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Database: PDB
Entry: 4G3D
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HEADER    TRANSFERASE                             13-JUL-12   4G3D              
TITLE     CRYSTAL STRUCTURE OF HUMAN NF-KAPPAB INDUCING KINASE (NIK)            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NF-KAPPA-BETA-INDUCING KINASE;                             
COMPND   3 CHAIN: A, B, D, E;                                                   
COMPND   4 SYNONYM: HSNIK, SERINE/THREONINE-PROTEIN KINASE NIK;                 
COMPND   5 EC: 2.7.11.25;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MAP3K14, NF-KAPPAB INDUCING KINASE (NIK), NIK;                 
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS TRANSFER VECTOR;          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PACGP67                                   
KEYWDS    NON-RD KINASE, PROTEIN SERINE/THREONINE KINASE, NF-KAPPAB, MAP3K14,   
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.G.HYMOWITZ,DE LEON-BOENIG G.                                        
REVDAT   2   23-JAN-13 4G3D    1       JRNL                                     
REVDAT   1   15-AUG-12 4G3D    0                                                
JRNL        AUTH   G.DE LEON-BOENIG,K.K.BOWMAN,J.A.FENG,T.CRAWFORD,C.EVERETT,   
JRNL        AUTH 2 Y.FRANKE,A.OH,M.STANLEY,S.T.STABEN,M.A.STAROVASNIK,          
JRNL        AUTH 3 H.J.WALLWEBER,J.WU,L.C.WU,A.R.JOHNSON,S.G.HYMOWITZ           
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE         
JRNL        TITL 2 NF-KAPPAB INDUCING KINASE REVEALS A NARROW BUT FLEXIBLE      
JRNL        TITL 3 ACTIVE SITE.                                                 
JRNL        REF    STRUCTURE                     V.  20  1704 2012              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   22921830                                                     
JRNL        DOI    10.1016/J.STR.2012.07.013                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 47.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 31030                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2687                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 25                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.96                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1625                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.80                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2560                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 0                            
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9325                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 3                                       
REMARK   3   SOLVENT ATOMS            : 18                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 80.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.77000                                              
REMARK   3    B22 (A**2) : -3.53000                                             
REMARK   3    B33 (A**2) : -1.24000                                             
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): 0.443         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.314         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 35.575        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.887                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9527 ; 0.005 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12889 ; 1.039 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1199 ; 5.154 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   411 ;32.894 ;23.698       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1601 ;16.730 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    65 ;19.030 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1413 ; 0.064 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7193 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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  : 8                                          
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 :   A   332        A   470                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.1373  30.5034  39.3384              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3750 T22:   0.3781                                     
REMARK   3      T33:   0.4569 T12:  -0.0298                                     
REMARK   3      T13:   0.0005 T23:  -0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9839 L22:   2.7521                                     
REMARK   3      L33:   0.3204 L12:   0.5904                                     
REMARK   3      L13:   0.0709 L23:  -0.7855                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1485 S12:  -0.1635 S13:   0.0389                       
REMARK   3      S21:  -0.2912 S22:  -0.1038 S23:   0.0039                       
REMARK   3      S31:   0.0720 S32:   0.0364 S33:  -0.0448                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   471        A   671                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.7148   6.2349  53.3823              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2848 T22:   0.4745                                     
REMARK   3      T33:   0.4145 T12:  -0.0308                                     
REMARK   3      T13:   0.0024 T23:   0.0689                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0452 L22:   1.9936                                     
REMARK   3      L33:   0.9146 L12:   0.0519                                     
REMARK   3      L13:  -0.0652 L23:  -0.8700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1426 S12:   0.1008 S13:   0.1043                       
REMARK   3      S21:   0.1758 S22:  -0.1717 S23:   0.0200                       
REMARK   3      S31:   0.0209 S32:   0.0792 S33:   0.0290                       
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 :   B   332        B   470                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.6835  60.7860  30.8365              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4410 T22:   0.3374                                     
REMARK   3      T33:   0.4185 T12:   0.0204                                     
REMARK   3      T13:   0.0471 T23:  -0.0458                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9425 L22:   1.0184                                     
REMARK   3      L33:   2.7663 L12:   0.6480                                     
REMARK   3      L13:  -0.1957 L23:  -0.4311                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0035 S12:   0.0218 S13:  -0.0901                       
REMARK   3      S21:  -0.2215 S22:   0.0532 S23:  -0.0359                       
REMARK   3      S31:  -0.2037 S32:  -0.0375 S33:  -0.0567                       
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   471        B   666                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.5762  52.1493  57.3259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2782 T22:   0.4367                                     
REMARK   3      T33:   0.4734 T12:  -0.0095                                     
REMARK   3      T13:  -0.0514 T23:   0.0129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4657 L22:   0.5655                                     
