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Database: PDB
Entry: 2ZVN
LinkDB: 2ZVN
Original site: 2ZVN 
HEADER    SIGNALING PROTEIN/TRANSCRIPTION         12-NOV-08   2ZVN              
TITLE     NEMO COZI DOMAIN INCOMPLEX WITH DIUBIQUITIN IN P212121 SPACE GROUP    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBC PROTEIN;                                               
COMPND   3 CHAIN: A, G, C, E;                                                   
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, F, H;                                                   
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                                                      
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: BL21;                                      
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, SIGNALING PROTEIN-   
KEYWDS   4 TRANSCRIPTION 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 2ZVN    1       REMARK                                   
REVDAT   2   14-APR-09 2ZVN    1       JRNL                                     
REVDAT   1   24-MAR-09 2ZVN    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.    3.00 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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.75                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 23571                          
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) : 0.263                           
REMARK   3   R VALUE            (WORKING SET) : 0.261                           
REMARK   3   FREE R VALUE                     : 0.303                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1267                            
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) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1634                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.76                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3610                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 84                           
REMARK   3   BIN FREE R VALUE                    : 0.3890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7533                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 65                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 77.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.23000                                             
REMARK   3    B22 (A**2) : 0.17000                                              
REMARK   3    B33 (A**2) : 2.06000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.526         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.911                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7609 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10215 ; 1.390 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   923 ; 4.370 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   378 ;45.261 ;26.296       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1602 ;19.411 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    42 ;19.120 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1185 ; 0.166 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5526 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3815 ; 0.275 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5226 ; 0.313 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   277 ; 0.237 ; 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):    73 ; 0.234 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.202 ; 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):  4635 ; 3.502 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7516 ; 3.571 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2974 ; 1.725 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2699 ; 3.156 ; 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 2ZVN 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_1000028482.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-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) : 1.00000                            
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   : 24893                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
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     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.9340                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60400                            
