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Database: PDB
Entry: 2ZVO
LinkDB: 2ZVO
Original site: 2ZVO 
HEADER    TRANSCRIPTION/SIGNALING PROTEIN         12-NOV-08   2ZVO              
TITLE     NEMO COZI DOMAIN IN COMPLEX WITH DIUBIQUITIN IN C2 SPACE GROUP        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBC PROTEIN;                                               
COMPND   3 CHAIN: A, G;                                                         
COMPND   4 FRAGMENT: UBIQUITIN;                                                 
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: NF-KAPPA-B ESSENTIAL MODULATOR;                            
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 FRAGMENT: CC2-LZ, COZI DOMAIN;                                       
COMPND  10 SYNONYM: NEMO, NF-KAPPA-B ESSENTIAL MODIFIER, INHIBITOR OF NUCLEAR   
COMPND  11 FACTOR KAPPA-B KINASE SUBUNIT GAMMA, IKB KINASE SUBUNIT GAMMA, I-    
COMPND  12 KAPPA-B KINASE GAMMA, IKK-GAMMA, IKKG, IKB KINASE-ASSOCIATED PROTEIN 
COMPND  13 1, IKKAP1, MFIP-3;                                                   
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: DL41;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX4T1;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: MOUSE;                                              
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PGEX4T1                                   
KEYWDS    NF-KB SIGNALING, UBIQUITIN BINDING, COILED COIL, CYTOPLASM, METAL-    
KEYWDS   2 BINDING, NUCLEUS, PHOSPHOPROTEIN, TRANSCRIPTION, TRANSCRIPTION       
KEYWDS   3 REGULATION, UBL CONJUGATION, ZINC, ZINC-FINGER, TRANSCRIPTION-       
KEYWDS   4 SIGNALING PROTEIN COMPLEX                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.RAHIGHI,F.IKEDA,M.KAWASAKI,M.AKUTSU,N.SUZUKI,R.KATO,T.KENSCHE,      
AUTHOR   2 T.UEJIMA,S.BLOOR,D.KOMANDER,F.RANDOW,S.WAKATSUKI,I.DIKIC             
REVDAT   3   11-OCT-17 2ZVO    1       REMARK                                   
REVDAT   2   14-APR-09 2ZVO    1       JRNL                                     
REVDAT   1   24-MAR-09 2ZVO    0                                                
JRNL        AUTH   S.RAHIGHI,F.IKEDA,M.KAWASAKI,M.AKUTSU,N.SUZUKI,R.KATO,       
JRNL        AUTH 2 T.KENSCHE,T.UEJIMA,S.BLOOR,D.KOMANDER,F.RANDOW,S.WAKATSUKI,  
JRNL        AUTH 3 I.DIKIC                                                      
JRNL        TITL   SPECIFIC RECOGNITION OF LINEAR UBIQUITIN CHAINS BY NEMO IS   
JRNL        TITL 2 IMPORTANT FOR NF-KAPPAB ACTIVATION                           
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 136  1098 2009              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   19303852                                                     
JRNL        DOI    10.1016/J.CELL.2009.03.007                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 11951                          
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) : 0.240                           
REMARK   3   R VALUE            (WORKING SET) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 646                             
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.97                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 760                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.57                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2980                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 29                           
REMARK   3   BIN FREE R VALUE                    : 0.4980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3791                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 174                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.86                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.48000                                             
REMARK   3    B22 (A**2) : 1.09000                                              
REMARK   3    B33 (A**2) : 1.32000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.57000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.488         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.355         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.759        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.909                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.897                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3833 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5149 ; 1.282 ; 1.992       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   467 ; 5.273 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   189 ;42.788 ;26.296       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   800 ;19.649 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;23.149 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   596 ; 0.158 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2801 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1931 ; 0.245 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2610 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   170 ; 0.182 ; 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):    82 ; 0.270 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.093 ; 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):  2417 ; 0.552 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3800 ; 0.958 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1530 ; 1.120 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1349 ; 1.827 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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 2ZVO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-NOV-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000028483.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUN-08                          
