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Database: PDB
Entry: 5NB8
LinkDB: 5NB8
Original site: 5NB8 
HEADER    SIGNALING PROTEIN                       01-MAR-17   5NB8              
TITLE     STRUCTURE OF VWC DOMAIN FROM CCN3                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN NOV HOMOLOG;                                       
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 100-195;                                      
COMPND   5 SYNONYM: NOVH,CCN FAMILY MEMBER 3,NEPHROBLASTOMA-OVEREXPRESSED GENE  
COMPND   6 PROTEIN HOMOLOG;                                                     
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: NOV, CCN3;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PBAT4                                     
KEYWDS    CCN3, VWC, DOMAINS, SIGNALLING, BMP, SIGNALING PROTEIN                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.-R.XU,M.HYVONEN                                                     
REVDAT   2   09-AUG-17 5NB8    1       JRNL                                     
REVDAT   1   14-JUN-17 5NB8    0                                                
JRNL        AUTH   E.R.XU,E.E.BLYTHE,G.FISCHER,M.HYVONEN                        
JRNL        TITL   STRUCTURAL ANALYSES OF VON WILLEBRAND FACTOR C DOMAINS OF    
JRNL        TITL 2 COLLAGEN 2A AND CCN3 REVEAL AN ALTERNATIVE MODE OF BINDING   
JRNL        TITL 3 TO BONE MORPHOGENETIC PROTEIN-2.                             
JRNL        REF    J. BIOL. CHEM.                V. 292 12516 2017              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   28584056                                                     
JRNL        DOI    10.1074/JBC.M117.788992                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.58                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.980                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 25446                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1298                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 28.5831 -  4.3636    0.98     2678   148  0.1709 0.1912        
REMARK   3     2  4.3636 -  3.4654    0.99     2694   156  0.1646 0.1946        
REMARK   3     3  3.4654 -  3.0279    0.99     2691   144  0.1865 0.2115        
REMARK   3     4  3.0279 -  2.7513    0.99     2696   138  0.2064 0.2335        
REMARK   3     5  2.7513 -  2.5543    0.99     2703   143  0.2117 0.2444        
REMARK   3     6  2.5543 -  2.4038    0.98     2661   140  0.2179 0.2753        
REMARK   3     7  2.4038 -  2.2834    0.99     2744   147  0.2243 0.2257        
REMARK   3     8  2.2834 -  2.1841    0.97     2667   137  0.2407 0.2827        
REMARK   3     9  2.1841 -  2.1000    0.95     2614   145  0.2530 0.3019        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.720           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           2255                                  
REMARK   3   ANGLE     :  0.872           3063                                  
REMARK   3   CHIRALITY :  0.055            303                                  
REMARK   3   PLANARITY :  0.007            418                                  
REMARK   3   DIHEDRAL  : 17.184           1403                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   1.6965  -4.3400   6.9438              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2730 T22:   0.3223                                     
REMARK   3      T33:   0.3248 T12:   0.0224                                     
REMARK   3      T13:  -0.0393 T23:   0.0191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4505 L22:   1.8572                                     
REMARK   3      L33:   2.4872 L12:   0.8293                                     
REMARK   3      L13:  -0.9646 L23:  -1.4495                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0164 S12:   0.1593 S13:  -0.0561                       
REMARK   3      S21:   0.0651 S22:  -0.0015 S23:  -0.0251                       
REMARK   3      S31:  -0.0483 S32:   0.0377 S33:  -0.0493                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.8853   5.0488  -7.2081              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2771 T22:   0.3368                                     
REMARK   3      T33:   0.2647 T12:   0.0344                                     
REMARK   3      T13:  -0.0290 T23:   0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3541 L22:   3.0654                                     
REMARK   3      L33:   3.8229 L12:   2.4487                                     
REMARK   3      L13:  -2.0060 L23:  -1.8552                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0013 S12:   0.3583 S13:   0.0749                       
REMARK   3      S21:  -0.0654 S22:   0.0057 S23:   0.0532                       
REMARK   3      S31:  -0.1142 S32:   0.1547 S33:  -0.0388                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN D                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.2503  17.3388  15.8033              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2626 T22:   0.2538                                     
REMARK   3      T33:   0.3005 T12:  -0.0170                                     
