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Database: PDB
Entry: 2V4H
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Original site: 2V4H 
HEADER    TRANSCRIPTION                           22-SEP-08   2V4H              
TITLE     NEMO CC2-LZ DOMAIN - 1D5 DARPIN COMPLEX                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NF-KAPPA-B ESSENTIAL MODULATOR;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CC2-LZ DOMAIN, RESIDUES 251-337;                           
COMPND   5 SYNONYM: NF-KAPPA-B ESSENTIAL MODIFIER, INHIBITOR OF NUCLEAR FACTOR  
COMPND   6  KAPPA-B KINASE SUBUNIT GAMMA, IKB KINASE-ASSOCIATED PROTEIN 1,      
COMPND   7  NEMO;                                                               
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: 1D5 DARPIN;                                                
COMPND  11 CHAIN: C, D;                                                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 OTHER_DETAILS: SEE SECONDARY REFERENCE                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28B;                                   
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630;                                               
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE;                                  
SOURCE  15 EXPRESSION_SYSTEM_PLASMID: PQE-30                                    
KEYWDS    TRANSCRIPTION, METAL-BINDING, NEMO - IKK GAMMA - NFKB PATHWAY -       
KEYWDS   2 DARPIN, TRANSCRIPTION REGULATION                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.GRUBISHA,S.DUQUERROY,F.CORDIER,A.HAOUZ,M.DELEPIERRE,M.VERON,F.AGOU  
REVDAT   4   21-DEC-16 2V4H    1       SOURCE AUTHOR                            
REVDAT   3   13-JUL-11 2V4H    1       VERSN                                    
REVDAT   2   08-DEC-09 2V4H    1       JRNL                                     
REVDAT   1   03-NOV-09 2V4H    0                                                
JRNL        AUTH   O.GRUBISHA,M.KAMINSKA,S.DUQUERROY,E.FONTAN,F.CORDIER,        
JRNL        AUTH 2 A.HAOUZ,B.RAYNAL,J.CHIARAVALLI,M.DELEPIERRE,A.ISRAEL,        
JRNL        AUTH 3 M.VERON,F.AGOU                                               
JRNL        TITL   DARPIN-ASSISTED CRYSTALLOGRAPHY OF THE CC2-LZ DOMAIN OF      
JRNL        TITL 2 NEMO REVEALS A COUPLING BETWEEN DIMERIZATION AND             
JRNL        TITL 3 UBIQUITIN-BINDING.                                           
JRNL        REF    J.MOL.BIOL.                   V. 395    89 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   19854204                                                     
JRNL        DOI    10.1016/J.JMB.2009.10.018                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.WYLER,M.KAMINSKA,Y.COIC,F.BALEUX,M.VERON,F.AGOU            
REMARK   1  TITL   INHIBITION OF NF-KAPPAB ACTIVATION WITH DESIGNED             
REMARK   1  TITL 2 ANKYRIN-REPEAT PROTEINS TARGETING THE UBIQUITIN-             
REMARK   1  TITL 3 BINDING/OLIGOMERIZATION DOMAIN OF NEMO.                      
