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Database: PDB
Entry: 6B2E
LinkDB: 6B2E
Original site: 6B2E 
HEADER    TRANSFERASE                             19-SEP-17   6B2E              
TITLE     STRUCTURE OF FULL LENGTH HUMAN AMPK (A2B2G1) IN COMPLEX WITH A SMALL  
TITLE    2 MOLECULE ACTIVATOR SC4.                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-2; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: AMPK SUBUNIT ALPHA-2,ACETYL-COA CARBOXYLASE KINASE,ACACA    
COMPND   5 KINASE,HYDROXYMETHYLGLUTARYL-COA REDUCTASE KINASE,HMGCR KINASE;      
COMPND   6 EC: 2.7.11.1,2.7.11.27,2.7.11.31;                                    
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2;            
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: AMPK SUBUNIT BETA-2;                                        
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;           
COMPND  15 CHAIN: C;                                                            
COMPND  16 SYNONYM: AMPKG;                                                      
COMPND  17 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: PRKAA2, AMPK, AMPK2;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);                             
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PETDUET-1;                                
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: PRKAB2;                                                        
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);                             
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PRSFDUET-1;                               
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 GENE: PRKAG1;                                                        
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  26 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);                             
SOURCE  27 EXPRESSION_SYSTEM_PLASMID: PETDUET-1                                 
KEYWDS    PHOSPHORYLATED, ACTIVE, HETEROTRIMER, KINASE., TRANSFERASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.R.W.NGOEI,C.G.LANGENDORF,N.X.Y.LING,A.HOQUE,S.JOHNSON,M.C.CAMERINO, 
AUTHOR   2 S.R.WALKER,Y.E.BOZIKIS,T.A.DITE,A.J.OVENS,W.J.SMILES,R.JACOBS,       
AUTHOR   3 H.HUANG,M.W.PARKER,J.W.SCOTT,M.H.RIDER,B.E.KEMP,R.C.FOITZIK,         
AUTHOR   4 J.B.BAELL,J.S.OAKHILL                                                
REVDAT   4   01-JAN-20 6B2E    1       REMARK                                   
REVDAT   3   04-JUL-18 6B2E    1       JRNL                                     
REVDAT   2   02-MAY-18 6B2E    1       JRNL                                     
REVDAT   1   25-APR-18 6B2E    0                                                
JRNL        AUTH   K.R.W.NGOEI,C.G.LANGENDORF,N.X.Y.LING,A.HOQUE,S.VARGHESE,    
JRNL        AUTH 2 M.A.CAMERINO,S.R.WALKER,Y.E.BOZIKIS,T.A.DITE,A.J.OVENS,      
JRNL        AUTH 3 W.J.SMILES,R.JACOBS,H.HUANG,M.W.PARKER,J.W.SCOTT,M.H.RIDER,  
JRNL        AUTH 4 R.C.FOITZIK,B.E.KEMP,J.B.BAELL,J.S.OAKHILL                   
JRNL        TITL   STRUCTURAL DETERMINANTS FOR SMALL-MOLECULE ACTIVATION OF     
JRNL        TITL 2 SKELETAL MUSCLE AMPK ALPHA 2 BETA 2 GAMMA 1 BY THE GLUCOSE   
JRNL        TITL 3 IMPORTAGOG SC4.                                              
JRNL        REF    CELL CHEM BIOL                V.  25   728 2018              
JRNL        REFN                   ESSN 2451-9448                               
JRNL        PMID   29657085                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2018.03.008                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.15                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 17764                          
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)  : 0.246                          
REMARK   3   R VALUE            (WORKING SET)  : 0.244                          
REMARK   3   FREE R VALUE                      : 0.277                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.180                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 920                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 9                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.80                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 4.03                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 83.29                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2512                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2680                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2379                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2670                   
REMARK   3   BIN FREE R VALUE                        : 0.2840                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.29                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 133                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6528                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 192                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 89.66                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 136.9                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 11.52240                                             
REMARK   3    B22 (A**2) : -16.35700                                            
REMARK   3    B33 (A**2) : 4.83470                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.630               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.658               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.895                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.886                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 7098   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 9751   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2232   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 115    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1050   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 7098   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1031   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7482   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.01                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.34                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.56                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|9 - A|552 A|601 - A|601 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -18.6611  -20.5496   15.8347           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.4847 T22:   -0.1769                                    
REMARK   3     T33:   -0.2514 T12:    0.1438                                    
REMARK   3     T13:    0.0672 T23:    0.0757                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1155 L22:    3.2536                                    
REMARK   3     L33:    2.8008 L12:   -0.4531                                    
REMARK   3     L13:   -0.8657 L23:    2.0652                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0087 S12:    0.0066 S13:   -0.1455                     
REMARK   3     S21:    0.3517 S22:   -0.0502 S23:    0.2623                     
REMARK   3     S31:    0.2468 S32:   -0.0367 S33:    0.0589                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|59 - B|272 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):  -31.4872  -34.3204   13.2296           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3950 T22:   -0.4119                                    
REMARK   3     T33:   -0.1499 T12:    0.0025                                    
REMARK   3     T13:    0.2156 T23:    0.1044                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9287 L22:    2.2293                                    
REMARK   3     L33:    3.3594 L12:    0.5128                                    
REMARK   3     L13:    0.2894 L23:    2.6167                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0331 S12:   -0.1364 S13:   -0.5852                     
REMARK   3     S21:    0.7034 S22:   -0.0831 S23:    0.2423                     
REMARK   3     S31:    0.7823 S32:   -0.2177 S33:    0.1162                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { B|301 - B|301 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -32.6858   19.6855   26.1641           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.5181 T22:   -0.4628                                    
