HEADER RNA BINDING PROTEIN 12-OCT-11 4A4E
TITLE SOLUTION STRUCTURE OF SMN TUDOR DOMAIN IN COMPLEX WITH SYMMETRICALLY
TITLE 2 DIMETHYLATED ARGININE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SURVIVAL MOTOR NEURON PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TUDOR DOMAIN, RESIDUES 84-147;
COMPND 5 SYNONYM: SURVIVAL MOTOR NEURON PROTEIN SMN, COMPONENT OF GEMS 1,
COMPND 6 GEMIN-1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.TRIPSIANES,T.MADL,M.MACHYNA,D.FESSAS,C.ENGLBRECHT,U.FISCHER,
AUTHOR 2 K.M.NEUGEBAUER,M.SATTLER
REVDAT 4 14-JUN-23 4A4E 1 REMARK
REVDAT 3 28-DEC-11 4A4E 1 ATOM
REVDAT 2 14-DEC-11 4A4E 1 JRNL
REVDAT 1 30-NOV-11 4A4E 0
JRNL AUTH K.TRIPSIANES,T.MADL,M.MACHYNA,D.FESSAS,C.ENGLBRECHT,
JRNL AUTH 2 U.FISCHER,K.M.NEUGEBAUER,M.SATTLER
JRNL TITL STRUCTURAL BASIS FOR DIMETHYL-ARGININE RECOGNITION BY THE
JRNL TITL 2 TUDOR DOMAINS OF HUMAN SMN AND SPF30 PROTEINS
JRNL REF NAT.STRUCT.MOL.BIOL. V. 18 1414 2011
JRNL REFN ISSN 1545-9993
JRNL PMID 22101937
JRNL DOI 10.1038/NSMB.2185
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,READ, RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4A4E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1290049970.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0; 298.0; 298.0; 298.0;
REMARK 210 298.0; 298.0
REMARK 210 PH : 6.5; 6.5; 6.5; 6.5; 6.5; 6.5
REMARK 210 IONIC STRENGTH : 50; 50; 50; 50; 50; 50
REMARK 210 PRESSURE : 1.0 ATM; 1.0 ATM; 1.0 ATM; 1.0
REMARK 210 ATM; 1.0 ATM; 1.0 ATM
REMARK 210 SAMPLE CONTENTS : 93% WATER/7% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-EDITED 3D NOESY; F1 15N/13C
REMARK 210 FILTERED; 15N- EDITED 3D NOESY;
REMARK 210 13C- EDITED 3D NOESY (ALIPHATICS)
REMARK 210 ; 13C-EDITED 3D NOESY
REMARK 210 (ALIPHATICS); 13C- EDITED 3D
REMARK 210 NOESY (AROMATICS); 13C-EDITED 3D
REMARK 210 NOESY (AROMATICS)
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : TALOS, CYANA, CNS
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NONE
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 HZ1 LYS A 93 OD2 ASP A 96 1.57
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 2 ALA A 86 -35.92 74.60
REMARK 500 2 ALA A 87 109.91 -53.56
REMARK 500 3 ALA A 86 103.08 -169.44
REMARK 500 3 ALA A 87 109.92 76.60
REMARK 500 7 CYS A 146 43.70 -82.38
REMARK 500 8 ALA A 87 96.22 68.94
REMARK 500 9 THR A 85 -167.52 56.01
REMARK 500 9 SER A 88 19.50 -164.11
REMARK 500 9 GLN A 90 -0.43 -141.88
REMARK 500 9 CYS A 146 98.68 -162.85
REMARK 500 10 ALA A 87 81.67 67.74
REMARK 500 11 CYS A 98 -168.60 -162.77
REMARK 500 15 CYS A 146 24.95 -140.80
REMARK 500 16 SER A 88 90.47 -69.57
REMARK 500 17 ALA A 86 -55.75 -160.47
REMARK 500 18 ALA A 86 -83.11 -177.99
REMARK 500 18 ALA A 87 -82.39 47.64
REMARK 500 18 CYS A 146 -1.77 74.81
REMARK 500 19 ALA A 86 -49.61 73.81
REMARK 500 19 SER A 88 19.33 -152.44
REMARK 500 19 LEU A 89 58.01 -91.18
REMARK 500 19 GLN A 90 11.91 -154.39
REMARK 500 20 ALA A 86 -8.20 72.72
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 2MR A 1148
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G5V RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE TUDOR DOMAIN OF THE HUMAN SMNPROTEIN
REMARK 900 RELATED ID: 1MHN RELATED DB: PDB
REMARK 900 HIGH RESOLUTION CRYSTAL STRUCTURE OF THE SMN TUDOR DOMAIN
REMARK 900 RELATED ID: 4A4G RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF SMN TUDOR DOMAIN IN COMPLEX WITH
REMARK 900 ASYMMETRICALLY DIMETHYLATED ARGININE
REMARK 900 RELATED ID: 4A4F RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF SPF30 TUDOR DOMAIN IN COMPLEX WITH
REMARK 900 SYMMETRICALLY DIMETHYLATED ARGININE
REMARK 900 RELATED ID: 4A4H RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF SPF30 TUDOR DOMAIN IN COMPLEX WITH
REMARK 900 ASYMMETRICALLY DIMETHYLATED ARGININE
REMARK 900 RELATED ID: 18005 RELATED DB: BMRB
DBREF 4A4E A 84 147 UNP Q16637 SMN_HUMAN 84 147
SEQRES 1 A 64 ASN THR ALA ALA SER LEU GLN GLN TRP LYS VAL GLY ASP
SEQRES 2 A 64 LYS CYS SER ALA ILE TRP SER GLU ASP GLY CYS ILE TYR
SEQRES 3 A 64 PRO ALA THR ILE ALA SER ILE ASP PHE LYS ARG GLU THR
SEQRES 4 A 64 CYS VAL VAL VAL TYR THR GLY TYR GLY ASN ARG GLU GLU
SEQRES 5 A 64 GLN ASN LEU SER ASP LEU LEU SER PRO ILE CYS GLU
HET 2MR A1148 33
HETNAM 2MR N3, N4-DIMETHYLARGININE
FORMUL 2 2MR C8 H18 N4 O2
HELIX 1 1 SER A 139 LEU A 141 5 3
SHEET 1 AA 4 LYS A 97 ILE A 101 0
SHEET 2 AA 4 ILE A 108 ASP A 117 -1 O TYR A 109 N ALA A 100
SHEET 3 AA 4 THR A 122 TYR A 127 -1 O THR A 122 N ASP A 117
SHEET 4 AA 4 ARG A 133 ASN A 137 -1 O GLU A 134 N VAL A 125
SITE 1 AC1 6 TRP A 102 ASP A 105 TYR A 109 TYR A 127
SITE 2 AC1 6 TYR A 130 ASN A 132
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