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Database: PDB
Entry: 6FAX
LinkDB: 6FAX
Original site: 6FAX 
HEADER    IMMUNE SYSTEM                           18-DEC-17   6FAX              
TITLE     COMPLEX OF HUMAN CD40 ECTODOMAIN WITH LOB 7.4 FAB                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LOB 7.4 LIGHT CHAIN;                                       
COMPND   3 CHAIN: L;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: LOB 7.4 HEAVY CHAIN;                                       
COMPND   7 CHAIN: H;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: RESIDUES 141 - 146 NOT VISIBLE IN ELECTRON DENSITY.   
COMPND  10 PRE CRYSTALLISATION, CONSTRUCT WAS TREATED WITH PEPSIN, EXPECTED     
COMPND  11 CLEAVAGE SITE ~ RESIDUE 240. RESIDUES 227 ONWARDS ARE NOT VISIBLE IN 
COMPND  12 THE ELECTRON DENSITY.;                                               
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 5;       
COMPND  15 CHAIN: R;                                                            
COMPND  16 SYNONYM: B-CELL SURFACE ANTIGEN CD40,BP50,CD40L RECEPTOR,CDW40;      
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 OTHER_DETAILS: RESIDUES 1 - 20 ARE POST-TRANSLATIONALLY CLEAVED.     
COMPND  19 RESIDUES 124 - 194 ARE NOT VISIBLE IN THE ELECTRON DENSITY           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   6 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  12 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 GENE: CD40, TNFRSF5;                                                 
SOURCE  18 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  20 EXPRESSION_SYSTEM_CELL_LINE: HEK293                                  
KEYWDS    CD40, ENGINEERED FAB, AGONIST, MAB, IMMUNE SYSTEM                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.M.ORR,I.TEWS,A.R.PEARSON                                            
REVDAT   3   18-APR-18 6FAX    1       JRNL                                     
REVDAT   2   04-APR-18 6FAX    1       JRNL                                     
REVDAT   1   07-FEB-18 6FAX    0                                                
JRNL        AUTH   X.YU,H.T.C.CHAN,C.M.ORR,O.DADAS,S.G.BOOTH,L.N.DAHAL,         
JRNL        AUTH 2 C.A.PENFOLD,L.O'BRIEN,C.I.MOCKRIDGE,R.R.FRENCH,P.DURIEZ,     
JRNL        AUTH 3 L.R.DOUGLAS,A.R.PEARSON,M.S.CRAGG,I.TEWS,M.J.GLENNIE,        
JRNL        AUTH 4 A.L.WHITE                                                    
JRNL        TITL   COMPLEX INTERPLAY BETWEEN EPITOPE SPECIFICITY AND ISOTYPE    
JRNL        TITL 2 DICTATES THE BIOLOGICAL ACTIVITY OF ANTI-HUMAN CD40          
JRNL        TITL 3 ANTIBODIES.                                                  
JRNL        REF    CANCER CELL                   V.  33   664 2018              
JRNL        REFN                   ISSN 1878-3686                               
JRNL        PMID   29576376                                                     
JRNL        DOI    10.1016/J.CCELL.2018.02.009                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.99 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
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) : 2.99                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 137.48                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 26355                          
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) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1319                            
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) : 2.99                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.07                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1866                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 78                           
REMARK   3   BIN FREE R VALUE                    : 0.3900                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4057                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 21                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 84.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.59000                                              
REMARK   3    B22 (A**2) : 2.59000                                              
REMARK   3    B33 (A**2) : -8.41000                                             
REMARK   3    B12 (A**2) : 1.30000                                              
