HEADER PROTEIN TRANSPORT 02-JAN-11 2RRL
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF THE FLIK
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLAGELLAR HOOK-LENGTH CONTROL PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 204-370;
COMPND 5 SYNONYM: FLIK;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: SUBSTRATE SPECIFICITY SWITCH (T3S4) DOMAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 90371;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PCOLD-I
KEYWDS FLIK, FLHB, BACTERIAL FLAGELLA MOTOR, HOOK-LENGTH CONTROL, PROTEIN
KEYWDS 2 TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR S.MIZUNO,S.TATE,N.KOBAYASHI,H.AMIDA
REVDAT 3 14-JUN-23 2RRL 1 REMARK SEQADV
REVDAT 2 28-DEC-11 2RRL 1 JRNL VERSN
REVDAT 1 18-MAY-11 2RRL 0
JRNL AUTH S.MIZUNO,H.AMIDA,N.KOBAYASHI,S.AIZAWA,S.TATE
JRNL TITL THE NMR STRUCTURE OF FLIK, THE TRIGGER FOR THE SWITCH OF
JRNL TITL 2 SUBSTRATE SPECIFICITY IN THE FLAGELLAR TYPE III SECRETION
JRNL TITL 3 APPARATUS
JRNL REF J.MOL.BIOL. V. 409 558 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21510958
JRNL DOI 10.1016/J.JMB.2011.04.008
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA, TALOS, X-PLOR NIH
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER AND WUTHRICH (CYANA),
REMARK 3 CORNILESCU, DELAGLIO AND BAX (TALOS), SCHWIETERS,
REMARK 3 KUSZEWSKI, TJANDRA AND CLORE (X-PLOR NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2RRL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1000150202.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM [U-13C; U-15N] PROTEIN-1;
REMARK 210 50MM SODIUM PHOSPHATE-2; 1MM
REMARK 210 EDTA-3; 90% H2O/10% D2O; 1MM [U-
REMARK 210 13C; U-15N] PROTEIN-4; 50MM
REMARK 210 SODIUM PHOSPHATE-5; 1MM EDTA-6;
REMARK 210 100% D2O; 1MM [U-15N] PROTEIN-7;
REMARK 210 50MM SODIUM PHOSPHATE-8; 1MM
REMARK 210 EDTA-9; 90% H2O/10% D2O; 0.5MM
REMARK 210 [U-15N] PROTEIN-10; 50MM SODIUM
REMARK 210 PHOSPHATE-11; 1MM EDTA-12; 100%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC
REMARK 210 ALIPHATIC; 2D 1H-13C HSQC
REMARK 210 AROMATIC; 3D HNCO; 3D HNCA; 3D
REMARK 210 HN(CO)CA; 3D HCACO; 3D HNCACB;
REMARK 210 3D CBCA(CO)NH; 3D C(CO)NH; 3D
REMARK 210 HNCANNH; 3D HBHA(CO)NH; 3D HCCH-
REMARK 210 TOCSY; 3D HCCH-COSY; 3D 1H-13C
REMARK 210 DEC NOESY; 3D 1H-13C NOESY
REMARK 210 ALIPHATIC; 3D 1H-13C NOESY
REMARK 210 AROMATIC; 3D 1H-15N NOESY; 3D 1H-
REMARK 210 15N TOCSY; 3D HNHA; 2D 1H-1H
REMARK 210 NOESY; 2D 1H-1H TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
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: 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 2 171.08 73.80
REMARK 500 1 ASP A 6 118.68 67.71
REMARK 500 1 ALA A 8 -6.11 -165.66
REMARK 500 1 ALA A 12 84.52 -166.30
REMARK 500 1 LEU A 16 115.52 -161.67
REMARK 500 1 ALA A 19 106.64 -168.47
REMARK 500 1 ALA A 20 113.49 -169.01
REMARK 500 1 ALA A 21 102.76 -166.54
REMARK 500 1 SER A 24 119.45 -164.87
REMARK 500 1 ALA A 25 75.20 -168.19
REMARK 500 1 VAL A 27 147.20 72.95
REMARK 500 1 GLU A 28 89.91 67.96
REMARK 500 1 VAL A 29 146.19 -171.25
REMARK 500 1 ASP A 30 167.07 70.03
REMARK 500 1 ALA A 40 -172.51 63.96
REMARK 500 1 ALA A 41 -30.32 -161.92
REMARK 500 1 MET A 42 99.11 65.91
REMARK 500 1 VAL A 60 -176.49 55.33