REMARK   3     T33:   -0.7714 T12:    0.2237                                    
REMARK   3     T13:    0.0469 T23:    0.1203                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4124 L22:    6.4808                                    
REMARK   3     L33:    4.5312 L12:   -1.8865                                    
REMARK   3     L13:   -1.1867 L23:    2.2976                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2445 S12:    0.3394 S13:    0.2515                     
REMARK   3     S21:   -1.2246 S22:   -0.4172 S23:    0.1296                     
REMARK   3     S31:   -0.9460 S32:   -0.3132 S33:    0.1727                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6B2E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000230157.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUL-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17814                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.150                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.20200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.86800                            
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                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6BIU, 4RER                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6-8% PEG 3350, 0.1 M MGCL2, 0.001%       
REMARK 280  COCAMIDOPROPYL BETAINE AND 0.1 M IMIDAZOLE, PH 6.0, VAPOR           
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       56.96800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.04800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.42400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.04800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       56.96800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.42400            
REMARK 290   SMTRY3   4  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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14990 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 44300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -114.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     GLN A    -1                                                      
REMARK 465     ASP A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     ASP A   319                                                      
REMARK 465     GLN A   320                                                      
REMARK 465     LEU A   321                                                      
REMARK 465     ALA A   322                                                      
REMARK 465     VAL A   323                                                      
REMARK 465     PRO A   348                                                      
REMARK 465     SER A   349                                                      
REMARK 465     GLY A   350                                                      
REMARK 465     SER A   351                                                      
REMARK 465     PHE A   352                                                      
REMARK 465     MET A   353                                                      
REMARK 465     ASP A   354                                                      
REMARK 465     ASP A   355                                                      
REMARK 465     SER A   356                                                      
REMARK 465     ALA A   357                                                      
REMARK 465     MET A   358                                                      
REMARK 465     HIS A   359                                                      
REMARK 465     ILE A   360                                                      
REMARK 465     PRO A   361                                                      
REMARK 465     PRO A   362                                                      
REMARK 465     GLY A   363                                                      
REMARK 465     ASP A   377                                                      
REMARK 465     SER A   378                                                      
REMARK 465     PRO A   379                                                      
REMARK 465     LYS A   380                                                      
REMARK 465     ALA A   381                                                      
REMARK 465     ARG A   382                                                      
REMARK 465     CYS A   383                                                      
REMARK 465     PRO A   384                                                      
REMARK 465     LEU A   385                                                      
REMARK 465     ASP A   386                                                      
REMARK 465     ALA A   387                                                      
REMARK 465     LEU A   388                                                      
REMARK 465     ASN A   389                                                      
REMARK 465     THR A   390                                                      
REMARK 465     THR A   391                                                      
REMARK 465     LYS A   392                                                      
REMARK 465     PRO A   393                                                      
REMARK 465     LYS A   394                                                      
REMARK 465     SER A   395                                                      
REMARK 465     LEU A   396                                                      
REMARK 465     ALA A   397                                                      
REMARK 465     VAL A   398                                                      
REMARK 465     GLU A   476                                                      
REMARK 465     VAL A   477                                                      
REMARK 465     VAL A   478                                                      
REMARK 465     GLU A   479                                                      
REMARK 465     GLN A   480                                                      
REMARK 465     ARG A   481                                                      
REMARK 465     SER A   482                                                      
REMARK 465     GLY A   483                                                      
REMARK 465     SER A   484                                                      
REMARK 465     SER A   485                                                      
REMARK 465     THR A   486                                                      
REMARK 465     PRO A   487                                                      
REMARK 465     GLN A   488                                                      
REMARK 465     ARG A   489                                                      
REMARK 465     SER A   490                                                      
REMARK 465     CYS A   491                                                      
REMARK 465     SER A   492                                                      
REMARK 465     ALA A   493                                                      
REMARK 465     ALA A   494                                                      
REMARK 465     GLY A   495                                                      
REMARK 465     LEU A   496                                                      
REMARK 465     HIS A   497                                                      
REMARK 465     ARG A   498                                                      
REMARK 465     PRO A   499                                                      
REMARK 465     ARG A   500                                                      
REMARK 465     SER A   501                                                      
REMARK 465     SER A   502                                                      
REMARK 465     PHE A   503                                                      
REMARK 465     ASP A   504                                                      
REMARK 465     SER A   505                                                      
REMARK 465     THR A   506                                                      