REMARK   1  REF    PROTEIN SCI.                  V.  16  2013 2007              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   1  PMID   17766391                                                     
REMARK   1  DOI    10.1110/PS.072924907                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.9  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0069                                      
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) : 47.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.48                          
REMARK   3   NUMBER OF REFLECTIONS             : 17155                          
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) : 0.21051                         
REMARK   3   R VALUE            (WORKING SET) : 0.20754                         
REMARK   3   FREE R VALUE                     : 0.26821                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.9                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 883                             
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) : 2.900                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.975                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 680                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.298                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 31                           
REMARK   3   BIN FREE R VALUE                    : 0.420                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3491                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 51                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.694                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.66                                                
REMARK   3    B22 (A**2) : -1.66                                                
REMARK   3    B33 (A**2) : 3.33                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.700         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.377         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.283         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.453        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.889                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES    COUNT    RMS    WEIGHT          
REMARK   3   BOND LENGTHS REFINED           (A):  3532 ; 0.015 ; 0.021          
REMARK   3   BOND LENGTHS OTHERS            (A):  NULL ;  NULL ;  NULL          
REMARK   3   BOND ANGLES REFINED      (DEGREES):  4752 ; 1.586 ; 1.967          
REMARK   3   BOND ANGLES OTHERS       (DEGREES):  NULL ;  NULL ;  NULL          
REMARK   3   TORSION ANGLES, PERIOD 1 (DEGREES):   438 ; 6.139 ; 5.000          
REMARK   3   TORSION ANGLES, PERIOD 2 (DEGREES):   191 ;44.431 ;26.440          
REMARK   3   TORSION ANGLES, PERIOD 3 (DEGREES):   677 ;23.565 ;15.000          
REMARK   3   TORSION ANGLES, PERIOD 4 (DEGREES):    15 ;19.766 ;15.000          
REMARK   3   CHIRAL-CENTER RESTRAINTS    (A**3):   533 ; 0.103 ; 0.200          
REMARK   3   GENERAL PLANES REFINED         (A):  2673 ; 0.005 ; 0.020          
REMARK   3   GENERAL PLANES OTHERS          (A):  NULL ;  NULL ;  NULL          
REMARK   3   NON-BONDED CONTACTS REFINED    (A):  NULL ;  NULL ;  NULL          
REMARK   3   NON-BONDED CONTACTS OTHERS     (A):  NULL ;  NULL ;  NULL          
REMARK   3   NON-BONDED TORSION REFINED     (A):  NULL ;  NULL ;  NULL          
REMARK   3   NON-BONDED TORSION OTHERS      (A):  NULL ;  NULL ;  NULL          
REMARK   3   H-BOND (X...Y) REFINED         (A):  NULL ;  NULL ;  NULL          
REMARK   3   SYMMETRY VDW REFINED           (A):  NULL ;  NULL ;  NULL          
REMARK   3   SYMMETRY VDW OTHERS            (A):  NULL ;  NULL ;  NULL          
REMARK   3   SYMMETRY H-BOND REFINED        (A):  NULL ;  NULL ;  NULL          
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT  RMS   WEIGHT            
REMARK   3   MAIN-CHAIN BOND REFINED   (A**2):  2194 ; 0.562 ; 1.500            
REMARK   3   MAIN-CHAIN ANGLE REFINED  (A**2):  3485 ; 1.111 ; 2.000            
REMARK   3   SIDE-CHAIN BOND REFINED   (A**2):  1338 ; 1.742 ; 3.000            
REMARK   3   SIDE-CHAIN ANGLE REFINED  (A**2):  1267 ; 3.062 ; 4.500            
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF NCS GROUPS : 3                                           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               :   1                                
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP :    1                            
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    251       A     290      5                      
REMARK   3           1     B    251       B     290      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1   A     (A):    156 ;  0.41 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1   B     (A):    165 ;  1.06 ;  5.00           
REMARK   3   MEDIUM THERMAL     1   A  (A**2):    156 ;  0.39 ;  2.00           
REMARK   3   LOOSE THERMAL      1   B  (A**2):    165 ;  0.63 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               :   2                                
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP :    1                            
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C     12       C     136      5                      
REMARK   3           1     D      9       D     136      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2   C     (A):    500 ;  0.32 ;  0.50           
REMARK   3   LOOSE POSITIONAL   2   D     (A):    449 ;  0.74 ;  5.00           
REMARK   3   MEDIUM THERMAL     2   C  (A**2):    500 ;  2.11 ;  2.00           
REMARK   3   LOOSE THERMAL      2   D  (A**2):    449 ;  2.59 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               :   3                                
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP :    1                            
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    291       A     337      5                      
REMARK   3           1     B    291       B     337      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3   A     (A):    188 ;  0.52 ;  0.50           
REMARK   3   LOOSE POSITIONAL   3   B     (A):    215 ;  0.92 ;  5.00           
REMARK   3   MEDIUM THERMAL     3   A  (A**2):    188 ;  1.23 ;  2.00           
REMARK   3   LOOSE THERMAL      3   B  (A**2):    215 ;  2.60 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP :     1                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    12        C   136                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.1830  58.9480 172.3550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1093 T22:   0.2135                                     
REMARK   3      T33:  -0.1277 T12:   0.2483                                     