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               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9790                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15653                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.9                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.16200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.4620                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 53.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, SITTING DROP            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       65.43050            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.18600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       65.43050            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       49.18600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G, B, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -1                                                      
REMARK 465     LEU A   149                                                      
REMARK 465     ARG A   150                                                      
REMARK 465     GLY A   151                                                      
REMARK 465     GLY A   152                                                      
REMARK 465     GLY G    -1                                                      
REMARK 465     SER G     0                                                      
REMARK 465     LEU G   147                                                      
REMARK 465     ARG G   148                                                      
REMARK 465     LEU G   149                                                      
REMARK 465     ARG G   150                                                      
REMARK 465     GLY G   151                                                      
REMARK 465     GLY G   152                                                      
REMARK 465     GLY B   248                                                      
REMARK 465     SER B   249                                                      
REMARK 465     VAL B   338                                                      
REMARK 465     GLY B   339                                                      
REMARK 465     GLY D   248                                                      
REMARK 465     SER D   249                                                      
REMARK 465     VAL D   338                                                      
REMARK 465     GLY D   339                                                      
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   NH2  ARG B   309     OE2  GLU D   308              2.15            
REMARK 500   O    GLY A    75     O    HOH A   153              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO G  38   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    MET A   1     -174.63    -58.09                                   
REMARK 500    LYS A  11       98.70     84.82                                   
REMARK 500    LEU A  84       28.21    -69.87                                   
REMARK 500    ALA A 122       74.48     43.20                                   
REMARK 500    ASN A 136       63.09     21.03                                   
REMARK 500    LYS G  11       83.37     60.63                                   
REMARK 500    GLU G  64        6.13     55.51                                   
REMARK 500    PRO G  95       49.91    -68.23                                   
REMARK 500    SER G  96      -24.35   -152.62                                   
REMARK 500    ALA G 122       73.60     45.99                                   
REMARK 500    LYS G 124      100.37     76.74                                   
REMARK 500    MET B 251      -18.97     60.17                                   
REMARK 500    MET D 251       -9.39    -56.92                                   
REMARK 500    LEU D 253       33.30    -81.75                                   
REMARK 500    ALA D 285      -39.38    -39.01                                   
REMARK 500    GLN D 328        5.33    -58.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ZVN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3F89   RELATED DB: PDB                                   
DBREF  2ZVO A    1   152  UNP    Q96C32   Q96C32_HUMAN     1    152             
DBREF  2ZVO G    1   152  UNP    Q96C32   Q96C32_HUMAN     1    152             
DBREF  2ZVO B  250   339  UNP    O88522   NEMO_MOUSE     250    339             
DBREF  2ZVO D  250   339  UNP    O88522   NEMO_MOUSE     250    339             
SEQADV 2ZVO GLY A   -1  UNP  Q96C32              EXPRESSION TAG                 
SEQADV 2ZVO SER A    0  UNP  Q96C32              EXPRESSION TAG                 
SEQADV 2ZVO GLY G   -1  UNP  Q96C32              EXPRESSION TAG                 
SEQADV 2ZVO SER G    0  UNP  Q96C32              EXPRESSION TAG                 
SEQADV 2ZVO GLY B  248  UNP  O88522              EXPRESSION TAG                 
SEQADV 2ZVO SER B  249  UNP  O88522              EXPRESSION TAG                 
SEQADV 2ZVO ALA B  282  UNP  O88522    GLU   282 ENGINEERED                     
SEQADV 2ZVO ALA B  285  UNP  O88522    LYS   285 ENGINEERED                     
SEQADV 2ZVO GLY D  248  UNP  O88522              EXPRESSION TAG                 
SEQADV 2ZVO SER D  249  UNP  O88522              EXPRESSION TAG                 
SEQADV 2ZVO ALA D  282  UNP  O88522    GLU   282 ENGINEERED                     
SEQADV 2ZVO ALA D  285  UNP  O88522    LYS   285 ENGINEERED                     
SEQRES   1 A  154  GLY SER MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS          
SEQRES   2 A  154  THR ILE THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU          
SEQRES   3 A  154  ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO          
SEQRES   4 A  154  PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU          
SEQRES   5 A  154  GLU ASP GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS          