REMARK 465     THR A   507                                                      
REMARK 465     ALA A   508                                                      
REMARK 465     GLU A   509                                                      
REMARK 465     SER A   510                                                      
REMARK 465     HIS A   511                                                      
REMARK 465     SER A   512                                                      
REMARK 465     LEU A   513                                                      
REMARK 465     SER A   514                                                      
REMARK 465     GLY A   515                                                      
REMARK 465     SER A   516                                                      
REMARK 465     LEU A   517                                                      
REMARK 465     THR A   518                                                      
REMARK 465     GLY A   519                                                      
REMARK 465     SER A   520                                                      
REMARK 465     LEU A   521                                                      
REMARK 465     THR A   522                                                      
REMARK 465     GLY A   523                                                      
REMARK 465     SER A   524                                                      
REMARK 465     THR A   525                                                      
REMARK 465     LEU A   526                                                      
REMARK 465     SER A   527                                                      
REMARK 465     SER A   528                                                      
REMARK 465     VAL A   529                                                      
REMARK 465     SER A   530                                                      
REMARK 465     PRO A   531                                                      
REMARK 465     ARG A   532                                                      
REMARK 465     ARG A   553                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     ASP B     7                                                      
REMARK 465     ARG B     8                                                      
REMARK 465     VAL B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     GLU B    12                                                      
REMARK 465     ARG B    13                                                      
REMARK 465     HIS B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     ALA B    16                                                      
REMARK 465     LYS B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     ARG B    20                                                      
REMARK 465     SER B    21                                                      
REMARK 465     GLU B    22                                                      
REMARK 465     GLY B    23                                                      
REMARK 465     ALA B    24                                                      
REMARK 465     GLY B    25                                                      
REMARK 465     GLY B    26                                                      
REMARK 465     HIS B    27                                                      
REMARK 465     ALA B    28                                                      
REMARK 465     PRO B    29                                                      
REMARK 465     GLY B    30                                                      
REMARK 465     LYS B    31                                                      
REMARK 465     GLU B    32                                                      
REMARK 465     HIS B    33                                                      
REMARK 465     LYS B    34                                                      
REMARK 465     ILE B    35                                                      
REMARK 465     MET B    36                                                      
REMARK 465     VAL B    37                                                      
REMARK 465     GLY B    38                                                      
REMARK 465     SER B    39                                                      
REMARK 465     THR B    40                                                      
REMARK 465     ASP B    41                                                      
REMARK 465     ASP B    42                                                      
REMARK 465     PRO B    43                                                      
REMARK 465     SER B    44                                                      
REMARK 465     VAL B    45                                                      
REMARK 465     PHE B    46                                                      
REMARK 465     SER B    47                                                      
REMARK 465     LEU B    48                                                      
REMARK 465     PRO B    49                                                      
REMARK 465     ASP B    50                                                      
REMARK 465     SER B    51                                                      
REMARK 465     LYS B    52                                                      
REMARK 465     LEU B    53                                                      
REMARK 465     PRO B    54                                                      
REMARK 465     GLY B    55                                                      
REMARK 465     ASP B    56                                                      
REMARK 465     LYS B    57                                                      
REMARK 465     GLU B    58                                                      
REMARK 465     GLU B   172                                                      
REMARK 465     SER B   173                                                      
REMARK 465     SER B   174                                                      
REMARK 465     GLU B   175                                                      
REMARK 465     THR B   176                                                      
REMARK 465     SER B   177                                                      
REMARK 465     CYS B   178                                                      
REMARK 465     ARG B   179                                                      
REMARK 465     ASP B   180                                                      
REMARK 465     LEU B   181                                                      
REMARK 465     SER B   182                                                      
REMARK 465     SER B   183                                                      
REMARK 465     SER B   184                                                      
REMARK 465     PRO B   185                                                      
REMARK 465     PRO B   186                                                      
REMARK 465     GLY B   187                                                      
REMARK 465     PRO B   188                                                      
REMARK 465     TYR B   189                                                      
REMARK 465     ARG B   201                                                      
REMARK 465     PHE B   202                                                      
REMARK 465     LYS B   203                                                      
REMARK 465     MET C    -4                                                      
REMARK 465     ALA C    -3                                                      
REMARK 465     ASP C    -2                                                      
REMARK 465     LEU C    -1                                                      
REMARK 465     ASN C     0                                                      
REMARK 465     TRP C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     VAL C     4                                                      
REMARK 465     ILE C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     SER C     7                                                      
REMARK 465     ASP C     8                                                      