REMARK   3      T13:   0.0045 T23:   0.0450                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3051 L22:   3.1577                                     
REMARK   3      L33:   7.9121 L12:   0.4699                                     
REMARK   3      L13:   3.3057 L23:   0.4958                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2021 S12:  -0.3084 S13:   0.3086                       
REMARK   3      S21:  -0.1346 S22:   0.1312 S23:   0.2047                       
REMARK   3      S31:  -0.6922 S32:  -1.3658 S33:   0.0710                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     2                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     9        D   136                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.3760  55.5780 155.2180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3002 T22:  -0.2499                                     
REMARK   3      T33:  -0.0991 T12:   0.0796                                     
REMARK   3      T13:   0.0129 T23:  -0.0303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4845 L22:   7.1782                                     
REMARK   3      L33:   6.1966 L12:   1.5493                                     
REMARK   3      L13:  -0.7726 L23:  -2.2809                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0407 S12:   0.3828 S13:  -0.1132                       
REMARK   3      S21:  -0.4670 S22:   0.0507 S23:  -0.1598                       
REMARK   3      S31:  -0.0529 S32:  -0.0027 S33:  -0.0099                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     3                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   291        A   337                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.9510  58.8360 167.6090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1073 T22:  -0.2450                                     
REMARK   3      T33:  -0.1475 T12:   0.0552                                     
REMARK   3      T13:  -0.0600 T23:  -0.0164                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2862 L22:   5.6648                                     
REMARK   3      L33:  16.4604 L12:  -2.6236                                     
REMARK   3      L13:   3.9563 L23:  -6.0525                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3431 S12:   0.0391 S13:   0.2752                       
REMARK   3      S21:   0.1792 S22:   0.1425 S23:   0.0036                       
REMARK   3      S31:  -0.7008 S32:  -0.4763 S33:   0.2005                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     4                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   291        B   337                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.3960  53.9300 167.5410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1798 T22:  -0.1583                                     
REMARK   3      T33:  -0.1364 T12:  -0.0354                                     
REMARK   3      T13:  -0.1115 T23:  -0.0876                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9619 L22:   5.7053                                     
REMARK   3      L33:  20.2311 L12:  -4.3764                                     
REMARK   3      L13:   8.4871 L23:  -7.0463                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0993 S12:   0.3587 S13:  -0.3891                       
REMARK   3      S21:  -0.3713 S22:   0.1907 S23:   0.3027                       
REMARK   3      S31:   0.1868 S32:  -0.1409 S33:  -0.2901                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     5                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   251        A   290                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.4540  31.3520 223.3900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3833 T22:   0.5278                                     
REMARK   3      T33:  -0.1382 T12:   0.1618                                     
REMARK   3      T13:  -0.0458 T23:   0.1762                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6765 L22:   2.9401                                     
REMARK   3      L33:  54.8359 L12:  -2.6850                                     
REMARK   3      L13:  11.0871 L23:  -9.6404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3155 S12:   0.0602 S13:  -0.3083                       
REMARK   3      S21:  -0.7044 S22:   0.3135 S23:   0.2448                       
REMARK   3      S31:   0.9186 S32:  -0.3315 S33:  -0.6289                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     6                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   247        B   290                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.1780  33.2850 224.8080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5016 T22:   0.6183                                     
REMARK   3      T33:   0.0589 T12:   0.2328                                     
REMARK   3      T13:  -0.0181 T23:   0.0808                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0369 L22:   3.3287                                     
REMARK   3      L33:  14.2959 L12:  -3.3457                                     
REMARK   3      L13:   6.7732 L23:  -5.8785                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0538 S12:   0.7380 S13:   0.3712                       
REMARK   3      S21:  -0.6973 S22:  -0.8223 S23:  -0.8368                       
REMARK   3      S31:   0.5028 S32:   1.6324 S33:   0.8762                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     7                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   240        A   250                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.7890  36.1870 245.3380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5113 T22:   0.5449                                     
REMARK   3      T33:  -0.0552 T12:   0.1037                                     
REMARK   3      T13:  -0.0210 T23:   0.2308                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0131 L22:   1.7032                                     
REMARK   3      L33:  48.3596 L12:  -0.1491                                     
REMARK   3      L13:   0.7948 L23:  -9.0755                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3761 S12:   0.5494 S13:  -0.1931                       
REMARK   3      S21:  -0.7649 S22:   0.8162 S23:   0.5755                       
REMARK   3      S31:  -3.4832 S32:   2.3789 S33:  -0.4401                       
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          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   3   SOME RESIDUES COMING FROM THE TAG WERE VISIBLE IN THE              
REMARK   3   DENSITY. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY              
REMARK   4                                                                      
REMARK   4 2V4H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-SEP-08.                  
