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Database: PDB
Entry: 4I0P
LinkDB: 4I0P
Original site: 4I0P 
HEADER    IMMUNE SYSTEM                           18-NOV-12   4I0P              
TITLE     HLA-DO IN COMPLEX WITH HLA-DM                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA-DMA PROTEIN;                                           
COMPND   3 CHAIN: A, E;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DM BETA CHAIN;    
COMPND   7 CHAIN: B, F;                                                         
COMPND   8 SYNONYM: MHC CLASS II ANTIGEN DMB, REALLY INTERESTING NEW GENE 7     
COMPND   9 PROTEIN;                                                             
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DO ALPHA CHAIN;   
COMPND  13 CHAIN: C, G;                                                         
COMPND  14 SYNONYM: MHC DN-ALPHA, MHC DZ ALPHA, MHC CLASS II ANTIGEN DOA;       
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DO BETA CHAIN;    
COMPND  18 CHAIN: D, H;                                                         
COMPND  19 SYNONYM: MHC CLASS II ANTIGEN DOB;                                   
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 STRAIN: HOMO SAPIENS;                                                
SOURCE   6 GENE: 3108, HLA-DMA;                                                 
SOURCE   7 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SCHNEIDER-2;                               
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 STRAIN: HOMO SAPIENS;                                                
SOURCE  16 GENE: 3109, DMB, HLA-DMB, RING7;                                     
SOURCE  17 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: SCHNEIDER-2;                               
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 STRAIN: HOMO SAPIENS;                                                
SOURCE  26 GENE: 3111, HLA-DNA, HLA-DOA, HLA-DZA;                               
SOURCE  27 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE  29 EXPRESSION_SYSTEM_STRAIN: SCHNEIDER-2;                               
SOURCE  30 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  31 MOL_ID: 4;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  33 ORGANISM_COMMON: HUMAN;                                              
SOURCE  34 ORGANISM_TAXID: 9606;                                                
SOURCE  35 STRAIN: HOMO SAPIENS;                                                
SOURCE  36 GENE: 3112, HLA-DOB;                                                 
SOURCE  37 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE  38 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE  39 EXPRESSION_SYSTEM_STRAIN: SCHNEIDER-2;                               
SOURCE  40 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    HLA-DM, HLA-DO, HLA-DR, PEPTIDE LOADING, IMMUNE SYSTEM, INHIBITOR,    
KEYWDS   2 ENZYME HLA-DM                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.I.GUCE,S.E.MORTIMER,L.J.STERN                                       
REVDAT   3   29-JUL-20 4I0P    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE                                     
REVDAT   2   16-JAN-13 4I0P    1       JRNL                                     
REVDAT   1   26-DEC-12 4I0P    0                                                
SPRSDE     26-DEC-12 4I0P      3USA                                             
JRNL        AUTH   A.I.GUCE,S.E.MORTIMER,T.YOON,C.A.PAINTER,W.JIANG,            
JRNL        AUTH 2 E.D.MELLINS,L.J.STERN                                        
JRNL        TITL   HLA-DO ACTS AS A SUBSTRATE MIMIC TO INHIBIT HLA-DM BY A      
JRNL        TITL 2 COMPETITIVE MECHANISM.                                       
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  20    90 2013              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   23222639                                                     
JRNL        DOI    10.1038/NSMB.2460                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.91                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 34364                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1856                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 43.9128 -  7.5127    1.00     2710   163  0.1845 0.2050        
REMARK   3     2  7.5127 -  5.9678    0.99     2608   177  0.1946 0.2356        
REMARK   3     3  5.9678 -  5.2148    0.99     2715    89  0.1739 0.2634        
REMARK   3     4  5.2148 -  4.7386    0.99     2575   224  0.1392 0.1965        
REMARK   3     5  4.7386 -  4.3993    0.99     2644   135  0.1432 0.1935        
REMARK   3     6  4.3993 -  4.1402    0.97     2571   137  0.1609 0.1821        
REMARK   3     7  4.1402 -  3.9329    0.93     2490   159  0.1844 0.2563        
REMARK   3     8  3.9329 -  3.7618    0.91     2353   168  0.2098 0.2754        
REMARK   3     9  3.7618 -  3.6171    0.90     2541     0  0.2073 0.0000        
REMARK   3    10  3.6171 -  3.4923    0.89     2306   182  0.2154 0.2832        
REMARK   3    11  3.4923 -  3.3832    0.88     2274   198  0.2402 0.3105        
REMARK   3    12  3.3832 -  3.2865    0.89     2480     0  0.2444 0.0000        