REMARK 465     SER C     9                                                      
REMARK 465     SER C    10                                                      
REMARK 465     PRO C    11                                                      
REMARK 465     ALA C    12                                                      
REMARK 465     VAL C    13                                                      
REMARK 465     GLU C    14                                                      
REMARK 465     ASN C    15                                                      
REMARK 465     GLU C    16                                                      
REMARK 465     HIS C    17                                                      
REMARK 465     PRO C    18                                                      
REMARK 465     GLN C    19                                                      
REMARK 465     GLU C    20                                                      
REMARK 465     THR C    21                                                      
REMARK 465     PRO C    22                                                      
REMARK 465     GLU C    23                                                      
REMARK 465     SER C    24                                                      
REMARK 465     GLN C   123                                                      
REMARK 465     ASP C   124                                                      
REMARK 465     SER C   125                                                      
REMARK 465     PHE C   126                                                      
REMARK 465     LYS C   127                                                      
REMARK 465     THR C   325                                                      
REMARK 465     GLY C   326                                                      
REMARK 465     GLY C   327                                                      
REMARK 465     GLU C   328                                                      
REMARK 465     LYS C   329                                                      
REMARK 465     LYS C   330                                                      
REMARK 465     PRO C   331                                                      
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     ARG A  10    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  12    CE   NZ                                             
REMARK 470     LYS A  29    CG   CD   CE   NZ                                   
REMARK 470     LYS A  31    CG   CD   CE   NZ                                   
REMARK 470     ILE A  32    CG1  CG2  CD1                                       
REMARK 470     GLN A  36    CD   OE1  NE2                                       
REMARK 470     ARG A  49    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  51    CG   CD   CE   NZ                                   
REMARK 470     ARG A  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  60    CG   CD   CE   NZ                                   
REMARK 470     LYS A  62    CG   CD   CE   NZ                                   
REMARK 470     ARG A  63    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  69    CG   CD   CE   NZ                                   
REMARK 470     ARG A  72    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  78    CE   NZ                                             
REMARK 470     GLU A 100    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 103    CG   OD1  OD2                                       
REMARK 470     LYS A 107    CG   CD   CE   NZ                                   
REMARK 470     HIS A 108    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL A 111    CG1  CG2                                            
REMARK 470     GLU A 112    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 113    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 154    CD   CE   NZ                                        
REMARK 470     LEU A 160    CG   CD1  CD2                                       
REMARK 470     GLU A 168    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 171    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 188    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 224    CG   CD   CE   NZ                                   
REMARK 470     LYS A 225    CE   NZ                                             
REMARK 470     ARG A 227    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A 235    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 239    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 255    CG   CD   CE   NZ                                   
REMARK 470     ILE A 259    CG1  CG2  CD1                                       
REMARK 470     LYS A 260    CG   CD   CE   NZ                                   
REMARK 470     ARG A 263    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 266    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 269    CG   CD   CE   NZ                                   
REMARK 470     ASP A 280    CG   OD1  OD2                                       
REMARK 470     TYR A 283    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN A 286    CG   OD1  ND2                                       
REMARK 470     ILE A 288    CG1  CG2  CD1                                       
REMARK 470     ASP A 290    CG   OD1  OD2                                       
REMARK 470     GLU A 291    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 294    CG   CD   CE   NZ                                   
REMARK 470     GLU A 295    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 298    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 299    CG   CD   CE   NZ                                   
REMARK 470     PHE A 300    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 301    CG   CD   OE1  OE2                                  
REMARK 470     THR A 303    OG1  CG2                                            
REMARK 470     GLU A 304    CG   CD   OE1  OE2                                  
REMARK 470     SER A 305    OG                                                  
REMARK 470     VAL A 307    CG1  CG2                                            
REMARK 470     MET A 308    CG   SD   CE                                        
REMARK 470     ASN A 309    CG   OD1  ND2                                       
REMARK 470     SER A 310    OG                                                  
REMARK 470     TYR A 325    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 327    CG   CD1  CD2                                       
REMARK 470     ILE A 328    CG1  CG2  CD1                                       
REMARK 470     ILE A 329    CG1  CG2  CD1                                       
REMARK 470     ASP A 330    CG   OD1  OD2                                       
REMARK 470     ASN A 331    CG   OD1  ND2                                       
REMARK 470     ARG A 332    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 333    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 335    CG   SD   CE                                        
REMARK 470     GLN A 337    CG   CD   OE1  NE2                                  
REMARK 470     PHE A 341    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     TYR A 342    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 364    CG   CD1  CD2                                       
REMARK 470     LYS A 365    CG   CD   CE   NZ                                   
REMARK 470     GLU A 369    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 374    CG   CD1  CD2                                       
REMARK 470     LYS A 399    CG   CD   CE   NZ                                   
REMARK 470     LYS A 400    CG   CD   CE   NZ                                   
REMARK 470     LYS A 402    CG   CD   CE   NZ                                   
REMARK 470     ARG A 408    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 410    CD   OE1  NE2                                       
REMARK 470     GLU A 419    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 422    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 424    CG   SD   CE                                        
REMARK 470     LYS A 425    CG   CD   CE   NZ                                   
REMARK 470     GLU A 430    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 432    CG   CD   CE   NZ                                   