REMARK   3      T13:  -0.0358 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8627 L22:   2.1797                                     
REMARK   3      L33:   3.0677 L12:  -1.7187                                     
REMARK   3      L13:  -1.5096 L23:   2.1235                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0361 S12:  -0.0814 S13:   0.0166                       
REMARK   3      S21:  -0.0300 S22:   0.0006 S23:  -0.0336                       
REMARK   3      S31:  -0.0620 S32:  -0.0571 S33:  -0.0543                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.6063  26.6756  29.9002              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3172 T22:   0.3291                                     
REMARK   3      T33:   0.2709 T12:  -0.0083                                     
REMARK   3      T13:  -0.0247 T23:   0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3500 L22:   2.0638                                     
REMARK   3      L33:   4.2563 L12:  -1.3416                                     
REMARK   3      L13:  -1.7496 L23:   1.7242                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0864 S12:  -0.3208 S13:  -0.0008                       
REMARK   3      S21:   0.0634 S22:   0.0104 S23:   0.0700                       
REMARK   3      S31:  -0.2251 S32:  -0.0227 S33:  -0.1066                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5NB8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-MAR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003653.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUL-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9173                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25475                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.580                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.9200                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M NA/K TARTRATE, 0.4M NACL, 0.1 M    
REMARK 280  IMIDAZOLE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     SER A   169                                                      
REMARK 465     GLU A   170                                                      
REMARK 465     GLU A   171                                                      
REMARK 465     LYS A   172                                                      
REMARK 465     GLY A   173                                                      
REMARK 465     THR A   174                                                      
REMARK 465     LEU A   175                                                      
REMARK 465     GLY A   176                                                      
REMARK 465     GLY A   177                                                      
REMARK 465     LEU A   178                                                      
REMARK 465     ALA A   179                                                      
REMARK 465     LEU A   180                                                      
REMARK 465     PRO A   181                                                      
REMARK 465     ALA A   182                                                      
REMARK 465     TYR A   183                                                      
REMARK 465     ARG A   184                                                      
REMARK 465     PRO A   185                                                      
REMARK 465     GLU A   186                                                      
REMARK 465     ALA A   187                                                      
REMARK 465     THR A   188                                                      
REMARK 465     VAL A   189                                                      
REMARK 465     GLY A   190                                                      
REMARK 465     VAL A   191                                                      
REMARK 465     GLU A   192                                                      
REMARK 465     LEU A   193                                                      
REMARK 465     SER A   194                                                      
REMARK 465     ASP A   195                                                      
REMARK 465     SER B   169                                                      
REMARK 465     GLU B   170                                                      
REMARK 465     GLU B   171                                                      
REMARK 465     LYS B   172                                                      
REMARK 465     GLY B   173                                                      
REMARK 465     THR B   174                                                      
REMARK 465     LEU B   175                                                      
REMARK 465     GLY B   176                                                      
REMARK 465     GLY B   177                                                      
REMARK 465     LEU B   178                                                      
REMARK 465     ALA B   179                                                      
REMARK 465     LEU B   180                                                      
REMARK 465     PRO B   181                                                      
REMARK 465     ALA B   182                                                      
