HEADER MEMBRANE PROTEIN 24-JUL-09 2KM7
TITLE SOLUTION STRUCTURE OF BAME, A COMPONENT OF THE OUTER MEMBRANE PROTEIN
TITLE 2 ASSEMBLY MACHINERY IN ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SMALL PROTEIN A;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 4 ORGANISM_TAXID: 83333
KEYWDS BAME, SMPA, BAM COMPLEX, OMP85, YAET, CELL MEMBRANE, CELL OUTER
KEYWDS 2 MEMBRANE, LIPOPROTEIN, MEMBRANE, PALMITATE, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.J.KNOWLES,P.SRIDHAR,S.RAJESH,E.MANOLI,I.R.HENDERSON,M.OVERDUIN
REVDAT 3 13-OCT-21 2KM7 1 SEQADV
REVDAT 2 19-JUN-13 2KM7 1 JRNL VERSN
REVDAT 1 02-FEB-11 2KM7 0
JRNL AUTH T.J.KNOWLES,D.F.BROWNING,M.JEEVES,R.MADERBOCUS,S.RAJESH,
JRNL AUTH 2 P.SRIDHAR,E.MANOLI,D.EMERY,U.SOMMER,A.SPENCER,D.L.LEYTON,
JRNL AUTH 3 D.SQUIRE,R.R.CHAUDHURI,M.R.VIANT,A.F.CUNNINGHAM,
JRNL AUTH 4 I.R.HENDERSON,M.OVERDUIN
JRNL TITL STRUCTURE AND FUNCTION OF BAME WITHIN THE OUTER MEMBRANE AND
JRNL TITL 2 THE BETA-BARREL ASSEMBLY MACHINE.
JRNL REF EMBO REP. V. 12 123 2011
JRNL REFN ISSN 1469-221X
JRNL PMID 21212804
JRNL DOI 10.1038/EMBOR.2010.202
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 1.0.5, CYANA 1.0.5
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER AND WUTHRICH (CYANA),
REMARK 3 GUNTERT, MUMENTHALER AND WUTHRICH (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CYANA, ARIA
REMARK 4
REMARK 4 2KM7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000101294.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.0 MM [U-100% 13C; U-100% 15N]
REMARK 210 BAME, 50 MM SODIUM PHOSPHATE, 50
REMARK 210 MM SODIUM CHLORIDE, 90% H2O/10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D BEST HNCA; 3D BEST HN(CO)CA;
REMARK 210 3D BEST CBCA(CO)NH; 3D BEST
REMARK 210 HNCACB; 3D BEST HNCO; 3D BEST
REMARK 210 HN(CA)CO; 2D BEST 1H-15N HSQC;
REMARK 210 3D HCCH-TOCSY; 3D CCH-TOCSY; 3D
REMARK 210 1H-15N NOESY; 3D 1H-13C NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 1.0.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 150
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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 HB2 LYS A 107 HB2 ASN A 113 1.26
REMARK 500 OE1 GLU A 84 HD1 HIS A 117 1.59
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 PRO A 30 45.36 -77.52
REMARK 500 1 GLN A 34 67.50 -106.93
REMARK 500 1 ASN A 36 -79.11 67.98
REMARK 500 1 ASN A 71 49.55 -101.25
REMARK 500 1 GLN A 79 -30.74 -150.60
REMARK 500 1 HIS A 83 -41.14 -175.20
REMARK 500 1 LEU A 101 105.48 -55.14
REMARK 500 1 ALA A 109 42.79 -83.08
REMARK 500 1 SER A 111 96.30 68.95
REMARK 500 1 HIS A 118 122.56 68.34
REMARK 500 2 LEU A 23 28.55 -155.04
REMARK 500 2 ARG A 25 74.89 -169.95
REMARK 500 2 ASP A 31 -133.15 -159.47
REMARK 500 2 ILE A 32 134.85 75.56