REMARK 100 THE PDBE ID CODE IS EBI-37632.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-NOV-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1741                             
REMARK 200  MONOCHROMATOR                  : SI(111) MONOCHROMATOR              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : PSI                                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 86037                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.90                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.8                               
REMARK 200  DATA REDUNDANCY                : 4.9                                
REMARK 200  R MERGE                    (I) : 0.13                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.60                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 42.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.2                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.45                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.80                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 2JAB                                       
REMARK 200                                                                      
REMARK 200 REMARK: THEORETICAL MODEL OF NEMO CC2 AND LZ HELICES USED            
REMARK 200  FOR MOLECULAR REPLACEMENT                                           
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% MPD, 5% ETHANOL, 100 MM HEPES,        
REMARK 280  PH 7.5                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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      218.45850            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       31.51000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       31.51000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      327.68775            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       31.51000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       31.51000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      109.22925            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       31.51000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       31.51000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      327.68775            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       31.51000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       31.51000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      109.22925            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      218.45850            
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: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 22000 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 55160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -173.5 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      436.91700            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   228                                                      
REMARK 465     GLY A   229                                                      
REMARK 465     SER A   230                                                      
REMARK 465     SER A   231                                                      
REMARK 465     HIS A   232                                                      
REMARK 465     HIS A   233                                                      
REMARK 465     HIS A   234                                                      
REMARK 465     HIS A   235                                                      
REMARK 465     HIS A   236                                                      
REMARK 465     HIS A   237                                                      
REMARK 465     SER A   238                                                      
REMARK 465     SER A   239                                                      
REMARK 465     MET B   228                                                      
REMARK 465     GLY B   229                                                      
REMARK 465     SER B   230                                                      
REMARK 465     SER B   231                                                      
REMARK 465     HIS B   232                                                      
REMARK 465     HIS B   233                                                      
REMARK 465     HIS B   234                                                      
REMARK 465     HIS B   235                                                      
REMARK 465     HIS B   236                                                      
REMARK 465     HIS B   237                                                      
REMARK 465     SER B   238                                                      
REMARK 465     SER B   239                                                      
REMARK 465     GLY B   240                                                      
REMARK 465     LEU B   241                                                      
REMARK 465     VAL B   242                                                      
REMARK 465     PRO B   243                                                      
REMARK 465     ARG B   244                                                      
REMARK 465     GLY B   245                                                      
REMARK 465     SER B   246                                                      
REMARK 465     HIS C     1                                                      
REMARK 465     HIS C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     HIS C     4                                                      
REMARK 465     HIS C     5                                                      
REMARK 465     HIS C     6                                                      
REMARK 465     HIS C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     HIS C     9                                                      
REMARK 465     HIS C    10                                                      
