  435  ASP ILE LEU ASN ALA HIS GLY ARG PRO ILE PHE PHE GLY          
SEQRES  14 B  435  VAL VAL LYS PRO ASN ILE GLY LEU SER PRO GLY GLU PHE          
SEQRES  15 B  435  ALA GLU ILE ALA TYR GLN SER TRP LEU GLY GLY LEU ASP          
SEQRES  16 B  435  ILE ALA LYS ASP ASP GLU MET LEU ALA ASP VAL THR TRP          
SEQRES  17 B  435  SER SER ILE GLU GLU ARG ALA ALA HIS LEU GLY LYS ALA          
SEQRES  18 B  435  ARG ARG LYS ALA GLU ALA GLU THR GLY GLU PRO LYS ILE          
SEQRES  19 B  435  TYR LEU ALA ASN ILE THR ASP GLU VAL ASP SER LEU MET          
SEQRES  20 B  435  GLU LYS HIS ASP VAL ALA VAL ARG ASN GLY ALA ASN ALA          
SEQRES  21 B  435  LEU LEU ILE ASN ALA LEU PRO VAL GLY LEU SER ALA VAL          
SEQRES  22 B  435  ARG MET LEU SER ASN TYR THR GLN VAL PRO LEU ILE GLY          
SEQRES  23 B  435  HIS PHE PRO PHE ILE ALA SER PHE SER ARG MET GLU LYS          
SEQRES  24 B  435  TYR GLY ILE HIS SER LYS VAL MET THR LYS LEU GLN ARG          
SEQRES  25 B  435  LEU ALA GLY LEU ASP ALA VAL ILE MET PRO GLY PHE GLY          
SEQRES  26 B  435  ASP ARG VAL MET THR PRO GLU GLU GLU VAL LEU GLU ASN          
SEQRES  27 B  435  VAL ILE GLU CYS THR LYS PRO MET GLY ARG ILE LYS PRO          
SEQRES  28 B  435  CYS LEU PRO VAL PRO GLY GLY SER ASP SER ALA LEU THR          
SEQRES  29 B  435  LEU GLN THR VAL TYR GLU LYS VAL GLY ASN VAL ASP PHE          
SEQRES  30 B  435  GLY PHE VAL PRO GLY ARG GLY VAL PHE GLY HIS PRO MET          
SEQRES  31 B  435  GLY PRO LYS ALA GLY ALA LYS SER ILE ARG GLN ALA TRP          
SEQRES  32 B  435  GLU ALA ILE GLU GLN GLY ILE SER ILE GLU THR TRP ALA          
SEQRES  33 B  435  GLU THR HIS PRO GLU LEU GLN ALA MET VAL ASP GLN SER          
SEQRES  34 B  435  LEU LEU LYS LYS GLN ASP                                      
FORMUL   3  HOH   *317(H2 O)                                                    
HELIX    1   1 ASP A    5  PHE A    9  5                                   5    
HELIX    2   2 SER A   12  SER A   15  5                                   4    
HELIX    3   3 ASP A   17  GLN A   20  5                                   4    
HELIX    4   4 ASP A   33  GLU A   44  1                                  12    
HELIX    5   5 HIS A  102  GLY A  106  5                                   5    
HELIX    6   6 LYS A  108  CYS A  117  1                                  10    
HELIX    7   7 GLU A  119  PHE A  123  1                                   5    
HELIX    8   8 PRO A  138  ALA A  143  1                                   6    
HELIX    9   9 PHE A  150  ASN A  160  1                                  11    
HELIX   10  10 SER A  178  GLY A  192  1                                  15    
HELIX   11  11 SER A  210  GLY A  230  1                                  21    
HELIX   12  12 GLU A  242  SER A  245  5                                   4    
HELIX   13  13 SER A  245  GLY A  257  1                                  13    
HELIX   14  14 ALA A  265  GLY A  269  1                                   5    
HELIX   15  15 GLY A  269  THR A  280  1                                  12    
HELIX   16  16 ILE A  291  PHE A  294  1                                   4    
HELIX   17  17 HIS A  303  GLY A  315  1                                  13    
HELIX   18  18 PRO A  331  LYS A  344  1                                  14    
HELIX   19  19 THR A  364  GLY A  373  1                                  10    
HELIX   20  20 GLY A  391  GLN A  408  1                                  18    
HELIX   21  21 SER A  411  GLU A  417  1                                   7    
HELIX   22  22 HIS A  419  GLN A  428  1                                  10    
HELIX   23  23 ASP B    5  PHE B    9  5                                   5    
HELIX   24  24 SER B   12  SER B   15  5                                   4    
HELIX   25  25 ASP B   17  GLN B   20  5                                   4    
HELIX   26  26 ASP B   33  GLU B   44  1                                  12    
HELIX   27  27 HIS B  102  GLY B  106  5                                   5    