REMARK   3      L33:   1.2314 L12:   0.4782                                     
REMARK   3      L13:   0.0050 L23:   0.3290                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2758 S12:  -0.1189 S13:  -0.2476                       
REMARK   3      S21:   0.1237 S22:  -0.1548 S23:  -0.0269                       
REMARK   3      S31:   0.0048 S32:   0.0175 S33:  -0.1210                       
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 :   D   338        D   470                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.0912   4.2040 110.3310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7045 T22:   0.3211                                     
REMARK   3      T33:   0.1884 T12:   0.0036                                     
REMARK   3      T13:   0.1020 T23:  -0.0334                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6269 L22:   2.3124                                     
REMARK   3      L33:   3.8664 L12:   0.4678                                     
REMARK   3      L13:  -1.5049 L23:  -0.9303                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1784 S12:  -0.0067 S13:  -0.0073                       
REMARK   3      S21:   0.3785 S22:  -0.2296 S23:   0.2159                       
REMARK   3      S31:  -0.2890 S32:   0.2511 S33:   0.0512                       
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 :   D   471        D   657                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.2202  16.8088  85.9221              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8244 T22:   0.1508                                     
REMARK   3      T33:   0.2599 T12:  -0.0931                                     
REMARK   3      T13:   0.1240 T23:   0.0462                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1549 L22:   1.5099                                     
REMARK   3      L33:   3.1946 L12:   0.0605                                     
REMARK   3      L13:  -0.4983 L23:  -1.0531                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1306 S12:   0.1685 S13:   0.0637                       
REMARK   3      S21:  -0.0399 S22:   0.1295 S23:  -0.1310                       
REMARK   3      S31:  -0.8046 S32:  -0.1557 S33:  -0.2602                       
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 :   E   332        E   470                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.7148  75.5088  90.2764              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6484 T22:   0.2654                                     
REMARK   3      T33:   0.2430 T12:   0.0000                                     
REMARK   3      T13:  -0.1067 T23:   0.0119                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6113 L22:   2.5195                                     
REMARK   3      L33:   2.4438 L12:   0.2929                                     
REMARK   3      L13:  -0.5506 L23:  -0.1836                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0493 S12:   0.1337 S13:   0.0827                       
REMARK   3      S21:   0.2169 S22:   0.0141 S23:  -0.0033                       
REMARK   3      S31:   0.3387 S32:   0.0196 S33:  -0.0634                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   471        E   663                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.8730  47.8533  95.7349              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2697 T22:   0.0684                                     
REMARK   3      T33:   0.1038 T12:   0.0573                                     
REMARK   3      T13:  -0.0878 T23:  -0.0114                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4558 L22:   4.2014                                     
REMARK   3      L33:   0.7401 L12:   0.5521                                     
REMARK   3      L13:  -1.1153 L23:  -1.0715                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1256 S12:   0.1520 S13:  -0.1676                       
REMARK   3      S21:   0.4173 S22:   0.0531 S23:  -0.0426                       
REMARK   3      S31:   0.2472 S32:  -0.0341 S33:   0.0725                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4G3D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073686.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAY-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97945                            
REMARK 200  MONOCHROMATOR                  : 0.97945                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35489                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.8000                            
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) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.61100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:1 PROTEIN AND WELL SOLUTION OF 100     
REMARK 280  MM IMIDAZOLE (PH 6.5), 1 M SODIUM ACETATE TRI-HYDRATE, 7.5% 1,6-    
REMARK 280  HEXANEDIOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K         
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       22.87300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      115.40900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.92550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      115.40900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.87300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.92550            
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, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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   306                                                      
REMARK 465     SER A   307                                                      
REMARK 465     ASP A   308                                                      
REMARK 465     SER A   309                                                      
REMARK 465     PRO A   310                                                      
REMARK 465     LYS A   311                                                      
REMARK 465     PRO A   312                                                      
REMARK 465     LEU A   313                                                      
REMARK 465     PRO A   314                                                      
REMARK 465     GLY A   315                                                      
REMARK 465     PRO A   316                                                      
REMARK 465     HIS A   317                                                      
REMARK 465     LEU A   318                                                      
REMARK 465     GLU A   319                                                      
REMARK 465     PRO A   320                                                      
REMARK 465     SER A   321                                                      
REMARK 465     CYS A   322                                                      
REMARK 465     LEU A   323                                                      
REMARK 465     SER A   324                                                      
REMARK 465     ARG A   325                                                      
REMARK 465     GLY A   326                                                      
REMARK 465     ALA A   327                                                      
REMARK 465     HIS A   328                                                      
REMARK 465     GLU A   329                                                      