REMARK 465     GLY C    11                                                      
REMARK 465     HIS D     1                                                      
REMARK 465     HIS D     2                                                      
REMARK 465     HIS D     3                                                      
REMARK 465     HIS D     4                                                      
REMARK 465     HIS D     5                                                      
REMARK 465     HIS D     6                                                      
REMARK 465     HIS D     7                                                      
REMARK 465     HIS D     8                                                      
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    ASP C  56   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 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 251       58.74   -142.66                                   
REMARK 500    ASP A 255      -54.26    -29.29                                   
REMARK 500    ALA A 296      -70.75    -56.82                                   
REMARK 500    LEU B 336       30.48    -91.10                                   
REMARK 500    HIS C  92       50.83    -90.21                                   
REMARK 500    LEU C  93      -51.06    -21.97                                   
REMARK 500    ASN C 125       86.90    -65.43                                   
REMARK 500    ASP C 127      -60.16   -102.40                                   
REMARK 500    HIS D  10       57.81    -68.63                                   
REMARK 500    GLN D  26       97.71    -69.44                                   
REMARK 500    ALA D  38      126.46    -26.97                                   
REMARK 500    LYS D  46        1.88    -57.23                                   
REMARK 500    HIS D  69       32.85    -98.28                                   
REMARK 500    ASP D  77     -174.96    -61.04                                   
REMARK 500    ASP D 110     -159.64    -67.12                                   
REMARK 500    LYS D 134        0.19    -59.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 CHAINS C AND D CORRESPOND TO GENBANK REFERENCE AY326425 OR           
REMARK 999 GENPEPT REFERENCE AAQ93812.                                          
REMARK 999                                                                      
REMARK 999 THE MUTATIONS INTRODUCED IN CHAINS C AND D ARE DESCRIBED             
REMARK 999 BELOW:                                                               
REMARK 999 DESIGNED DARPIN TARGETING NEMO CC2-LZ DOMAIN MUTATIONS 43N-          
REMARK 999 45R-46K-48N-56D-57Y-58D-69H- 76H-78N-79D-81S-89L-90F-102H            
DBREF  2V4H A  251   337  UNP    O88522   NEMO_MOUSE     251    337             
DBREF  2V4H B  251   337  UNP    O88522   NEMO_MOUSE     251    337             
DBREF  2V4H C    1   136  PDB    2V4H     2V4H             1    136             
DBREF  2V4H D    1   136  PDB    2V4H     2V4H             1    136             
SEQADV 2V4H MET A  228  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H GLY A  229  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H SER A  230  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H SER A  231  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H HIS A  232  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H HIS A  233  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H HIS A  234  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H HIS A  235  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H HIS A  236  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H HIS A  237  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H SER A  238  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H SER A  239  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H GLY A  240  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H LEU A  241  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H VAL A  242  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H PRO A  243  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H ARG A  244  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H GLY A  245  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H SER A  246  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H HIS A  247  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H MET A  248  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H ALA A  249  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H SER A  250  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H MET B  228  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H GLY B  229  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H SER B  230  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H SER B  231  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H HIS B  232  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H HIS B  233  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H HIS B  234  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H HIS B  235  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H HIS B  236  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H HIS B  237  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H SER B  238  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H SER B  239  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H GLY B  240  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H LEU B  241  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H VAL B  242  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H PRO B  243  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H ARG B  244  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H GLY B  245  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H SER B  246  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H HIS B  247  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H MET B  248  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H ALA B  249  UNP  O88522              EXPRESSION TAG                 
SEQADV 2V4H SER B  250  UNP  O88522              EXPRESSION TAG                 