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): 0.359         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.277         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.235         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.084        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4166 ; 0.018 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  3642 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5668 ; 2.134 ; 1.948       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8546 ; 1.154 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   529 ;10.747 ; 5.076       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   172 ;41.454 ;25.116       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   682 ;20.700 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;18.582 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   636 ; 0.108 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4606 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   794 ; 0.002 ; 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):  2109 ; 7.148 ; 8.425       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2108 ; 7.135 ; 8.422       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2631 ;10.217 ;12.623       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2632 ;10.215 ;12.627       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2057 ; 8.250 ; 8.932       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2058 ; 8.250 ; 8.935       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3038 ;11.561 ;13.140       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4385 ;14.058 ;96.602       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4386 ;14.057 ;96.628       
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                                                           
REMARK   4                                                                      
REMARK   4 6FAX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200001230.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-APR-15; 05-APR-15               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : ESRF; ESRF                         
REMARK 200  BEAMLINE                       : ID23-1; ID23-1                     
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976254; 0.969995                 
REMARK 200  MONOCHROMATOR                  : SI111; SI111                       
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL; PIXEL                       
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F; DECTRIS      
REMARK 200                                   PILATUS 6M-F                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2 0.4.0.338-G7E19E23-DIALS      
REMARK 200                                   -1.2                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.27                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27589                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.990                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 52.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 13.70                              
REMARK 200  R MERGE                    (I) : 0.16100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.99                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1U6A                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NA, VAPOR DIFFUSION, SITTING DROP,       
REMARK 280  TEMPERATURE 293K. NA, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE    
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       31.20733            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       62.41467            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       62.41467            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       31.20733            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, R                               
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 L   212                                                      
REMARK 465     GLU L   213                                                      
REMARK 465     CYS L   214                                                      
REMARK 465     SER H   137                                                      
REMARK 465     LYS H   138                                                      
REMARK 465     SER H   139                                                      
REMARK 465     THR H   140                                                      
REMARK 465     SER H   141                                                      
REMARK 465     GLY H   142                                                      
REMARK 465     GLY H   143                                                      
REMARK 465     CYS H   224                                                      
REMARK 465     CYS H   225                                                      
REMARK 465     ASP H   226                                                      
REMARK 465     LYS H   227                                                      
REMARK 465     THR H   228                                                      
REMARK 465     HIS H   229                                                      
REMARK 465     THR H   230                                                      
REMARK 465     CYS H   231                                                      
REMARK 465     PRO H   232                                                      
REMARK 465     PRO H   233                                                      