REMARK 465     LYS A   330                                                      
REMARK 465     PHE A   331                                                      
REMARK 465     ARG A   363                                                      
REMARK 465     GLY A   364                                                      
REMARK 465     SER A   365                                                      
REMARK 465     ARG A   366                                                      
REMARK 465     SER A   367                                                      
REMARK 465     ARG A   368                                                      
REMARK 465     GLU A   369                                                      
REMARK 465     PRO A   370                                                      
REMARK 465     SER A   371                                                      
REMARK 465     PRO A   372                                                      
REMARK 465     LYS A   373                                                      
REMARK 465     THR A   374                                                      
REMARK 465     GLU A   375                                                      
REMARK 465     GLN A   403                                                      
REMARK 465     LEU A   404                                                      
REMARK 465     ARG A   405                                                      
REMARK 465     LEU A   406                                                      
REMARK 465     ARG A   673                                                      
REMARK 465     GLY A   674                                                      
REMARK 465     ASN A   675                                                      
REMARK 465     SER A   676                                                      
REMARK 465     GLY B   306                                                      
REMARK 465     SER B   307                                                      
REMARK 465     ASP B   308                                                      
REMARK 465     SER B   309                                                      
REMARK 465     PRO B   310                                                      
REMARK 465     LYS B   311                                                      
REMARK 465     PRO B   312                                                      
REMARK 465     LEU B   313                                                      
REMARK 465     PRO B   314                                                      
REMARK 465     GLY B   315                                                      
REMARK 465     PRO B   316                                                      
REMARK 465     HIS B   317                                                      
REMARK 465     LEU B   318                                                      
REMARK 465     GLU B   319                                                      
REMARK 465     PRO B   320                                                      
REMARK 465     SER B   321                                                      
REMARK 465     CYS B   322                                                      
REMARK 465     LEU B   323                                                      
REMARK 465     SER B   324                                                      
REMARK 465     ARG B   325                                                      
REMARK 465     GLY B   326                                                      
REMARK 465     ALA B   327                                                      
REMARK 465     HIS B   328                                                      
REMARK 465     GLU B   329                                                      
REMARK 465     LYS B   330                                                      
REMARK 465     PHE B   331                                                      
REMARK 465     ARG B   363                                                      
REMARK 465     GLY B   364                                                      
REMARK 465     SER B   365                                                      
REMARK 465     ARG B   366                                                      
REMARK 465     SER B   367                                                      
REMARK 465     ARG B   368                                                      
REMARK 465     GLU B   369                                                      
REMARK 465     PRO B   370                                                      
REMARK 465     SER B   371                                                      
REMARK 465     PRO B   372                                                      
REMARK 465     LYS B   373                                                      
REMARK 465     THR B   374                                                      
REMARK 465     GLU B   375                                                      
REMARK 465     GLN B   403                                                      
REMARK 465     LEU B   404                                                      
REMARK 465     ARG B   405                                                      
REMARK 465     LEU B   406                                                      
REMARK 465     GLY B   667                                                      
REMARK 465     GLU B   668                                                      
REMARK 465     TYR B   669                                                      
REMARK 465     LYS B   670                                                      
REMARK 465     GLU B   671                                                      
REMARK 465     PRO B   672                                                      
REMARK 465     ARG B   673                                                      
REMARK 465     GLY B   674                                                      
REMARK 465     ASN B   675                                                      
REMARK 465     SER B   676                                                      
REMARK 465     GLY D   306                                                      
REMARK 465     SER D   307                                                      
REMARK 465     ASP D   308                                                      
REMARK 465     SER D   309                                                      
REMARK 465     PRO D   310                                                      
REMARK 465     LYS D   311                                                      
REMARK 465     PRO D   312                                                      
REMARK 465     LEU D   313                                                      
REMARK 465     PRO D   314                                                      
REMARK 465     GLY D   315                                                      
REMARK 465     PRO D   316                                                      
REMARK 465     HIS D   317                                                      
REMARK 465     LEU D   318                                                      
REMARK 465     GLU D   319                                                      
REMARK 465     PRO D   320                                                      
REMARK 465     SER D   321                                                      
REMARK 465     CYS D   322                                                      