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   (%): 54.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       29.59750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.08950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       70.64400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       72.08950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.59750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       70.64400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 9030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, E, F, H                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
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   251                                                      
REMARK 465     LYS B   337                                                      
REMARK 465     GLY D   251                                                      
REMARK 465     SER D   252                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     LEU C   149                                                      
REMARK 465     ARG C   150                                                      
REMARK 465     GLY C   151                                                      
REMARK 465     GLY C   152                                                      
REMARK 465     GLY E    -1                                                      
REMARK 465     SER E     0                                                      
REMARK 465     LEU E   147                                                      
REMARK 465     ARG E   148                                                      
REMARK 465     LEU E   149                                                      
REMARK 465     ARG E   150                                                      
REMARK 465     GLY E   151                                                      
REMARK 465     GLY E   152                                                      
REMARK 465     GLY F   251                                                      
REMARK 465     GLY H   251                                                      
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    SER H   252     N    GLU H   254              1.28            
REMARK 500   CD2  LEU D   253     OD1  ASP D   255              1.31            
REMARK 500   O    SER B   252     N    GLU B   254              1.51            
REMARK 500   CD2  LEU D   253     CG   ASP D   255              1.63            
REMARK 500   O    SER B   252     N    ASP B   255              1.70            
REMARK 500   C    SER B   252     N    GLU B   254              1.74            
REMARK 500   O    LEU D   253     N    ASP D   255              1.84            
REMARK 500   C    SER H   252     N    GLU H   254              2.05            
REMARK 500   O    SER B   252     CA   GLU B   254              2.10            
REMARK 500   NZ   LYS A   105     O    HOH A   156              2.12            
REMARK 500   O    SER B   252     C    GLU B   254              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A  42   CZ    ARG A  42   NH1     0.115                       
REMARK 500    GLU D 254   CD    GLU D 254   OE1     0.066                       
REMARK 500    HIS C 144   CG    HIS C 144   CD2     0.060                       
REMARK 500    GLU F 265   CB    GLU F 265   CG      0.125                       
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    ARG A  42   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG G 118   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    PRO C  38   C   -  N   -  CA  ANGL. DEV. =  10.7 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    GLN A   2       87.60   -158.81                                   
REMARK 500    LEU A   8       31.95    -78.19                                   
REMARK 500    PRO A  19       43.39    -65.28                                   
REMARK 500    SER A  20      -37.27   -130.24                                   
REMARK 500    ASP A  21      156.46    -49.90                                   
REMARK 500    TYR A  59       27.59    -76.88                                   
REMARK 500    GLU A  64       22.95     48.17                                   
REMARK 500    LYS A 109      -74.33    -70.09                                   
REMARK 500    ILE A 112      127.83    -31.33                                   
REMARK 500    PRO A 114       30.91    -69.54                                   
REMARK 500    ASP A 115       -3.11   -141.54                                   
REMARK 500    ASP A 128      -42.84    -28.60                                   
REMARK 500    ASN A 136       71.02     54.42                                   
REMARK 500    GLU A 140      -10.71     62.04                                   
REMARK 500    LYS G  11       97.06     83.42                                   
REMARK 500    GLU G  34      -11.02   -147.20                                   
REMARK 500    LEU G  50      160.75    -48.88                                   
