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Database: PDB
Entry: 2K2D
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Original site: 2K2D 
HEADER    METAL BINDING PROTEIN                   31-MAR-08   2K2D              
TITLE     SOLUTION NMR STRUCTURE OF C-TERMINAL DOMAIN OF HUMAN PIRH2. NORTHEAST 
TITLE    2 STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET HT2C                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RING FINGER AND CHY ZINC FINGER DOMAIN-CONTAINING PROTEIN  
COMPND   3 1;                                                                   
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: C-TERMINAL DOMAIN: RESIDUES 187-261;                       
COMPND   6 SYNONYM: ZINC FINGER PROTEIN 363, CH-RICH-INTERACTING MATCH WITH     
COMPND   7 PLAG1, ANDROGEN RECEPTOR N-TERMINAL-INTERACTING PROTEIN, P53-INDUCED 
COMPND   8 RING-H2 PROTEIN, HPIRH2, RING FINGER PROTEIN 199;                    
COMPND   9 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: RCHY1, ARNIP, CHIMP, PIRH2, RNF199, ZNF363;                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    ZINC-BINDING PROTEIN, CYTOPLASM, METAL-BINDING, NUCLEUS, ZINC-FINGER, 
KEYWDS   2 METAL BINDING PROTEIN, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE 
KEYWDS   3 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG           
EXPDTA    SOLUTION NMR                                                          
NUMMDL    15                                                                    
AUTHOR    A.LEMAK,Y.SHENG,M.KARRA,S.SRISAILAM,R.C.LAISTER,S.DUAN,               
AUTHOR   2 C.H.ARROWSMITH,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)       
REVDAT   4   19-FEB-20 2K2D    1       REMARK SEQADV                            
REVDAT   3   28-APR-09 2K2D    1       JRNL                                     
REVDAT   2   24-FEB-09 2K2D    1       VERSN                                    
REVDAT   1   15-APR-08 2K2D    0                                                
JRNL        AUTH   Y.SHENG,R.C.LAISTER,A.LEMAK,B.WU,E.TAI,S.DUAN,J.LUKIN,       
JRNL        AUTH 2 M.SUNNERHAGEN,S.SRISAILAM,M.KARRA,S.BENCHIMOL,C.H.ARROWSMITH 
JRNL        TITL   MOLECULAR BASIS OF PIRH2-MEDIATED P53 UBIQUITYLATION.        
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  15  1334 2008              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   19043414                                                     
JRNL        DOI    10.1038/NSMB.1521                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : NMRPIPE 2.3, CNS                                     
REMARK   3   AUTHORS     : DELAGLIO, GRZESIEK, VUISTER, ZHU, PFEIFER AND BAX    
REMARK   3                 (NMRPIPE), BRUNGER, ADAMS, CLORE, GROS, NILGES AND   
REMARK   3                 READ (CNS)                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2K2D COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-APR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000100588.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : 7                                  
REMARK 210  IONIC STRENGTH                 : 150                                
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 1 MM [U-99% 13C; U-99% 15N] C      
REMARK 210                                   -TERMINAL DOMAIN OF HUMAN PIRH2,   
REMARK 210                                   50 MM SODIUM PHOSPHATE, 150 MM     
REMARK 210                                   POTASSIUM CHLORIDE, 10 UM ZNCL2,   
REMARK 210                                   0.8 MM DTT, 90% H2O/10% D2O; 1     
REMARK 210                                   MM [U-99% 13C; U-99% 15N] C-       
REMARK 210                                   TERMINAL DOMAIN OF HUMAN PIRH2,    
REMARK 210                                   50 MM SODIUM PHOSPHATE, 150 MM     
REMARK 210                                   POTASSIUM CHLORIDE, 10 UM ZNCL2,   
REMARK 210                                   0.8 MM DTT, 100% D2O               
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D HNCO; 3D HNCA; 3D CBCA(CO)NH;   
REMARK 210                                   3D HBHA(CO)NH; 3D H(CCO)NH; 3D     
REMARK 210                                   C(CO)NH; 3D HCCH-TOCSY; 3D 1H-     
REMARK 210                                   15N NOESY; 3D 1H-13C NOESY; 3D     
REMARK 210                                   1H-13C-AROMATIC NOESY              
REMARK 210  SPECTROMETER FIELD STRENGTH    : 500 MHZ; 600 MHZ; 800 MHZ          
REMARK 210  SPECTROMETER MODEL             : AVANCE; INOVA                      
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER; VARIAN                     
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : SPARKY, CYANA, AUTOSTRUCTURE,      
REMARK 210                                   TALOS                              
REMARK 210   METHOD USED                   : MOLECULAR DYNAMICS                 
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 15                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST         
REMARK 210                                   ENERGY                             
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;                   
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                            
REMARK 465   MODELS 1-15                                                        
REMARK 465     RES C SSSEQI                                                     
REMARK 465     GLY A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     MET A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     ASP A    10                                                      
REMARK 465     MET A    11                                                      