REMARK 465     LEU D   323                                                      
REMARK 465     SER D   324                                                      
REMARK 465     ARG D   325                                                      
REMARK 465     GLY D   326                                                      
REMARK 465     ALA D   327                                                      
REMARK 465     HIS D   328                                                      
REMARK 465     GLU D   329                                                      
REMARK 465     LYS D   330                                                      
REMARK 465     PHE D   331                                                      
REMARK 465     SER D   332                                                      
REMARK 465     VAL D   333                                                      
REMARK 465     GLU D   334                                                      
REMARK 465     GLU D   335                                                      
REMARK 465     TYR D   336                                                      
REMARK 465     LEU D   337                                                      
REMARK 465     ARG D   363                                                      
REMARK 465     GLY D   364                                                      
REMARK 465     SER D   365                                                      
REMARK 465     ARG D   366                                                      
REMARK 465     SER D   367                                                      
REMARK 465     ARG D   368                                                      
REMARK 465     GLU D   369                                                      
REMARK 465     PRO D   370                                                      
REMARK 465     SER D   371                                                      
REMARK 465     PRO D   372                                                      
REMARK 465     LYS D   373                                                      
REMARK 465     THR D   374                                                      
REMARK 465     GLU D   375                                                      
REMARK 465     GLN D   403                                                      
REMARK 465     LEU D   404                                                      
REMARK 465     ARG D   405                                                      
REMARK 465     LEU D   406                                                      
REMARK 465     ASP D   544                                                      
REMARK 465     GLY D   545                                                      
REMARK 465     LEU D   546                                                      
REMARK 465     GLY D   547                                                      
REMARK 465     LYS D   548                                                      
REMARK 465     SER D   549                                                      
REMARK 465     LEU D   550                                                      
REMARK 465     LEU D   551                                                      
REMARK 465     THR D   552                                                      
REMARK 465     GLY D   553                                                      
REMARK 465     ASP D   554                                                      
REMARK 465     TYR D   555                                                      
REMARK 465     ILE D   556                                                      
REMARK 465     VAL D   658                                                      
REMARK 465     GLY D   659                                                      
REMARK 465     GLY D   660                                                      
REMARK 465     LEU D   661                                                      
REMARK 465     LYS D   662                                                      
REMARK 465     SER D   663                                                      
REMARK 465     PRO D   664                                                      
REMARK 465     TRP D   665                                                      
REMARK 465     ARG D   666                                                      
REMARK 465     GLY D   667                                                      
REMARK 465     GLU D   668                                                      
REMARK 465     TYR D   669                                                      
REMARK 465     LYS D   670                                                      
REMARK 465     GLU D   671                                                      
REMARK 465     PRO D   672                                                      
REMARK 465     ARG D   673                                                      
REMARK 465     GLY D   674                                                      
REMARK 465     ASN D   675                                                      
REMARK 465     SER D   676                                                      
REMARK 465     GLY E   306                                                      
REMARK 465     SER E   307                                                      
REMARK 465     ASP E   308                                                      
REMARK 465     SER E   309                                                      
REMARK 465     PRO E   310                                                      
REMARK 465     LYS E   311                                                      
REMARK 465     PRO E   312                                                      
REMARK 465     LEU E   313                                                      
REMARK 465     PRO E   314                                                      
REMARK 465     GLY E   315                                                      
REMARK 465     PRO E   316                                                      
REMARK 465     HIS E   317                                                      
REMARK 465     LEU E   318                                                      
REMARK 465     GLU E   319                                                      
REMARK 465     PRO E   320                                                      
REMARK 465     SER E   321                                                      
REMARK 465     CYS E   322                                                      
REMARK 465     LEU E   323                                                      
REMARK 465     SER E   324                                                      
REMARK 465     ARG E   325                                                      
REMARK 465     GLY E   326                                                      
REMARK 465     ALA E   327                                                      
REMARK 465     HIS E   328                                                      
REMARK 465     GLU E   329                                                      
REMARK 465     LYS E   330                                                      
REMARK 465     PHE E   331                                                      
REMARK 465     ARG E   363                                                      
REMARK 465     GLY E   364                                                      
REMARK 465     SER E   365                                                      
