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Database: PDB
Entry: 6MAC
LinkDB: 6MAC
Original site: 6MAC 
HEADER    SIGNALING PROTEIN                       27-AUG-18   6MAC              
TITLE     TERNARY STRUCTURE OF GDF11 BOUND TO ACTRIIB-ECD AND ALK5-ECD          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GROWTH/DIFFERENTIATION FACTOR 11;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: GDF-11,BONE MORPHOGENETIC PROTEIN 11,BMP-11;                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ACTIVIN RECEPTOR TYPE-2B;                                  
COMPND   8 CHAIN: C;                                                            
COMPND   9 SYNONYM: ACTIVIN RECEPTOR TYPE IIB,ACTR-IIB;                         
COMPND  10 EC: 2.7.11.30;                                                       
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: TGF-BETA RECEPTOR TYPE-1;                                  
COMPND  14 CHAIN: K;                                                            
COMPND  15 SYNONYM: TGFR-1,ACTIVIN A RECEPTOR TYPE II-LIKE PROTEIN KINASE OF    
COMPND  16 53KD,ACTIVIN RECEPTOR-LIKE KINASE 5,ALK5,SERINE/THREONINE-PROTEIN    
COMPND  17 KINASE RECEPTOR R4,SKR4,TGF-BETA TYPE I RECEPTOR,TRANSFORMING GROWTH 
COMPND  18 FACTOR-BETA RECEPTOR TYPE I,TBETAR-I;                                
COMPND  19 EC: 2.7.11.30;                                                       
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GDF11, BMP11;                                                  
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  10 ORGANISM_COMMON: RAT;                                                
SOURCE  11 ORGANISM_TAXID: 10116;                                               
SOURCE  12 GENE: ACVR2B, ACTRIIB;                                               
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: TGFBR1, ALK5, SKR4;                                            
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GROWTH FACTOR, RECEPTOR, TGFB, SIGNALING, SIGNALING PROTEIN           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.J.GOEBEL,T.B.THOMPSON                                               
REVDAT   3   14-AUG-19 6MAC    1       JRNL                                     
REVDAT   2   31-JUL-19 6MAC    1       JRNL                                     
REVDAT   1   17-JUL-19 6MAC    0                                                
JRNL        AUTH   E.J.GOEBEL,R.A.CORPINA,C.S.HINCK,M.CZEPNIK,R.CASTONGUAY,     
JRNL        AUTH 2 R.GRENHA,A.BOISVERT,G.MIKLOSSY,P.T.FULLERTON,M.M.MATZUK,     
JRNL        AUTH 3 V.J.IDONE,A.N.ECONOMIDES,R.KUMAR,A.P.HINCK,T.B.THOMPSON      
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF AN ACTIVIN CLASS TERNARY      
JRNL        TITL 2 RECEPTOR COMPLEX REVEALS A THIRD PARADIGM FOR RECEPTOR       
JRNL        TITL 3 SPECIFICITY.                                                 
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 116 15505 2019              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   31315975                                                     
JRNL        DOI    10.1073/PNAS.1906253116                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.34 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.13_2998                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.430                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 18656                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1865                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 50.5114 -  5.5000    1.00     1347   145  0.1984 0.2726        
REMARK   3     2  5.5000 -  4.3663    1.00     1290   146  0.1758 0.2061        
REMARK   3     3  4.3663 -  3.8146    1.00     1292   148  0.1944 0.2353        
REMARK   3     4  3.8146 -  3.4659    1.00     1317   140  0.2257 0.2609        
REMARK   3     5  3.4659 -  3.2175    1.00     1274   139  0.2445 0.2658        
REMARK   3     6  3.2175 -  3.0279    1.00     1297   145  0.2498 0.3112        
REMARK   3     7  3.0279 -  2.8762    1.00     1286   147  0.2652 0.3315        
REMARK   3     8  2.8762 -  2.7511    1.00     1278   139  0.2744 0.3251        
REMARK   3     9  2.7511 -  2.6452    1.00     1287   142  0.2805 0.3153        
REMARK   3    10  2.6452 -  2.5539    1.00     1265   142  0.3020 0.3371        
REMARK   3    11  2.5539 -  2.4740    1.00     1289   144  0.3473 0.4133        
REMARK   3    12  2.4740 -  2.4033    1.00     1281   144  0.3692 0.4367        