HELIX   28  28 LYS B  108  CYS B  117  1                                  10    
HELIX   29  29 GLU B  119  PHE B  123  1                                   5    
HELIX   30  30 PRO B  138  ALA B  143  1                                   6    
HELIX   31  31 PHE B  150  ASN B  160  1                                  11    
HELIX   32  32 SER B  178  GLY B  192  1                                  15    
HELIX   33  33 SER B  210  GLY B  230  1                                  21    
HELIX   34  34 GLU B  242  SER B  245  5                                   4    
HELIX   35  35 SER B  245  GLY B  257  1                                  13    
HELIX   36  36 ALA B  265  GLY B  269  1                                   5    
HELIX   37  37 GLY B  269  THR B  280  1                                  12    
HELIX   38  38 ILE B  291  PHE B  294  1                                   4    
HELIX   39  39 HIS B  303  GLY B  315  1                                  13    
HELIX   40  40 PRO B  331  LYS B  344  1                                  14    
HELIX   41  41 THR B  364  GLY B  373  1                                  10    
HELIX   42  42 GLY B  391  GLN B  408  1                                  18    
HELIX   43  43 SER B  411  GLU B  417  1                                   7    
HELIX   44  44 HIS B  419  GLN B  428  1                                  10    
SHEET    1   A 5 LYS A  66  LEU A  76  0                                        
SHEET    2   A 5 ILE A  91  PRO A 101 -1  O  ARG A  95   N  GLU A  71           
SHEET    3   A 5 TYR A  21  VAL A  31 -1  N  LEU A  22   O  HIS A 100           
SHEET    4   A 5 VAL A 129  HIS A 136 -1  O  LYS A 131   N  TYR A  27           
SHEET    5   A 5 GLY A 301  ILE A 302  1  O  GLY A 301   N  VAL A 130           
SHEET    1   B 8 LEU A 353  GLY A 357  0                                        
SHEET    2   B 8 ALA A 318  PRO A 322  1  N  MET A 321   O  GLY A 357           
SHEET    3   B 8 LEU A 284  HIS A 287  1  N  GLY A 286   O  ILE A 320           
SHEET    4   B 8 ALA A 260  ASN A 264  1  N  LEU A 261   O  ILE A 285           
SHEET    5   B 8 ILE A 234  ASN A 238  1  N  ALA A 237   O  LEU A 262           
SHEET    6   B 8 ILE A 196  LYS A 198  1  N  ALA A 197   O  ILE A 234           
SHEET    7   B 8 ILE A 166  VAL A 170  1  N  GLY A 169   O  ILE A 196           
SHEET    8   B 8 GLY A 378  PHE A 379  1  O  PHE A 379   N  PHE A 168           
SHEET    1   C 5 LYS B  66  LEU B  76  0                                        
SHEET    2   C 5 ILE B  91  PRO B 101 -1  O  ARG B  95   N  GLU B  71           
SHEET    3   C 5 TYR B  21  VAL B  31 -1  N  LEU B  22   O  HIS B 100           
SHEET    4   C 5 VAL B 129  HIS B 136 -1  O  LYS B 131   N  TYR B  27           
SHEET    5   C 5 GLY B 301  ILE B 302  1  O  GLY B 301   N  VAL B 130           
SHEET    1   D 8 LEU B 353  GLY B 357  0                                        
SHEET    2   D 8 ALA B 318  PRO B 322  1  N  MET B 321   O  GLY B 357           
SHEET    3   D 8 LEU B 284  HIS B 287  1  N  GLY B 286   O  ILE B 320           
SHEET    4   D 8 ALA B 260  ASN B 264  1  N  LEU B 261   O  ILE B 285           
SHEET    5   D 8 ILE B 234  ASN B 238  1  N  ALA B 237   O  LEU B 262           
SHEET    6   D 8 ILE B 196  LYS B 198  1  N  ALA B 197   O  ILE B 234           
SHEET    7   D 8 ILE B 166  VAL B 170  1  N  GLY B 169   O  LYS B 198           
SHEET    8   D 8 GLY B 378  PHE B 379  1  O  PHE B 379   N  PHE B 168           
CISPEP   1 LYS A  172    PRO A  173          0        10.14                     
CISPEP   2 LYS B  172    PRO B  173          0        -2.17                     
CRYST1   67.348   78.451   90.369  90.00  99.95  90.00 P 1 21 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      0.014848  0.000000  0.002605        0.00000                         
SCALE2      0.000000  0.012747  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011235        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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