REMARK 465     ARG E   366                                                      
REMARK 465     SER E   367                                                      
REMARK 465     ARG E   368                                                      
REMARK 465     GLU E   369                                                      
REMARK 465     PRO E   370                                                      
REMARK 465     SER E   371                                                      
REMARK 465     PRO E   372                                                      
REMARK 465     LYS E   373                                                      
REMARK 465     THR E   374                                                      
REMARK 465     GLU E   375                                                      
REMARK 465     GLN E   403                                                      
REMARK 465     LEU E   404                                                      
REMARK 465     ARG E   405                                                      
REMARK 465     LEU E   406                                                      
REMARK 465     PRO E   543                                                      
REMARK 465     ASP E   544                                                      
REMARK 465     GLY E   545                                                      
REMARK 465     LEU E   546                                                      
REMARK 465     GLY E   547                                                      
REMARK 465     LYS E   548                                                      
REMARK 465     SER E   549                                                      
REMARK 465     LEU E   550                                                      
REMARK 465     LEU E   551                                                      
REMARK 465     THR E   552                                                      
REMARK 465     GLY E   553                                                      
REMARK 465     ASP E   554                                                      
REMARK 465     TYR E   555                                                      
REMARK 465     ILE E   556                                                      
REMARK 465     GLU E   560                                                      
REMARK 465     TRP E   596                                                      
REMARK 465     THR E   597                                                      
REMARK 465     GLN E   598                                                      
REMARK 465     PHE E   599                                                      
REMARK 465     PHE E   600                                                      
REMARK 465     ARG E   601                                                      
REMARK 465     GLY E   602                                                      
REMARK 465     PRO E   603                                                      
REMARK 465     LEU E   604                                                      
REMARK 465     CYS E   605                                                      
REMARK 465     LEU E   606                                                      
REMARK 465     LYS E   607                                                      
REMARK 465     ILE E   608                                                      
REMARK 465     ALA E   609                                                      
REMARK 465     SER E   610                                                      
REMARK 465     GLU E   611                                                      
REMARK 465     PRO E   612                                                      
REMARK 465     PRO E   664                                                      
REMARK 465     TRP E   665                                                      
REMARK 465     ARG E   666                                                      
REMARK 465     GLY E   667                                                      
REMARK 465     GLU E   668                                                      
REMARK 465     TYR E   669                                                      
REMARK 465     LYS E   670                                                      
REMARK 465     GLU E   671                                                      
REMARK 465     PRO E   672                                                      
REMARK 465     ARG E   673                                                      
REMARK 465     GLY E   674                                                      
REMARK 465     ASN E   675                                                      
REMARK 465     SER E   676                                                      
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    LEU A 512   CA  -  CB  -  CG  ANGL. DEV. =  14.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 396      -13.63     70.23                                   
REMARK 500    ALA A 443       34.82    -89.37                                   
REMARK 500    CYS A 444      -49.07   -157.83                                   
REMARK 500    GLN A 484       59.43   -117.73                                   
REMARK 500    ASP A 515       61.30   -150.38                                   
REMARK 500    ASP A 534       85.96     43.20                                   
REMARK 500    PRO A 543      -29.12    -27.49                                   
REMARK 500    ASP A 544       33.94    -90.59                                   
REMARK 500    LYS A 548     -105.37     84.58                                   
REMARK 500    SER A 549      134.53    108.78                                   
REMARK 500    TRP A 596      -33.33     67.81                                   
REMARK 500    PRO A 603       93.67    -65.53                                   
REMARK 500    PRO A 614        6.91    -58.55                                   
REMARK 500    VAL A 615      -34.05    -30.63                                   
REMARK 500    GLU B 396       -8.52     68.54                                   
REMARK 500    CYS B 426     -159.34   -152.42                                   
REMARK 500    CYS B 444      -37.04   -146.27                                   
REMARK 500    ASP B 515       58.17   -161.38                                   
REMARK 500    ASP B 534       87.75     59.52                                   
REMARK 500    ASP B 544     -134.98    -87.43                                   
REMARK 500    LEU B 546     -104.76   -139.06                                   
REMARK 500    TRP B 596      -43.81     74.17                                   
REMARK 500    THR B 597      -61.53    -12.14                                   
REMARK 500    PRO B 614       14.35    -62.67                                   
REMARK 500    TYR D 393       76.44   -155.26                                   
REMARK 500    GLU D 396      -18.59     71.46                                   
REMARK 500    ARG D 408       84.23   -150.96                                   
REMARK 500    CYS D 444      -40.90   -144.84                                   
REMARK 500    ASP D 534       77.31     56.52                                   
REMARK 500    GLN D 542      127.92    -33.33                                   
REMARK 500    TRP D 596      -39.29     70.12                                   
REMARK 500    PHE D 599      -79.24    -86.72                                   