REMARK   3    13  3.2865 -  3.2000    0.89     2241   224  0.2633 0.3511        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.460            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.150           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003          12506                                  
REMARK   3   ANGLE     :  0.853          17035                                  
REMARK   3   CHIRALITY :  0.048           1851                                  
REMARK   3   PLANARITY :  0.004           2204                                  
REMARK   3   DIHEDRAL  : 14.388           4510                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 6                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND RESSEQ 15:90) OR (CHAIN B      
REMARK   3                          AND RESSEQ 5:90)                            
REMARK   3     SELECTION          : (CHAIN E AND RESSEQ 15:90) OR (CHAIN E      
REMARK   3                          AND RESSEQ 5:90)                            
REMARK   3     ATOM PAIRS NUMBER  : 623                                         
REMARK   3     RMSD               : 0.012                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND RESSEQ 91:197                   
REMARK   3     SELECTION          : CHAIN E AND RESSEQ 91:197                   
REMARK   3     ATOM PAIRS NUMBER  : 847                                         
REMARK   3     RMSD               : 0.012                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN B AND RESSEQ 91:138) OR (CHAIN B     
REMARK   3                          AND RESSEQ 147:176)                         
REMARK   3     SELECTION          : (CHAIN F AND RESSEQ 91:138) OR (CHAIN F     
REMARK   3                          AND RESSEQ 147:176)                         
REMARK   3     ATOM PAIRS NUMBER  : 621                                         
REMARK   3     RMSD               : 0.014                                       
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN C AND RESSEQ 5:75) OR (CHAIN D AND   
REMARK   3                          RESSEQ 6:90)                                
REMARK   3     SELECTION          : (CHAIN G AND RESSEQ 5:75) OR (CHAIN H AND   
REMARK   3                          RESSEQ 6:90)                                
REMARK   3     ATOM PAIRS NUMBER  : 1262                                        
REMARK   3     RMSD               : 0.011                                       
REMARK   3   NCS GROUP : 5                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C AND RESSEQ 91:150                   
REMARK   3     SELECTION          : CHAIN G AND RESSEQ 91:150                   
REMARK   3     ATOM PAIRS NUMBER  : 489                                         
REMARK   3     RMSD               : 0.011                                       
REMARK   3   NCS GROUP : 6                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND RESSEQ 91:170                   
REMARK   3     SELECTION          : CHAIN H AND RESSEQ 91:170                   
REMARK   3     ATOM PAIRS NUMBER  : 639                                         
REMARK   3     RMSD               : 0.012                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4I0P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-NOV-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000076157.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.10                               
REMARK 200  MONOCHROMATOR                  : SI-111 DOUBLE CRYSTAL              
REMARK 200  OPTICS                         : PT-COATED TOROIDAL SI MIRROR FOR   
REMARK 200                                   HORIZONTAL AND VERTICAL            
REMARK 200                                   FOCUSSING FOLLOWED BY DOUBLE       
REMARK 200                                   FLAT SI CRYSTAL MONOCHROMATOR      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36565                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.68300                            
REMARK 200  R SYM                      (I) : 0.68300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.68300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.68300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.400                              
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: PDB ENTRIES 2BC4 (DM), 1KLU (DR1)                    
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NA ACETATE, 8% PEG 4K, PH 4.6,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       73.55000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14530 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 33660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15400 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
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     SER B   142                                                      
REMARK 465     SER B   143                                                      
REMARK 465     ALA B   144                                                      
REMARK 465     HIS B   145                                                      
REMARK 465     LEU B   193                                                      
REMARK 465     SER D   192                                                      
