HEADER MEMBRANE PROTEIN 07-JAN-10 2KSM
TITLE CENTRAL B DOMAIN OF RV0899 FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYCOBACTERIUM TUBERCULOSIS RV0899/MT0922/OMPATB;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BON DOMAIN CONTAINING REGION;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: H37RV NCTC 7416;
SOURCE 5 GENE: MT0922, MTCY31.27, RV0899;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: C41(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS OMPATB, BON DOMAIN, MEMBRANE PROTEIN, TRANSMEMBRANE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.TERIETE,Y.YAO,A.KOLODZIK,J.YU,H.SONG,M.NIEDERWEIS,F.M.MARASSI
REVDAT 6 16-MAR-22 2KSM 1 REMARK
REVDAT 5 14-APR-10 2KSM 1 JRNL
REVDAT 4 16-MAR-10 2KSM 1 JRNL
REVDAT 3 16-FEB-10 2KSM 1 COMPND REMARK
REVDAT 2 09-FEB-10 2KSM 1 AUTHOR KEYWDS TITLE
REVDAT 1 02-FEB-10 2KSM 0
JRNL AUTH P.TERIETE,Y.YAO,A.KOLODZIK,J.YU,H.SONG,M.NIEDERWEIS,
JRNL AUTH 2 F.M.MARASSI
JRNL TITL MYCOBACTERIUM TUBERCULOSIS RV0899 ADOPTS A MIXED
JRNL TITL 2 ALPHA/BETA-STRUCTURE AND DOES NOT FORM A TRANSMEMBRANE
JRNL TITL 3 BETA-BARREL.
JRNL REF BIOCHEMISTRY V. 49 2768 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 20199110
JRNL DOI 10.1021/BI100158S
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 3.0, X-PLOR NIH 2.24
REMARK 3 AUTHORS : DELAGLIO, F. ET AL. (NMRPIPE), SCHWIETERS, C.D. ET
REMARK 3 AL. (X-PLOR NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: XPLOR-NIH, XPLOR-NIH INTERNAL VARIABLE
REMARK 3 DYNAMICS MODULE (IVM)
REMARK 4
REMARK 4 2KSM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000101523.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 0.005
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.7 MM [U-99% 15N] RV0899(73
REMARK 210 -220), 1 MM [U-99% 13C; U-99%
REMARK 210 15N] RV0899(73-220), 95% H2O/5%
REMARK 210 D2O; 1 MM [U-99% 13C; U-99% 15N]
REMARK 210 RV0899(73-220), 0.3 MM [U-99%
REMARK 210 15N] RV0899(73-220), 100% D2O;
REMARK 210 0.4 MM [U-99% 15N] RV0899(73-220)
REMARK 210 , 95% H2O/5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; IPAP; 2D 1H-13C
REMARK 210 HSQC; 3D HNCA; 3D HNCACB; 3D
REMARK 210 C(CO)NH; 3D HCCH-TOCSY; 3D 1H-
REMARK 210 15N NOESY; 3D 1H-15N TOCSY; 3D
REMARK 210 1H-13C NOESY; 3D HNCO
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.115, TALOS, REDCAT,
REMARK 210 PYMOL
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
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 O PHE A 135 H ALA A 138 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 SER A 75 -179.44 49.19
REMARK 500 1 LEU A 77 35.50 -90.59
REMARK 500 1 ASN A 89 -74.02 -42.87
REMARK 500 1 ASP A 127 77.53 -162.90
REMARK 500 1 PRO A 128 3.00 -51.18
REMARK 500 1 PRO A 147 19.21 -60.70
REMARK 500 1 GLU A 156 -149.52 -101.14
REMARK 500 1 PRO A 167 -2.27 -52.77
REMARK 500 1 SER A 168 -113.81 -109.96