REMARK 470     ARG A 440    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 442    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 444    CG   CD   CE   NZ                                   
REMARK 470     ASP A 462    CG   OD1  OD2                                       
REMARK 470     ARG A 464    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 467    CG   CD1  CD2                                       
REMARK 470     ASP A 475    CG   OD1  OD2                                       
REMARK 470     SER A 535    OG                                                  
REMARK 470     THR A 537    OG1  CG2                                            
REMARK 470     PHE B  59    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL B  60    CG1  CG2                                            
REMARK 470     TRP B  62    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B  62    CZ3  CH2                                            
REMARK 470     GLN B  63    CG   CD   OE1  NE2                                  
REMARK 470     ASP B  65    CG   OD1  OD2                                       
REMARK 470     LEU B  66    CG   CD1  CD2                                       
REMARK 470     GLU B  67    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  68    CG   OD1  OD2                                       
REMARK 470     VAL B  70    CG1  CG2                                            
REMARK 470     LYS B  71    CG   CD   CE   NZ                                   
REMARK 470     GLN B  75    CG   CD   OE1  NE2                                  
REMARK 470     ARG B  77    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B  80    CG1  CG2                                            
REMARK 470     ILE B  81    CG1  CG2  CD1                                       
REMARK 470     GLU B  85    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  88    CG   CD   CE   NZ                                   
REMARK 470     PHE B  91    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE B  92    CG1  CG2  CD1                                       
REMARK 470     PHE B  96    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN B  97    CG   OD1  ND2                                       
REMARK 470     ASN B  98    CG   OD1  ND2                                       
REMARK 470     TRP B  99    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B  99    CZ3  CH2                                            
REMARK 470     LYS B 102    CG   CD   CE   NZ                                   
REMARK 470     LYS B 107    CG   CD   CE   NZ                                   
REMARK 470     ASN B 110    CG   OD1  ND2                                       
REMARK 470     VAL B 113    CG1  CG2                                            
REMARK 470     LEU B 118    CG   CD1  CD2                                       
REMARK 470     GLU B 120    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 122    CG   CD   OE1  OE2                                  
REMARK 470     HIS B 123    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN B 124    CG   CD   OE1  NE2                                  
REMARK 470     TYR B 125    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B 126    CG   CD   CE   NZ                                   
REMARK 470     PHE B 128    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN B 132    OE1  NE2                                            
REMARK 470     TRP B 133    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 133    CZ3  CH2                                            
REMARK 470     VAL B 141    CG1  CG2                                            
REMARK 470     VAL B 142    CG1  CG2                                            
REMARK 470     THR B 143    OG1  CG2                                            
REMARK 470     SER B 144    OG                                                  
REMARK 470     GLN B 145    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 146    CG   CD1  CD2                                       
REMARK 470     THR B 148    OG1  CG2                                            
REMARK 470     ILE B 149    CG1  CG2  CD1                                       
REMARK 470     ASN B 151    CG   OD1  ND2                                       
REMARK 470     LEU B 152    CG   CD1  CD2                                       
REMARK 470     ILE B 153    CG1  CG2  CD1                                       
REMARK 470     VAL B 155    CG1  CG2                                            
REMARK 470     LYS B 156    CG   CD   CE   NZ                                   
REMARK 470     LYS B 157    CG   CD   CE   NZ                                   
REMARK 470     PHE B 160    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE B 163    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP B 164    CG   OD1  OD2                                       
REMARK 470     LEU B 166    CG   CD1  CD2                                       
REMARK 470     LEU B 168    CG   CD1  CD2                                       
REMARK 470     ASP B 169    CG   OD1  OD2                                       
REMARK 470     MET B 171    CG   SD   CE                                        
REMARK 470     GLN B 191    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 192    CG   CD   OE1  OE2                                  
REMARK 470     MET B 193    CG   SD   CE                                        
REMARK 470     TYR B 194    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE B 196    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B 197    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 199    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 200    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 213    CG   CD1  CD2                                       
REMARK 470     LYS B 219    CG   CD   CE   NZ                                   
REMARK 470     GLU B 232    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 241    CG   CD1  CD2                                       
REMARK 470     LYS B 247    CE   NZ                                             
REMARK 470     ARG B 258    NE   CZ   NH1  NH2                                  
REMARK 470     TYR B 259    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B 260    CG   CD   CE   NZ                                   
REMARK 470     LYS B 261    CG   CD   CE   NZ                                   
REMARK 470     LYS B 262    CG   CD   CE   NZ                                   
REMARK 470     LYS B 270    CG   CD   CE   NZ                                   
REMARK 470     ILE B 272    CG1  CG2  CD1                                       
REMARK 470     ASN C  25    CG   OD1  ND2                                       
REMARK 470     ASN C  26    CG   OD1  ND2                                       
REMARK 470     TYR C  29    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE C  32    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     MET C  33    CG   SD   CE                                        
REMARK 470     LYS C  34    CG   CD   CE   NZ                                   
REMARK 470     HIS C  36    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG C  37    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C  40    CG   OD1  OD2                                       
REMARK 470     LYS C  47    CG   CD   CE   NZ                                   
REMARK 470     GLN C  56    CG   CD   OE1  NE2                                  
REMARK 470     LYS C  58    CG   CD   CE   NZ                                   
REMARK 470     LYS C  59    CG   CD   CE   NZ                                   
REMARK 470     LYS C  78    CG   CD   CE   NZ                                   
REMARK 470     LYS C  79    CG   CD   CE   NZ                                   
REMARK 470     HIS C  96    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG C  97    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 100    CG   CD   CE   NZ                                   
REMARK 470     GLN C 105    CD   OE1  NE2                                       
REMARK 470     GLU C 111    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 113    CG   CD   CE   NZ                                   
REMARK 470     ILE C 114    CG1  CG2  CD1                                       