REMARK 465     SER F   142                                                      
REMARK 465     SER F   143                                                      
REMARK 465     ALA F   144                                                      
REMARK 465     HIS F   145                                                      
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    SER G    77     N    ARG G    79              2.12            
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    ASP A  38     -133.41     51.04                                   
REMARK 500    GLU A  65      125.82    -39.09                                   
REMARK 500    ASP A  91      113.81    -33.77                                   
REMARK 500    PRO A 141      151.43    -46.49                                   
REMARK 500    SER A 157     -169.93   -109.16                                   
REMARK 500    ASP A 183        2.73     80.20                                   
REMARK 500    PHE B  48       69.96   -118.21                                   
REMARK 500    PRO B 124     -170.20    -68.21                                   
REMARK 500    SER B 167       34.92   -141.31                                   
REMARK 500    TYR B 168      -69.05     58.54                                   
REMARK 500    PHE C  51      -44.05     77.82                                   
REMARK 500    ARG C  53      -64.61     80.61                                   
REMARK 500    PRO C  56     -134.71    -80.11                                   
REMARK 500    GLN C  57      -28.35     74.70                                   
REMARK 500    LEU C  60      -53.68     71.38                                   
REMARK 500    ALA D  13       79.06   -106.70                                   
REMARK 500    ASN D  33     -103.91     49.51                                   
REMARK 500    THR D  90      -75.26   -124.95                                   
REMARK 500    ARG D 105       89.90     23.23                                   
REMARK 500    THR D 106      119.69    -20.76                                   
REMARK 500    HIS D 110       -0.01     68.13                                   
REMARK 500    GLU D 137      105.32    -59.93                                   
REMARK 500    ALA D 140      124.16    148.67                                   
REMARK 500    ARG D 189      -79.39    -77.80                                   
REMARK 500    ALA D 190      -72.74    -91.10                                   
REMARK 500    ASP E  38     -131.58     50.85                                   
REMARK 500    ASP E  91      114.70    -33.83                                   
REMARK 500    PRO E 141      150.43    -47.21                                   
REMARK 500    SER E 157     -169.93   -109.59                                   
REMARK 500    ASP E 183        2.76     81.90                                   
REMARK 500    PHE F  48       70.14   -117.74                                   
REMARK 500    PRO F 124     -171.71    -67.87                                   
REMARK 500    SER F 167      -34.86   -136.55                                   
REMARK 500    TYR F 168      -67.49    124.86                                   
REMARK 500    PHE G  51      -44.00     76.36                                   
REMARK 500    ARG G  53      -64.02     79.21                                   
REMARK 500    PRO G  56     -138.08    -81.14                                   
REMARK 500    GLN G  57      -27.62     74.15                                   
REMARK 500    LEU G  60      -52.85     70.43                                   
REMARK 500    ASN G  78       51.22     -3.19                                   
REMARK 500    ALA H  13       78.69   -106.98                                   
REMARK 500    ASN H  33     -104.10     49.94                                   
REMARK 500    THR H  90      -74.80   -124.32                                   
REMARK 500    ARG H 105       95.91     29.81                                   
REMARK 500    THR H 106      117.45    -23.58                                   
REMARK 500    ALA H 140      120.99    141.94                                   
REMARK 500    ARG H 189      -78.64    -83.62                                   
REMARK 500    ALA H 190       99.54     78.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PHE C   51     ALA C   52                  149.60                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4I0P A   13   200  UNP    Q6ICR9   Q6ICR9_HUMAN    39    226             
DBREF  4I0P B    3   193  UNP    P28068   DMB_HUMAN       21    211             
DBREF  4I0P C    2   181  UNP    P06340   DOA_HUMAN       27    207             
DBREF  4I0P D    4   192  UNP    P13765   DOB_HUMAN       30    218             
DBREF  4I0P E   13   200  UNP    Q6ICR9   Q6ICR9_HUMAN    39    226             
DBREF  4I0P F    3   193  UNP    P28068   DMB_HUMAN       21    211             
DBREF  4I0P G    2   181  UNP    P06340   DOA_HUMAN       27    207             
DBREF  4I0P H    4   192  UNP    P13765   DOB_HUMAN       30    218             
SEQRES   1 A  188  LEU GLN ASN HIS THR PHE LEU HIS THR VAL TYR CYS GLN          