REMARK 500 1 GLN A 87 -29.68 -166.41
REMARK 500 1 GLN A 100 111.77 -168.08
REMARK 500 1 ASP A 109 -91.50 49.78
REMARK 500 1 ASN A 110 24.11 -148.71
REMARK 500 1 GLU A 153 -46.84 -152.84
REMARK 500 1 SER A 162 33.65 -162.79
REMARK 500 1 SER A 163 97.64 -67.46
REMARK 500 1 GLN A 165 75.54 71.55
REMARK 500 2 ALA A 3 -152.68 -171.16
REMARK 500 2 ASP A 6 92.72 59.44
REMARK 500 2 ALA A 20 103.19 -168.97
REMARK 500 2 SER A 24 109.94 -161.97
REMARK 500 2 LYS A 26 31.53 74.53
REMARK 500 2 VAL A 27 26.62 -153.90
REMARK 500 2 PRO A 35 -144.74 -85.26
REMARK 500 2 ALA A 40 38.40 -163.46
REMARK 500 2 ALA A 41 57.70 -162.56
REMARK 500 2 ASP A 109 -81.59 48.09
REMARK 500 2 ASN A 110 26.10 -142.89
REMARK 500 2 SER A 121 -175.00 -174.05
REMARK 500 2 LEU A 145 -84.20 -63.43
REMARK 500 2 GLU A 153 -44.86 -162.04
REMARK 500 2 GLN A 159 116.74 -160.56
REMARK 500 2 SER A 167 -166.89 -165.29
REMARK 500 3 SER A 4 96.51 62.62
REMARK 500 3 ASP A 6 124.86 71.03
REMARK 500 3 PRO A 15 -166.97 -70.14
REMARK 500 3 ALA A 21 110.29 -163.75
REMARK 500 3 ALA A 22 113.09 -161.09
REMARK 500 3 SER A 24 113.48 -162.80
REMARK 500 3 ALA A 25 104.18 -167.94
REMARK 500 3 ALA A 40 92.14 -165.84
REMARK 500
REMARK 500 THIS ENTRY HAS 265 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 11423 RELATED DB: BMRB
DBREF 2RRL A 3 169 UNP P26416 FLIK_SALTY 204 370
SEQADV 2RRL HIS A 1 UNP P26416 EXPRESSION TAG
SEQADV 2RRL MET A 2 UNP P26416 EXPRESSION TAG
SEQRES 1 A 169 HIS MET ALA SER ASP ASP ARG ALA THR GLY PRO ALA LEU
SEQRES 2 A 169 THR PRO LEU VAL VAL ALA ALA ALA ALA THR SER ALA LYS
SEQRES 3 A 169 VAL GLU VAL ASP SER PRO PRO ALA PRO VAL THR HIS GLY
SEQRES 4 A 169 ALA ALA MET PRO THR LEU SER SER ALA THR ALA GLN PRO
SEQRES 5 A 169 LEU PRO VAL ALA SER ALA PRO VAL LEU SER ALA PRO LEU
SEQRES 6 A 169 GLY SER HIS GLU TRP GLN GLN THR PHE SER GLN GLN VAL
SEQRES 7 A 169 MET LEU PHE THR ARG GLN GLY GLN GLN SER ALA GLN LEU
SEQRES 8 A 169 ARG LEU HIS PRO GLU GLU LEU GLY GLN VAL HIS ILE SER
SEQRES 9 A 169 LEU LYS LEU ASP ASP ASN GLN ALA GLN LEU GLN MET VAL
SEQRES 10 A 169 SER PRO HIS SER HIS VAL ARG ALA ALA LEU GLU ALA ALA
SEQRES 11 A 169 LEU PRO MET LEU ARG THR GLN LEU ALA GLU SER GLY ILE
SEQRES 12 A 169 GLN LEU GLY GLN SER SER ILE SER SER GLU SER PHE ALA
SEQRES 13 A 169 GLY GLN GLN GLN SER SER SER GLN GLN GLN SER SER ARG
HELIX 1 1 SER A 67 GLY A 85 1 19
HELIX 2 2 PRO A 95 GLY A 99 5 5
HELIX 3 3 SER A 121 ALA A 130 1 10
HELIX 4 4 ALA A 130 GLU A 140 1 11
SHEET 1 A 4 SER A 88 LEU A 91 0
SHEET 2 A 4 VAL A 101 ASP A 108 -1 O ILE A 103 N ALA A 89
SHEET 3 A 4 GLN A 111 VAL A 117 -1 O GLN A 113 N LYS A 106
SHEET 4 A 4 GLN A 144 SER A 151 1 O SER A 149 N LEU A 114
CISPEP 1 HIS A 94 PRO A 95 1 0.49
CISPEP 2 HIS A 94 PRO A 95 2 1.32
CISPEP 3 HIS A 94 PRO A 95 3 1.17
CISPEP 4 HIS A 94 PRO A 95 4 2.72
CISPEP 5 HIS A 94 PRO A 95 5 1.67
CISPEP 6 HIS A 94 PRO A 95 6 0.76
CISPEP 7 HIS A 94 PRO A 95 7 1.26
CISPEP 8 HIS A 94 PRO A 95 8 0.89
CISPEP 9 HIS A 94 PRO A 95 9 0.38
CISPEP 10 HIS A 94 PRO A 95 10 -0.59
CISPEP 11 HIS A 94 PRO A 95 11 2.03
CISPEP 12 HIS A 94 PRO A 95 12 2.15
CISPEP 13 HIS A 94 PRO A 95 13 3.50
CISPEP 14 HIS A 94 PRO A 95 14 2.41
CISPEP 15 HIS A 94 PRO A 95 15 1.76
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