REMARK 470     GLU C 115    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 118    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 119    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 122    CG   CD1  CD2                                       
REMARK 470     PHE C 139    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU C 145    CG   CD1  CD2                                       
REMARK 470     LYS C 149    CG   CD   CE   NZ                                   
REMARK 470     ARG C 152    CZ   NH1  NH2                                       
REMARK 470     ASP C 157    CG   OD1  OD2                                       
REMARK 470     GLU C 159    CG   CD   OE1  OE2                                  
REMARK 470     SER C 160    OG                                                  
REMARK 470     ASN C 162    CG   OD1  ND2                                       
REMARK 470     LYS C 170    CG   CD   CE   NZ                                   
REMARK 470     LYS C 174    CG   CD   CE   NZ                                   
REMARK 470     LYS C 177    CG   CD   CE   NZ                                   
REMARK 470     PHE C 179    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE C 180    CG1  CG2  CD1                                       
REMARK 470     GLU C 182    CG   CD   OE1  OE2                                  
REMARK 470     PHE C 183    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS C 185    CG   CD   CE   NZ                                   
REMARK 470     GLU C 187    CG   CD   OE1  OE2                                  
REMARK 470     MET C 189    CG   SD   CE                                        
REMARK 470     LYS C 191    CG   CD   CE   NZ                                   
REMARK 470     LEU C 193    CG   CD1  CD2                                       
REMARK 470     GLU C 194    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 195    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 196    CG   CD1  CD2                                       
REMARK 470     GLN C 197    CG   CD   OE1  NE2                                  
REMARK 470     ILE C 198    CG1  CG2  CD1                                       
REMARK 470     TYR C 201    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET C 206    CG   SD   CE                                        
REMARK 470     SER C 226    OG                                                  
REMARK 470     LYS C 234    CG   CD   CE   NZ                                   
REMARK 470     ARG C 236    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL C 237    CG1  CG2                                            
REMARK 470     GLU C 252    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 253    CG   CD   CE   NZ                                   
REMARK 470     LYS C 264    CG   CD   CE   NZ                                   
REMARK 470     HIS C 271    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU C 274    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 277    CG   CD1  CD2                                       
REMARK 470     LYS C 278    CE   NZ                                             
REMARK 470     GLU C 283    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 286    CG   CD   OE1  OE2                                  
REMARK 470     ILE C 288    CG1  CG2  CD1                                       
REMARK 470     ASN C 290    CG   OD1  ND2                                       
REMARK 470     ARG C 291    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C 292    CG   CD1  CD2                                       
REMARK 470     GLU C 294    CG   CD   OE1  OE2                                  
REMARK 470     VAL C 297    CG1  CG2                                            
REMARK 470     ARG C 299    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 304    CG   OD1  OD2                                       
REMARK 470     GLU C 305    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 307    CG   OD1  OD2                                       
REMARK 470     VAL C 309    CG1  CG2                                            
REMARK 470     LYS C 310    CG   CD   CE   NZ                                   
REMARK 470     ILE C 312    CG1  CG2  CD1                                       
REMARK 470     GLN C 320    CG   CD   OE1  NE2                                  
REMARK 470     LEU C 324    CG   CD1  CD2                                       
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    LYS B   260     OH   TYR C    39              1.85            
REMARK 500   O    ASN A   309     CD2  TYR A   312              2.11            
REMARK 500   O    ASN A   309     CE2  TYR A   312              2.11            
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 A  38      -61.69    -94.73                                   
REMARK 500    ARG A  72       72.31   -152.95                                   
REMARK 500    ASP A 139       53.88   -104.66                                   
REMARK 500    ASP A 148     -169.82   -114.01                                   
REMARK 500    MET A 151       77.62     56.99                                   
REMARK 500    ASP A 157       73.12     60.25                                   
REMARK 500    TYR A 179       -7.49     66.63                                   
REMARK 500    LEU A 249       70.91   -107.42                                   
REMARK 500    CYS A 302      -59.23   -131.49                                   
REMARK 500    GLU A 306        3.08     83.25                                   
REMARK 500    ASP A 315        3.24     81.21                                   
REMARK 500    TRP A 431     -165.79   -129.64                                   
REMARK 500    ASP A 462     -167.73   -122.56                                   
REMARK 500    LYS B 156      -52.85   -120.03                                   
REMARK 500    ASN B 239        6.74     81.32                                   
REMARK 500    LYS C  34      -52.32     70.11                                   
REMARK 500    LYS C 100      -60.13    -96.56                                   
REMARK 500    GLU C 274       41.18    -95.90                                   
REMARK 500    GLU C 305      -59.23     70.45                                   
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 residue STU A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CG7 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCD B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP C 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP C 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6BIU   RELATED DB: PDB                                   
REMARK 900 6BIU HAS A DIFFERENT AMPK BETA-SUBUNIT ISOFORM (1).                  
DBREF  6B2E A    2   553  UNP    P54646   AAPK2_HUMAN      2    552             
DBREF  6B2E B    1   272  UNP    O43741   AAKB2_HUMAN      1    272             
DBREF  6B2E C    2   331  UNP    P54619   AAKG1_HUMAN      2    331             
SEQADV 6B2E MET A  -12  UNP  P54646              INITIATING METHIONINE          
SEQADV 6B2E GLY A  -11  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E SER A  -10  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E SER A   -9  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E HIS A   -8  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E HIS A   -7  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E HIS A   -6  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E HIS A   -5  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E HIS A   -4  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E HIS A   -3  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E SER A   -2  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E GLN A   -1  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E ASP A    0  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E PRO A    1  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E GLY A  271  UNP  P54646    ASP   271 CONFLICT                       
SEQADV 6B2E MET C   -4  UNP  P54619              INITIATING METHIONINE          
SEQADV 6B2E ALA C   -3  UNP  P54619              EXPRESSION TAG                 
SEQADV 6B2E ASP C   -2  UNP  P54619              EXPRESSION TAG                 
SEQADV 6B2E LEU C   -1  UNP  P54619              EXPRESSION TAG                 
SEQADV 6B2E ASN C    0  UNP  P54619              EXPRESSION TAG                 