REMARK 500    PRO D 612      160.73    -47.27                                   
REMARK 500    PRO D 614       36.81    -73.03                                   
REMARK 500    GLU E 396      -13.40     69.35                                   
REMARK 500    ARG E 408       83.49   -155.20                                   
REMARK 500    PHE E 411       13.17   -145.45                                   
REMARK 500    CYS E 426     -157.06   -138.96                                   
REMARK 500    CYS E 444      -37.02   -142.39                                   
REMARK 500    ASP E 515       66.84   -152.93                                   
REMARK 500    ASP E 534       79.67     53.74                                   
REMARK 500    PRO E 614       30.21    -62.36                                   
REMARK 500    LEU E 634       51.44   -113.21                                   
REMARK 500    VAL E 658       35.13    -80.58                                   
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 ALA B  443     CYS B  444                 -149.53                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 701  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 534   OD2                                                    
REMARK 620 2 ASN D 520   OD1  76.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 701  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 520   OD1                                                    
REMARK 620 2 ASP A 534   OD2  79.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 701                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4G3C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4G3E   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4G3F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4G3G   RELATED DB: PDB                                   
DBREF  4G3D A  308   673  UNP    Q99558   M3K14_HUMAN    308    673             
DBREF  4G3D B  308   673  UNP    Q99558   M3K14_HUMAN    308    673             
DBREF  4G3D D  308   673  UNP    Q99558   M3K14_HUMAN    308    673             
DBREF  4G3D E  308   673  UNP    Q99558   M3K14_HUMAN    308    673             
SEQADV 4G3D GLY A  306  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D SER A  307  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D GLY A  674  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D ASN A  675  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D SER A  676  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D GLY B  306  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D SER B  307  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D GLY B  674  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D ASN B  675  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D SER B  676  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D GLY D  306  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D SER D  307  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D GLY D  674  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D ASN D  675  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D SER D  676  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D GLY E  306  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D SER E  307  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D GLY E  674  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D ASN E  675  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4G3D SER E  676  UNP  Q99558              EXPRESSION TAG                 
SEQRES   1 A  371  GLY SER ASP SER PRO LYS PRO LEU PRO GLY PRO HIS LEU          
SEQRES   2 A  371  GLU PRO SER CYS LEU SER ARG GLY ALA HIS GLU LYS PHE          
SEQRES   3 A  371  SER VAL GLU GLU TYR LEU VAL HIS ALA LEU GLN GLY SER          
SEQRES   4 A  371  VAL SER SER GLY GLN ALA HIS SER LEU THR SER LEU ALA          
SEQRES   5 A  371  LYS THR TRP ALA ALA ARG GLY SER ARG SER ARG GLU PRO          
SEQRES   6 A  371  SER PRO LYS THR GLU ASP ASN GLU GLY VAL LEU LEU THR          
SEQRES   7 A  371  GLU LYS LEU LYS PRO VAL ASP TYR GLU TYR ARG GLU GLU          
SEQRES   8 A  371  VAL HIS TRP ALA THR HIS GLN LEU ARG LEU GLY ARG GLY          
SEQRES   9 A  371  SER PHE GLY GLU VAL HIS ARG MET GLU ASP LYS GLN THR          
SEQRES  10 A  371  GLY PHE GLN CYS ALA VAL LYS LYS VAL ARG LEU GLU VAL          
SEQRES  11 A  371  PHE ARG ALA GLU GLU LEU MET ALA CYS ALA GLY LEU THR          
SEQRES  12 A  371  SER PRO ARG ILE VAL PRO LEU TYR GLY ALA VAL ARG GLU          
SEQRES  13 A  371  GLY PRO TRP VAL ASN ILE PHE MET GLU LEU LEU GLU GLY          
SEQRES  14 A  371  GLY SER LEU GLY GLN LEU VAL LYS GLU GLN GLY CYS LEU          
SEQRES  15 A  371  PRO GLU ASP ARG ALA LEU TYR TYR LEU GLY GLN ALA LEU          
SEQRES  16 A  371  GLU GLY LEU GLU TYR LEU HIS SER ARG ARG ILE LEU HIS          
SEQRES  17 A  371  GLY ASP VAL LYS ALA ASP ASN VAL LEU LEU SER SER ASP          
SEQRES  18 A  371  GLY SER HIS ALA ALA LEU CYS ASP PHE GLY HIS ALA VAL          
SEQRES  19 A  371  CYS LEU GLN PRO ASP GLY LEU GLY LYS SER LEU LEU THR          
SEQRES  20 A  371  GLY ASP TYR ILE PRO GLY THR GLU THR HIS MET ALA PRO          
SEQRES  21 A  371  GLU VAL VAL LEU GLY ARG SER CYS ASP ALA LYS VAL ASP          
SEQRES  22 A  371  VAL TRP SER SER CYS CYS MET MET LEU HIS MET LEU ASN          
SEQRES  23 A  371  GLY CYS HIS PRO TRP THR GLN PHE PHE ARG GLY PRO LEU          
SEQRES  24 A  371  CYS LEU LYS ILE ALA SER GLU PRO PRO PRO VAL ARG GLU          
SEQRES  25 A  371  ILE PRO PRO SER CYS ALA PRO LEU THR ALA GLN ALA ILE          
SEQRES  26 A  371  GLN GLU GLY LEU ARG LYS GLU PRO ILE HIS ARG VAL SER          
SEQRES  27 A  371  ALA ALA GLU LEU GLY GLY LYS VAL ASN ARG ALA LEU GLN          
SEQRES  28 A  371  GLN VAL GLY GLY LEU LYS SER PRO TRP ARG GLY GLU TYR          
SEQRES  29 A  371  LYS GLU PRO ARG GLY ASN SER                                  
SEQRES   1 B  371  GLY SER ASP SER PRO LYS PRO LEU PRO GLY PRO HIS LEU          
SEQRES   2 B  371  GLU PRO SER CYS LEU SER ARG GLY ALA HIS GLU LYS PHE          
SEQRES   3 B  371  SER VAL GLU GLU TYR LEU VAL HIS ALA LEU GLN GLY SER          
SEQRES   4 B  371  VAL SER SER GLY GLN ALA HIS SER LEU THR SER LEU ALA          
SEQRES   5 B  371  LYS THR TRP ALA ALA ARG GLY SER ARG SER ARG GLU PRO          
SEQRES   6 B  371  SER PRO LYS THR GLU ASP ASN GLU GLY VAL LEU LEU THR          
SEQRES   7 B  371  GLU LYS LEU LYS PRO VAL ASP TYR GLU TYR ARG GLU GLU          
SEQRES   8 B  371  VAL HIS TRP ALA THR HIS GLN LEU ARG LEU GLY ARG GLY          
SEQRES   9 B  371  SER PHE GLY GLU VAL HIS ARG MET GLU ASP LYS GLN THR          
SEQRES  10 B  371  GLY PHE GLN CYS ALA VAL LYS LYS VAL ARG LEU GLU VAL          
SEQRES  11 B  371  PHE ARG ALA GLU GLU LEU MET ALA CYS ALA GLY LEU THR          
SEQRES  12 B  371  SER PRO ARG ILE VAL PRO LEU TYR GLY ALA VAL ARG GLU          
SEQRES  13 B  371  GLY PRO TRP VAL ASN ILE PHE MET GLU LEU LEU GLU GLY          
SEQRES  14 B  371  GLY SER LEU GLY GLN LEU VAL LYS GLU GLN GLY CYS LEU          
SEQRES  15 B  371  PRO GLU ASP ARG ALA LEU TYR TYR LEU GLY GLN ALA LEU          
SEQRES  16 B  371  GLU GLY LEU GLU TYR LEU HIS SER ARG ARG ILE LEU HIS          
SEQRES  17 B  371  GLY ASP VAL LYS ALA ASP ASN VAL LEU LEU SER SER ASP          
SEQRES  18 B  371  GLY SER HIS ALA ALA LEU CYS ASP PHE GLY HIS ALA VAL          
SEQRES  19 B  371  CYS LEU GLN PRO ASP GLY LEU GLY LYS SER LEU LEU THR          
SEQRES  20 B  371  GLY ASP TYR ILE PRO GLY THR GLU THR HIS MET ALA PRO          