REMARK 465     CYS H   234                                                      
REMARK 465     PRO H   235                                                      
REMARK 465     ALA H   236                                                      
REMARK 465     PRO H   237                                                      
REMARK 465     GLU H   238                                                      
REMARK 465     LEU H   239                                                      
REMARK 465     LEU H   240                                                      
REMARK 465     LEU R   121                                                      
REMARK 465     HIS R   122                                                      
REMARK 465     ARG R   123                                                      
REMARK 465     SER R   124                                                      
REMARK 465     CYS R   125                                                      
REMARK 465     SER R   126                                                      
REMARK 465     PRO R   127                                                      
REMARK 465     GLY R   128                                                      
REMARK 465     PHE R   129                                                      
REMARK 465     GLY R   130                                                      
REMARK 465     VAL R   131                                                      
REMARK 465     LYS R   132                                                      
REMARK 465     GLN R   133                                                      
REMARK 465     ILE R   134                                                      
REMARK 465     ALA R   135                                                      
REMARK 465     THR R   136                                                      
REMARK 465     GLY R   137                                                      
REMARK 465     VAL R   138                                                      
REMARK 465     SER R   139                                                      
REMARK 465     ASP R   140                                                      
REMARK 465     THR R   141                                                      
REMARK 465     ILE R   142                                                      
REMARK 465     CYS R   143                                                      
REMARK 465     GLU R   144                                                      
REMARK 465     PRO R   145                                                      
REMARK 465     CYS R   146                                                      
REMARK 465     PRO R   147                                                      
REMARK 465     VAL R   148                                                      
REMARK 465     GLY R   149                                                      
REMARK 465     PHE R   150                                                      
REMARK 465     PHE R   151                                                      
REMARK 465     SER R   152                                                      
REMARK 465     ASN R   153                                                      
REMARK 465     VAL R   154                                                      
REMARK 465     SER R   155                                                      
REMARK 465     SER R   156                                                      
REMARK 465     ALA R   157                                                      
REMARK 465     PHE R   158                                                      
REMARK 465     GLU R   159                                                      
REMARK 465     LYS R   160                                                      
REMARK 465     CYS R   161                                                      
REMARK 465     HIS R   162                                                      
REMARK 465     PRO R   163                                                      
REMARK 465     TRP R   164                                                      
REMARK 465     THR R   165                                                      
REMARK 465     SER R   166                                                      
REMARK 465     CYS R   167                                                      
REMARK 465     GLU R   168                                                      
REMARK 465     THR R   169                                                      
REMARK 465     LYS R   170                                                      
REMARK 465     ASP R   171                                                      
REMARK 465     LEU R   172                                                      
REMARK 465     VAL R   173                                                      
REMARK 465     VAL R   174                                                      
REMARK 465     GLN R   175                                                      