SEQRES   2 A  188  ASP GLY SER PRO SER VAL GLY LEU SER GLU ALA TYR ASP          
SEQRES   3 A  188  GLU ASP GLN LEU PHE PHE PHE ASP PHE SER GLN ASN THR          
SEQRES   4 A  188  ARG VAL PRO ARG LEU PRO GLU PHE ALA ASP TRP ALA GLN          
SEQRES   5 A  188  GLU GLN GLY ASP ALA PRO ALA ILE LEU PHE ASP LYS GLU          
SEQRES   6 A  188  PHE CYS GLU TRP MET ILE GLN GLN ILE GLY PRO LYS LEU          
SEQRES   7 A  188  ASP GLY LYS ILE PRO VAL SER ARG GLY PHE PRO ILE ALA          
SEQRES   8 A  188  GLU VAL PHE THR LEU LYS PRO LEU GLU PHE GLY LYS PRO          
SEQRES   9 A  188  ASN THR LEU VAL CYS PHE VAL SER ASN LEU PHE PRO PRO          
SEQRES  10 A  188  MET LEU THR VAL ASN TRP GLN HIS HIS SER VAL PRO VAL          
SEQRES  11 A  188  GLU GLY PHE GLY PRO THR PHE VAL SER ALA VAL ASP GLY          
SEQRES  12 A  188  LEU SER PHE GLN ALA PHE SER TYR LEU ASN PHE THR PRO          
SEQRES  13 A  188  GLU PRO SER ASP ILE PHE SER CYS ILE VAL THR HIS GLU          
SEQRES  14 A  188  ILE ASP ARG TYR THR ALA ILE ALA TYR TRP VAL PRO ARG          
SEQRES  15 A  188  ASN ALA LEU PRO SER ASP                                      
SEQRES   1 B  191  PHE VAL ALA HIS VAL GLU SER THR CYS LEU LEU ASP ASP          
SEQRES   2 B  191  ALA GLY THR PRO LYS ASP PHE THR TYR CYS ILE SER PHE          
SEQRES   3 B  191  ASN LYS ASP LEU LEU THR CYS TRP ASP PRO GLU GLU ASN          
SEQRES   4 B  191  LYS MET ALA PRO CYS GLU PHE GLY VAL LEU ASN SER LEU          
SEQRES   5 B  191  ALA ASN VAL LEU SER GLN HIS LEU ASN GLN LYS ASP THR          
SEQRES   6 B  191  LEU MET GLN ARG LEU ARG ASN GLY LEU GLN ASN CYS ALA          
SEQRES   7 B  191  THR HIS THR GLN PRO PHE TRP GLY SER LEU THR ASN ARG          
SEQRES   8 B  191  THR ARG PRO PRO SER VAL GLN VAL ALA LYS THR THR PRO          
SEQRES   9 B  191  PHE ASN THR ARG GLU PRO VAL MET LEU ALA CYS TYR VAL          
SEQRES  10 B  191  TRP GLY PHE TYR PRO ALA GLU VAL THR ILE THR TRP ARG          
SEQRES  11 B  191  LYS ASN GLY LYS LEU VAL MET PRO HIS SER SER ALA HIS          
SEQRES  12 B  191  LYS THR ALA GLN PRO ASN GLY ASP TRP THR TYR GLN THR          
SEQRES  13 B  191  LEU SER HIS LEU ALA LEU THR PRO SER TYR GLY ASP THR          
SEQRES  14 B  191  TYR THR CYS VAL VAL GLU HIS ILE GLY ALA PRO GLU PRO          
SEQRES  15 B  191  ILE LEU ARG ASP TRP THR PRO GLY LEU                          
SEQRES   1 C  181  LYS ALA ASP HIS MET GLY SER TYR GLY PRO ALA PHE TYR          
SEQRES   2 C  181  GLN SER TYR GLY ALA SER GLY GLN PHE THR HIS GLU PHE          
SEQRES   3 C  181  ASP GLU GLU GLN LEU PHE SER VAL ASP LEU LYS LYS SER          
SEQRES   4 C  181  GLU ALA VAL TRP ARG LEU PRO GLU PHE GLY ASP PHE ALA          
SEQRES   5 C  181  ARG PHE ASP PRO GLN GLY GLY LEU ALA GLY ILE ALA ALA          
SEQRES   6 C  181  ILE LYS ALA HIS LEU ASP ILE LEU VAL GLU ARG SER ASN          
SEQRES   7 C  181  ARG SER ARG ALA ILE ASN VAL PRO PRO ARG VAL THR VAL          
SEQRES   8 C  181  LEU PRO LYS SER ARG VAL GLU LEU GLY GLN PRO ASN ILE          
SEQRES   9 C  181  LEU ILE CYS ILE VAL ASP ASN ILE PHE PRO PRO VAL ILE          
SEQRES  10 C  181  ASN ILE THR TRP LEU ARG ASN GLY GLN THR VAL THR GLU          
SEQRES  11 C  181  GLY VAL ALA GLN THR SER PHE TYR SER GLN PRO ASP HIS          
SEQRES  12 C  181  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE VAL PRO SER          
SEQRES  13 C  181  ALA GLU ASP VAL TYR ASP CYS GLN VAL GLU HIS TRP GLY          
SEQRES  14 C  181  LEU ASP ALA PRO LEU LEU ARG HIS TRP GLU LEU GLN              
SEQRES   1 D  189  PRO GLU ASP PHE VAL ILE GLN ALA LYS ALA ASP CYS TYR          
SEQRES   2 D  189  PHE THR ASN GLY THR GLU LYS VAL GLN PHE VAL VAL ARG          
SEQRES   3 D  189  PHE ILE PHE ASN LEU GLU GLU TYR VAL ARG PHE ASP SER          
SEQRES   4 D  189  ASP VAL GLY MET PHE VAL ALA LEU THR LYS LEU GLY GLN          
SEQRES   5 D  189  PRO ASP ALA GLU GLN TRP ASN SER ARG LEU ASP LEU LEU          
SEQRES   6 D  189  GLU ARG SER ARG GLN ALA VAL ASP GLY VAL CYS ARG HIS          
SEQRES   7 D  189  ASN TYR ARG LEU GLY ALA PRO PHE THR VAL GLY ARG LYS          
SEQRES   8 D  189  VAL GLN PRO GLU VAL THR VAL TYR PRO GLU ARG THR PRO          
SEQRES   9 D  189  LEU LEU HIS GLN HIS ASN LEU LEU HIS CYS SER VAL THR          
SEQRES  10 D  189  GLY PHE TYR PRO GLY ASP ILE LYS ILE LYS TRP PHE LEU          
SEQRES  11 D  189  ASN GLY GLN GLU GLU ARG ALA GLY VAL MET SER THR GLY          
SEQRES  12 D  189  PRO ILE ARG ASN GLY ASP TRP THR PHE GLN THR VAL VAL          
SEQRES  13 D  189  MET LEU GLU MET THR PRO GLU LEU GLY HIS VAL TYR THR          
SEQRES  14 D  189  CYS LEU VAL ASP HIS SER SER LEU LEU SER PRO VAL SER          
SEQRES  15 D  189  VAL GLU TRP ARG ALA GLN SER                                  
SEQRES   1 E  188  LEU GLN ASN HIS THR PHE LEU HIS THR VAL TYR CYS GLN          
SEQRES   2 E  188  ASP GLY SER PRO SER VAL GLY LEU SER GLU ALA TYR ASP          
SEQRES   3 E  188  GLU ASP GLN LEU PHE PHE PHE ASP PHE SER GLN ASN THR          
SEQRES   4 E  188  ARG VAL PRO ARG LEU PRO GLU PHE ALA ASP TRP ALA GLN          
SEQRES   5 E  188  GLU GLN GLY ASP ALA PRO ALA ILE LEU PHE ASP LYS GLU          
SEQRES   6 E  188  PHE CYS GLU TRP MET ILE GLN GLN ILE GLY PRO LYS LEU          
SEQRES   7 E  188  ASP GLY LYS ILE PRO VAL SER ARG GLY PHE PRO ILE ALA          