SEQRES  21 B  371  GLU VAL VAL LEU GLY ARG SER CYS ASP ALA LYS VAL ASP          
SEQRES  22 B  371  VAL TRP SER SER CYS CYS MET MET LEU HIS MET LEU ASN          
SEQRES  23 B  371  GLY CYS HIS PRO TRP THR GLN PHE PHE ARG GLY PRO LEU          
SEQRES  24 B  371  CYS LEU LYS ILE ALA SER GLU PRO PRO PRO VAL ARG GLU          
SEQRES  25 B  371  ILE PRO PRO SER CYS ALA PRO LEU THR ALA GLN ALA ILE          
SEQRES  26 B  371  GLN GLU GLY LEU ARG LYS GLU PRO ILE HIS ARG VAL SER          
SEQRES  27 B  371  ALA ALA GLU LEU GLY GLY LYS VAL ASN ARG ALA LEU GLN          
SEQRES  28 B  371  GLN VAL GLY GLY LEU LYS SER PRO TRP ARG GLY GLU TYR          
SEQRES  29 B  371  LYS GLU PRO ARG GLY ASN SER                                  
SEQRES   1 D  371  GLY SER ASP SER PRO LYS PRO LEU PRO GLY PRO HIS LEU          
SEQRES   2 D  371  GLU PRO SER CYS LEU SER ARG GLY ALA HIS GLU LYS PHE          
SEQRES   3 D  371  SER VAL GLU GLU TYR LEU VAL HIS ALA LEU GLN GLY SER          
SEQRES   4 D  371  VAL SER SER GLY GLN ALA HIS SER LEU THR SER LEU ALA          
SEQRES   5 D  371  LYS THR TRP ALA ALA ARG GLY SER ARG SER ARG GLU PRO          
SEQRES   6 D  371  SER PRO LYS THR GLU ASP ASN GLU GLY VAL LEU LEU THR          
SEQRES   7 D  371  GLU LYS LEU LYS PRO VAL ASP TYR GLU TYR ARG GLU GLU          
SEQRES   8 D  371  VAL HIS TRP ALA THR HIS GLN LEU ARG LEU GLY ARG GLY          
SEQRES   9 D  371  SER PHE GLY GLU VAL HIS ARG MET GLU ASP LYS GLN THR          
SEQRES  10 D  371  GLY PHE GLN CYS ALA VAL LYS LYS VAL ARG LEU GLU VAL          
SEQRES  11 D  371  PHE ARG ALA GLU GLU LEU MET ALA CYS ALA GLY LEU THR          
SEQRES  12 D  371  SER PRO ARG ILE VAL PRO LEU TYR GLY ALA VAL ARG GLU          
SEQRES  13 D  371  GLY PRO TRP VAL ASN ILE PHE MET GLU LEU LEU GLU GLY          
SEQRES  14 D  371  GLY SER LEU GLY GLN LEU VAL LYS GLU GLN GLY CYS LEU          
SEQRES  15 D  371  PRO GLU ASP ARG ALA LEU TYR TYR LEU GLY GLN ALA LEU          
SEQRES  16 D  371  GLU GLY LEU GLU TYR LEU HIS SER ARG ARG ILE LEU HIS          
SEQRES  17 D  371  GLY ASP VAL LYS ALA ASP ASN VAL LEU LEU SER SER ASP          
SEQRES  18 D  371  GLY SER HIS ALA ALA LEU CYS ASP PHE GLY HIS ALA VAL          
SEQRES  19 D  371  CYS LEU GLN PRO ASP GLY LEU GLY LYS SER LEU LEU THR          
SEQRES  20 D  371  GLY ASP TYR ILE PRO GLY THR GLU THR HIS MET ALA PRO          
SEQRES  21 D  371  GLU VAL VAL LEU GLY ARG SER CYS ASP ALA LYS VAL ASP          
SEQRES  22 D  371  VAL TRP SER SER CYS CYS MET MET LEU HIS MET LEU ASN          
SEQRES  23 D  371  GLY CYS HIS PRO TRP THR GLN PHE PHE ARG GLY PRO LEU          
SEQRES  24 D  371  CYS LEU LYS ILE ALA SER GLU PRO PRO PRO VAL ARG GLU          
SEQRES  25 D  371  ILE PRO PRO SER CYS ALA PRO LEU THR ALA GLN ALA ILE          
SEQRES  26 D  371  GLN GLU GLY LEU ARG LYS GLU PRO ILE HIS ARG VAL SER          
SEQRES  27 D  371  ALA ALA GLU LEU GLY GLY LYS VAL ASN ARG ALA LEU GLN          
SEQRES  28 D  371  GLN VAL GLY GLY LEU LYS SER PRO TRP ARG GLY GLU TYR          
SEQRES  29 D  371  LYS GLU PRO ARG GLY ASN SER                                  
SEQRES   1 E  371  GLY SER ASP SER PRO LYS PRO LEU PRO GLY PRO HIS LEU          
SEQRES   2 E  371  GLU PRO SER CYS LEU SER ARG GLY ALA HIS GLU LYS PHE          
SEQRES   3 E  371  SER VAL GLU GLU TYR LEU VAL HIS ALA LEU GLN GLY SER          
SEQRES   4 E  371  VAL SER SER GLY GLN ALA HIS SER LEU THR SER LEU ALA          
SEQRES   5 E  371  LYS THR TRP ALA ALA ARG GLY SER ARG SER ARG GLU PRO          
SEQRES   6 E  371  SER PRO LYS THR GLU ASP ASN GLU GLY VAL LEU LEU THR          
SEQRES   7 E  371  GLU LYS LEU LYS PRO VAL ASP TYR GLU TYR ARG GLU GLU          
SEQRES   8 E  371  VAL HIS TRP ALA THR HIS GLN LEU ARG LEU GLY ARG GLY          
SEQRES   9 E  371  SER PHE GLY GLU VAL HIS ARG MET GLU ASP LYS GLN THR          
SEQRES  10 E  371  GLY PHE GLN CYS ALA VAL LYS LYS VAL ARG LEU GLU VAL          
SEQRES  11 E  371  PHE ARG ALA GLU GLU LEU MET ALA CYS ALA GLY LEU THR          
SEQRES  12 E  371  SER PRO ARG ILE VAL PRO LEU TYR GLY ALA VAL ARG GLU          
SEQRES  13 E  371  GLY PRO TRP VAL ASN ILE PHE MET GLU LEU LEU GLU GLY          
SEQRES  14 E  371  GLY SER LEU GLY GLN LEU VAL LYS GLU GLN GLY CYS LEU          
SEQRES  15 E  371  PRO GLU ASP ARG ALA LEU TYR TYR LEU GLY GLN ALA LEU          
SEQRES  16 E  371  GLU GLY LEU GLU TYR LEU HIS SER ARG ARG ILE LEU HIS          
SEQRES  17 E  371  GLY ASP VAL LYS ALA ASP ASN VAL LEU LEU SER SER ASP          
SEQRES  18 E  371  GLY SER HIS ALA ALA LEU CYS ASP PHE GLY HIS ALA VAL          
SEQRES  19 E  371  CYS LEU GLN PRO ASP GLY LEU GLY LYS SER LEU LEU THR          
SEQRES  20 E  371  GLY ASP TYR ILE PRO GLY THR GLU THR HIS MET ALA PRO          
SEQRES  21 E  371  GLU VAL VAL LEU GLY ARG SER CYS ASP ALA LYS VAL ASP          
SEQRES  22 E  371  VAL TRP SER SER CYS CYS MET MET LEU HIS MET LEU ASN          
SEQRES  23 E  371  GLY CYS HIS PRO TRP THR GLN PHE PHE ARG GLY PRO LEU          
SEQRES  24 E  371  CYS LEU LYS ILE ALA SER GLU PRO PRO PRO VAL ARG GLU          
SEQRES  25 E  371  ILE PRO PRO SER CYS ALA PRO LEU THR ALA GLN ALA ILE          
SEQRES  26 E  371  GLN GLU GLY LEU ARG LYS GLU PRO ILE HIS ARG VAL SER          
SEQRES  27 E  371  ALA ALA GLU LEU GLY GLY LYS VAL ASN ARG ALA LEU GLN          
SEQRES  28 E  371  GLN VAL GLY GLY LEU LYS SER PRO TRP ARG GLY GLU TYR          
SEQRES  29 E  371  LYS GLU PRO ARG GLY ASN SER                                  
HET     MG  A 701       1                                                       
HET     MG  D 701       1                                                       
HET     MG  E 701       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   5   MG    3(MG 2+)                                                     
FORMUL   8  HOH   *18(H2 O)                                                     
HELIX    1   1 SER A  332  GLN A  342  1                                  11    
HELIX    2   2 GLN A  349  ALA A  361  1                                  13    
HELIX    3   3 ALA A  438  ALA A  443  1                                   6    
HELIX    4   4 SER A  476  GLN A  484  1                                   9    
HELIX    5   5 PRO A  488  ARG A  509  1                                  22    
HELIX    6   6 LYS A  517  ASP A  519  5                                   3    
HELIX    7   7 THR A  559  MET A  563  5                                   5    
HELIX    8   8 ALA A  564  LEU A  569  1                                   6    
HELIX    9   9 ALA A  575  GLY A  592  1                                  18    
HELIX   10  10 PRO A  603  GLU A  611  1                                   9    
HELIX   11  11 PRO A  613  ILE A  618  5                                   6    
HELIX   12  12 ALA A  623  LEU A  634  1                                  12    
HELIX   13  13 SER A  643  VAL A  658  1                                  16    
HELIX   14  14 LEU B  337  GLN B  342  1                                   6    
HELIX   15  15 GLN B  349  ALA B  361  1                                  13    
HELIX   16  16 ALA B  438  ALA B  443  1                                   6    
HELIX   17  17 SER B  476  GLN B  484  1                                   9    
HELIX   18  18 PRO B  488  ARG B  509  1                                  22    
HELIX   19  19 LYS B  517  ASP B  519  5                                   3    
HELIX   20  20 THR B  559  MET B  563  5                                   5    
HELIX   21  21 ALA B  564  LEU B  569  1                                   6    