REMARK 465     GLN R   176                                                      
REMARK 465     ALA R   177                                                      
REMARK 465     GLY R   178                                                      
REMARK 465     THR R   179                                                      
REMARK 465     ASN R   180                                                      
REMARK 465     LYS R   181                                                      
REMARK 465     THR R   182                                                      
REMARK 465     ASP R   183                                                      
REMARK 465     VAL R   184                                                      
REMARK 465     VAL R   185                                                      
REMARK 465     CYS R   186                                                      
REMARK 465     GLY R   187                                                      
REMARK 465     PRO R   188                                                      
REMARK 465     GLN R   189                                                      
REMARK 465     ASP R   190                                                      
REMARK 465     ARG R   191                                                      
REMARK 465     LEU R   192                                                      
REMARK 465     ARG R   193                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG L 108   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    VAL L 110   CB  -  CA  -  C   ANGL. DEV. = -12.4 DEGREES          
REMARK 500    MET H  81   CG  -  SD  -  CE  ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    LEU H 187   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    TRP R 109   CA  -  CB  -  CG  ANGL. DEV. =  13.4 DEGREES          
REMARK 500    CYS R 111   CA  -  CB  -  SG  ANGL. DEV. =   7.8 DEGREES          
REMARK 500    CYS R 116   CA  -  CB  -  SG  ANGL. DEV. =   7.2 DEGREES          
REMARK 500    CYS R 119   CA  -  CB  -  SG  ANGL. DEV. =  10.9 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    THR L  51      -42.16     70.16                                   
REMARK 500    SER L  52       -4.62   -147.15                                   
REMARK 500    SER L  56      -81.96    -12.80                                   
REMARK 500    ASN L  77       81.52     48.08                                   
REMARK 500    LYS L 126      -38.98    -38.16                                   
REMARK 500    ASP L 151       70.66     19.68                                   
REMARK 500    ASN L 152       10.39     57.34                                   
REMARK 500    ALA L 184      -81.38    -20.75                                   
REMARK 500    PRO L 204      146.80    -38.92                                   
REMARK 500    ALA H  92      174.39    179.67                                   
REMARK 500    TYR H 106     -125.10     60.27                                   
REMARK 500    THR H 169      -40.07   -142.56                                   
REMARK 500    ASN H 213       52.96     20.19                                   
REMARK 500    ALA R  25      141.86     67.97                                   
REMARK 500    CYS R  26     -141.98   -108.54                                   
REMARK 500    LYS R  29       33.96    -90.31                                   
REMARK 500    ASN R  34     -128.29     41.91                                   
REMARK 500    THR R  57      121.61    -32.29                                   
REMARK 500    GLU R  64      -66.50     -6.79                                   
REMARK 500    ASP R 100      142.26     96.64                                   
REMARK 500    GLU R 107      -94.13    -56.31                                   
REMARK 500    CYS R 116       81.52     57.38                                   
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 CYS R   83     ASP R   84                 -149.58                    
REMARK 500 GLU R  106     GLU R  107                 -147.72                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6FAX L    1   214  PDB    6FAX     6FAX             1    214             
DBREF  6FAX H    1   240  PDB    6FAX     6FAX             1    240             
DBREF  6FAX R   21   193  UNP    P25942   TNR5_HUMAN      21    193             
SEQRES   1 L  214  ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA          
SEQRES   2 L  214  SER LEU GLY ASP ARG VAL THR ILE THR CYS SER ALA SER          
SEQRES   3 L  214  GLN GLY ILE ASN ASN TYR LEU ASN TRP TYR GLN GLN LYS          
SEQRES   4 L  214  PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER          
SEQRES   5 L  214  SER LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU          
SEQRES   7 L  214  GLU PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR          