SEQRES   1 A  110  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  110  LEU VAL PRO ARG GLY SER HIS MET ALA SER MET GLN LEU          
SEQRES   3 A  110  GLU ASP LEU ARG GLN GLN LEU GLN GLN ALA GLU GLU ALA          
SEQRES   4 A  110  LEU VAL ALA LYS GLN GLU LEU ILE ASP LYS LEU LYS GLU          
SEQRES   5 A  110  GLU ALA GLU GLN HIS LYS ILE VAL MET GLU THR VAL PRO          
SEQRES   6 A  110  VAL LEU LYS ALA GLN ALA ASP ILE TYR LYS ALA ASP PHE          
SEQRES   7 A  110  GLN ALA GLU ARG HIS ALA ARG GLU LYS LEU VAL GLU LYS          
SEQRES   8 A  110  LYS GLU TYR LEU GLN GLU GLN LEU GLU GLN LEU GLN ARG          
SEQRES   9 A  110  GLU PHE ASN LYS LEU LYS                                      
SEQRES   1 B  110  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  110  LEU VAL PRO ARG GLY SER HIS MET ALA SER MET GLN LEU          
SEQRES   3 B  110  GLU ASP LEU ARG GLN GLN LEU GLN GLN ALA GLU GLU ALA          
SEQRES   4 B  110  LEU VAL ALA LYS GLN GLU LEU ILE ASP LYS LEU LYS GLU          
SEQRES   5 B  110  GLU ALA GLU GLN HIS LYS ILE VAL MET GLU THR VAL PRO          
SEQRES   6 B  110  VAL LEU LYS ALA GLN ALA ASP ILE TYR LYS ALA ASP PHE          
SEQRES   7 B  110  GLN ALA GLU ARG HIS ALA ARG GLU LYS LEU VAL GLU LYS          
SEQRES   8 B  110  LYS GLU TYR LEU GLN GLU GLN LEU GLU GLN LEU GLN ARG          
SEQRES   9 B  110  GLU PHE ASN LYS LEU LYS                                      
SEQRES   1 C  136  HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS GLY SER ASP          
SEQRES   2 C  136  LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN          
SEQRES   3 C  136  ASP ASP GLU VAL ARG ILE LEU MET ALA ASN GLY ALA ASP          
SEQRES   4 C  136  VAL ASN ALA ASN ASP ARG LYS GLY ASN THR PRO LEU HIS          
SEQRES   5 C  136  LEU ALA ALA ASP TYR ASP HIS LEU GLU ILE VAL GLU VAL          
SEQRES   6 C  136  LEU LEU LYS HIS GLY ALA ASP VAL ASN ALA HIS ASP ASN          
SEQRES   7 C  136  ASP GLY SER THR PRO LEU HIS LEU ALA ALA LEU PHE GLY          
SEQRES   8 C  136  HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS HIS GLY ALA          
SEQRES   9 C  136  ASP VAL ASN ALA GLN ASP LYS PHE GLY LYS THR ALA PHE          
SEQRES  10 C  136  ASP ILE SER ILE ASP ASN GLY ASN GLU ASP LEU ALA GLU          
SEQRES  11 C  136  ILE LEU GLN LYS LEU ASN                                      
SEQRES   1 D  136  HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS GLY SER ASP          
SEQRES   2 D  136  LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN          
SEQRES   3 D  136  ASP ASP GLU VAL ARG ILE LEU MET ALA ASN GLY ALA ASP          
SEQRES   4 D  136  VAL ASN ALA ASN ASP ARG LYS GLY ASN THR PRO LEU HIS          
SEQRES   5 D  136  LEU ALA ALA ASP TYR ASP HIS LEU GLU ILE VAL GLU VAL          
SEQRES   6 D  136  LEU LEU LYS HIS GLY ALA ASP VAL ASN ALA HIS ASP ASN          
SEQRES   7 D  136  ASP GLY SER THR PRO LEU HIS LEU ALA ALA LEU PHE GLY          
SEQRES   8 D  136  HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS HIS GLY ALA          
SEQRES   9 D  136  ASP VAL ASN ALA GLN ASP LYS PHE GLY LYS THR ALA PHE          
SEQRES  10 D  136  ASP ILE SER ILE ASP ASN GLY ASN GLU ASP LEU ALA GLU          
SEQRES  11 D  136  ILE LEU GLN LYS LEU ASN                                      
FORMUL   5  HOH   *51(H2 O)                                                     
HELIX    1   1 MET A  251  GLU A  289  1                                  39    
HELIX    2   2 GLU A  289  ASN A  334  1                                  46    
HELIX    3   3 MET B  248  GLU B  289  1                                  42    
HELIX    4   4 GLU B  289  LEU B  336  1                                  48    
HELIX    5   5 ASP C   13  GLY C   25  1                                  13    
HELIX    6   6 GLN C   26  ASN C   36  1                                  11    
HELIX    7   7 THR C   49  TYR C   57  1                                   9    
HELIX    8   8 HIS C   59  LYS C   68  1                                  10    
HELIX    9   9 THR C   82  PHE C   90  1                                   9    
HELIX   10  10 HIS C   92  HIS C  102  1                                  11    
HELIX   11  11 THR C  115  GLY C  124  1                                  10    
HELIX   12  12 ASN C  125  ILE C  131  1                                   7    
HELIX   13  13 ASP D   13  GLY D   25  1                                  13    
HELIX   14  14 GLN D   26  ASN D   36  1                                  11    
HELIX   15  15 THR D   49  TYR D   57  1                                   9    
HELIX   16  16 HIS D   59  HIS D   69  1                                  11    
HELIX   17  17 THR D   82  GLY D   91  1                                  10    
HELIX   18  18 HIS D   92  HIS D  102  1                                  11    
HELIX   19  19 THR D  115  GLY D  124  1                                  10    
HELIX   20  20 ASN D  125  LYS D  134  1                                  10    
CRYST1   63.020   63.020  436.917  90.00  90.00  90.00 P 43 21 2    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      0.015868  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015868  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002289        0.00000                         
MTRIX1   1 -0.712260 -0.403160  0.574580      -19.12920    1                    
MTRIX2   1 -0.132830 -0.726380 -0.674330      215.30067    1                    
MTRIX3   1  0.689230 -0.556620  0.463820      100.09966    1                    
MTRIX1   2 -0.610810 -0.097230  0.785790      -76.43774    1                    
MTRIX2   2 -0.446560 -0.777220 -0.443290      188.67770    1                    
MTRIX3   2  0.653830 -0.621670  0.431320      110.26794    1                    
MTRIX1   3 -0.622250 -0.323100  0.713030      -50.05271    1                    
MTRIX2   3 -0.231360 -0.794250 -0.561810      202.21927    1                    
MTRIX3   3  0.747850 -0.514560  0.419470      102.71049    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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