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Database: PDB
Entry: 6RLX
LinkDB: 6RLX
Original site: 6RLX 
HEADER    HORMONE(MUSCLE RELAXANT)                21-JUN-91   6RLX              
TITLE     X-RAY STRUCTURE OF HUMAN RELAXIN AT 1.5 ANGSTROMS. COMPARISON TO      
TITLE    2 INSULIN AND IMPLICATIONS FOR RECEPTOR BINDING DETERMINANTS           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RELAXIN, A-CHAIN;                                          
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: RELAXIN, B-CHAIN;                                          
COMPND   7 CHAIN: B, D;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HORMONE(MUSCLE RELAXANT)                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.EIGENBROT,M.RANDAL,A.A.KOSSIAKOFF                                   
REVDAT   7   25-DEC-19 6RLX    1       SEQRES                                   
REVDAT   6   14-AUG-19 6RLX    1       REMARK                                   
REVDAT   5   17-JUL-19 6RLX    1       REMARK LINK                              
REVDAT   4   16-NOV-11 6RLX    1       VERSN  HETATM                            
REVDAT   3   24-FEB-09 6RLX    1       VERSN                                    
REVDAT   2   01-APR-03 6RLX    1       JRNL                                     
REVDAT   1   31-OCT-93 6RLX    0                                                
JRNL        AUTH   C.EIGENBROT,M.RANDAL,C.QUAN,J.BURNIER,L.O'CONNELL,           
JRNL        AUTH 2 E.RINDERKNECHT,A.A.KOSSIAKOFF                                
JRNL        TITL   X-RAY STRUCTURE OF HUMAN RELAXIN AT 1.5 A. COMPARISON TO     
JRNL        TITL 2 INSULIN AND IMPLICATIONS FOR RECEPTOR BINDING DETERMINANTS.  
JRNL        REF    J.MOL.BIOL.                   V. 221    15 1991              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   1656049                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 768                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 73                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6RLX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000179862.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       30.84000            
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       30.84000            
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       26.98500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       28.44000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       26.98500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       28.44000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       30.84000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       26.98500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       28.44000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       30.84000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       26.98500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       28.44000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
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 300 REMARK: PSEUDO TWO-FOLD CALCULATED FROM C ALPHA PORTIONS A 6 - A 20  
REMARK 300 AND B 7 - B 19 AND THE CORRESPONDING ATOMS OF MOLECULE 2.            
REMARK 300 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL           
REMARK 300 YIELD APPROXIMATE COORDINATES FOR CHAINS *C* AND *D* WHEN            
REMARK 300 APPLIED TO CHAINS *A* AND *B*, RESPECTIVELY.                         
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 5620 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH C  71  LIES ON A SPECIAL POSITION.                          
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     SER B    25                                                      
REMARK 465     THR D    23                                                      
REMARK 465     TRP D    24                                                      
REMARK 465     SER D    25                                                      
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     PCA A  -3    CG   CD   OE                                        
REMARK 470     SER D  22    CB   OG                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH2  ARG B     9     NH2  ARG B     9     4566     1.94            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    TYR A  -1   CB  -  CG  -  CD2 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    TYR A  -1   CB  -  CG  -  CD1 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ASN A   4   O   -  C   -  N   ANGL. DEV. =  10.8 DEGREES          
REMARK 500    LYS A   5   CA  -  C   -  N   ANGL. DEV. =  14.8 DEGREES          
REMARK 500    LYS A   5   O   -  C   -  N   ANGL. DEV. = -12.7 DEGREES          
REMARK 500    ARG A  14   CD  -  NE  -  CZ  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ARG A  18   CD  -  NE  -  CZ  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ARG A  18   NE  -  CZ  -  NH1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    MET B   0   CA  -  CB  -  CG  ANGL. DEV. = -10.6 DEGREES          
REMARK 500    LEU B   6   O   -  C   -  N   ANGL. DEV. =  12.3 DEGREES          
REMARK 500    ARG B   9   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG B   9   CA  -  C   -  O   ANGL. DEV. =  14.5 DEGREES          
REMARK 500    GLU B  10   OE1 -  CD  -  OE2 ANGL. DEV. =   7.8 DEGREES          
REMARK 500    GLU B  10   CG  -  CD  -  OE1 ANGL. DEV. = -17.9 DEGREES          
REMARK 500    GLU B  10   CG  -  CD  -  OE2 ANGL. DEV. =  17.0 DEGREES          
REMARK 500    GLU B  10   CG  -  CD  -  OE2 ANGL. DEV. = -19.2 DEGREES          
REMARK 500    ARG B  13   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ALA B  14   O   -  C   -  N   ANGL. DEV. =  11.9 DEGREES          
REMARK 500    TYR C  -1   O   -  C   -  N   ANGL. DEV. = -11.4 DEGREES          
REMARK 500    ARG C  14   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG C  14   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ALA C  17   O   -  C   -  N   ANGL. DEV. =   9.9 DEGREES          