SEQRES   8 E  188  GLU VAL PHE THR LEU LYS PRO LEU GLU PHE GLY LYS PRO          
SEQRES   9 E  188  ASN THR LEU VAL CYS PHE VAL SER ASN LEU PHE PRO PRO          
SEQRES  10 E  188  MET LEU THR VAL ASN TRP GLN HIS HIS SER VAL PRO VAL          
SEQRES  11 E  188  GLU GLY PHE GLY PRO THR PHE VAL SER ALA VAL ASP GLY          
SEQRES  12 E  188  LEU SER PHE GLN ALA PHE SER TYR LEU ASN PHE THR PRO          
SEQRES  13 E  188  GLU PRO SER ASP ILE PHE SER CYS ILE VAL THR HIS GLU          
SEQRES  14 E  188  ILE ASP ARG TYR THR ALA ILE ALA TYR TRP VAL PRO ARG          
SEQRES  15 E  188  ASN ALA LEU PRO SER ASP                                      
SEQRES   1 F  191  PHE VAL ALA HIS VAL GLU SER THR CYS LEU LEU ASP ASP          
SEQRES   2 F  191  ALA GLY THR PRO LYS ASP PHE THR TYR CYS ILE SER PHE          
SEQRES   3 F  191  ASN LYS ASP LEU LEU THR CYS TRP ASP PRO GLU GLU ASN          
SEQRES   4 F  191  LYS MET ALA PRO CYS GLU PHE GLY VAL LEU ASN SER LEU          
SEQRES   5 F  191  ALA ASN VAL LEU SER GLN HIS LEU ASN GLN LYS ASP THR          
SEQRES   6 F  191  LEU MET GLN ARG LEU ARG ASN GLY LEU GLN ASN CYS ALA          
SEQRES   7 F  191  THR HIS THR GLN PRO PHE TRP GLY SER LEU THR ASN ARG          
SEQRES   8 F  191  THR ARG PRO PRO SER VAL GLN VAL ALA LYS THR THR PRO          
SEQRES   9 F  191  PHE ASN THR ARG GLU PRO VAL MET LEU ALA CYS TYR VAL          
SEQRES  10 F  191  TRP GLY PHE TYR PRO ALA GLU VAL THR ILE THR TRP ARG          
SEQRES  11 F  191  LYS ASN GLY LYS LEU VAL MET PRO HIS SER SER ALA HIS          
SEQRES  12 F  191  LYS THR ALA GLN PRO ASN GLY ASP TRP THR TYR GLN THR          
SEQRES  13 F  191  LEU SER HIS LEU ALA LEU THR PRO SER TYR GLY ASP THR          
SEQRES  14 F  191  TYR THR CYS VAL VAL GLU HIS ILE GLY ALA PRO GLU PRO          
SEQRES  15 F  191  ILE LEU ARG ASP TRP THR PRO GLY LEU                          
SEQRES   1 G  181  LYS ALA ASP HIS MET GLY SER TYR GLY PRO ALA PHE TYR          
SEQRES   2 G  181  GLN SER TYR GLY ALA SER GLY GLN PHE THR HIS GLU PHE          
SEQRES   3 G  181  ASP GLU GLU GLN LEU PHE SER VAL ASP LEU LYS LYS SER          
SEQRES   4 G  181  GLU ALA VAL TRP ARG LEU PRO GLU PHE GLY ASP PHE ALA          
SEQRES   5 G  181  ARG PHE ASP PRO GLN GLY GLY LEU ALA GLY ILE ALA ALA          
SEQRES   6 G  181  ILE LYS ALA HIS LEU ASP ILE LEU VAL GLU ARG SER ASN          
SEQRES   7 G  181  ARG SER ARG ALA ILE ASN VAL PRO PRO ARG VAL THR VAL          
SEQRES   8 G  181  LEU PRO LYS SER ARG VAL GLU LEU GLY GLN PRO ASN ILE          
SEQRES   9 G  181  LEU ILE CYS ILE VAL ASP ASN ILE PHE PRO PRO VAL ILE          
SEQRES  10 G  181  ASN ILE THR TRP LEU ARG ASN GLY GLN THR VAL THR GLU          
SEQRES  11 G  181  GLY VAL ALA GLN THR SER PHE TYR SER GLN PRO ASP HIS          
SEQRES  12 G  181  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE VAL PRO SER          
SEQRES  13 G  181  ALA GLU ASP VAL TYR ASP CYS GLN VAL GLU HIS TRP GLY          
SEQRES  14 G  181  LEU ASP ALA PRO LEU LEU ARG HIS TRP GLU LEU GLN              
SEQRES   1 H  189  PRO GLU ASP PHE VAL ILE GLN ALA LYS ALA ASP CYS TYR          
SEQRES   2 H  189  PHE THR ASN GLY THR GLU LYS VAL GLN PHE VAL VAL ARG          
SEQRES   3 H  189  PHE ILE PHE ASN LEU GLU GLU TYR VAL ARG PHE ASP SER          
SEQRES   4 H  189  ASP VAL GLY MET PHE VAL ALA LEU THR LYS LEU GLY GLN          
SEQRES   5 H  189  PRO ASP ALA GLU GLN TRP ASN SER ARG LEU ASP LEU LEU          
SEQRES   6 H  189  GLU ARG SER ARG GLN ALA VAL ASP GLY VAL CYS ARG HIS          
SEQRES   7 H  189  ASN TYR ARG LEU GLY ALA PRO PHE THR VAL GLY ARG LYS          
SEQRES   8 H  189  VAL GLN PRO GLU VAL THR VAL TYR PRO GLU ARG THR PRO          
SEQRES   9 H  189  LEU LEU HIS GLN HIS ASN LEU LEU HIS CYS SER VAL THR          
SEQRES  10 H  189  GLY PHE TYR PRO GLY ASP ILE LYS ILE LYS TRP PHE LEU          
SEQRES  11 H  189  ASN GLY GLN GLU GLU ARG ALA GLY VAL MET SER THR GLY          
SEQRES  12 H  189  PRO ILE ARG ASN GLY ASP TRP THR PHE GLN THR VAL VAL          
SEQRES  13 H  189  MET LEU GLU MET THR PRO GLU LEU GLY HIS VAL TYR THR          
SEQRES  14 H  189  CYS LEU VAL ASP HIS SER SER LEU LEU SER PRO VAL SER          
SEQRES  15 H  189  VAL GLU TRP ARG ALA GLN SER                                  
MODRES 4I0P ASN D   19  ASN  GLYCOSYLATION SITE                                 
MODRES 4I0P ASN C  118  ASN  GLYCOSYLATION SITE                                 
MODRES 4I0P ASN G   78  ASN  GLYCOSYLATION SITE                                 
MODRES 4I0P ASN E   15  ASN  GLYCOSYLATION SITE                                 
MODRES 4I0P ASN A   15  ASN  GLYCOSYLATION SITE                                 
MODRES 4I0P ASN G  118  ASN  GLYCOSYLATION SITE                                 
MODRES 4I0P ASN H   19  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 301      14                                                       
HET    NAG  C 201      14                                                       
HET    NAG  D 201      14                                                       
HET    GOL  D 202       6                                                       
HET    NAG  E 301      14                                                       
HET    GOL  F 201       6                                                       
