HEADER CHAPERONE/MEMBRANE PROTEIN 03-JUN-13 2M8S
TITLE NMR STRUCTURE OF THE CYTOPLASMIC TAIL OF THE MEMBRANE FORM OF HEPARIN-
TITLE 2 BINDING EGF-LIKE GROWTH FACTOR (PROHB-EGF-CT) COMPLEXED WITH THE
TITLE 3 UBIQUITIN HOMOLOGY DOMAIN OF BCL-2-ASSOCIATED ATHANOGENE 1 FROM MUS
TITLE 4 MUSCULUS (MBAG-1-UBH)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 137-233;
COMPND 5 SYNONYM: BAG-1, BCL-2-ASSOCIATED ATHANOGENE 1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROHEPARIN-BINDING EGF-LIKE GROWTH FACTOR;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 185-208;
COMPND 11 SYNONYM: HEPARIN-BINDING EGF-LIKE GROWTH FACTOR, HB-EGF, HBEGF,
COMPND 12 DIPHTHERIA TOXIN RECEPTOR, DT-R;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: BAG1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PGEX-4T1;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: HBEGF, DTR, DTS, HEGFL;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR: PGEX-4T1
KEYWDS MBAG-1, PROHB-EGF-CT, CHAPERONE-MEMBRANE PROTEIN COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR H.W.HUANG,C.YU
REVDAT 1 16-APR-14 2M8S 0
JRNL AUTH K.W.HUNG,H.W.HUANG,C.C.CHO,S.C.CHANG,C.YU
JRNL TITL NUCLEAR MAGNETIC RESONANCE STRUCTURE OF THE CYTOPLASMIC TAIL
JRNL TITL 2 OF HEPARIN BINDING EGF-LIKE GROWTH FACTOR (PROHB-EGF-CT)
JRNL TITL 3 COMPLEXED WITH THE UBIQUITIN HOMOLOGY DOMAIN OF
JRNL TITL 4 BCL-2-ASSOCIATED ATHANOGENE 1 FROM MUS MUSCULUS
JRNL TITL 5 (MBAG-1-UBH).
JRNL REF BIOCHEMISTRY V. 53 1935 2014
JRNL REFN ISSN 0006-2960
JRNL PMID 24628338
JRNL DOI 10.1021/BI5003019
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-KUNSTLEVE,
REMARK 3 JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2M8S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JUN-13.
REMARK 100 THE RCSB ID CODE IS RCSB103352.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 0.1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0 MM [U-100% 13C; U-100% 15N]
REMARK 210 UBIQUITIN HOMOLOGY DOMAIN OF
REMARK 210 MOUSE BAG-1-1, 20 MM SODIUM
REMARK 210 PHOSPHATE-2, 100 MM SODIUM
REMARK 210 CHLORIDE-3, 5 MM DTT-4, 90% H2O/
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D C(CO)NH; 3D
REMARK 210 HNCO; 3D HNCA; 3D HNCACB; 3D
REMARK 210 HBHA(CO)NH; 3D HN(CO)CA; 3D
REMARK 210 H(CCO)NH; 3D HCCH-TOCSY; 3D HCCH-
REMARK 210 COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : VNMR
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 5000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 OE2 GLU A 27 HZ3 LYS A 95 1.58
REMARK 500 OE1 GLU A 27 HH22 ARG B 188 1.58
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 THR A 4 -58.38 -150.39
REMARK 500 1 GLU A 6 -70.40 -134.52
REMARK 500 1 GLN A 9 -112.09 -121.12
REMARK 500 1 SER A 25 -48.55 70.57
REMARK 500 1 ASN A 26 -31.84 -156.79
REMARK 500 1 PRO A 35 -150.98 -84.57