REMARK 465     TYR B   183                                                      
REMARK 465     ARG B   184                                                      
REMARK 465     PRO B   185                                                      
REMARK 465     GLU B   186                                                      
REMARK 465     ALA B   187                                                      
REMARK 465     THR B   188                                                      
REMARK 465     VAL B   189                                                      
REMARK 465     GLY B   190                                                      
REMARK 465     VAL B   191                                                      
REMARK 465     GLU B   192                                                      
REMARK 465     LEU B   193                                                      
REMARK 465     SER B   194                                                      
REMARK 465     ASP B   195                                                      
REMARK 465     SER C   169                                                      
REMARK 465     GLU C   170                                                      
REMARK 465     GLU C   171                                                      
REMARK 465     LYS C   172                                                      
REMARK 465     GLY C   173                                                      
REMARK 465     THR C   174                                                      
REMARK 465     LEU C   175                                                      
REMARK 465     GLY C   176                                                      
REMARK 465     GLY C   177                                                      
REMARK 465     LEU C   178                                                      
REMARK 465     ALA C   179                                                      
REMARK 465     LEU C   180                                                      
REMARK 465     PRO C   181                                                      
REMARK 465     ALA C   182                                                      
REMARK 465     TYR C   183                                                      
REMARK 465     ARG C   184                                                      
REMARK 465     PRO C   185                                                      
REMARK 465     GLU C   186                                                      
REMARK 465     ALA C   187                                                      
REMARK 465     THR C   188                                                      
REMARK 465     VAL C   189                                                      
REMARK 465     GLY C   190                                                      
REMARK 465     VAL C   191                                                      
REMARK 465     GLU C   192                                                      
REMARK 465     LEU C   193                                                      
REMARK 465     SER C   194                                                      
REMARK 465     ASP C   195                                                      
REMARK 465     SER D   169                                                      
REMARK 465     GLU D   170                                                      
REMARK 465     GLU D   171                                                      
REMARK 465     LYS D   172                                                      
REMARK 465     GLY D   173                                                      
REMARK 465     THR D   174                                                      
REMARK 465     LEU D   175                                                      
REMARK 465     GLY D   176                                                      
REMARK 465     GLY D   177                                                      
REMARK 465     LEU D   178                                                      
REMARK 465     ALA D   179                                                      
REMARK 465     LEU D   180                                                      
REMARK 465     PRO D   181                                                      
REMARK 465     ALA D   182                                                      
REMARK 465     TYR D   183                                                      
REMARK 465     ARG D   184                                                      
REMARK 465     PRO D   185                                                      
REMARK 465     GLU D   186                                                      
REMARK 465     ALA D   187                                                      
REMARK 465     THR D   188                                                      
REMARK 465     VAL D   189                                                      
REMARK 465     GLY D   190                                                      
REMARK 465     VAL D   191                                                      
REMARK 465     GLU D   192                                                      
REMARK 465     LEU D   193                                                      