REMARK 500 1 SER A 169 -96.16 -173.86
REMARK 500 2 LEU A 77 -76.34 -136.93
REMARK 500 2 SER A 87 68.75 -174.51
REMARK 500 2 PRO A 128 -74.03 -39.66
REMARK 500 2 VAL A 129 45.33 -159.57
REMARK 500 2 PRO A 147 19.17 -64.77
REMARK 500 2 GLU A 156 -149.24 -100.15
REMARK 500 2 ASP A 158 -12.55 -164.45
REMARK 500 2 PRO A 167 -1.52 -51.18
REMARK 500 2 SER A 168 -124.30 -95.87
REMARK 500 2 SER A 169 -103.29 -161.28
REMARK 500 2 LYS A 187 109.67 -50.61
REMARK 500 2 GLN A 197 173.48 52.31
REMARK 500 2 PRO A 200 -14.54 -42.73
REMARK 500 3 ALA A 74 153.57 60.88
REMARK 500 3 SER A 87 133.83 -175.43
REMARK 500 3 ASN A 89 -30.76 -138.25
REMARK 500 3 ASP A 127 78.64 -154.58
REMARK 500 3 PRO A 128 -2.03 -52.88
REMARK 500 3 GLU A 156 -149.73 -95.12
REMARK 500 3 PRO A 167 -1.20 -49.89
REMARK 500 3 SER A 168 -131.20 -94.14
REMARK 500 3 SER A 169 -103.88 -158.75
REMARK 500 3 THR A 195 100.97 -43.03
REMARK 500 3 GLN A 197 12.73 58.50
REMARK 500 3 PRO A 200 89.67 -46.19
REMARK 500 4 LEU A 114 104.13 -39.72
REMARK 500 4 ASP A 127 79.49 -159.75
REMARK 500 4 PRO A 128 0.94 -55.92
REMARK 500 4 VAL A 130 -166.92 -69.95
REMARK 500 4 PRO A 147 19.26 -64.69
REMARK 500 4 GLU A 156 -149.74 -98.83
REMARK 500 4 PRO A 167 -1.72 -55.61
REMARK 500 4 SER A 168 103.49 84.90
REMARK 500 4 SER A 169 167.83 164.91
REMARK 500 4 GLN A 197 -169.28 46.80
REMARK 500 4 PRO A 200 -177.64 -45.28
REMARK 500 5 LEU A 77 92.94 -62.52
REMARK 500 5 SER A 80 89.26 -162.89
REMARK 500 5 ASN A 111 -19.97 -44.20
REMARK 500 5 ASP A 127 82.98 -162.02
REMARK 500
REMARK 500 THIS ENTRY HAS 273 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2KSM A 73 203 UNP P65593 Y899_MYCTU 73 203
SEQRES 1 A 131 GLY ALA SER ALA LEU SER LEU SER LEU LEU SER ILE SER
SEQRES 2 A 131 ARG SER GLY ASN THR VAL THR LEU ILE GLY ASP PHE PRO
SEQRES 3 A 131 ASP GLU ALA ALA LYS ALA ALA LEU MET THR ALA LEU ASN
SEQRES 4 A 131 GLY LEU LEU ALA PRO GLY VAL ASN VAL ILE ASP GLN ILE
SEQRES 5 A 131 HIS VAL ASP PRO VAL VAL ARG SER LEU ASP PHE SER SER
SEQRES 6 A 131 ALA GLU PRO VAL PHE THR ALA SER VAL PRO ILE PRO ASP
SEQRES 7 A 131 PHE GLY LEU LYS VAL GLU ARG ASP THR VAL THR LEU THR
SEQRES 8 A 131 GLY THR ALA PRO SER SER GLU HIS LYS ASP ALA VAL LYS
SEQRES 9 A 131 ARG ALA ALA THR SER THR TRP PRO ASP MET LYS ILE VAL
SEQRES 10 A 131 ASN ASN ILE GLU VAL THR GLY GLN ALA PRO PRO GLY PRO
SEQRES 11 A 131 PRO
HELIX 1 1 GLU A 100 ASN A 111 1 12
HELIX 2 2 ASP A 134 SER A 136 5 3
HELIX 3 3 SER A 137 SER A 145 1 9
HELIX 4 4 GLU A 170 TRP A 183 1 14
SHEET 1 A 6 ASN A 119 VAL A 126 0
SHEET 2 A 6 THR A 90 PHE A 97 1 N PHE A 97 O HIS A 125
SHEET 3 A 6 LEU A 82 ARG A 86 -1 N SER A 85 O THR A 92
SHEET 4 A 6 PHE A 151 VAL A 155 -1 O LEU A 153 N ILE A 84
SHEET 5 A 6 THR A 159 GLY A 164 -1 O THR A 161 N LYS A 154
SHEET 6 A 6 LYS A 187 ASN A 190 1 O LYS A 187 N VAL A 160
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