REMARK 500    PHE C  19   CB  -  CG  -  CD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    MET D   0   CA  -  CB  -  CG  ANGL. DEV. = -14.0 DEGREES          
REMARK 500    LEU D   6   O   -  C   -  N   ANGL. DEV. =  17.3 DEGREES          
REMARK 500    ARG D   9   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    GLU D  10   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.3 DEGREES          
REMARK 500    GLU D  10   CG  -  CD  -  OE2 ANGL. DEV. =  13.1 DEGREES          
REMARK 500    ARG D  13   CD  -  NE  -  CZ  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    ARG D  13   NE  -  CZ  -  NH1 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ARG D  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 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    SER B  22       49.26    -83.44                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG C  14         0.24    SIDE CHAIN                              
REMARK 500    ARG D   9         0.09    SIDE CHAIN                              
REMARK 500    ARG D  13         0.10    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 NUMBERING OF THE RESIDUES IS BASED ON INSULIN (EG. 1INS OF           
REMARK 999 PROTEIN DATA BANK).  WEAK OR NONEXISTENT ELECTRON DENSITY            
REMARK 999 PREVENTS IDENTIFICATION OF THE FOLLOWING:  SOME ATOMS OF             
REMARK 999 PCA A(-3); RESIDUES SER B 25, THR D 23, TRP D 24 AND SER D           
REMARK 999 25.  MULTIPLE ATOMIC POSITIONS ARE INCLUDED FOR SIDE CHAIN           
REMARK 999 ATOMS OF THE FOLLOWING RESIDUES:  SER A 15, GLU B 10, TRP B          
REMARK 999 24, AND ARG C 14.                                                    
DBREF  6RLX A   -2    20  UNP    P04090   REL2_HUMAN     162    185             
DBREF  6RLX B   -2    25  UNP    P04090   REL2_HUMAN      26     53             
DBREF  6RLX C   -2    20  UNP    P04090   REL2_HUMAN     162    185             
DBREF  6RLX D   -2    25  UNP    P04090   REL2_HUMAN      26     53             
SEQRES   1 A   24  PCA LEU TYR SER ALA LEU ALA ASN LYS CYS CYS HIS VAL          
SEQRES   2 A   24  GLY CYS THR LYS ARG SER LEU ALA ARG PHE CYS                  
SEQRES   1 B   28  SER TRP MET GLU GLU VAL ILE LYS LEU CYS GLY ARG GLU          
SEQRES   2 B   28  LEU VAL ARG ALA GLN ILE ALA ILE CYS GLY MET SER THR          
SEQRES   3 B   28  TRP SER                                                      
SEQRES   1 C   24  PCA LEU TYR SER ALA LEU ALA ASN LYS CYS CYS HIS VAL          
SEQRES   2 C   24  GLY CYS THR LYS ARG SER LEU ALA ARG PHE CYS                  
SEQRES   1 D   28  SER TRP MET GLU GLU VAL ILE LYS LEU CYS GLY ARG GLU          
SEQRES   2 D   28  LEU VAL ARG ALA GLN ILE ALA ILE CYS GLY MET SER THR          
SEQRES   3 D   28  TRP SER                                                      
MODRES 6RLX PCA A   -3  GLN  PYROGLUTAMIC ACID                                  
MODRES 6RLX PCA C   -3  GLN  PYROGLUTAMIC ACID                                  
HET    PCA  A  -3       5                                                       
HET    PCA  C  -3       8                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
FORMUL   1  PCA    2(C5 H7 N O3)                                                
FORMUL   5  HOH   *73(H2 O)                                                     
HELIX    1  A1 PCA A   -3  VAL A    9  1                                  13    
HELIX    2  A2 LYS A   13  CYS A   20  1IRREGULAR; ALSO CLASS 5            8    
HELIX    3  B1 SER B   -2  GLU B    2  5                                   5    
HELIX    4  B2 CYS B    7  SER B   22  1                                  16    
HELIX    5  C1 PCA C   -3  VAL C    9  1                                  13    
HELIX    6  C2 LYS C   13  CYS C   20  1IRREGULAR; ALSO CLASS 5            8    
HELIX    7  D1 SER D   -2  GLU D    2  5                                   5    
HELIX    8  D2 CYS D    7  SER D   22  1                                  16    
SHEET    1   A 2 CYS A  11  THR A  12  0                                        
SHEET    2   A 2 VAL B   3  ILE B   4 -1  O  ILE B   4   N  CYS A  11           
SHEET    1   B 2 CYS C  11  THR C  12  0                                        
SHEET    2   B 2 VAL D   3  ILE D   4 -1  N  ILE D   4   O  CYS C  11           
SSBOND   1 CYS A    6    CYS A   11                          1555   1555  2.06  
SSBOND   2 CYS A    7    CYS B    7                          1555   1555  2.06  
SSBOND   3 CYS A   20    CYS B   19                          1555   1555  2.00  
SSBOND   4 CYS C    6    CYS C   11                          1555   1555  2.01  
SSBOND   5 CYS C    7    CYS D    7                          1555   1555  2.06  
SSBOND   6 CYS C   20    CYS D   19                          1555   1555  2.02  
LINK         C   PCA A  -3                 N   LEU A  -2     1555   1555  1.31  
LINK         C   PCA C  -3                 N   LEU C  -2     1555   1555  1.31  
CRYST1   53.970   56.880   61.680  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      0.018529  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017581  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016213        0.00000                         
MTRIX1   1  0.830125  0.207228 -0.517638       19.36984    1                    
MTRIX2   1  0.164367 -0.978064 -0.127962       28.26602    1                    
MTRIX3   1 -0.532801  0.021142 -0.845977       77.56604    1                    
HETATM    1  N   PCA A  -3      47.559  10.287  34.369  1.00 51.69           N  
HETATM    2  CA  PCA A  -3      48.049  10.648  33.032  1.00 50.45           C  
HETATM    3  CB  PCA A  -3      49.359   9.916  32.795  1.00 53.08           C  
HETATM    4  C   PCA A  -3      47.020  10.314  31.952  1.00 49.10           C  
HETATM    5  O   PCA A  -3      46.954  10.993  30.919  1.00 51.02           O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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