SEQADV 6B2E TRP C    1  UNP  P54619              EXPRESSION TAG                 
SEQRES   1 A  565  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 A  565  PRO ALA GLU LYS GLN LYS HIS ASP GLY ARG VAL LYS ILE          
SEQRES   3 A  565  GLY HIS TYR VAL LEU GLY ASP THR LEU GLY VAL GLY THR          
SEQRES   4 A  565  PHE GLY LYS VAL LYS ILE GLY GLU HIS GLN LEU THR GLY          
SEQRES   5 A  565  HIS LYS VAL ALA VAL LYS ILE LEU ASN ARG GLN LYS ILE          
SEQRES   6 A  565  ARG SER LEU ASP VAL VAL GLY LYS ILE LYS ARG GLU ILE          
SEQRES   7 A  565  GLN ASN LEU LYS LEU PHE ARG HIS PRO HIS ILE ILE LYS          
SEQRES   8 A  565  LEU TYR GLN VAL ILE SER THR PRO THR ASP PHE PHE MET          
SEQRES   9 A  565  VAL MET GLU TYR VAL SER GLY GLY GLU LEU PHE ASP TYR          
SEQRES  10 A  565  ILE CYS LYS HIS GLY ARG VAL GLU GLU MET GLU ALA ARG          
SEQRES  11 A  565  ARG LEU PHE GLN GLN ILE LEU SER ALA VAL ASP TYR CYS          
SEQRES  12 A  565  HIS ARG HIS MET VAL VAL HIS ARG ASP LEU LYS PRO GLU          
SEQRES  13 A  565  ASN VAL LEU LEU ASP ALA HIS MET ASN ALA LYS ILE ALA          
SEQRES  14 A  565  ASP PHE GLY LEU SER ASN MET MET SER ASP GLY GLU PHE          
SEQRES  15 A  565  LEU ARG TPO SER CYS GLY SER PRO ASN TYR ALA ALA PRO          
SEQRES  16 A  565  GLU VAL ILE SER GLY ARG LEU TYR ALA GLY PRO GLU VAL          
SEQRES  17 A  565  ASP ILE TRP SER CYS GLY VAL ILE LEU TYR ALA LEU LEU          
SEQRES  18 A  565  CYS GLY THR LEU PRO PHE ASP ASP GLU HIS VAL PRO THR          
SEQRES  19 A  565  LEU PHE LYS LYS ILE ARG GLY GLY VAL PHE TYR ILE PRO          
SEQRES  20 A  565  GLU TYR LEU ASN ARG SER VAL ALA THR LEU LEU MET HIS          
SEQRES  21 A  565  MET LEU GLN VAL ASP PRO LEU LYS ARG ALA THR ILE LYS          
SEQRES  22 A  565  ASP ILE ARG GLU HIS GLU TRP PHE LYS GLN GLY LEU PRO          
SEQRES  23 A  565  SER TYR LEU PHE PRO GLU ASP PRO SER TYR ASP ALA ASN          
SEQRES  24 A  565  VAL ILE ASP ASP GLU ALA VAL LYS GLU VAL CYS GLU LYS          
SEQRES  25 A  565  PHE GLU CYS THR GLU SER GLU VAL MET ASN SER LEU TYR          
SEQRES  26 A  565  SER GLY ASP PRO GLN ASP GLN LEU ALA VAL ALA TYR HIS          
SEQRES  27 A  565  LEU ILE ILE ASP ASN ARG ARG ILE MET ASN GLN ALA SER          
SEQRES  28 A  565  GLU PHE TYR LEU ALA SER SER PRO PRO SER GLY SER PHE          
SEQRES  29 A  565  MET ASP ASP SER ALA MET HIS ILE PRO PRO GLY LEU LYS          
SEQRES  30 A  565  PRO HIS PRO GLU ARG MET PRO PRO LEU ILE ALA ASP SER          
SEQRES  31 A  565  PRO LYS ALA ARG CYS PRO LEU ASP ALA LEU ASN THR THR          
SEQRES  32 A  565  LYS PRO LYS SER LEU ALA VAL LYS LYS ALA LYS TRP HIS          
SEQRES  33 A  565  LEU GLY ILE ARG SER GLN SER LYS PRO TYR ASP ILE MET          
SEQRES  34 A  565  ALA GLU VAL TYR ARG ALA MET LYS GLN LEU ASP PHE GLU          
SEQRES  35 A  565  TRP LYS VAL VAL ASN ALA TYR HIS LEU ARG VAL ARG ARG          
SEQRES  36 A  565  LYS ASN PRO VAL THR GLY ASN TYR VAL LYS MET SER LEU          
SEQRES  37 A  565  GLN LEU TYR LEU VAL ASP ASN ARG SER TYR LEU LEU ASP          
SEQRES  38 A  565  PHE LYS SER ILE ASP ASP GLU VAL VAL GLU GLN ARG SER          
SEQRES  39 A  565  GLY SER SER THR PRO GLN ARG SER CYS SER ALA ALA GLY          
SEQRES  40 A  565  LEU HIS ARG PRO ARG SER SER PHE ASP SER THR THR ALA          
SEQRES  41 A  565  GLU SER HIS SER LEU SER GLY SER LEU THR GLY SER LEU          
SEQRES  42 A  565  THR GLY SER THR LEU SER SER VAL SER PRO ARG LEU GLY          
SEQRES  43 A  565  SER HIS THR MET ASP PHE PHE GLU MET CYS ALA SER LEU          
SEQRES  44 A  565  ILE THR THR LEU ALA ARG                                      
SEQRES   1 B  272  MET GLY ASN THR THR SER ASP ARG VAL SER GLY GLU ARG          
SEQRES   2 B  272  HIS GLY ALA LYS ALA ALA ARG SER GLU GLY ALA GLY GLY          
SEQRES   3 B  272  HIS ALA PRO GLY LYS GLU HIS LYS ILE MET VAL GLY SER          
SEQRES   4 B  272  THR ASP ASP PRO SER VAL PHE SER LEU PRO ASP SER LYS          
SEQRES   5 B  272  LEU PRO GLY ASP LYS GLU PHE VAL SER TRP GLN GLN ASP          
SEQRES   6 B  272  LEU GLU ASP SER VAL LYS PRO THR GLN GLN ALA ARG PRO          
SEQRES   7 B  272  THR VAL ILE ARG TRP SER GLU GLY GLY LYS GLU VAL PHE          
SEQRES   8 B  272  ILE SER GLY SER PHE ASN ASN TRP SER THR LYS ILE PRO          
SEQRES   9 B  272  LEU ILE LYS SEP HIS ASN ASP PHE VAL ALA ILE LEU ASP          
SEQRES  10 B  272  LEU PRO GLU GLY GLU HIS GLN TYR LYS PHE PHE VAL ASP          
SEQRES  11 B  272  GLY GLN TRP VAL HIS ASP PRO SER GLU PRO VAL VAL THR          
SEQRES  12 B  272  SER GLN LEU GLY THR ILE ASN ASN LEU ILE HIS VAL LYS          
SEQRES  13 B  272  LYS SER ASP PHE GLU VAL PHE ASP ALA LEU LYS LEU ASP          
SEQRES  14 B  272  SER MET GLU SER SER GLU THR SER CYS ARG ASP LEU SER          
SEQRES  15 B  272  SER SER PRO PRO GLY PRO TYR GLY GLN GLU MET TYR ALA          
SEQRES  16 B  272  PHE ARG SER GLU GLU ARG PHE LYS SER PRO PRO ILE LEU          
SEQRES  17 B  272  PRO PRO HIS LEU LEU GLN VAL ILE LEU ASN LYS ASP THR          
SEQRES  18 B  272  ASN ILE SER CYS ASP PRO ALA LEU LEU PRO GLU PRO ASN          
SEQRES  19 B  272  HIS VAL MET LEU ASN HIS LEU TYR ALA LEU SER ILE LYS          
SEQRES  20 B  272  ASP SER VAL MET VAL LEU SER ALA THR HIS ARG TYR LYS          
SEQRES  21 B  272  LYS LYS TYR VAL THR THR LEU LEU TYR LYS PRO ILE              
SEQRES   1 C  336  MET ALA ASP LEU ASN TRP GLU THR VAL ILE SER SER ASP          
SEQRES   2 C  336  SER SER PRO ALA VAL GLU ASN GLU HIS PRO GLN GLU THR          
SEQRES   3 C  336  PRO GLU SER ASN ASN SER VAL TYR THR SER PHE MET LYS          
SEQRES   4 C  336  SER HIS ARG CYS TYR ASP LEU ILE PRO THR SER SER LYS          
SEQRES   5 C  336  LEU VAL VAL PHE ASP THR SER LEU GLN VAL LYS LYS ALA          
SEQRES   6 C  336  PHE PHE ALA LEU VAL THR ASN GLY VAL ARG ALA ALA PRO          
SEQRES   7 C  336  LEU TRP ASP SER LYS LYS GLN SER PHE VAL GLY MET LEU          
SEQRES   8 C  336  THR ILE THR ASP PHE ILE ASN ILE LEU HIS ARG TYR TYR          
SEQRES   9 C  336  LYS SER ALA LEU VAL GLN ILE TYR GLU LEU GLU GLU HIS          
SEQRES  10 C  336  LYS ILE GLU THR TRP ARG GLU VAL TYR LEU GLN ASP SER          
SEQRES  11 C  336  PHE LYS PRO LEU VAL CYS ILE SER PRO ASN ALA SER LEU          
SEQRES  12 C  336  PHE ASP ALA VAL SER SER LEU ILE ARG ASN LYS ILE HIS          
SEQRES  13 C  336  ARG LEU PRO VAL ILE ASP PRO GLU SER GLY ASN THR LEU          
SEQRES  14 C  336  TYR ILE LEU THR HIS LYS ARG ILE LEU LYS PHE LEU LYS          
SEQRES  15 C  336  LEU PHE ILE THR GLU PHE PRO LYS PRO GLU PHE MET SER          
SEQRES  16 C  336  LYS SER LEU GLU GLU LEU GLN ILE GLY THR TYR ALA ASN          
SEQRES  17 C  336  ILE ALA MET VAL ARG THR THR THR PRO VAL TYR VAL ALA          
SEQRES  18 C  336  LEU GLY ILE PHE VAL GLN HIS ARG VAL SER ALA LEU PRO          
SEQRES  19 C  336  VAL VAL ASP GLU LYS GLY ARG VAL VAL ASP ILE TYR SER          
SEQRES  20 C  336  LYS PHE ASP VAL ILE ASN LEU ALA ALA GLU LYS THR TYR          
SEQRES  21 C  336  ASN ASN LEU ASP VAL SER VAL THR LYS ALA LEU GLN HIS          
SEQRES  22 C  336  ARG SER HIS TYR PHE GLU GLY VAL LEU LYS CYS TYR LEU          
SEQRES  23 C  336  HIS GLU THR LEU GLU THR ILE ILE ASN ARG LEU VAL GLU          
SEQRES  24 C  336  ALA GLU VAL HIS ARG LEU VAL VAL VAL ASP GLU ASN ASP          
SEQRES  25 C  336  VAL VAL LYS GLY ILE VAL SER LEU SER ASP ILE LEU GLN          
SEQRES  26 C  336  ALA LEU VAL LEU THR GLY GLY GLU LYS LYS PRO                  
MODRES 6B2E TPO A  172  THR  MODIFIED RESIDUE                                   
MODRES 6B2E SEP B  108  SER  MODIFIED RESIDUE                                   
HET    TPO  A 172      11                                                       
HET    SEP  B 108      10                                                       
HET    STU  A 601      35                                                       
HET    CG7  A 602      34                                                       
HET    BCD  B 301      77                                                       
HET    AMP  C 400      23                                                       
HET    AMP  C 401      23                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     STU STAUROSPORINE                                                    
HETNAM     CG7 5-{[6-CHLORO-5-(2'-HYDROXY[1,1'-BIPHENYL]-4-YL)-1H-              
HETNAM   2 CG7  IMIDAZO[4,5-B]PYRIDIN-2-YL]OXY}-2-METHYLBENZOIC ACID            
HETNAM     BCD BETA-CYCLODEXTRIN                                                