REMARK 500    GLU G  64       13.22     50.19                                   
REMARK 500    ARG G  72     -174.41    -68.06                                   
REMARK 500    THR G  83       24.45    -72.26                                   
REMARK 500    LEU G  84      -12.96     77.29                                   
REMARK 500    THR G  85      -28.26   -162.25                                   
REMARK 500    PRO G  95      -19.33    -47.82                                   
REMARK 500    GLU G 110       11.85   -140.76                                   
REMARK 500    LYS G 124      126.96     72.80                                   
REMARK 500    LYS G 139      140.11    -35.31                                   
REMARK 500    GLU G 140      -16.61     82.11                                   
REMARK 500    LEU B 253      -24.10      8.14                                   
REMARK 500    LYS B 276      -76.17    -56.87                                   
REMARK 500    GLU B 289        5.43    -64.36                                   
REMARK 500    GLU D 254      -56.44      3.50                                   
REMARK 500    GLN D 328      -77.73    -56.47                                   
REMARK 500    LEU D 329      -23.87    -37.68                                   
REMARK 500    THR C   7     -167.72    -78.48                                   
REMARK 500    PRO C  19       10.04    -48.50                                   
REMARK 500    SER C  20       53.27   -156.66                                   
REMARK 500    ALA C  46       23.42     49.34                                   
REMARK 500    GLU C  64        9.00     52.03                                   
REMARK 500    VAL C 102      -70.34    -56.50                                   
REMARK 500    ILE C 112      114.87    -38.51                                   
REMARK 500    PRO C 114      -11.46    -43.17                                   
REMARK 500    GLN C 116       31.07    -92.36                                   
REMARK 500    LYS C 139      161.82    -47.95                                   
REMARK 500    LEU C 147       73.45   -107.25                                   
REMARK 500    LYS E  11       88.93     70.86                                   
REMARK 500    GLU E  34       -4.73   -152.47                                   
REMARK 500    ASP E  58        4.37    -60.56                                   
REMARK 500    GLU E  64       10.32     42.88                                   
REMARK 500    LEU E  67      104.11   -160.91                                   
REMARK 500    THR E  83     -158.44    -73.67                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      58 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER B  252     LEU B  253                  130.50                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ZVO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3F89   RELATED DB: PDB                                   
DBREF  2ZVN A    1   152  UNP    Q96C32   Q96C32_HUMAN     1    152             
DBREF  2ZVN G    1   152  UNP    Q96C32   Q96C32_HUMAN     1    152             
DBREF  2ZVN B  253   337  UNP    O88522   NEMO_MOUSE     253    337             
DBREF  2ZVN D  253   337  UNP    O88522   NEMO_MOUSE     253    337             
DBREF  2ZVN C    1   152  UNP    Q96C32   Q96C32_HUMAN     1    152             
DBREF  2ZVN E    1   152  UNP    Q96C32   Q96C32_HUMAN     1    152             
DBREF  2ZVN F  253   337  UNP    O88522   NEMO_MOUSE     253    337             
DBREF  2ZVN H  253   337  UNP    O88522   NEMO_MOUSE     253    337             
SEQADV 2ZVN GLY A   -1  UNP  Q96C32              EXPRESSION TAG                 
SEQADV 2ZVN SER A    0  UNP  Q96C32              EXPRESSION TAG                 
SEQADV 2ZVN GLY G   -1  UNP  Q96C32              EXPRESSION TAG                 
SEQADV 2ZVN SER G    0  UNP  Q96C32              EXPRESSION TAG                 
SEQADV 2ZVN GLY B  251  UNP  O88522              EXPRESSION TAG                 
SEQADV 2ZVN SER B  252  UNP  O88522              EXPRESSION TAG                 
SEQADV 2ZVN GLY D  251  UNP  O88522              EXPRESSION TAG                 
SEQADV 2ZVN SER D  252  UNP  O88522              EXPRESSION TAG                 
SEQADV 2ZVN GLY C   -1  UNP  Q96C32              EXPRESSION TAG                 
SEQADV 2ZVN SER C    0  UNP  Q96C32              EXPRESSION TAG                 
SEQADV 2ZVN GLY E   -1  UNP  Q96C32              EXPRESSION TAG                 
SEQADV 2ZVN SER E    0  UNP  Q96C32              EXPRESSION TAG                 
SEQADV 2ZVN GLY F  251  UNP  O88522              EXPRESSION TAG                 
SEQADV 2ZVN SER F  252  UNP  O88522              EXPRESSION TAG                 