REMARK   3    13  2.4033 -  2.3400    1.00     1288   144  0.3917 0.3778        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.270           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 66.62                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 73.71                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6MAC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-AUG-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000236512.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUN-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : 4.5-6.3                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033202                           
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 : DIALS                              
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18669                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.340                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.02690                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.0700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40220                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.510                              
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: 5E4G, 3KFD, 1NYS                                     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: .05-.15M SODIUM ACETATE 12-24%           
REMARK 280  POLYETHYLENE GLYCOL 8000 .05-.15M SODIUM THIOCYANATE, VAPOR         
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293.15K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 1 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -Y,-X,-Z+1/3                                            
REMARK 290       5555   -X+Y,Y,-Z+2/3                                           
REMARK 290       6555   X,X-Y,-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 -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       37.75000            
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       18.87500            
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       18.87500            
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       37.75000            
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        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 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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, K                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
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   O    HOH C   303     O    HOH C   305              1.95            
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    ASN A  41      174.99     64.61                                   
REMARK 500    PRO A  66     -167.75    -67.47                                   
REMARK 500    LEU K  10      113.95     63.08                                   
REMARK 500    ARG K  58       80.31   -169.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 201 bound   
REMARK 800  to ASN C 42                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 202 bound   
REMARK 800  to ASN C 65                                                         
DBREF  6MAC A    2   109  UNP    O95390   GDF11_HUMAN    300    407             
DBREF  6MAC C   26   120  UNP    P38445   AVR2B_RAT       26    120             
DBREF  6MAC K    9    88  UNP    P36897   TGFR1_HUMAN     33    112             
SEQRES   1 A  108  LEU GLY LEU ASP CYS ASP GLU HIS SER SER GLU SER ARG          
SEQRES   2 A  108  CYS CYS ARG TYR PRO LEU THR VAL ASP PHE GLU ALA PHE          
SEQRES   3 A  108  GLY TRP ASP TRP ILE ILE ALA PRO LYS ARG TYR LYS ALA          
SEQRES   4 A  108  ASN TYR CYS SER GLY GLN CYS GLU TYR MET PHE MET GLN          
SEQRES   5 A  108  LYS TYR PRO HIS THR HIS LEU VAL GLN GLN ALA ASN PRO          
SEQRES   6 A  108  ARG GLY SER ALA GLY PRO CYS CYS THR PRO THR LYS MET          
SEQRES   7 A  108  SER PRO ILE ASN MET LEU TYR PHE ASN ASP LYS GLN GLN          
SEQRES   8 A  108  ILE ILE TYR GLY LYS ILE PRO GLY MET VAL VAL ASP ARG          
SEQRES   9 A  108  CYS GLY CYS SER                                              
SEQRES   1 C   95  THR ARG GLU CYS ILE TYR TYR ASN ALA ASN TRP GLU LEU          
SEQRES   2 C   95  GLU ARG THR ASN GLN SER GLY LEU GLU ARG CYS GLU GLY          
SEQRES   3 C   95  GLU GLN ASP LYS ARG LEU HIS CYS TYR ALA SER TRP ARG          
SEQRES   4 C   95  ASN SER SER GLY THR ILE GLU LEU VAL LYS LYS GLY CYS          
SEQRES   5 C   95  TRP LEU ASP ASP PHE ASN CYS TYR ASP ARG GLN GLU CYS          
SEQRES   6 C   95  VAL ALA THR GLU GLU ASN PRO GLN VAL TYR PHE CYS CYS          
SEQRES   7 C   95  CYS GLU GLY ASN PHE CYS ASN GLU ARG PHE THR HIS LEU          
SEQRES   8 C   95  PRO GLU PRO GLY                                              
SEQRES   1 K   80  ALA LEU GLN CYS PHE CYS HIS LEU CYS THR LYS ASP ASN          
SEQRES   2 K   80  PHE THR CYS VAL THR ASP GLY LEU CYS PHE VAL SER VAL          