REMARK 465     SER D   194                                                      
REMARK 465     ASP D   195                                                      
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     MET D  99    CG   SD   CE                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   335     O    HOH B   337              1.82            
REMARK 500   O    PRO D   147     O    HOH D   301              1.92            
REMARK 500   O    GLY D   168     O    HOH D   302              2.04            
REMARK 500   O    HOH B   320     O    HOH B   332              2.07            
REMARK 500   O    HOH D   336     O    HOH D   337              2.16            
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    LEU B 140       50.13   -103.61                                   
REMARK 500    LEU D 140       52.76   -105.46                                   
REMARK 500    ASP D 148        5.90     82.28                                   
REMARK 500    CYS D 149       70.82   -153.04                                   
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 IMD A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD D 201                 
DBREF  5NB8 A  100   195  UNP    Q9QZQ5   NOV_RAT        100    195             
DBREF  5NB8 B  100   195  UNP    Q9QZQ5   NOV_RAT        100    195             
DBREF  5NB8 C  100   195  UNP    Q9QZQ5   NOV_RAT        100    195             
DBREF  5NB8 D  100   195  UNP    Q9QZQ5   NOV_RAT        100    195             
SEQADV 5NB8 MET A   99  UNP  Q9QZQ5              INITIATING METHIONINE          
SEQADV 5NB8 MET B   99  UNP  Q9QZQ5              INITIATING METHIONINE          
SEQADV 5NB8 MET C   99  UNP  Q9QZQ5              INITIATING METHIONINE          
SEQADV 5NB8 MET D   99  UNP  Q9QZQ5              INITIATING METHIONINE          
SEQRES   1 A   97  MET GLU GLY ASP ASN CYS VAL PHE ASP GLY VAL ILE TYR          
SEQRES   2 A   97  ARG ASN GLY GLU LYS PHE GLU PRO ASN CYS GLN TYR HIS          
SEQRES   3 A   97  CYS THR CYS ARG ASP GLY GLN ILE GLY CYS VAL PRO ARG          
SEQRES   4 A   97  CYS GLN LEU ASP VAL LEU LEU PRO GLY PRO ASP CYS PRO          
SEQRES   5 A   97  ALA PRO LYS LYS VAL ALA VAL PRO GLY GLU CYS CYS GLU          
SEQRES   6 A   97  LYS TRP THR CYS GLY SER GLU GLU LYS GLY THR LEU GLY          
SEQRES   7 A   97  GLY LEU ALA LEU PRO ALA TYR ARG PRO GLU ALA THR VAL          
SEQRES   8 A   97  GLY VAL GLU LEU SER ASP                                      
SEQRES   1 B   97  MET GLU GLY ASP ASN CYS VAL PHE ASP GLY VAL ILE TYR          
SEQRES   2 B   97  ARG ASN GLY GLU LYS PHE GLU PRO ASN CYS GLN TYR HIS          
SEQRES   3 B   97  CYS THR CYS ARG ASP GLY GLN ILE GLY CYS VAL PRO ARG          
SEQRES   4 B   97  CYS GLN LEU ASP VAL LEU LEU PRO GLY PRO ASP CYS PRO          
SEQRES   5 B   97  ALA PRO LYS LYS VAL ALA VAL PRO GLY GLU CYS CYS GLU          
SEQRES   6 B   97  LYS TRP THR CYS GLY SER GLU GLU LYS GLY THR LEU GLY          
SEQRES   7 B   97  GLY LEU ALA LEU PRO ALA TYR ARG PRO GLU ALA THR VAL          
SEQRES   8 B   97  GLY VAL GLU LEU SER ASP                                      
SEQRES   1 C   97  MET GLU GLY ASP ASN CYS VAL PHE ASP GLY VAL ILE TYR          
SEQRES   2 C   97  ARG ASN GLY GLU LYS PHE GLU PRO ASN CYS GLN TYR HIS          
SEQRES   3 C   97  CYS THR CYS ARG ASP GLY GLN ILE GLY CYS VAL PRO ARG          
SEQRES   4 C   97  CYS GLN LEU ASP VAL LEU LEU PRO GLY PRO ASP CYS PRO          
SEQRES   5 C   97  ALA PRO LYS LYS VAL ALA VAL PRO GLY GLU CYS CYS GLU          
SEQRES   6 C   97  LYS TRP THR CYS GLY SER GLU GLU LYS GLY THR LEU GLY          
SEQRES   7 C   97  GLY LEU ALA LEU PRO ALA TYR ARG PRO GLU ALA THR VAL          
SEQRES   8 C   97  GLY VAL GLU LEU SER ASP                                      
SEQRES   1 D   97  MET GLU GLY ASP ASN CYS VAL PHE ASP GLY VAL ILE TYR          
SEQRES   2 D   97  ARG ASN GLY GLU LYS PHE GLU PRO ASN CYS GLN TYR HIS          
SEQRES   3 D   97  CYS THR CYS ARG ASP GLY GLN ILE GLY CYS VAL PRO ARG          
SEQRES   4 D   97  CYS GLN LEU ASP VAL LEU LEU PRO GLY PRO ASP CYS PRO          
SEQRES   5 D   97  ALA PRO LYS LYS VAL ALA VAL PRO GLY GLU CYS CYS GLU          
SEQRES   6 D   97  LYS TRP THR CYS GLY SER GLU GLU LYS GLY THR LEU GLY          
SEQRES   7 D   97  GLY LEU ALA LEU PRO ALA TYR ARG PRO GLU ALA THR VAL          
SEQRES   8 D   97  GLY VAL GLU LEU SER ASP                                      
HET    IMD  A 201       5                                                       
HET    IMD  A 202       5                                                       
HET    GOL  B 201       6                                                       
HET    IMD  B 202       5                                                       
HET    IMD  C 201       5                                                       
HET    IMD  D 201       5                                                       
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  IMD    5(C3 H5 N2 1+)                                               
FORMUL   7  GOL    C3 H8 O3                                                     
FORMUL  11  HOH   *155(H2 O)                                                    
SHEET    1 AA1 2 CYS A 104  PHE A 106  0                                        
SHEET    2 AA1 2 VAL A 109  TYR A 111 -1  O  TYR A 111   N  CYS A 104           
