HEADER TRANSCRIPTION REGULATOR 13-OCT-16 5TMX
TITLE SOLUTION STRUCTURE OF SINI, ANTAGONIST TO THE MASTER BIOFILM-REGULATOR
TITLE 2 SINR IN BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN SINI;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-57;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS (STRAIN 168);
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 STRAIN: 168;
SOURCE 5 GENE: SINI, BSU24600;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS SPORULATION, REPRESSOR, BIOFILM, TRANSCRIPTION REGULATOR
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR G.L.DRAUGHN,B.G.BOBAY,S.D.STOWE,R.J.THOMPSON,J.CAVANAGH
REVDAT 4 14-JUN-23 5TMX 1 REMARK
REVDAT 3 25-DEC-19 5TMX 1 REMARK
REVDAT 2 09-OCT-19 5TMX 1 JRNL REMARK
REVDAT 1 25-OCT-17 5TMX 0
JRNL AUTH M.E.MILTON,G.L.DRAUGHN,B.G.BOBAY,S.D.STOWE,A.L.OLSON,
JRNL AUTH 2 E.A.FELDMANN,R.J.THOMPSON,K.H.MYERS,M.T.SANTORO,D.B.KEARNS,
JRNL AUTH 3 J.CAVANAGH
JRNL TITL THE SOLUTION STRUCTURES AND INTERACTION OF SINR AND SINI:
JRNL TITL 2 ELUCIDATING THE MECHANISM OF ACTION OF THE MASTER REGULATOR
JRNL TITL 3 SWITCH FOR BIOFILM FORMATION IN BACILLUS SUBTILIS.
JRNL REF J.MOL.BIOL. 2019
JRNL REFN ESSN 1089-8638
JRNL PMID 31493408
JRNL DOI 10.1016/J.JMB.2019.08.019
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER 14
REMARK 3 AUTHORS : CASE, DARDEN, CHEATHAM III, SIMMERLING, WANG,
REMARK 3 DUKE, LUO, AND KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5TMX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000224514.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : 200
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM [U-15N] SINI, 20 MM MES,
REMARK 210 200 MM SODIUM CHLORIDE, 90% H2O/
REMARK 210 10% D2O; 1 MM [U-13C; U-15N]
REMARK 210 SINI, 20 MM MES, 200 MM NACL, 90%
REMARK 210 H2O/10% D2O; 1 MM [U-13C; U-15N]
REMARK 210 SINI, 20 MM MES, 200 MM NACL,
REMARK 210 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D HNCA; 3D HN(CO)CA; 3D HNCACB;
REMARK 210 3D CBCA(CO)NH; 3D HNCO; 3D
REMARK 210 HNCACO; 3D 1H-15N TOCSY; 3D C(CO)
REMARK 210 NH; 3D 1H-15N NOESY; 3D 1H-13C
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW, CYANA 3.0, NMRPIPE
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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 300 REMARK: DIMER AS DETERMINED BY GEL FILTRATION
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 ARG A 39 NE - CZ - NH2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 ARG B 39 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 3 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 4 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 4 TYR A 41 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 4 ARG B 39 NE - CZ - NH2 ANGL. DEV. = 4.1 DEGREES
REMARK 500 4 TYR B 41 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 5 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 5 ARG B 39 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 6 ARG A 39 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 6 TYR A 41 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 6 ARG B 39 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 7 ARG B 39 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 8 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 8 ARG B 39 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 9 ARG A 39 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 9 ARG B 39 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 10 ARG B 39 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 10 TYR B 41 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
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 ASP A 18 -73.02 -154.15