SEQADV 2ZVN GLY H  251  UNP  O88522              EXPRESSION TAG                 
SEQADV 2ZVN SER H  252  UNP  O88522              EXPRESSION TAG                 
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   87  GLY SER LEU GLU ASP LEU ARG GLN GLN LEU GLN GLN ALA          
SEQRES   2 B   87  GLU GLU ALA LEU VAL ALA LYS GLN GLU LEU ILE ASP LYS          
SEQRES   3 B   87  LEU LYS GLU GLU ALA GLU GLN HIS LYS ILE VAL MET GLU          
SEQRES   4 B   87  THR VAL PRO VAL LEU LYS ALA GLN ALA ASP ILE TYR LYS          
SEQRES   5 B   87  ALA ASP PHE GLN ALA GLU ARG HIS ALA ARG GLU LYS LEU          
SEQRES   6 B   87  VAL GLU LYS LYS GLU TYR LEU GLN GLU GLN LEU GLU GLN          
SEQRES   7 B   87  LEU GLN ARG GLU PHE ASN LYS LEU LYS                          
SEQRES   1 D   87  GLY SER LEU GLU ASP LEU ARG GLN GLN LEU GLN GLN ALA          
SEQRES   2 D   87  GLU GLU ALA LEU VAL ALA LYS GLN GLU LEU ILE ASP LYS          
SEQRES   3 D   87  LEU LYS GLU GLU ALA GLU GLN HIS LYS ILE VAL MET GLU          
SEQRES   4 D   87  THR VAL PRO VAL LEU LYS ALA GLN ALA ASP ILE TYR LYS          
SEQRES   5 D   87  ALA ASP PHE GLN ALA GLU ARG HIS ALA ARG GLU LYS LEU          
SEQRES   6 D   87  VAL GLU LYS LYS GLU TYR LEU GLN GLU GLN LEU GLU GLN          
SEQRES   7 D   87  LEU GLN ARG GLU PHE ASN LYS LEU LYS                          
SEQRES   1 C  154  GLY SER MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS          
SEQRES   2 C  154  THR ILE THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU          
SEQRES   3 C  154  ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO          
SEQRES   4 C  154  PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU          
SEQRES   5 C  154  GLU ASP GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS          
SEQRES   6 C  154  GLU SER THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY          
SEQRES   7 C  154  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   8 C  154  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   9 C  154  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES  10 C  154  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES  11 C  154  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES  12 C  154  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 E  154  GLY SER MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS          
SEQRES   2 E  154  THR ILE THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU          
SEQRES   3 E  154  ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO          
SEQRES   4 E  154  PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU          
SEQRES   5 E  154  GLU ASP GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS          
SEQRES   6 E  154  GLU SER THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY          
SEQRES   7 E  154  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   8 E  154  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   9 E  154  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES  10 E  154  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES  11 E  154  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES  12 E  154  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 F   87  GLY SER LEU GLU ASP LEU ARG GLN GLN LEU GLN GLN ALA          
SEQRES   2 F   87  GLU GLU ALA LEU VAL ALA LYS GLN GLU LEU ILE ASP LYS          
SEQRES   3 F   87  LEU LYS GLU GLU ALA GLU GLN HIS LYS ILE VAL MET GLU          
SEQRES   4 F   87  THR VAL PRO VAL LEU LYS ALA GLN ALA ASP ILE TYR LYS          
SEQRES   5 F   87  ALA ASP PHE GLN ALA GLU ARG HIS ALA ARG GLU LYS LEU          
SEQRES   6 F   87  VAL GLU LYS LYS GLU TYR LEU GLN GLU GLN LEU GLU GLN          
SEQRES   7 F   87  LEU GLN ARG GLU PHE ASN LYS LEU LYS                          
SEQRES   1 H   87  GLY SER LEU GLU ASP LEU ARG GLN GLN LEU GLN GLN ALA          
SEQRES   2 H   87  GLU GLU ALA LEU VAL ALA LYS GLN GLU LEU ILE ASP LYS          
SEQRES   3 H   87  LEU LYS GLU GLU ALA GLU GLN HIS LYS ILE VAL MET GLU          
SEQRES   4 H   87  THR VAL PRO VAL LEU LYS ALA GLN ALA ASP ILE TYR LYS          
SEQRES   5 H   87  ALA ASP PHE GLN ALA GLU ARG HIS ALA ARG GLU LYS LEU          
SEQRES   6 H   87  VAL GLU LYS LYS GLU TYR LEU GLN GLU GLN LEU GLU GLN          
SEQRES   7 H   87  LEU GLN ARG GLU PHE ASN LYS LEU LYS                          
FORMUL   9  HOH   *65(H2 O)                                                     
HELIX    1   1 THR A   22  GLU A   34  1                                  13    
HELIX    2   2 PRO A   37  ASP A   39  5                                   3    
HELIX    3   3 THR A   98  GLY A  111  1                                  14    
HELIX    4   4 THR G   22  LYS G   33  1                                  12    