SEQRES   8 L  214  SER ASN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 L  214  GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 L  214  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 L  214  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 L  214  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 L  214  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 L  214  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 L  214  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 L  214  PHE ASN ARG GLY GLU CYS                                      
SEQRES   1 H  240  GLU VAL GLN LEU GLN GLN SER GLY PRO ASP LEU VAL LYS          
SEQRES   2 H  240  PRO GLY ALA SER VAL LYS ILE SER CYS LYS THR SER GLY          
SEQRES   3 H  240  TYR THR PHE THR GLU TYR ILE MET HIS TRP VAL LYS GLN          
SEQRES   4 H  240  SER HIS GLY LYS SER LEU GLU TRP ILE GLY GLY ILE ILE          
SEQRES   5 H  240  PRO ASN ASN GLY GLY THR SER TYR ASN GLN LYS PHE LYS          
SEQRES   6 H  240  ASP LYS ALA THR MET THR VAL ASP LYS SER SER SER THR          
SEQRES   7 H  240  GLY TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER          
SEQRES   8 H  240  ALA VAL TYR TYR CYS THR ARG ARG GLU VAL TYR GLY ARG          
SEQRES   9 H  240  ASN TYR TYR ALA LEU ASP TYR TRP GLY GLN GLY THR LEU          
SEQRES  10 H  240  VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL          
SEQRES  11 H  240  PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY          
SEQRES  12 H  240  THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO          
SEQRES  13 H  240  GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR          
SEQRES  14 H  240  SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER          
SEQRES  15 H  240  GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER          
SEQRES  16 H  240  SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN          
SEQRES  17 H  240  HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU          
SEQRES  18 H  240  PRO LYS CYS CYS ASP LYS THR HIS THR CYS PRO PRO CYS          
SEQRES  19 H  240  PRO ALA PRO GLU LEU LEU                                      
SEQRES   1 R  173  GLU PRO PRO THR ALA CYS ARG GLU LYS GLN TYR LEU ILE          
SEQRES   2 R  173  ASN SER GLN CYS CYS SER LEU CYS GLN PRO GLY GLN LYS          
SEQRES   3 R  173  LEU VAL SER ASP CYS THR GLU PHE THR GLU THR GLU CYS          
SEQRES   4 R  173  LEU PRO CYS GLY GLU SER GLU PHE LEU ASP THR TRP ASN          
SEQRES   5 R  173  ARG GLU THR HIS CYS HIS GLN HIS LYS TYR CYS ASP PRO          
SEQRES   6 R  173  ASN LEU GLY LEU ARG VAL GLN GLN LYS GLY THR SER GLU          
SEQRES   7 R  173  THR ASP THR ILE CYS THR CYS GLU GLU GLY TRP HIS CYS          
SEQRES   8 R  173  THR SER GLU ALA CYS GLU SER CYS VAL LEU HIS ARG SER          
SEQRES   9 R  173  CYS SER PRO GLY PHE GLY VAL LYS GLN ILE ALA THR GLY          
SEQRES  10 R  173  VAL SER ASP THR ILE CYS GLU PRO CYS PRO VAL GLY PHE          
SEQRES  11 R  173  PHE SER ASN VAL SER SER ALA PHE GLU LYS CYS HIS PRO          
SEQRES  12 R  173  TRP THR SER CYS GLU THR LYS ASP LEU VAL VAL GLN GLN          
SEQRES  13 R  173  ALA GLY THR ASN LYS THR ASP VAL VAL CYS GLY PRO GLN          
SEQRES  14 R  173  ASP ARG LEU ARG                                              
FORMUL   4  HOH   *21(H2 O)                                                     
HELIX    1 AA1 SER L  121  SER L  127  1                                   7    
HELIX    2 AA2 LYS L  183  HIS L  189  1                                   7    
HELIX    3 AA3 THR H   28  THR H   30  5                                   3    
HELIX    4 AA4 GLN H   62  LYS H   65  5                                   4    
HELIX    5 AA5 THR H   87  SER H   91  5                                   5    
HELIX    6 AA6 SER H  165  ALA H  167  5                                   3    
HELIX    7 AA7 PRO H  194  LEU H  198  5                                   5    
HELIX    8 AA8 LYS H  210  ASN H  213  5                                   4    
HELIX    9 AA9 ASP R   84  LEU R   87  5                                   4    
SHEET    1 AA1 4 MET L   4  GLN L   6  0                                        
SHEET    2 AA1 4 VAL L  19  ALA L  25 -1  O  SER L  24   N  THR L   5           
SHEET    3 AA1 4 ASP L  70  ILE L  75 -1  O  LEU L  73   N  ILE L  21           
SHEET    4 AA1 4 PHE L  62  SER L  67 -1  N  SER L  63   O  THR L  74           
SHEET    1 AA2 6 SER L  10  SER L  14  0                                        
SHEET    2 AA2 6 THR L 102  LYS L 107  1  O  GLU L 105   N  LEU L  11           
SHEET    3 AA2 6 ALA L  84  GLN L  90 -1  N  ALA L  84   O  LEU L 104           
SHEET    4 AA2 6 LEU L  33  GLN L  38 -1  N  TYR L  36   O  TYR L  87           
SHEET    5 AA2 6 VAL L  44  TYR L  49 -1  O  ILE L  48   N  TRP L  35           
SHEET    6 AA2 6 SER L  53  LEU L  54 -1  O  SER L  53   N  TYR L  49           
SHEET    1 AA3 4 SER L  10  SER L  14  0                                        
SHEET    2 AA3 4 THR L 102  LYS L 107  1  O  GLU L 105   N  LEU L  11           
SHEET    3 AA3 4 ALA L  84  GLN L  90 -1  N  ALA L  84   O  LEU L 104           