HET    NAG  G 201      14                                                       
HET    NAG  G 202      14                                                       
HET    NAG  H 201      14                                                       
HET    PGE  H 202      10                                                       
HET    ACT  H 203       4                                                       
HET    GOL  H 204       6                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     GOL GLYCEROL                                                         
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     ACT ACETATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   9  NAG    7(C8 H15 N O6)                                               
FORMUL  12  GOL    3(C3 H8 O3)                                                  
FORMUL  18  PGE    C6 H14 O4                                                    
FORMUL  19  ACT    C2 H3 O2 1-                                                  
FORMUL  21  HOH   *6(H2 O)                                                      
HELIX    1   1 LEU A   56  GLN A   64  5                                   9    
HELIX    2   2 ASP A   68  ILE A   86  1                                  19    
HELIX    3   3 LEU B   51  GLN B   64  1                                  14    
HELIX    4   4 ASP B   66  ASN B   74  1                                   9    
HELIX    5   5 ASN B   74  ASN B   92  1                                  19    
HELIX    6   6 TYR C   16  ALA C   18  5                                   3    
HELIX    7   7 LEU C   45  GLY C   49  5                                   5    
HELIX    8   8 LEU C   60  HIS C   69  1                                  10    
HELIX    9   9 HIS C   69  SER C   77  1                                   9    
HELIX   10  10 THR D   51  LEU D   53  5                                   3    
HELIX   11  11 GLY D   54  ARG D   64  1                                  11    
HELIX   12  12 ARG D   64  VAL D   78  1                                  15    
HELIX   13  13 VAL D   78  ALA D   87  1                                  10    
HELIX   14  14 PRO D   88  THR D   90  5                                   3    
HELIX   15  15 LEU E   56  ALA E   63  5                                   8    
HELIX   16  16 ASP E   68  ILE E   86  1                                  19    
HELIX   17  17 LEU F   51  GLN F   64  1                                  14    
HELIX   18  18 LYS F   65  ASN F   74  1                                  10    
HELIX   19  19 ASN F   74  GLN F   84  1                                  11    
HELIX   20  20 TYR G   16  ALA G   18  5                                   3    
HELIX   21  21 LEU G   45  GLY G   49  5                                   5    
HELIX   22  22 LEU G   60  HIS G   69  1                                  10    
HELIX   23  23 HIS G   69  SER G   77  1                                   9    
HELIX   24  24 THR H   51  LEU H   53  5                                   3    
HELIX   25  25 GLY H   54  ARG H   64  1                                  11    
HELIX   26  26 ARG H   64  VAL H   78  1                                  15    
HELIX   27  27 VAL H   78  ALA H   87  1                                  10    
HELIX   28  28 PRO H   88  THR H   90  5                                   3    
SHEET    1   A 8 THR A  51  PRO A  54  0                                        
SHEET    2   A 8 ASP A  40  ASP A  46 -1  N  PHE A  44   O  VAL A  53           
SHEET    3   A 8 VAL A  31  TYR A  37 -1  N  GLU A  35   O  PHE A  43           
SHEET    4   A 8 ASN A  15  GLN A  25 -1  N  TYR A  23   O  GLY A  32           
SHEET    5   A 8 VAL B   4  ASP B  14 -1  O  SER B   9   N  HIS A  20           
SHEET    6   A 8 PRO B  19  PHE B  28 -1  O  LYS B  20   N  LEU B  12           
SHEET    7   A 8 ASP B  31  ASP B  37 -1  O  THR B  34   N  ILE B  26           
SHEET    8   A 8 LYS B  42  PRO B  45 -1  O  ALA B  44   N  CYS B  35           
SHEET    1   B 9 VAL A  96  ARG A  98  0                                        
SHEET    2   B 9 GLU C  40  TRP C  43  1  O  ALA C  41   N  ARG A  98           
SHEET    3   B 9 GLU C  29  ASP C  35 -1  N  SER C  33   O  VAL C  42           
SHEET    4   B 9 SER C  19  PHE C  26 -1  N  PHE C  26   O  GLU C  29           
SHEET    5   B 9 HIS C   5  GLN C  14 -1  N  SER C   8   O  GLU C  25           
SHEET    6   B 9 VAL D   8  THR D  18 -1  O  CYS D  15   N  GLY C   7           
SHEET    7   B 9 LYS D  23  PHE D  32 -1  O  VAL D  27   N  ASP D  14           
SHEET    8   B 9 GLU D  35  ASP D  41 -1  O  GLU D  35   N  PHE D  32           
SHEET    9   B 9 PHE D  47  ALA D  49 -1  O  VAL D  48   N  ARG D  39           
SHEET    1   C 4 ILE A 102  THR A 107  0                                        
SHEET    2   C 4 ASN A 117  LEU A 126 -1  O  SER A 124   N  ILE A 102           
SHEET    3   C 4 SER A 157  PHE A 166 -1  O  SER A 162   N  CYS A 121           
SHEET    4   C 4 PHE A 149  VAL A 153 -1  N  SER A 151   O  GLN A 159           
SHEET    1   D 4 PRO A 141  VAL A 142  0                                        
SHEET    2   D 4 LEU A 131  HIS A 137 -1  N  TRP A 135   O  VAL A 142           
SHEET    3   D 4 PHE A 174  HIS A 180 -1  O  ILE A 177   N  ASN A 134           
