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Database: PDB
Entry: 6J7W
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HEADER    IMMUNE SYSTEM                           18-JAN-19   6J7W              
TITLE     CRYSTAL STRUCTURE OF HUMAN BCMA IN COMPLEX WITH UNIAB(TM) VH          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UNIAB;                                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 OTHER_DETAILS: HEAVY CHAIN ANTIBODY;                                 
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 17;      
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 SYNONYM: B-CELL MATURATION PROTEIN;                                  
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 OTHER_DETAILS: HUMAN B-CELL MATURATION ANTIGEN                       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: HEK 293;                                
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: BCMA;                                                          
SOURCE  13 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  15 EXPRESSION_SYSTEM_CELL_LINE: HEK 293                                 
KEYWDS    HEAVY CHAIN ANTIBODIES, VH DOMAINS, DOMAIN ANTIBODIES, IMMUNE SYSTEM  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.C.CLARKE,B.MA,N.D.TRINKLEIN,U.SCHELLENBERGER,M.OSBORN,L.OUISSE,     
AUTHOR   2 A.BOUDREAU,L.DAVISON,K.E.HARRIS,H.UGAMRAJ,A.BALASUBRAMANI,K.DANG,    
AUTHOR   3 B.JORGENSEN,H.OGANA,D.PHAM,P.PRATAP,P.SANKARAN,I.ANEGON,W.VAN        
AUTHOR   4 SCHOOTEN,M.BRUGGEMANN,R.BUELOW,S.FORCE ALDRED                        
REVDAT   1   06-FEB-19 6J7W    0                                                
JRNL        AUTH   S.C.CLARKE,B.MA,N.D.TRINKLEIN,U.SCHELLENBERGER,M.J.OSBORN,   
JRNL        AUTH 2 L.H.OUISSE,A.BOUDREAU,L.M.DAVISON,K.E.HARRIS,H.S.UGAMRAJ,    
JRNL        AUTH 3 A.BALASUBRAMANI,K.H.DANG,B.JORGENSEN,H.A.N.OGANA,D.T.PHAM,   
JRNL        AUTH 4 P.P.PRATAP,P.SANKARAN,I.ANEGON,W.C.VAN SCHOOTEN,             
JRNL        AUTH 5 M.BRUGGEMANN,R.BUELOW,S.FORCE ALDRED                         
JRNL        TITL   MULTISPECIFIC ANTIBODY DEVELOPMENT PLATFORM BASED ON HUMAN   
JRNL        TITL 2 HEAVY CHAIN ANTIBODIES                                       
JRNL        REF    FRONT IMMUNOL                 V.   9  3037 2018              
JRNL        REFN                   ESSN 1664-3224                               
JRNL        PMID   30666250                                                     
JRNL        DOI    10.3389/FIMMU.2018.03037                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0230                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 9739                           
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) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 514                             
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 701                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2790                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 32                           
REMARK   3   BIN FREE R VALUE                    : 0.3860                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2311                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 34                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.68000                                             
REMARK   3    B22 (A**2) : 0.90000                                              
REMARK   3    B33 (A**2) : 1.78000                                              
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): 1.410         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.352         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.278         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.200        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2365 ; 0.009 ; 0.014       
REMARK   3   BOND LENGTHS OTHERS               (A):  1963 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3210 ; 1.350 ; 1.654       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4621 ; 0.868 ; 1.644       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   307 ; 7.555 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   119 ;31.997 ;21.933       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   354 ;20.844 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;17.815 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   299 ; 0.063 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2743 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   445 ; 0.001 ; 0.020       