REMARK 500 1 GLN A 37 -81.82 -153.33
REMARK 500 1 ASN A 39 -83.68 46.94
REMARK 500 1 THR A 55 8.54 -154.46
REMARK 500 1 LYS A 69 -175.53 -170.61
REMARK 500 1 GLU A 75 -85.32 -130.37
REMARK 500 1 PRO A 77 150.28 -43.87
REMARK 500 1 GLN A 84 -159.88 -168.29
REMARK 500 1 CYS A 87 -155.21 70.42
REMARK 500 1 GLU A 94 -167.82 -102.21
REMARK 500 1 ARG B 189 79.32 62.89
REMARK 500 1 TYR B 192 -158.74 -140.36
REMARK 500 1 VAL B 194 -24.32 -174.14
REMARK 500 1 GLU B 197 151.88 71.43
REMARK 500 1 SER B 207 -31.81 -152.49
REMARK 500 2 THR A 4 -33.41 -132.61
REMARK 500 2 MET A 7 -74.63 66.75
REMARK 500 2 GLN A 9 -101.33 -125.16
REMARK 500 2 ARG A 17 66.14 60.63
REMARK 500 2 SER A 25 -85.89 66.52
REMARK 500 2 PRO A 35 -115.47 -89.29
REMARK 500 2 GLN A 37 -84.45 -129.94
REMARK 500 2 ASN A 39 -93.73 42.32
REMARK 500 2 THR A 55 28.93 -146.13
REMARK 500 2 PRO A 60 5.38 -68.10
REMARK 500 2 MET A 74 105.46 -164.91
REMARK 500 2 GLU A 75 -93.96 -111.66
REMARK 500 2 PRO A 77 144.19 -39.79
REMARK 500 2 CYS A 87 -157.01 73.07
REMARK 500 2 TYR B 192 -168.58 -166.41
REMARK 500 2 VAL B 194 -31.54 -177.52
REMARK 500 2 GLU B 197 143.25 73.29
REMARK 500 2 VAL B 200 75.30 51.00
REMARK 500 2 LYS B 201 -9.59 -157.14
REMARK 500 2 SER B 207 26.25 -145.29
REMARK 500 3 THR A 4 -39.97 -150.93
REMARK 500 3 GLU A 6 -74.43 -105.87
REMARK 500 3 GLN A 9 -101.61 -134.26
REMARK 500 3 GLU A 12 -150.84 -131.23
REMARK 500 3 SER A 25 -67.52 69.72
REMARK 500 3 PRO A 35 -147.48 -85.24
REMARK 500 3 GLN A 37 -82.72 -150.25
REMARK 500 3 ASN A 39 -92.63 45.48
REMARK 500 3 THR A 55 21.81 -154.85
REMARK 500 3 PHE A 66 -179.86 -174.46
REMARK 500
REMARK 500 THIS ENTRY HAS 385 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 18416 RELATED DB: BMRB
DBREF 2M8S A 1 97 UNP Q60739 BAG1_MOUSE 137 233
DBREF 2M8S B 185 208 UNP Q99075 HBEGF_HUMAN 185 208
SEQRES 1 A 97 MET ALA LYS THR GLU GLU MET VAL GLN THR GLU GLU MET
SEQRES 2 A 97 GLU THR PRO ARG LEU SER VAL ILE VAL THR HIS SER ASN
SEQRES 3 A 97 GLU ARG TYR ASP LEU LEU VAL THR PRO GLN GLN GLY ASN
SEQRES 4 A 97 SER GLU PRO VAL VAL GLN ASP LEU ALA GLN LEU VAL GLU
SEQRES 5 A 97 GLU ALA THR GLY VAL PRO LEU PRO PHE GLN LYS LEU ILE
SEQRES 6 A 97 PHE LYS GLY LYS SER LEU LYS GLU MET GLU THR PRO LEU
SEQRES 7 A 97 SER ALA LEU GLY MET GLN ASN GLY CYS ARG VAL MET LEU
SEQRES 8 A 97 ILE GLY GLU LYS SER ASN
SEQRES 1 B 24 ARG TYR HIS ARG ARG GLY GLY TYR ASP VAL GLU ASN GLU
SEQRES 2 B 24 GLU LYS VAL LYS LEU GLY MET THR ASN SER HIS
HELIX 1 1 GLN A 45 ALA A 54 1 10
HELIX 2 2 PRO A 58 GLN A 62 5 5
HELIX 3 3 PRO A 77 LEU A 81 5 5
SHEET 1 A 3 GLU A 27 LEU A 32 0
SHEET 2 A 3 SER A 19 HIS A 24 -1 N HIS A 24 O GLU A 27
SHEET 3 A 3 ARG A 88 MET A 90 1 O VAL A 89 N THR A 23
SHEET 1 B 2 ILE A 65 PHE A 66 0
SHEET 2 B 2 LYS A 69 SER A 70 -1 O LYS A 69 N PHE A 66
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