SEQRES   6 A  154  GLU SER THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY          
SEQRES   7 A  154  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   8 A  154  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   9 A  154  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES  10 A  154  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES  11 A  154  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES  12 A  154  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 G  154  GLY SER MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS          
SEQRES   2 G  154  THR ILE THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU          
SEQRES   3 G  154  ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO          
SEQRES   4 G  154  PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU          
SEQRES   5 G  154  GLU ASP GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS          
SEQRES   6 G  154  GLU SER THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY          
SEQRES   7 G  154  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   8 G  154  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   9 G  154  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES  10 G  154  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES  11 G  154  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES  12 G  154  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 B   92  GLY SER GLY MET GLN LEU GLU ASP LEU ARG GLN GLN LEU          
SEQRES   2 B   92  GLN GLN ALA GLU GLU ALA LEU VAL ALA LYS GLN GLU LEU          
SEQRES   3 B   92  ILE ASP LYS LEU LYS GLU GLU ALA ALA GLN HIS ALA ILE          
SEQRES   4 B   92  VAL MET GLU THR VAL PRO VAL LEU LYS ALA GLN ALA ASP          
SEQRES   5 B   92  ILE TYR LYS ALA ASP PHE GLN ALA GLU ARG HIS ALA ARG          
SEQRES   6 B   92  GLU LYS LEU VAL GLU LYS LYS GLU TYR LEU GLN GLU GLN          
SEQRES   7 B   92  LEU GLU GLN LEU GLN ARG GLU PHE ASN LYS LEU LYS VAL          
SEQRES   8 B   92  GLY                                                          
SEQRES   1 D   92  GLY SER GLY MET GLN LEU GLU ASP LEU ARG GLN GLN LEU          
SEQRES   2 D   92  GLN GLN ALA GLU GLU ALA LEU VAL ALA LYS GLN GLU LEU          
SEQRES   3 D   92  ILE ASP LYS LEU LYS GLU GLU ALA ALA GLN HIS ALA ILE          
SEQRES   4 D   92  VAL MET GLU THR VAL PRO VAL LEU LYS ALA GLN ALA ASP          
SEQRES   5 D   92  ILE TYR LYS ALA ASP PHE GLN ALA GLU ARG HIS ALA ARG          
SEQRES   6 D   92  GLU LYS LEU VAL GLU LYS LYS GLU TYR LEU GLN GLU GLN          
SEQRES   7 D   92  LEU GLU GLN LEU GLN ARG GLU PHE ASN LYS LEU LYS VAL          
SEQRES   8 D   92  GLY                                                          
FORMUL   5  HOH   *174(H2 O)                                                    
HELIX    1   1 THR A   22  GLY A   35  1                                  14    
HELIX    2   2 PRO A   37  ASP A   39  5                                   3    
HELIX    3   3 LEU A   56  ASN A   60  5                                   5    
HELIX    4   4 ILE A   99  GLY A  111  1                                  13    
HELIX    5   5 PRO A  113  ASP A  115  5                                   3    
HELIX    6   6 LEU A  132  ASN A  136  5                                   5    
HELIX    7   7 THR G   22  GLY G   35  1                                  14    
HELIX    8   8 PRO G   37  ASP G   39  5                                   3    
HELIX    9   9 THR G   98  GLY G  111  1                                  14    
HELIX   10  10 PRO G  113  GLN G  117  5                                   5    
HELIX   11  11 LEU B  253  GLU B  289  1                                  37    
HELIX   12  12 THR B  290  LYS B  337  1                                  48    
HELIX   13  13 MET D  251  GLU D  289  1                                  39    
HELIX   14  14 GLU D  289  GLN D  325  1                                  37    
HELIX   15  15 LEU D  326  LEU D  336  1                                  11    
SHEET    1   A 5 THR A  12  GLU A  16  0                                        
SHEET    2   A 5 GLN A   2  LYS A   6 -1  N  VAL A   5   O  ILE A  13           
SHEET    3   A 5 THR A  66  LEU A  71  1  O  LEU A  67   N  PHE A   4           
SHEET    4   A 5 GLN A  41  PHE A  45 -1  N  ARG A  42   O  VAL A  70           
SHEET    5   A 5 LYS A  48  GLN A  49 -1  O  LYS A  48   N  PHE A  45           
SHEET    1   B 5 THR A  88  VAL A  93  0                                        
SHEET    2   B 5 MET A  77  THR A  83 -1  N  VAL A  81   O  ILE A  89           
SHEET    3   B 5 THR A 142  LEU A 147  1  O  LEU A 143   N  LYS A  82           
SHEET    4   B 5 GLN A 117  PHE A 121 -1  N  ARG A 118   O  VAL A 146           
SHEET    5   B 5 LYS A 124  GLN A 125 -1  O  LYS A 124   N  PHE A 121           
SHEET    1   C 5 THR G  12  GLU G  16  0                                        
SHEET    2   C 5 GLN G   2  THR G   7 -1  N  VAL G   5   O  ILE G  13           
SHEET    3   C 5 THR G  66  LEU G  71  1  O  LEU G  67   N  PHE G   4           
SHEET    4   C 5 GLN G  41  PHE G  45 -1  N  ILE G  44   O  HIS G  68           
SHEET    5   C 5 LYS G  48  GLN G  49 -1  O  LYS G  48   N  PHE G  45           
SHEET    1   D 4 THR G  88  VAL G  93  0                                        
SHEET    2   D 4 MET G  77  LYS G  82 -1  N  ILE G  79   O  LEU G  91           
SHEET    3   D 4 THR G 142  VAL G 146  1  O  LEU G 143   N  PHE G  80           
SHEET    4   D 4 ARG G 118  ILE G 120 -1  N  ARG G 118   O  VAL G 146           
CRYST1  130.861   98.372   50.616  90.00 101.96  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007642  0.000000  0.001619        0.00000                         
SCALE2      0.000000  0.010165  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020195        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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