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   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 6J7W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JAN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300010532.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-DEC-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : POINTLESS                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10364                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.590                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.990                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.59                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3ZHK, 4ZFO                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM MALONATE PH 4.0 AND 20%      
REMARK 280  PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
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   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.74550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.74550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       32.69600            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       36.90300            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       32.69600            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       36.90300            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       66.74550            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       32.69600            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       36.90300            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       66.74550            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       32.69600            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       36.90300            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7870 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7500 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASN D    41                                                      
REMARK 465     ALA D    42                                                      
REMARK 465     SER D    43                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  65    CG   CD   CE   NZ                                   
REMARK 470     ASN C  30    CG   OD1  ND2                                       
REMARK 470     ARG C  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  65    CG   CD   CE   NZ                                   
REMARK 470     ARG B  87    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN D   6    CG   CD   OE1  NE2                                  
REMARK 470     GLN D   9    CG   CD   OE1  NE2                                  
REMARK 470     ASN D  30    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP B    55     OG   SER B    57              2.14            
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    VAL A  48      -53.37   -137.09                                   
REMARK 500    SER A  63        0.01    -64.83                                   
REMARK 500    VAL A  64      -16.96   -145.63                                   
REMARK 500    CYS C  36       67.46   -106.06                                   
REMARK 500    VAL B  48      -44.08   -136.55                                   
REMARK 500    VAL B  64      -13.03   -142.33                                   
REMARK 500    GLN D  24      -38.93    -38.38                                   
REMARK 500    THR D  35       -1.95    -58.74                                   
REMARK 500    CYS D  36       50.85   -142.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6J7W A    1   118  PDB    6J7W     6J7W             1    118             
DBREF  6J7W C    5    43  UNP    Q02223   TNR17_HUMAN      6     44             
DBREF  6J7W B    1   118  PDB    6J7W     6J7W             1    118             
DBREF  6J7W D    5    43  UNP    Q02223   TNR17_HUMAN      6     44             
SEQRES   1 A  118  GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 A  118  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 A  118  PHE THR VAL SER SER TYR GLY MET SER TRP VAL ARG GLN          
SEQRES   4 A  118  ALA PRO GLY LYS GLY PRO GLU TRP VAL SER GLY ILE ARG          
SEQRES   5 A  118  GLY SER ASP GLY SER THR TYR TYR ALA ASP SER VAL LYS          
SEQRES   6 A  118  GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR          
SEQRES   7 A  118  LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR          
SEQRES   8 A  118  ALA VAL TYR TYR CYS ALA LYS GLN GLY GLU ASN ASP GLY          
SEQRES   9 A  118  PRO PHE ASP HIS ARG GLY GLN GLY THR LEU VAL THR VAL          
SEQRES  10 A  118  SER                                                          
SEQRES   1 C   39  GLY GLN CYS SER GLN ASN GLU TYR PHE ASP SER LEU LEU          
SEQRES   2 C   39  HIS ALA CYS ILE PRO CYS GLN LEU ARG CYS SER SER ASN          
SEQRES   3 C   39  THR PRO PRO LEU THR CYS GLN ARG TYR CYS ASN ALA SER          
SEQRES   1 B  118  GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 B  118  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 B  118  PHE THR VAL SER SER TYR GLY MET SER TRP VAL ARG GLN          
SEQRES   4 B  118  ALA PRO GLY LYS GLY PRO GLU TRP VAL SER GLY ILE ARG          