REMARK 500 1 ASN A 45 41.45 -84.85
REMARK 500 1 LYS B 46 45.11 -77.18
REMARK 500 2 MET A 4 18.91 55.80
REMARK 500 2 GLN A 12 39.56 -140.58
REMARK 500 2 GLN A 19 -5.19 58.58
REMARK 500 2 LYS A 46 38.95 -77.86
REMARK 500 2 HIS A 58 -20.12 66.22
REMARK 500 2 ASP B 18 35.13 -76.89
REMARK 500 2 GLN B 19 8.36 57.60
REMARK 500 3 LYS A 47 -38.79 56.66
REMARK 500 3 GLN B 19 -39.60 60.85
REMARK 500 3 LYS B 46 40.71 -77.84
REMARK 500 4 HIS A 3 18.99 58.39
REMARK 500 4 GLN A 19 -17.40 62.45
REMARK 500 4 ASN A 32 71.24 57.34
REMARK 500 4 ILE A 33 69.75 -105.25
REMARK 500 4 ASN B 9 -14.25 -145.96
REMARK 500 4 ASN B 45 31.97 -143.80
REMARK 500 4 LYS B 47 -146.63 45.96
REMARK 500 5 GLN A 12 36.22 -146.76
REMARK 500 5 GLN A 19 -1.22 61.93
REMARK 500 5 ALA A 54 166.74 59.22
REMARK 500 5 SER A 57 48.52 -74.59
REMARK 500 5 LEU B 17 -50.99 58.97
REMARK 500 5 GLN B 19 -27.39 59.05
REMARK 500 6 ASP A 18 -58.63 -162.61
REMARK 500 6 SER B 48 -179.42 59.99
REMARK 500 7 ALA A 10 173.59 59.21
REMARK 500 7 ASP A 18 -76.09 -146.22
REMARK 500 7 MET B 4 19.20 54.03
REMARK 500 7 SER B 48 173.13 -55.06
REMARK 500 7 SER B 57 169.52 62.03
REMARK 500 8 ALA A 5 -177.21 56.59
REMARK 500 8 GLU A 13 31.86 -84.54
REMARK 500 8 ASP A 18 47.42 -85.94
REMARK 500 8 GLN A 19 18.02 59.15
REMARK 500 8 LYS A 46 19.85 52.83
REMARK 500 8 SER B 2 144.36 65.24
REMARK 500 8 HIS B 3 166.01 59.69
REMARK 500 8 HIS B 14 18.08 -152.33
REMARK 500 8 ASP B 18 -51.34 -150.77
REMARK 500 8 ARG B 56 49.69 -79.11
REMARK 500 9 GLU A 16 40.88 -80.14
REMARK 500 9 ASP A 18 -58.13 -126.02
REMARK 500 9 SER A 48 7.55 59.98
REMARK 500 9 ASN A 61 -42.22 -152.06
REMARK 500 9 HIS B 14 48.57 -74.49
REMARK 500 9 ASP B 18 88.36 -69.32
REMARK 500 9 LYS B 47 -172.42 60.84
REMARK 500
REMARK 500 THIS ENTRY HAS 54 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 30192 RELATED DB: BMRB
REMARK 900 SOLUTION STRUCTURE OF SINI, ANTAGONIST TO THE MASTER BIOFILM-
REMARK 900 REGULATOR SINR IN BACILLUS SUBTILIS
REMARK 900 RELATED ID: 5TN0 RELATED DB: PDB
REMARK 900 RELATED ID: 5TN2 RELATED DB: PDB
DBREF 5TMX A 7 63 UNP P23308 SINI_BACSU 1 57
DBREF 5TMX B 7 63 UNP P23308 SINI_BACSU 1 57
SEQADV 5TMX GLY A 1 UNP P23308 EXPRESSION TAG
SEQADV 5TMX SER A 2 UNP P23308 EXPRESSION TAG
SEQADV 5TMX HIS A 3 UNP P23308 EXPRESSION TAG
SEQADV 5TMX MET A 4 UNP P23308 EXPRESSION TAG
SEQADV 5TMX ALA A 5 UNP P23308 EXPRESSION TAG
SEQADV 5TMX SER A 6 UNP P23308 EXPRESSION TAG
SEQADV 5TMX GLY B 1 UNP P23308 EXPRESSION TAG
SEQADV 5TMX SER B 2 UNP P23308 EXPRESSION TAG
SEQADV 5TMX HIS B 3 UNP P23308 EXPRESSION TAG
SEQADV 5TMX MET B 4 UNP P23308 EXPRESSION TAG
SEQADV 5TMX ALA B 5 UNP P23308 EXPRESSION TAG
SEQADV 5TMX SER B 6 UNP P23308 EXPRESSION TAG
SEQRES 1 A 63 GLY SER HIS MET ALA SER MET LYS ASN ALA LYS GLN GLU
SEQRES 2 A 63 HIS PHE GLU LEU ASP GLN GLU TRP VAL GLU LEU MET VAL
SEQRES 3 A 63 GLU ALA LYS GLU ALA ASN ILE SER PRO GLU GLU ILE ARG
SEQRES 4 A 63 LYS TYR LEU LEU LEU ASN LYS LYS SER ALA HIS PRO GLY
SEQRES 5 A 63 PRO ALA ALA ARG SER HIS THR VAL ASN PRO PHE
SEQRES 1 B 63 GLY SER HIS MET ALA SER MET LYS ASN ALA LYS GLN GLU
SEQRES 2 B 63 HIS PHE GLU LEU ASP GLN GLU TRP VAL GLU LEU MET VAL
SEQRES 3 B 63 GLU ALA LYS GLU ALA ASN ILE SER PRO GLU GLU ILE ARG
SEQRES 4 B 63 LYS TYR LEU LEU LEU ASN LYS LYS SER ALA HIS PRO GLY
SEQRES 5 B 63 PRO ALA ALA ARG SER HIS THR VAL ASN PRO PHE
HELIX 1 AA1 ASP A 18 ASN A 32 1 15
HELIX 2 AA2 PRO A 35 ASN A 45 1 11
HELIX 3 AA3 LEU B 17 ASN B 32 1 16
HELIX 4 AA4 PRO B 35 ASN B 45 1 11
CISPEP 1 MET B 7 LYS B 8 1 -8.50
CISPEP 2 LEU A 17 ASP A 18 5 2.36
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
