HEADER SIGNALING PROTEIN 15-MAY-14 2MPC
TITLE SOLUTION STRUCTURE OF THE PYRIN DOMAIN OF HUMAN PYRIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DAPIN DOMAIN (PYD), RESIDUES 1-92;
COMPND 5 SYNONYM: MARENOSTRIN;
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: MEFV, MEF;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET-28B
KEYWDS PYRIN DOMAIN, DEATH DOMAIN, INFLAMMATION, CS-ROSETTA, SIGNALING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR S.L.SOH,S.J.SMITH,J.M.HILL
REVDAT 2 24-AUG-22 2MPC 1 JRNL REMARK SEQADV
REVDAT 1 16-JUL-14 2MPC 0
JRNL AUTH P.R.VAJJHALA,S.KAISER,S.J.SMITH,Q.R.ONG,S.L.SOH,K.J.STACEY,
JRNL AUTH 2 J.M.HILL
JRNL TITL IDENTIFICATION OF MULTIFACETED BINDING MODES FOR PYRIN AND
JRNL TITL 2 ASC PYRIN DOMAINS GIVES INSIGHTS INTO PYRIN INFLAMMASOME
JRNL TITL 3 ASSEMBLY.
JRNL REF J.BIOL.CHEM. V. 289 23504 2014
JRNL REFN ESSN 1083-351X
JRNL PMID 25006247
JRNL DOI 10.1074/JBC.M114.553305
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TOPSPIN, CS-ROSETTA 3.4
REMARK 3 AUTHORS : BRUKER BIOSPIN (TOPSPIN), YANG SHEN, OLIVER LANGE,
REMARK 3 FRANK DELAGLIO, ET AL. (CS-ROSETTA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2MPC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000103889.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : 150
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.8 MM [U-100% 13C; U-100% 15N]
REMARK 210 PYRIN-1, 90 % H2O-2, 10 % D2O-3,
REMARK 210 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D HNCO; 3D
REMARK 210 HN(CA)CO; 3D CBCA(CO)NH; 3D
REMARK 210 HNCACB; 3D C(CO)NH; 3D HBHA(CO)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : TOPSPIN
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 5000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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 1-10
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 LYS A 3
REMARK 465 GLU A 94
REMARK 465 HIS A 95
REMARK 465 HIS A 96
REMARK 465 HIS A 97
REMARK 465 HIS A 98
REMARK 465 HIS A 99
REMARK 465 HIS A 100
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 GLN A 79 70.60 -107.44
REMARK 500 2 ASN A 78 60.73 60.24
REMARK 500 3 GLN A 79 71.85 -110.91
REMARK 500 5 ASN A 78 47.98 72.60
REMARK 500 8 GLN A 79 77.16 -114.40
REMARK 500 9 GLN A 79 78.24 -110.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 19875 RELATED DB: BMRB
DBREF 2MPC A 1 92 UNP O15553 MEFV_HUMAN 1 92
SEQADV 2MPC LEU A 93 UNP O15553 EXPRESSION TAG
SEQADV 2MPC GLU A 94 UNP O15553 EXPRESSION TAG
SEQADV 2MPC HIS A 95 UNP O15553 EXPRESSION TAG
SEQADV 2MPC HIS A 96 UNP O15553 EXPRESSION TAG
SEQADV 2MPC HIS A 97 UNP O15553 EXPRESSION TAG
SEQADV 2MPC HIS A 98 UNP O15553 EXPRESSION TAG
SEQADV 2MPC HIS A 99 UNP O15553 EXPRESSION TAG
SEQADV 2MPC HIS A 100 UNP O15553 EXPRESSION TAG
SEQRES 1 A 100 MET ALA LYS THR PRO SER ASP HIS LEU LEU SER THR LEU
SEQRES 2 A 100 GLU GLU LEU VAL PRO TYR ASP PHE GLU LYS PHE LYS PHE
SEQRES 3 A 100 LYS LEU GLN ASN THR SER VAL GLN LYS GLU HIS SER ARG
SEQRES 4 A 100 ILE PRO ARG SER GLN ILE GLN ARG ALA ARG PRO VAL LYS
SEQRES 5 A 100 MET ALA THR LEU LEU VAL THR TYR TYR GLY GLU GLU TYR
SEQRES 6 A 100 ALA VAL GLN LEU THR LEU GLN VAL LEU ARG ALA ILE ASN
SEQRES 7 A 100 GLN ARG LEU LEU ALA GLU GLU LEU HIS ARG ALA ALA ILE
SEQRES 8 A 100 GLN LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 THR A 4 LEU A 16 1 13
HELIX 2 2 VAL A 17 GLN A 29 1 13
HELIX 3 3 PRO A 41 ALA A 48 1 8
HELIX 4 4 LYS A 52 TYR A 61 1 10
HELIX 5 5 GLY A 62 ILE A 77 1 16
HELIX 6 6 GLN A 79 LEU A 93 1 15
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