REMARK 500 2 ASN A 71 45.77 -92.41
REMARK 500 2 HIS A 83 -65.72 71.37
REMARK 500 2 THR A 87 115.31 -162.81
REMARK 500 2 ALA A 109 67.70 -68.38
REMARK 500 2 ASN A 113 -60.75 -135.51
REMARK 500 2 HIS A 116 51.91 39.16
REMARK 500 3 ASP A 31 39.06 -88.18
REMARK 500 3 ASN A 33 48.41 -85.64
REMARK 500 3 ASN A 36 -79.65 69.11
REMARK 500 3 ASN A 71 50.58 -106.13
REMARK 500 3 GLN A 80 74.29 55.01
REMARK 500 3 GLU A 84 -45.64 76.60
REMARK 500 3 THR A 87 138.84 -175.53
REMARK 500 3 ASN A 113 -64.42 71.57
REMARK 500 3 GLU A 115 160.30 69.78
REMARK 500 3 HIS A 118 -57.34 -156.52
REMARK 500 3 HIS A 119 171.24 175.57
REMARK 500 3 HIS A 120 -80.35 -72.73
REMARK 500 4 ARG A 25 79.55 -103.68
REMARK 500 4 PRO A 30 35.88 -70.56
REMARK 500 4 ILE A 32 96.53 72.11
REMARK 500 4 ASN A 71 55.10 -97.14
REMARK 500 4 GLN A 79 -114.82 -105.61
REMARK 500 4 GLU A 84 108.17 69.38
REMARK 500 4 LEU A 110 -120.34 -152.26
REMARK 500 4 SER A 111 -66.80 66.75
REMARK 500 4 LEU A 114 -65.76 -129.18
REMARK 500 4 HIS A 120 -70.90 -149.18
REMARK 500 5 PRO A 30 43.48 -74.10
REMARK 500 5 ASN A 36 -133.43 59.86
REMARK 500 5 GLN A 79 11.18 -150.83
REMARK 500 5 PRO A 81 -165.41 -76.39
REMARK 500 5 HIS A 83 -75.25 -72.99
REMARK 500 5 LEU A 101 101.87 -54.66
REMARK 500 5 ALA A 109 77.11 -6.43
REMARK 500 5 LEU A 110 59.69 174.93
REMARK 500
REMARK 500 THIS ENTRY HAS 212 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 16424 RELATED DB: BMRB
DBREF 2KM7 A 20 113 UNP P0A937 SMPA_ECOLI 21 114
SEQADV 2KM7 SER A 20 UNP P0A937 CYS 21 ENGINEERED MUTATION
SEQADV 2KM7 LEU A 114 UNP P0A937 EXPRESSION TAG
SEQADV 2KM7 GLU A 115 UNP P0A937 EXPRESSION TAG
SEQADV 2KM7 HIS A 116 UNP P0A937 EXPRESSION TAG
SEQADV 2KM7 HIS A 117 UNP P0A937 EXPRESSION TAG
SEQADV 2KM7 HIS A 118 UNP P0A937 EXPRESSION TAG
SEQADV 2KM7 HIS A 119 UNP P0A937 EXPRESSION TAG
SEQADV 2KM7 HIS A 120 UNP P0A937 EXPRESSION TAG
SEQADV 2KM7 HIS A 121 UNP P0A937 EXPRESSION TAG
SEQRES 1 A 102 SER SER THR LEU GLU ARG VAL VAL TYR ARG PRO ASP ILE
SEQRES 2 A 102 ASN GLN GLY ASN TYR LEU THR ALA ASN ASP VAL SER LYS
SEQRES 3 A 102 ILE ARG VAL GLY MET THR GLN GLN GLN VAL ALA TYR ALA
SEQRES 4 A 102 LEU GLY THR PRO LEU MET SER ASP PRO PHE GLY THR ASN
SEQRES 5 A 102 THR TRP PHE TYR VAL PHE ARG GLN GLN PRO GLY HIS GLU
SEQRES 6 A 102 GLY VAL THR GLN GLN THR LEU THR LEU THR PHE ASN SER
SEQRES 7 A 102 SER GLY VAL LEU THR ASN ILE ASP ASN LYS PRO ALA LEU
SEQRES 8 A 102 SER GLY ASN LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 THR A 39 SER A 44 1 6
HELIX 2 2 THR A 51 GLY A 60 1 10
SHEET 1 A 3 THR A 72 TYR A 75 0
SHEET 2 A 3 LEU A 91 ASN A 96 -1 O LEU A 93 N TRP A 73
SHEET 3 A 3 VAL A 100 ASP A 105 -1 O ASP A 105 N THR A 92
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