REMARK 465     THR A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     TYR A    14                                                      
REMARK 465     TRP A    15                                                      
REMARK 465     ARG A    16                                                      
REMARK 465     GLN A    17                                                      
REMARK 465     LEU A    18                                                      
REMARK 465     ASP A    19                                                      
REMARK 465     ASP A    20                                                      
REMARK 465     GLU A    21                                                      
REMARK 465     VAL A    22                                                      
REMARK 465     ALA A    23                                                      
REMARK 465     GLN A    24                                                      
REMARK 465     THR A    25                                                      
REMARK 465     PRO A    26                                                      
REMARK 465     MET A    27                                                      
REMARK 465     PRO A    28                                                      
REMARK 465     SER A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     TYR A    31                                                      
REMARK 465     GLN A    32                                                      
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  2 SER A  75       77.59     59.29                                   
REMARK 500  4 SER A  75       55.87   -113.14                                   
REMARK 500  5 ASP A  42      -55.56   -127.43                                   
REMARK 500  6 ASN A  44       82.50     54.91                                   
REMARK 500  6 ASN A  65       39.26    -87.43                                   
REMARK 500  7 LEU A  54       38.09    -90.30                                   
REMARK 500  7 GLU A  62       34.44     70.96                                   
REMARK 500  8 CYS A  61       -7.91   -140.88                                   
REMARK 500  9 ASN A  44       83.21     50.97                                   
REMARK 500 11 ASN A  44       80.75     52.42                                   
REMARK 500 11 CYS A  61       -4.54   -140.90                                   
REMARK 500 12 LEU A  54       33.36    -92.83                                   
REMARK 500 12 CYS A  61       -4.45   -144.20                                   
REMARK 500 12 SER A  75       96.47    -67.16                                   
REMARK 500 13 ALA A  69      -71.18    -86.80                                   
REMARK 500 15 ASP A  42      -54.56   -126.50                                   
REMARK 500 15 LEU A  54       37.40    -90.82                                   
REMARK 500 15 ASP A  77       18.07   -154.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A  80  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  40   SG                                                     
REMARK 620 2 CYS A  43   SG  105.3                                              
REMARK 620 3 CYS A  58   SG  107.7 112.0                                        
REMARK 620 4 CYS A  61   SG  112.5 110.5 108.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 80                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: HT2C   RELATED DB: TARGETDB                              
REMARK 900 RELATED ID: 15701   RELATED DB: BMRB                                 
REMARK 900 RELATED ID: 2K2C   RELATED DB: PDB                                   
REMARK 900 SOLUTION NMR STRUCTURE OF N-TERMINAL DOMAIN OF HUMAN PIRH2, NESG     
REMARK 900 TARGET HT2A                                                          
DBREF  2K2D A    5    79  UNP    Q96PM5   ZN363_HUMAN    187    261             
SEQADV 2K2D GLY A    1  UNP  Q96PM5              EXPRESSION TAG                 
SEQADV 2K2D SER A    2  UNP  Q96PM5              EXPRESSION TAG                 
SEQADV 2K2D HIS A    3  UNP  Q96PM5              EXPRESSION TAG                 
SEQADV 2K2D MET A    4  UNP  Q96PM5              EXPRESSION TAG                 
SEQRES   1 A   79  GLY SER HIS MET MET HIS SER ALA LEU ASP MET THR ARG          
SEQRES   2 A   79  TYR TRP ARG GLN LEU ASP ASP GLU VAL ALA GLN THR PRO          
SEQRES   3 A   79  MET PRO SER GLU TYR GLN ASN MET THR VAL ASP ILE LEU          
SEQRES   4 A   79  CYS ASN ASP CYS ASN GLY ARG SER THR VAL GLN PHE HIS          
SEQRES   5 A   79  ILE LEU GLY MET LYS CYS LYS ILE CYS GLU SER TYR ASN          
SEQRES   6 A   79  THR ALA GLN ALA GLY GLY ARG ARG ILE SER LEU ASP GLN          
SEQRES   7 A   79  GLN                                                          
HET     ZN  A  80       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    ZN 2+                                                        
SHEET    1   A 3 ARG A  46  GLN A  50  0                                        
SHEET    2   A 3 THR A  35  CYS A  40 -1  N  ILE A  38   O  SER A  47           
SHEET    3   A 3 THR A  66  GLN A  68 -1  O  ALA A  67   N  LEU A  39           
LINK         SG  CYS A  40                ZN    ZN A  80     1555   1555  2.30  
LINK         SG  CYS A  43                ZN    ZN A  80     1555   1555  2.33  
LINK         SG  CYS A  58                ZN    ZN A  80     1555   1555  2.34  
LINK         SG  CYS A  61                ZN    ZN A  80     1555   1555  2.32  
SITE     1 AC1  4 CYS A  40  ASP A  42  CYS A  58  ILE A  60                    
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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