SHEET    4 AA3 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1 AA4 4 SER L 114  PHE L 118  0                                        
SHEET    2 AA4 4 THR L 129  PHE L 139 -1  O  ASN L 137   N  SER L 114           
SHEET    3 AA4 4 TYR L 173  SER L 182 -1  O  LEU L 179   N  VAL L 132           
SHEET    4 AA4 4 SER L 159  VAL L 163 -1  N  GLN L 160   O  THR L 178           
SHEET    1 AA5 4 ALA L 153  LEU L 154  0                                        
SHEET    2 AA5 4 LYS L 145  VAL L 150 -1  N  VAL L 150   O  ALA L 153           
SHEET    3 AA5 4 VAL L 191  THR L 197 -1  O  GLU L 195   N  GLN L 147           
SHEET    4 AA5 4 VAL L 205  ASN L 210 -1  O  LYS L 207   N  CYS L 194           
SHEET    1 AA6 4 GLN H   3  GLN H   6  0                                        
SHEET    2 AA6 4 VAL H  18  SER H  25 -1  O  SER H  25   N  GLN H   3           
SHEET    3 AA6 4 THR H  78  LEU H  83 -1  O  GLY H  79   N  CYS H  22           
SHEET    4 AA6 4 ALA H  68  ASP H  73 -1  N  THR H  71   O  TYR H  80           
SHEET    1 AA7 6 ASP H  10  VAL H  12  0                                        
SHEET    2 AA7 6 THR H 116  VAL H 120  1  O  THR H 119   N  ASP H  10           
SHEET    3 AA7 6 ALA H  92  GLU H 100 -1  N  ALA H  92   O  VAL H 118           
SHEET    4 AA7 6 TYR H  32  GLN H  39 -1  N  VAL H  37   O  TYR H  95           
SHEET    5 AA7 6 GLU H  46  ILE H  52 -1  O  ILE H  48   N  TRP H  36           
SHEET    6 AA7 6 GLY H  57  TYR H  60 -1  O  GLY H  57   N  ILE H  52           
SHEET    1 AA8 4 ASP H  10  VAL H  12  0                                        
SHEET    2 AA8 4 THR H 116  VAL H 120  1  O  THR H 119   N  ASP H  10           
SHEET    3 AA8 4 ALA H  92  GLU H 100 -1  N  ALA H  92   O  VAL H 118           
SHEET    4 AA8 4 LEU H 109  TRP H 112 -1  O  ASP H 110   N  ARG H  98           
SHEET    1 AA9 4 SER H 129  LEU H 133  0                                        
SHEET    2 AA9 4 ALA H 145  TYR H 154 -1  O  LYS H 152   N  SER H 129           
SHEET    3 AA9 4 TYR H 185  VAL H 193 -1  O  LEU H 187   N  VAL H 151           
SHEET    4 AA9 4 HIS H 173  THR H 174 -1  N  HIS H 173   O  VAL H 190           
SHEET    1 AB1 4 SER H 129  LEU H 133  0                                        
SHEET    2 AB1 4 ALA H 145  TYR H 154 -1  O  LYS H 152   N  SER H 129           
SHEET    3 AB1 4 TYR H 185  VAL H 193 -1  O  LEU H 187   N  VAL H 151           
SHEET    4 AB1 4 VAL H 178  LEU H 179 -1  N  VAL H 178   O  SER H 186           
SHEET    1 AB2 3 THR H 160  TRP H 163  0                                        
SHEET    2 AB2 3 ILE H 204  HIS H 209 -1  O  ASN H 206   N  SER H 162           
SHEET    3 AB2 3 THR H 214  LYS H 219 -1  O  VAL H 216   N  VAL H 207           
SHEET    1 AB3 2 GLN R  30  ILE R  33  0                                        
SHEET    2 AB3 2 GLN R  36  SER R  39 -1  O  GLN R  36   N  ILE R  33           
SHEET    1 AB4 2 GLN R  45  SER R  49  0                                        
SHEET    2 AB4 2 GLU R  58  PRO R  61 -1  O  LEU R  60   N  LYS R  46           
SHEET    1 AB5 2 GLU R  66  PHE R  67  0                                        
SHEET    2 AB5 2 HIS R  78  GLN R  79 -1  O  HIS R  78   N  PHE R  67           
SHEET    1 AB6 2 LEU R  89  GLN R  93  0                                        
SHEET    2 AB6 2 ILE R 102  CYS R 105 -1  O  ILE R 102   N  GLN R  93           
SSBOND   1 CYS L   23    CYS L   88                          1555   1555  2.14  
SSBOND   2 CYS L  134    CYS L  194                          1555   1555  2.01  
SSBOND   3 CYS H   22    CYS H   96                          1555   1555  2.12  
SSBOND   4 CYS H  149    CYS H  205                          1555   1555  2.02  
SSBOND   5 CYS R   26    CYS R   37                          1555   1555  2.03  
SSBOND   6 CYS R   38    CYS R   51                          1555   1555  2.05  
SSBOND   7 CYS R   41    CYS R   59                          1555   1555  2.04  
SSBOND   8 CYS R   62    CYS R   77                          1555   1555  2.07  
SSBOND   9 CYS R   83    CYS R  103                          1555   1555  2.07  
SSBOND  10 CYS R  105    CYS R  119                          1555   1555  2.07  
SSBOND  11 CYS R  111    CYS R  116                          1555   1555  2.07  
CISPEP   1 LEU L   94    PRO L   95          0        -0.36                     
CISPEP   2 TYR L  140    PRO L  141          0         5.24                     
CISPEP   3 PHE H  155    PRO H  156          0        -9.58                     
CISPEP   4 GLU H  157    PRO H  158          0        12.15                     
CRYST1  158.753  158.753   93.622  90.00  90.00 120.00 P 31 2 1      6          
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      0.006299  0.003637  0.000000        0.00000                         
SCALE2      0.000000  0.007274  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010681        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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