SEQRES   5 B  118  GLY SER ASP GLY SER THR TYR TYR ALA ASP SER VAL LYS          
SEQRES   6 B  118  GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR          
SEQRES   7 B  118  LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR          
SEQRES   8 B  118  ALA VAL TYR TYR CYS ALA LYS GLN GLY GLU ASN ASP GLY          
SEQRES   9 B  118  PRO PHE ASP HIS ARG GLY GLN GLY THR LEU VAL THR VAL          
SEQRES  10 B  118  SER                                                          
SEQRES   1 D   39  GLY GLN CYS SER GLN ASN GLU TYR PHE ASP SER LEU LEU          
SEQRES   2 D   39  HIS ALA CYS ILE PRO CYS GLN LEU ARG CYS SER SER ASN          
SEQRES   3 D   39  THR PRO PRO LEU THR CYS GLN ARG TYR CYS ASN ALA SER          
FORMUL   5  HOH   *34(H2 O)                                                     
HELIX    1 AA1 THR A   28  TYR A   32  5                                   5    
HELIX    2 AA2 ARG A   87  THR A   91  5                                   5    
HELIX    3 AA3 CYS C   23  SER C   28  1                                   6    
HELIX    4 AA4 THR B   28  TYR B   32  5                                   5    
HELIX    5 AA5 ARG B   87  THR B   91  5                                   5    
HELIX    6 AA6 GLN D   24  ARG D   26  5                                   3    
HELIX    7 AA7 PRO D   33  GLN D   37  5                                   5    
SHEET    1 AA1 4 GLN A   3  SER A   7  0                                        
SHEET    2 AA1 4 LEU A  18  SER A  25 -1  O  SER A  21   N  SER A   7           
SHEET    3 AA1 4 THR A  78  MET A  83 -1  O  MET A  83   N  LEU A  18           
SHEET    4 AA1 4 PHE A  68  ASP A  73 -1  N  THR A  69   O  GLN A  82           
SHEET    1 AA2 6 GLY A  10  VAL A  12  0                                        
SHEET    2 AA2 6 THR A 113  VAL A 117  1  O  THR A 116   N  GLY A  10           
SHEET    3 AA2 6 ALA A  92  GLN A  99 -1  N  TYR A  94   O  THR A 113           
SHEET    4 AA2 6 MET A  34  GLN A  39 -1  N  VAL A  37   O  TYR A  95           
SHEET    5 AA2 6 GLU A  46  ILE A  51 -1  O  ILE A  51   N  MET A  34           
SHEET    6 AA2 6 THR A  58  TYR A  60 -1  O  TYR A  59   N  GLY A  50           
SHEET    1 AA3 4 GLY A  10  VAL A  12  0                                        
SHEET    2 AA3 4 THR A 113  VAL A 117  1  O  THR A 116   N  GLY A  10           
SHEET    3 AA3 4 ALA A  92  GLN A  99 -1  N  TYR A  94   O  THR A 113           
SHEET    4 AA3 4 PHE A 106  ARG A 109 -1  O  ASP A 107   N  LYS A  98           
SHEET    1 AA4 2 GLU C  11  ASP C  14  0                                        
SHEET    2 AA4 2 ALA C  19  PRO C  22 -1  O  ALA C  19   N  ASP C  14           
SHEET    1 AA5 4 GLN B   3  SER B   7  0                                        
SHEET    2 AA5 4 LEU B  18  SER B  25 -1  O  SER B  21   N  SER B   7           
SHEET    3 AA5 4 THR B  78  MET B  83 -1  O  MET B  83   N  LEU B  18           
SHEET    4 AA5 4 PHE B  68  ASP B  73 -1  N  THR B  69   O  GLN B  82           
SHEET    1 AA6 6 GLY B  10  VAL B  12  0                                        
SHEET    2 AA6 6 THR B 113  VAL B 117  1  O  THR B 116   N  GLY B  10           
SHEET    3 AA6 6 ALA B  92  GLN B  99 -1  N  TYR B  94   O  THR B 113           
SHEET    4 AA6 6 MET B  34  GLN B  39 -1  N  VAL B  37   O  TYR B  95           
SHEET    5 AA6 6 GLU B  46  ILE B  51 -1  O  ILE B  51   N  MET B  34           
SHEET    6 AA6 6 THR B  58  TYR B  60 -1  O  TYR B  59   N  GLY B  50           
SHEET    1 AA7 4 GLY B  10  VAL B  12  0                                        
SHEET    2 AA7 4 THR B 113  VAL B 117  1  O  THR B 116   N  GLY B  10           
SHEET    3 AA7 4 ALA B  92  GLN B  99 -1  N  TYR B  94   O  THR B 113           
SHEET    4 AA7 4 PHE B 106  ARG B 109 -1  O  ASP B 107   N  LYS B  98           
SHEET    1 AA8 2 GLU D  11  ASP D  14  0                                        
SHEET    2 AA8 2 ALA D  19  PRO D  22 -1  O  ILE D  21   N  TYR D  12           
SSBOND   1 CYS A   22    CYS A   96                          1555   1555  2.04  
SSBOND   2 CYS C    7    CYS C   20                          1555   1555  1.90  
SSBOND   3 CYS C   23    CYS C   36                          1555   1555  2.04  
SSBOND   4 CYS C   27    CYS C   40                          1555   1555  2.03  
SSBOND   5 CYS B   22    CYS B   96                          1555   1555  2.03  
SSBOND   6 CYS D    7    CYS D   20                          1555   1555  2.02  
SSBOND   7 CYS D   23    CYS D   36                          1555   1555  1.92  
SSBOND   8 CYS D   27    CYS D   40                          1555   1555  2.03  
CRYST1   65.392   73.806  133.491  90.00  90.00  90.00 C 2 2 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      0.015292  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013549  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007491        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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