HELIX    5   5 PRO G   37  ASP G   39  5                                   3    
HELIX    6   6 LEU G   56  ASN G   60  5                                   5    
HELIX    7   7 THR G   98  GLY G  111  1                                  14    
HELIX    8   8 PRO G  113  GLN G  117  5                                   5    
HELIX    9   9 THR G  131  ASN G  136  5                                   6    
HELIX   10  10 LEU B  253  GLU B  289  1                                  37    
HELIX   11  11 THR B  290  ASN B  334  1                                  45    
HELIX   12  12 GLU D  254  GLU D  289  1                                  36    
HELIX   13  13 GLU D  289  LYS D  335  1                                  47    
HELIX   14  14 ILE C   23  GLU C   34  1                                  12    
HELIX   15  15 PRO C   37  ASP C   39  5                                   3    
HELIX   16  16 THR C   98  GLY C  111  1                                  14    
HELIX   17  17 PRO C  113  GLN C  117  5                                   5    
HELIX   18  18 LEU C  132  ASN C  136  5                                   5    
HELIX   19  19 THR E   22  LYS E   33  1                                  12    
HELIX   20  20 PRO E   37  ASP E   39  5                                   3    
HELIX   21  21 LEU E   56  ASN E   60  5                                   5    
HELIX   22  22 THR E   98  GLY E  111  1                                  14    
HELIX   23  23 PRO E  113  GLN E  117  5                                   5    
HELIX   24  24 SER F  252  GLU F  289  1                                  38    
HELIX   25  25 THR F  290  LYS F  337  1                                  48    
HELIX   26  26 GLU H  254  MET H  288  1                                  35    
HELIX   27  27 GLU H  289  LEU H  336  1                                  48    
SHEET    1   A 5 THR A  12  LEU A  15  0                                        
SHEET    2   A 5 ILE A   3  LYS A   6 -1  N  ILE A   3   O  LEU A  15           
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  ILE A  44   O  HIS A  68           
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  LYS A  82 -1  N  VAL A  81   O  ILE A  89           
SHEET    3   B 5 THR A 142  VAL A 146  1  O  LEU A 143   N  PHE A  80           
SHEET    4   B 5 ARG A 118  PHE A 121 -1  N  ILE A 120   O  HIS A 144           
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  ILE G   3   O  LEU G  15           
SHEET    3   C 5 THR G  66  LEU G  71  1  O  LEU G  69   N  LYS G   6           
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  GLU G  92  0                                        
SHEET    2   D 4 GLN G  78  LYS G  82 -1  N  VAL G  81   O  ILE G  89           
SHEET    3   D 4 THR G 142  LEU G 145  1  O  LEU G 143   N  PHE G  80           
SHEET    4   D 4 LEU G 119  ILE G 120 -1  N  ILE G 120   O  HIS G 144           
SHEET    1   E 5 THR C  12  GLU C  16  0                                        
SHEET    2   E 5 GLN C   2  LYS C   6 -1  N  VAL C   5   O  ILE C  13           
SHEET    3   E 5 THR C  66  LEU C  71  1  O  LEU C  67   N  PHE C   4           
SHEET    4   E 5 GLN C  41  PHE C  45 -1  N  ARG C  42   O  VAL C  70           
SHEET    5   E 5 LYS C  48  GLN C  49 -1  O  LYS C  48   N  PHE C  45           
SHEET    1   F 5 THR C  88  VAL C  93  0                                        
SHEET    2   F 5 MET C  77  LYS C  82 -1  N  ILE C  79   O  LEU C  91           
SHEET    3   F 5 THR C 142  LEU C 145  1  O  LEU C 143   N  PHE C  80           
SHEET    4   F 5 LEU C 119  PHE C 121 -1  N  ILE C 120   O  HIS C 144           
SHEET    5   F 5 LYS C 124  GLN C 125 -1  O  LYS C 124   N  PHE C 121           
SHEET    1   G 4 THR E  12  GLU E  16  0                                        
SHEET    2   G 4 GLN E   2  THR E   7 -1  N  VAL E   5   O  ILE E  13           
SHEET    3   G 4 HIS E  68  LEU E  71  1  O  LEU E  69   N  LYS E   6           
SHEET    4   G 4 GLN E  41  ILE E  44 -1  N  ARG E  42   O  VAL E  70           
SHEET    1   H 4 THR E  88  GLU E  92  0                                        
SHEET    2   H 4 GLN E  78  LYS E  82 -1  N  VAL E  81   O  ILE E  89           
SHEET    3   H 4 THR E 142  VAL E 146  1  O  LEU E 145   N  LYS E  82           
SHEET    4   H 4 ARG E 118  ILE E 120 -1  N  ILE E 120   O  HIS E 144           
CRYST1   59.195  141.288  144.179  90.00  90.00  90.00 P 21 21 21   16          
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      0.016893  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007078  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006936        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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