SHEET    4   D 4 TYR A 185  TRP A 191 -1  O  ALA A 187   N  VAL A 178           
SHEET    1   E 4 SER B  98  THR B 104  0                                        
SHEET    2   E 4 VAL B 113  PHE B 122 -1  O  TYR B 118   N  GLN B 100           
SHEET    3   E 4 TYR B 156  LEU B 164 -1  O  SER B 160   N  CYS B 117           
SHEET    4   E 4 GLN B 149  PRO B 150 -1  N  GLN B 149   O  GLN B 157           
SHEET    1   F 4 LEU B 137  VAL B 138  0                                        
SHEET    2   F 4 THR B 128  LYS B 133 -1  N  TRP B 131   O  VAL B 138           
SHEET    3   F 4 TYR B 172  GLU B 177 -1  O  THR B 173   N  ARG B 132           
SHEET    4   F 4 ILE B 185  TRP B 189 -1  O  ARG B 187   N  CYS B 174           
SHEET    1   G 4 ARG C  88  PRO C  93  0                                        
SHEET    2   G 4 ASN C 103  ILE C 112 -1  O  ILE C 108   N  THR C  90           
SHEET    3   G 4 PHE C 145  PHE C 153 -1  O  LEU C 151   N  LEU C 105           
SHEET    4   G 4 ALA C 133  GLN C 134 -1  N  ALA C 133   O  TYR C 150           
SHEET    1   H 4 ARG C  88  PRO C  93  0                                        
SHEET    2   H 4 ASN C 103  ILE C 112 -1  O  ILE C 108   N  THR C  90           
SHEET    3   H 4 PHE C 145  PHE C 153 -1  O  LEU C 151   N  LEU C 105           
SHEET    4   H 4 TYR C 138  SER C 139 -1  N  TYR C 138   O  ARG C 146           
SHEET    1   I 4 GLN C 126  VAL C 128  0                                        
SHEET    2   I 4 ASN C 118  ARG C 123 -1  N  ARG C 123   O  GLN C 126           
SHEET    3   I 4 TYR C 161  GLU C 166 -1  O  GLU C 166   N  ASN C 118           
SHEET    4   I 4 LEU C 174  TRP C 178 -1  O  ARG C 176   N  CYS C 163           
SHEET    1   J 4 GLU D  98  PRO D 103  0                                        
SHEET    2   J 4 ASN D 113  PHE D 122 -1  O  HIS D 116   N  TYR D 102           
SHEET    3   J 4 PHE D 155  MET D 163 -1  O  PHE D 155   N  PHE D 122           
SHEET    4   J 4 VAL D 142  MET D 143 -1  N  MET D 143   O  MET D 160           
SHEET    1   K 4 GLU D  98  PRO D 103  0                                        
SHEET    2   K 4 ASN D 113  PHE D 122 -1  O  HIS D 116   N  TYR D 102           
SHEET    3   K 4 PHE D 155  MET D 163 -1  O  PHE D 155   N  PHE D 122           
SHEET    4   K 4 ILE D 148  ARG D 149 -1  N  ILE D 148   O  GLN D 156           
SHEET    1   L 4 GLN D 136  GLU D 137  0                                        
SHEET    2   L 4 LYS D 128  LEU D 133 -1  N  LEU D 133   O  GLN D 136           
SHEET    3   L 4 TYR D 171  ASP D 176 -1  O  LEU D 174   N  LYS D 130           
SHEET    4   L 4 VAL D 184  TRP D 188 -1  O  VAL D 184   N  VAL D 175           
SHEET    1   M 8 THR E  51  PRO E  54  0                                        
SHEET    2   M 8 ASP E  40  ASP E  46 -1  N  PHE E  44   O  VAL E  53           
SHEET    3   M 8 VAL E  31  TYR E  37 -1  N  GLU E  35   O  PHE E  43           
SHEET    4   M 8 ASN E  15  GLN E  25 -1  N  LEU E  19   O  ALA E  36           
SHEET    5   M 8 VAL F   4  ASP F  14 -1  O  SER F   9   N  HIS E  20           
SHEET    6   M 8 PRO F  19  PHE F  28 -1  O  LYS F  20   N  LEU F  12           
SHEET    7   M 8 ASP F  31  ASP F  37 -1  O  TRP F  36   N  TYR F  24           
SHEET    8   M 8 LYS F  42  PRO F  45 -1  O  ALA F  44   N  CYS F  35           
SHEET    1   N 9 VAL E  96  ARG E  98  0                                        
SHEET    2   N 9 GLU G  40  TRP G  43  1  O  ALA G  41   N  ARG E  98           
SHEET    3   N 9 GLU G  29  ASP G  35 -1  N  SER G  33   O  VAL G  42           
SHEET    4   N 9 SER G  19  PHE G  26 -1  N  PHE G  26   O  GLU G  29           
SHEET    5   N 9 HIS G   5  GLN G  14 -1  N  SER G   8   O  GLU G  25           
SHEET    6   N 9 VAL H   8  THR H  18 -1  O  CYS H  15   N  GLY G   7           
SHEET    7   N 9 LYS H  23  PHE H  32 -1  O  VAL H  27   N  ASP H  14           
SHEET    8   N 9 GLU H  35  ASP H  41 -1  O  GLU H  35   N  PHE H  32           
SHEET    9   N 9 PHE H  47  ALA H  49 -1  O  VAL H  48   N  ARG H  39           
SHEET    1   O 4 ILE E 102  THR E 107  0                                        
SHEET    2   O 4 ASN E 117  LEU E 126 -1  O  VAL E 120   N  PHE E 106           
SHEET    3   O 4 PHE E 158  PHE E 166 -1  O  PHE E 166   N  ASN E 117           
SHEET    4   O 4 THR E 148  ALA E 152 -1  N  SER E 151   O  GLN E 159           
SHEET    1   P 4 PRO E 141  VAL E 142  0                                        
SHEET    2   P 4 LEU E 131  HIS E 137 -1  N  TRP E 135   O  VAL E 142           
SHEET    3   P 4 PHE E 174  HIS E 180 -1  O  THR E 179   N  THR E 132           
SHEET    4   P 4 TYR E 185  TRP E 191 -1  O  TYR E 185   N  HIS E 180           
SHEET    1   Q 4 SER F  98  THR F 104  0                                        
SHEET    2   Q 4 VAL F 113  PHE F 122 -1  O  ALA F 116   N  ALA F 102           
SHEET    3   Q 4 TYR F 156  LEU F 164 -1  O  LEU F 162   N  LEU F 115           
SHEET    4   Q 4 GLN F 149  PRO F 150 -1  N  GLN F 149   O  GLN F 157           
SHEET    1   R 4 LEU F 137  VAL F 138  0                                        
SHEET    2   R 4 THR F 128  LYS F 133 -1  N  TRP F 131   O  VAL F 138           
SHEET    3   R 4 TYR F 172  GLU F 177 -1  O  VAL F 175   N  THR F 130           