HELIX   22  22 ALA B  575  GLY B  592  1                                  18    
HELIX   23  23 PRO B  603  GLU B  611  1                                   9    
HELIX   24  24 PRO B  613  ILE B  618  5                                   6    
HELIX   25  25 ALA B  623  LEU B  634  1                                  12    
HELIX   26  26 SER B  643  VAL B  658  1                                  16    
HELIX   27  27 GLN D  349  ALA D  361  1                                  13    
HELIX   28  28 ALA D  438  ALA D  443  1                                   6    
HELIX   29  29 SER D  476  GLN D  484  1                                   9    
HELIX   30  30 PRO D  488  SER D  508  1                                  21    
HELIX   31  31 LYS D  517  ASP D  519  5                                   3    
HELIX   32  32 ALA D  564  GLY D  570  1                                   7    
HELIX   33  33 ALA D  575  GLY D  592  1                                  18    
HELIX   34  34 LEU D  604  GLU D  611  1                                   8    
HELIX   35  35 PRO D  613  ILE D  618  5                                   6    
HELIX   36  36 ALA D  623  LEU D  634  1                                  12    
HELIX   37  37 SER D  643  GLN D  657  1                                  15    
HELIX   38  38 TYR E  336  GLN E  342  1                                   7    
HELIX   39  39 GLN E  349  ALA E  361  1                                  13    
HELIX   40  40 ALA E  438  ALA E  443  1                                   6    
HELIX   41  41 SER E  476  GLN E  484  1                                   9    
HELIX   42  42 PRO E  488  ARG E  509  1                                  22    
HELIX   43  43 LYS E  517  ASP E  519  5                                   3    
HELIX   44  44 ALA E  564  LEU E  569  1                                   6    
HELIX   45  45 ALA E  575  GLY E  592  1                                  18    
HELIX   46  46 PRO E  613  ILE E  618  5                                   6    
HELIX   47  47 ALA E  623  LEU E  634  1                                  12    
HELIX   48  48 SER E  643  VAL E  658  1                                  16    
SHEET    1   A 7 VAL A 345  SER A 347  0                                        
SHEET    2   A 7 ASN A 377  LEU A 381  1  O  GLY A 379   N  SER A 346           
SHEET    3   A 7 LEU A 455  GLU A 461 -1  O  ARG A 460   N  GLU A 378           
SHEET    4   A 7 TRP A 464  MET A 469 -1  O  ASN A 466   N  VAL A 459           
SHEET    5   A 7 GLN A 425  ARG A 432 -1  N  VAL A 431   O  VAL A 465           
SHEET    6   A 7 VAL A 414  ASP A 419 -1  N  MET A 417   O  CYS A 426           
SHEET    7   A 7 TRP A 399  THR A 401 -1  N  ALA A 400   O  GLU A 418           
SHEET    1   B 2 ILE A 511  LEU A 512  0                                        
SHEET    2   B 2 VAL A 539  CYS A 540 -1  O  VAL A 539   N  LEU A 512           
SHEET    1   C 2 VAL A 521  LEU A 523  0                                        
SHEET    2   C 2 ALA A 530  LEU A 532 -1  O  ALA A 531   N  LEU A 522           
SHEET    1   D 7 VAL B 345  SER B 347  0                                        
SHEET    2   D 7 ASN B 377  LEU B 381  1  O  LEU B 381   N  SER B 346           
SHEET    3   D 7 LEU B 455  GLU B 461 -1  O  ARG B 460   N  GLU B 378           
SHEET    4   D 7 TRP B 464  MET B 469 -1  O  PHE B 468   N  GLY B 457           
SHEET    5   D 7 GLN B 425  ARG B 432 -1  N  LYS B 429   O  ILE B 467           
SHEET    6   D 7 VAL B 414  ASP B 419 -1  N  MET B 417   O  CYS B 426           
SHEET    7   D 7 TRP B 399  THR B 401 -1  N  ALA B 400   O  GLU B 418           
SHEET    1   E 2 ILE B 511  LEU B 512  0                                        
SHEET    2   E 2 VAL B 539  CYS B 540 -1  O  VAL B 539   N  LEU B 512           
SHEET    1   F 2 VAL B 521  LEU B 523  0                                        
SHEET    2   F 2 ALA B 530  LEU B 532 -1  O  ALA B 531   N  LEU B 522           
SHEET    1   G 7 VAL D 345  SER D 347  0                                        
SHEET    2   G 7 ASN D 377  LEU D 381  1  O  LEU D 381   N  SER D 346           
SHEET    3   G 7 LEU D 455  GLU D 461 -1  O  ARG D 460   N  GLU D 378           
SHEET    4   G 7 TRP D 464  MET D 469 -1  O  PHE D 468   N  GLY D 457           
SHEET    5   G 7 GLN D 425  ARG D 432 -1  N  LYS D 429   O  ILE D 467           
SHEET    6   G 7 VAL D 414  ASP D 419 -1  N  HIS D 415   O  VAL D 428           
SHEET    7   G 7 TRP D 399  THR D 401 -1  N  ALA D 400   O  GLU D 418           
SHEET    1   H 2 ILE D 511  LEU D 512  0                                        
SHEET    2   H 2 VAL D 539  CYS D 540 -1  O  VAL D 539   N  LEU D 512           
SHEET    1   I 2 VAL D 521  LEU D 523  0                                        
SHEET    2   I 2 ALA D 530  LEU D 532 -1  O  ALA D 531   N  LEU D 522           
SHEET    1   J 7 VAL E 345  SER E 347  0                                        
SHEET    2   J 7 ASN E 377  LEU E 381  1  O  GLY E 379   N  SER E 346           
SHEET    3   J 7 LEU E 455  GLU E 461 -1  O  ARG E 460   N  GLU E 378           
SHEET    4   J 7 TRP E 464  MET E 469 -1  O  PHE E 468   N  GLY E 457           
SHEET    5   J 7 GLN E 425  ARG E 432 -1  N  VAL E 431   O  VAL E 465           
SHEET    6   J 7 VAL E 414  ASP E 419 -1  N  MET E 417   O  CYS E 426           
SHEET    7   J 7 TRP E 399  THR E 401 -1  N  ALA E 400   O  GLU E 418           
SHEET    1   K 2 ILE E 511  LEU E 512  0                                        
SHEET    2   K 2 VAL E 539  CYS E 540 -1  O  VAL E 539   N  LEU E 512           
SHEET    1   L 2 VAL E 521  LEU E 523  0                                        
SHEET    2   L 2 ALA E 530  LEU E 532 -1  O  ALA E 531   N  LEU E 522           
LINK         OD2 ASP D 534                MG    MG D 701     1555   1555  2.52  
LINK         OD1 ASN A 520                MG    MG A 701     1555   1555  2.52  
LINK         OD1 ASN D 520                MG    MG D 701     1555   1555  2.73  
LINK         OD2 ASP E 534                MG    MG E 701     1555   1555  2.99  
LINK         OD2 ASP A 534                MG    MG A 701     1555   1555  3.00  
SITE     1 AC1  3 ASN A 520  ASP A 534  HOH A 805                               
SITE     1 AC2  3 SER D 410  ASN D 520  ASP D 534                               
SITE     1 AC3  2 ASN E 520  ASP E 534                                          
CRYST1   45.746  145.851  230.818  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      0.021860  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006856  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004332        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  0.998665  0.045220  0.024954       -8.16074    1                    
MTRIX2   2 -0.017572  0.751816 -0.659138        5.40880    1                    
MTRIX3   2 -0.048567  0.657820  0.751608      -23.18439    1                    
MTRIX1   3 -0.988703  0.130267 -0.074143       43.43270    1                    
MTRIX2   3 -0.065251  0.071258  0.995321      -78.60721    1                    
MTRIX3   3  0.134941  0.988915 -0.061953       38.17986    1                    
MTRIX1   4 -0.993738  0.073280  0.084353       37.34609    1                    
MTRIX2   4 -0.007207  0.711314 -0.702838       40.64146    1                    
MTRIX3   4 -0.111505 -0.699044 -0.706331      160.30974    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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