SEQRES   3 K   80  THR GLU THR THR ASP LYS VAL ILE HIS ASN SER MET CYS          
SEQRES   4 K   80  ILE ALA GLU ILE ASP LEU ILE PRO ARG ASP ARG PRO PHE          
SEQRES   5 K   80  VAL CYS ALA PRO SER SER LYS THR GLY SER VAL THR THR          
SEQRES   6 K   80  THR TYR CYS CYS ASN GLN ASP HIS CYS ASN LYS ILE GLU          
SEQRES   7 K   80  LEU PRO                                                      
HET    NAG  C 201      14                                                       
HET    NAG  C 202      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   4  NAG    2(C8 H15 N O6)                                               
FORMUL   6  HOH   *18(H2 O)                                                     
HELIX    1 AA1 GLU A   25  GLY A   28  5                                   4    
HELIX    2 AA2 TYR A   55  ASN A   65  1                                  11    
HELIX    3 AA3 ASN C   35  ARG C   40  1                                   6    
HELIX    4 AA4 ASP C   81  TYR C   85  5                                   5    
HELIX    5 AA5 ALA K   49  LEU K   53  5                                   5    
SHEET    1 AA1 2 CYS A  16  TYR A  18  0                                        
SHEET    2 AA1 2 TYR A  42  SER A  44 -1  O  SER A  44   N  CYS A  16           
SHEET    1 AA2 2 THR A  21  ASP A  23  0                                        
SHEET    2 AA2 2 ARG A  37  LYS A  39 -1  O  TYR A  38   N  VAL A  22           
SHEET    1 AA3 3 ILE A  32  ALA A  34  0                                        
SHEET    2 AA3 3 CYS A  73  PHE A  87 -1  O  LEU A  85   N  ALA A  34           
SHEET    3 AA3 3 ILE A  93  SER A 109 -1  O  GLY A 107   N  THR A  75           
SHEET    1 AA4 5 SER C  44  CYS C  49  0                                        
SHEET    2 AA4 5 ARG C  27  ASN C  33 -1  N  TYR C  31   O  GLY C  45           
SHEET    3 AA4 5 THR C  69  TRP C  78 -1  O  LYS C  75   N  TYR C  32           
SHEET    4 AA4 5 HIS C  58  SER C  66 -1  N  ARG C  64   O  GLU C  71           
SHEET    5 AA4 5 TYR C 100  CYS C 104 -1  O  CYS C 104   N  CYS C  59           
SHEET    1 AA5 2 CYS C  90  ALA C  92  0                                        
SHEET    2 AA5 2 PHE C 113  HIS C 115  1  O  THR C 114   N  ALA C  92           
SHEET    1 AA6 2 GLN K  11  PHE K  13  0                                        
SHEET    2 AA6 2 THR K  23  VAL K  25 -1  O  CYS K  24   N  CYS K  12           
SHEET    1 AA7 4 VAL K  41  ILE K  48  0                                        
SHEET    2 AA7 4 LEU K  29  THR K  37 -1  N  PHE K  31   O  MET K  46           
SHEET    3 AA7 4 SER K  70  CYS K  77 -1  O  CYS K  77   N  CYS K  30           
SHEET    4 AA7 4 SER K  65  LYS K  67 -1  N  LYS K  67   O  SER K  70           
SSBOND   1 CYS A    6    CYS A   16                          1555   1555  2.03  
SSBOND   2 CYS A   15    CYS A   74                          1555   1555  2.03  
SSBOND   3 CYS A   43    CYS A  106                          1555   1555  2.03  
SSBOND   4 CYS A   47    CYS A  108                          1555   1555  2.03  
SSBOND   5 CYS C   29    CYS C   59                          1555   1555  2.03  
SSBOND   6 CYS C   49    CYS C   77                          1555   1555  2.03  
SSBOND   7 CYS C   84    CYS C  103                          1555   1555  2.03  
SSBOND   8 CYS C   90    CYS C  102                          1555   1555  2.03  
SSBOND   9 CYS C  104    CYS C  109                          1555   1555  2.03  
SSBOND  10 CYS K   12    CYS K   30                          1555   1555  2.03  
SSBOND  11 CYS K   14    CYS K   17                          1555   1555  2.03  
SSBOND  12 CYS K   24    CYS K   47                          1555   1555  2.03  
SSBOND  13 CYS K   62    CYS K   76                          1555   1555  2.03  
SSBOND  14 CYS K   77    CYS K   82                          1555   1555  2.03  
LINK         ND2 ASN C  42                 C1  NAG C 201     1555   1555  1.44  
LINK         ND2 ASN C  65                 C1  NAG C 202     1555   1555  1.42  
CISPEP   1 ALA A   34    PRO A   35          0        -2.67                     
CISPEP   2 GLY A   68    SER A   69          0         7.99                     
CISPEP   3 ILE K   54    PRO K   55          0        -7.23                     
SITE     1 AC1  1 ASN C  42                                                     
SITE     1 AC2  4 TRP C  63  ASN C  65  TYR C 100  HIS C 115                    
CRYST1  116.624  116.624   56.625  90.00  90.00 120.00 P 32 1 2      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      0.008575  0.004951  0.000000        0.00000                         
SCALE2      0.000000  0.009901  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017660        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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