SHEET    4   R 4 ILE F 185  TRP F 189 -1  O  ILE F 185   N  VAL F 176           
SHEET    1   S 4 ARG G  88  PRO G  93  0                                        
SHEET    2   S 4 ASN G 103  ILE G 112 -1  O  ILE G 108   N  THR G  90           
SHEET    3   S 4 PHE G 145  PHE G 153 -1  O  PHE G 153   N  ASN G 103           
SHEET    4   S 4 ALA G 133  GLN G 134 -1  N  ALA G 133   O  TYR G 150           
SHEET    1   T 4 ARG G  88  PRO G  93  0                                        
SHEET    2   T 4 ASN G 103  ILE G 112 -1  O  ILE G 108   N  THR G  90           
SHEET    3   T 4 PHE G 145  PHE G 153 -1  O  PHE G 153   N  ASN G 103           
SHEET    4   T 4 TYR G 138  SER G 139 -1  N  TYR G 138   O  ARG G 146           
SHEET    1   U 4 GLN G 126  VAL G 128  0                                        
SHEET    2   U 4 ASN G 118  ARG G 123 -1  N  ARG G 123   O  GLN G 126           
SHEET    3   U 4 TYR G 161  GLU G 166 -1  O  GLU G 166   N  ASN G 118           
SHEET    4   U 4 LEU G 174  TRP G 178 -1  O  LEU G 174   N  VAL G 165           
SHEET    1   V 4 GLU H  98  PRO H 103  0                                        
SHEET    2   V 4 ASN H 113  PHE H 122 -1  O  HIS H 116   N  TYR H 102           
SHEET    3   V 4 PHE H 155  MET H 163 -1  O  PHE H 155   N  PHE H 122           
SHEET    4   V 4 VAL H 142  SER H 144 -1  N  MET H 143   O  MET H 160           
SHEET    1   W 4 GLU H  98  PRO H 103  0                                        
SHEET    2   W 4 ASN H 113  PHE H 122 -1  O  HIS H 116   N  TYR H 102           
SHEET    3   W 4 PHE H 155  MET H 163 -1  O  PHE H 155   N  PHE H 122           
SHEET    4   W 4 ILE H 148  ARG H 149 -1  N  ILE H 148   O  GLN H 156           
SHEET    1   X 4 GLN H 136  GLU H 137  0                                        
SHEET    2   X 4 LYS H 128  LEU H 133 -1  N  LEU H 133   O  GLN H 136           
SHEET    3   X 4 TYR H 171  ASP H 176 -1  O  ASP H 176   N  LYS H 128           
SHEET    4   X 4 VAL H 184  TRP H 188 -1  O  VAL H 184   N  VAL H 175           
SSBOND   1 CYS A   24    CYS A   79                          1555   1555  2.03  
SSBOND   2 CYS A  121    CYS A  176                          1555   1555  2.03  
SSBOND   3 CYS B   11    CYS B   79                          1555   1555  2.03  
SSBOND   4 CYS B   25    CYS B   35                          1555   1555  2.04  
SSBOND   5 CYS B  117    CYS B  174                          1555   1555  2.03  
SSBOND   6 CYS C  107    CYS C  163                          1555   1555  2.03  
SSBOND   7 CYS D   15    CYS D   79                          1555   1555  2.03  
SSBOND   8 CYS D  117    CYS D  173                          1555   1555  2.03  
SSBOND   9 CYS E   24    CYS E   79                          1555   1555  2.03  
SSBOND  10 CYS E  121    CYS E  176                          1555   1555  2.03  
SSBOND  11 CYS F   11    CYS F   79                          1555   1555  2.03  
SSBOND  12 CYS F   25    CYS F   35                          1555   1555  2.03  
SSBOND  13 CYS F  117    CYS F  174                          1555   1555  2.03  
SSBOND  14 CYS G  107    CYS G  163                          1555   1555  2.03  
SSBOND  15 CYS H   15    CYS H   79                          1555   1555  2.03  
SSBOND  16 CYS H  117    CYS H  173                          1555   1555  2.03  
LINK         ND2 ASN A  15                 C1  NAG A 301     1555   1555  1.45  
LINK         ND2 ASN C 118                 C1  NAG C 201     1555   1555  1.44  
LINK         ND2 ASN D  19                 C1  NAG D 201     1555   1555  1.44  
LINK         ND2 ASN E  15                 C1  NAG E 301     1555   1555  1.44  
LINK         ND2 ASN G  78                 C1  NAG G 201     1555   1555  1.44  
LINK         ND2 ASN G 118                 C1  NAG G 202     1555   1555  1.45  
LINK         ND2 ASN H  19                 C1  NAG H 201     1555   1555  1.47  
CISPEP   1 SER A   28    PRO A   29          0        -5.26                     
CISPEP   2 PHE A  127    PRO A  128          0         0.24                     
CISPEP   3 TYR B  123    PRO B  124          0        -3.69                     
CISPEP   4 PHE C  113    PRO C  114          0         0.00                     
CISPEP   5 TYR D  123    PRO D  124          0         3.08                     
CISPEP   6 ARG D  189    ALA D  190          0         0.97                     
CISPEP   7 SER E   28    PRO E   29          0        -5.75                     
CISPEP   8 PHE E  127    PRO E  128          0        -0.06                     
CISPEP   9 SER E  199    ASP E  200          0        -3.07                     
CISPEP  10 TYR F  123    PRO F  124          0        -2.92                     
CISPEP  11 PHE G  113    PRO G  114          0        -0.67                     
CISPEP  12 TYR H  123    PRO H  124          0         2.80                     
CRYST1   83.260  147.100   95.959  90.00 106.49  90.00 P 1 21 1      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      0.012011  0.000000  0.003555        0.00000                         
SCALE2      0.000000  0.006798  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010868        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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