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     BCD CYCLO-HEPTA-AMYLOSE                                              
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   2  SEP    C3 H8 N O6 P                                                 
FORMUL   4  STU    C28 H26 N4 O3                                                
FORMUL   5  CG7    C26 H18 CL N3 O4                                             
FORMUL   6  BCD    C42 H70 O35                                                  
FORMUL   7  AMP    2(C10 H14 N5 O7 P)                                           
HELIX    1 AA1 ARG A   49  SER A   54  1                                   6    
HELIX    2 AA2 VAL A   57  PHE A   71  1                                  15    
HELIX    3 AA3 LEU A  101  HIS A  108  1                                   8    
HELIX    4 AA4 GLU A  112  HIS A  133  1                                  22    
HELIX    5 AA5 ASP A  157  SER A  161  5                                   5    
HELIX    6 AA6 ALA A  181  GLY A  187  1                                   7    
HELIX    7 AA7 ALA A  191  GLY A  210  1                                  20    
HELIX    8 AA8 HIS A  218  GLY A  229  1                                  12    
HELIX    9 AA9 ASN A  238  LEU A  249  1                                  12    
HELIX   10 AB1 THR A  258  GLU A  264  1                                   7    
HELIX   11 AB2 HIS A  265  GLN A  270  1                                   6    
HELIX   12 AB3 GLU A  279  TYR A  283  5                                   5    
HELIX   13 AB4 GLU A  291  CYS A  302  1                                  12    
HELIX   14 AB5 MET A  308  ASP A  315  1                                   8    
HELIX   15 AB6 TYR A  325  ALA A  338  1                                  14    
HELIX   16 AB7 ALA A  338  LEU A  343  1                                   6    
HELIX   17 AB8 LYS A  412  LEU A  427  1                                  16    
HELIX   18 AB9 SER A  535  LEU A  551  1                                  17    
HELIX   19 AC1 VAL B   60  VAL B   70  1                                  11    
HELIX   20 AC2 ASP B  159  SER B  170  1                                  12    
HELIX   21 AC3 VAL C   28  MET C   33  1                                   6    
HELIX   22 AC4 ARG C   37  ILE C   42  5                                   6    
HELIX   23 AC5 GLN C   56  GLY C   68  1                                  13    
HELIX   24 AC6 THR C   87  TYR C   99  1                                  13    
HELIX   25 AC7 ILE C  106  HIS C  112  1                                   7    
HELIX   26 AC8 LYS C  113  TYR C  121  1                                   9    
HELIX   27 AC9 SER C  137  ASN C  148  1                                  12    
HELIX   28 AD1 THR C  168  ILE C  180  1                                  13    
HELIX   29 AD2 THR C  181  PHE C  183  5                                   3    
HELIX   30 AD3 PRO C  186  LYS C  191  5                                   6    
HELIX   31 AD4 PRO C  212  HIS C  223  1                                  12    
HELIX   32 AD5 PHE C  244  VAL C  246  5                                   3    
HELIX   33 AD6 ILE C  247  GLU C  252  1                                   6    
HELIX   34 AD7 SER C  261  LEU C  266  1                                   6    
HELIX   35 AD8 THR C  284  GLU C  296  1                                  13    
HELIX   36 AD9 LEU C  315  LEU C  324  1                                  10    
SHEET    1 AA1 6 LYS A  12  ILE A  13  0                                        
SHEET    2 AA1 6 TYR A  16  VAL A  24 -1  O  TYR A  16   N  ILE A  13           
SHEET    3 AA1 6 LYS A  29  HIS A  35 -1  O  GLU A  34   N  VAL A  17           
SHEET    4 AA1 6 LYS A  41  ASN A  48 -1  O  VAL A  42   N  GLY A  33           
SHEET    5 AA1 6 ASP A  88  GLU A  94 -1  O  PHE A  89   N  LEU A  47           
SHEET    6 AA1 6 LEU A  79  SER A  84 -1  N  ILE A  83   O  PHE A  90           
SHEET    1 AA2 3 GLY A  99  GLU A 100  0                                        
SHEET    2 AA2 3 VAL A 145  LEU A 147 -1  O  LEU A 147   N  GLY A  99           
SHEET    3 AA2 3 LYS A 154  ILE A 155 -1  O  LYS A 154   N  LEU A 146           
SHEET    1 AA3 2 VAL A 135  VAL A 136  0                                        
SHEET    2 AA3 2 ASN A 162  MET A 163 -1  O  ASN A 162   N  VAL A 136           
SHEET    1 AA4 7 HIS A 404  LEU A 405  0                                        
SHEET    2 AA4 7 TYR B 242  LEU B 244 -1  O  ALA B 243   N  HIS A 404           
SHEET    3 AA4 7 VAL B 250  TYR B 259 -1  O  SER B 254   N  TYR B 242           
SHEET    4 AA4 7 LYS B 262  PRO B 271 -1  O  VAL B 264   N  HIS B 257           
SHEET    5 AA4 7 SER C  45  ASP C  52  1  O  LEU C  48   N  LEU B 267           
SHEET    6 AA4 7 ALA C  72  ASP C  76  1  O  TRP C  75   N  PHE C  51           
SHEET    7 AA4 7 SER C  81  LEU C  86 -1  O  LEU C  86   N  ALA C  72           
SHEET    1 AA5 4 ILE A 407  SER A 409  0                                        
SHEET    2 AA5 4 TYR A 466  SER A 472 -1  O  TYR A 466   N  SER A 409           
SHEET    3 AA5 4 TYR A 451  TYR A 459 -1  N  TYR A 459   O  LEU A 467           
SHEET    4 AA5 4 HIS A 438  LYS A 444 -1  N  LEU A 439   O  LEU A 456           
SHEET    1 AA6 3 ARG B  82  SER B  84  0                                        
SHEET    2 AA6 3 ASP B 111  VAL B 113 -1  O  PHE B 112   N  TRP B  83           
SHEET    3 AA6 3 ILE B 106  LYS B 107 -1  N  ILE B 106   O  VAL B 113           
SHEET    1 AA7 5 ILE B 103  PRO B 104  0                                        
SHEET    2 AA7 5 VAL B  90  SER B  93 -1  N  ILE B  92   O  ILE B 103           
SHEET    3 AA7 5 GLY B 121  VAL B 129 -1  O  PHE B 128   N  PHE B  91           
SHEET    4 AA7 5 ILE B 149  VAL B 155 -1  O  ILE B 153   N  HIS B 123           
SHEET    5 AA7 5 VAL B 141  THR B 143 -1  N  VAL B 142   O  ASN B 150           
SHEET    1 AA8 2 LEU C 153  ILE C 156  0                                        
SHEET    2 AA8 2 THR C 163  LEU C 167 -1  O  TYR C 165   N  VAL C 155           
SHEET    1 AA9 2 ALA C 227  VAL C 231  0                                        
SHEET    2 AA9 2 VAL C 237  SER C 242 -1  O  TYR C 241   N  LEU C 228           
SHEET    1 AB1 3 LYS C 278  CYS C 279  0                                        
SHEET    2 AB1 3 ARG C 299  VAL C 302  1  O  VAL C 301   N  CYS C 279           
SHEET    3 AB1 3 VAL C 313  SER C 314 -1  O  VAL C 313   N  LEU C 300           
LINK         C   ARG A 171                 N   TPO A 172     1555   1555  1.33  
LINK         C   TPO A 172                 N   SER A 173     1555   1555  1.33  
LINK         C   LYS B 107                 N   SEP B 108     1555   1555  1.33  
LINK         C   SEP B 108                 N   HIS B 109     1555   1555  1.33  
SITE     1 AC1 14 LEU A  22  GLY A  23  VAL A  24  VAL A  30                    
SITE     2 AC1 14 ALA A  43  LYS A  45  ILE A  77  GLU A  94                    
SITE     3 AC1 14 TYR A  95  VAL A  96  GLU A 143  ASN A 144                    
SITE     4 AC1 14 LEU A 146  ASP A 157                                          
SITE     1 AC2 10 LEU A  18  GLY A  19  GLY A  28  ILE A  46                    
SITE     2 AC2 10 ASN A  48  ASP A  88  ARG B  82  LYS B 107                    
SITE     3 AC2 10 SEP B 108  VAL B 113                                          
SITE     1 AC3  3 GLN B 145  LEU B 146  ASN B 150                               
SITE     1 AC4 12 PRO A 368  ARG C  70  ILE C 240  SER C 242                    
SITE     2 AC4 12 PHE C 244  ASP C 245  ARG C 269  VAL C 276                    
SITE     3 AC4 12 LEU C 277  VAL C 297  HIS C 298  ARG C 299                    
SITE     1 AC5 13 HIS C 151  THR C 200  ILE C 204  ALA C 205                    
SITE     2 AC5 13 VAL C 225  SER C 226  ALA C 227  PRO C 229                    
SITE     3 AC5 13 HIS C 298  ILE C 312  SER C 314  SER C 316                    
SITE     4 AC5 13 ASP C 317                                                     
CRYST1  113.936  118.848  138.096  90.00  90.00  90.00 P 21 21 21    4          
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      0.008777  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008414  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007241        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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