SHEET    1 AA2 4 LYS A 116  PHE A 117  0                                        
SHEET    2 AA2 4 TYR A 123  ARG A 128 -1  O  CYS A 125   N  PHE A 117           
SHEET    3 AA2 4 GLN A 131  PRO A 136 -1  O  GLY A 133   N  THR A 126           
SHEET    4 AA2 4 VAL B 142  LEU B 143 -1  O  VAL B 142   N  CYS A 134           
SHEET    1 AA3 4 VAL A 142  LEU A 143  0                                        
SHEET    2 AA3 4 GLN B 131  PRO B 136 -1  O  CYS B 134   N  VAL A 142           
SHEET    3 AA3 4 TYR B 123  ARG B 128 -1  N  HIS B 124   O  VAL B 135           
SHEET    4 AA3 4 LYS B 116  ASN B 120 -1  N  PHE B 117   O  CYS B 125           
SHEET    1 AA4 2 PRO A 152  VAL A 155  0                                        
SHEET    2 AA4 2 LYS A 164  CYS A 167 -1  O  LYS A 164   N  VAL A 155           
SHEET    1 AA5 2 CYS B 104  PHE B 106  0                                        
SHEET    2 AA5 2 VAL B 109  TYR B 111 -1  O  TYR B 111   N  CYS B 104           
SHEET    1 AA6 2 PRO B 152  VAL B 155  0                                        
SHEET    2 AA6 2 LYS B 164  CYS B 167 -1  O  LYS B 164   N  VAL B 155           
SHEET    1 AA7 2 CYS C 104  PHE C 106  0                                        
SHEET    2 AA7 2 VAL C 109  TYR C 111 -1  O  TYR C 111   N  CYS C 104           
SHEET    1 AA8 4 LYS C 116  ASN C 120  0                                        
SHEET    2 AA8 4 TYR C 123  ARG C 128 -1  O  CYS C 125   N  PHE C 117           
SHEET    3 AA8 4 GLN C 131  PRO C 136 -1  O  GLY C 133   N  THR C 126           
SHEET    4 AA8 4 VAL D 142  LEU D 143 -1  O  VAL D 142   N  CYS C 134           
SHEET    1 AA9 4 VAL C 142  LEU C 143  0                                        
SHEET    2 AA9 4 GLN D 131  PRO D 136 -1  O  CYS D 134   N  VAL C 142           
SHEET    3 AA9 4 TYR D 123  ARG D 128 -1  N  ARG D 128   O  GLN D 131           
SHEET    4 AA9 4 LYS D 116  ASN D 120 -1  N  PHE D 117   O  CYS D 125           
SHEET    1 AB1 2 ALA C 151  VAL C 155  0                                        
SHEET    2 AB1 2 LYS C 164  GLY C 168 -1  O  LYS C 164   N  VAL C 155           
SHEET    1 AB2 2 CYS D 104  PHE D 106  0                                        
SHEET    2 AB2 2 VAL D 109  TYR D 111 -1  O  TYR D 111   N  CYS D 104           
SHEET    1 AB3 2 PRO D 152  VAL D 155  0                                        
SHEET    2 AB3 2 LYS D 164  CYS D 167 -1  O  LYS D 164   N  VAL D 155           
SSBOND   1 CYS A  104    CYS A  127                          1555   1555  2.03  
SSBOND   2 CYS A  121    CYS A  161                          1555   1555  2.06  
SSBOND   3 CYS A  125    CYS A  134                          1555   1555  2.05  
SSBOND   4 CYS A  138    CYS A  162                          1555   1555  2.03  
SSBOND   5 CYS A  149    CYS A  167                          1555   1555  2.08  
SSBOND   6 CYS B  104    CYS B  127                          1555   1555  2.04  
SSBOND   7 CYS B  121    CYS B  161                          1555   1555  2.05  
SSBOND   8 CYS B  125    CYS B  134                          1555   1555  2.04  
SSBOND   9 CYS B  138    CYS B  162                          1555   1555  2.03  
SSBOND  10 CYS B  149    CYS B  167                          1555   1555  2.08  
SSBOND  11 CYS C  104    CYS C  127                          1555   1555  2.04  
SSBOND  12 CYS C  121    CYS C  161                          1555   1555  2.04  
SSBOND  13 CYS C  125    CYS C  134                          1555   1555  2.05  
SSBOND  14 CYS C  138    CYS C  162                          1555   1555  2.03  
SSBOND  15 CYS C  149    CYS C  167                          1555   1555  2.07  
SSBOND  16 CYS D  104    CYS D  127                          1555   1555  2.03  
SSBOND  17 CYS D  121    CYS D  161                          1555   1555  2.05  
SSBOND  18 CYS D  125    CYS D  134                          1555   1555  2.04  
SSBOND  19 CYS D  138    CYS D  162                          1555   1555  2.03  
SSBOND  20 CYS D  149    CYS D  167                          1555   1555  2.09  
SITE     1 AC1  5 VAL A 157  LYS A 164  TRP A 165  VAL B 157                    
SITE     2 AC1  5 LYS B 164                                                     
SITE     1 AC2  6 ASP A 141  LYS A 154  GLU A 163  LYS A 164                    
SITE     2 AC2  6 TRP A 165  HOH A 322                                          
SITE     1 AC3  8 HIS B 124  CYS B 125  THR B 126  ARG B 128                    
SITE     2 AC3  8 GLY B 133  CYS B 134  HOH B 304  ASN C 103                    
SITE     1 AC4  4 ARG B 137  VAL C 109  ILE C 110  GLU C 115                    
SITE     1 AC5  3 ASP C 141  LYS C 154  HOH C 302                               
SITE     1 AC6  5 VAL C 157  LYS C 164  TRP C 165  VAL D 157                    
SITE     2 AC6  5 LYS D 164                                                     
CRYST1   38.400   43.100   72.300  75.30  82.00  89.90 P 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      0.026042 -0.000045 -0.003774        0.00000                         
SCALE2      0.000000  0.023202 -0.006145        0.00000                         
SCALE3      0.000000  0.000000  0.014449        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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