HEADER DNA BINDING PROTEIN 06-MAY-15 2N2C
TITLE NMR STRUCTURE OF TDP-43 PRION-LIKE HYDROPHOBIC HELIX IN DPC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TAR DNA-BINDING PROTEIN 43;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 307-349;
COMPND 5 SYNONYM: TDP-43;
COMPND 6 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: TARDBP, TDP43;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET28A
KEYWDS ALS, PRION-LIKE DOMAIN, HYDROPHOBIC HELICES, MEMBRANE INTERACTION,
KEYWDS 2 DPC, TAR DNA-BINDING PROTEIN-43, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 6
AUTHOR L.LIM,J.SONG
REVDAT 2 14-JUN-23 2N2C 1 REMARK
REVDAT 1 02-DEC-15 2N2C 0
JRNL AUTH L.LIM,J.SONG
JRNL TITL ALS-CAUSING MUTATIONS SIGNIFICANTLY PERTURB THE
JRNL TITL 2 SELF-ASSEMBLY AND INTERACTION WITH NUCLEIC ACID OF THE
JRNL TITL 3 INTRINSICALLY-DISORDERED PRION-LIKE DOMAIN OF TDP-43
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.1, AMBER
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER AND WUTHRICH (CYANA), CASE,
REMARK 3 DARDEN, CHEATHAM, III, SIMMERLING, WANG, DUKE, LUO,
REMARK 3 ... AND KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2N2C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000104333.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 4
REMARK 210 IONIC STRENGTH : 1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 300 UM [U-100% 15N] ENTITY-1, 60
REMARK 210 MM DPC-2, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 1H-15N NOESY; 3D 1H-15N
REMARK 210 TOCSY; 3D H(CCO)NH; 3D HCCH-
REMARK 210 TOCSY; 3D HNCACB
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 6
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 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
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 1 MET A 311 12.14 47.79
REMARK 500 1 PHE A 316 -57.56 -138.14
REMARK 500 1 ILE A 318 -55.16 -141.82
REMARK 500 1 ALA A 321 -34.94 58.54
REMARK 500 1 GLN A 346 32.50 -142.97
REMARK 500 2 PHE A 313 -41.94 -167.51
REMARK 500 2 PHE A 316 -44.76 -151.53
REMARK 500 2 SER A 317 16.06 -67.60
REMARK 500 2 ILE A 318 -48.24 -147.36
REMARK 500 2 ALA A 321 -30.69 57.18
REMARK 500 2 GLN A 346 44.85 -144.27
REMARK 500 3 MET A 311 6.63 51.44
REMARK 500 3 ASN A 312 -93.70 -76.35
REMARK 500 3 PHE A 316 -50.64 -150.56
REMARK 500 3 SER A 317 31.43 -74.40
REMARK 500 3 ILE A 318 -45.00 -152.02
REMARK 500 3 ALA A 321 -34.87 58.11
REMARK 500 3 GLN A 344 -34.43 -144.98
REMARK 500 3 GLN A 346 53.41 -145.37
REMARK 500 4 MET A 311 -14.31 54.84
REMARK 500 4 ASN A 312 6.34 -62.04
REMARK 500 4 PHE A 313 -19.35 -164.06
REMARK 500 4 PHE A 316 -44.54 -152.27
REMARK 500 4 SER A 317 20.12 -68.70
REMARK 500 4 ILE A 318 -48.07 -157.89
REMARK 500 4 ALA A 321 -20.34 57.84
REMARK 500 5 ASN A 312 18.91 -69.20
REMARK 500 5 PHE A 313 -22.85 174.86
REMARK 500 5 PHE A 316 -39.14 -157.58
REMARK 500 5 SER A 317 13.94 -69.31
REMARK 500 5 ILE A 318 -53.45 -150.27
REMARK 500 5 ALA A 321 -21.56 56.73
REMARK 500 5 GLN A 346 34.21 39.51
REMARK 500 5 SER A 347 47.42 -89.81
REMARK 500 6 PHE A 313 -17.49 -162.93
REMARK 500 6 PHE A 316 -42.29 -156.20
REMARK 500 6 SER A 317 14.02 -69.37
REMARK 500 6 ILE A 318 -42.21 -148.72
REMARK 500 6 ALA A 321 -10.33 55.78
REMARK 500 6 GLN A 343 -70.94 -106.54
REMARK 500 6 SER A 347 120.58 69.16
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 MET A 307 GLY A 308 4 -141.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 25595 RELATED DB: BMRB
DBREF 2N2C A 307 349 UNP Q13148 TADBP_HUMAN 307 349
SEQRES 1 A 43 MET GLY GLY GLY MET ASN PHE GLY ALA PHE SER ILE ASN
SEQRES 2 A 43 PRO ALA MET MET ALA ALA ALA GLN ALA ALA LEU GLN SER
SEQRES 3 A 43 SER TRP GLY MET MET GLY MET LEU ALA SER GLN GLN ASN
SEQRES 4 A 43 GLN SER GLY PRO
HELIX 1 1 ALA A 321 ASN A 345 1 25
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
