HEADER LIGAND BINDING PROTEIN 27-JUL-06 2DUW
TITLE SOLUTION STRUCTURE OF PUTATIVE COA-BINDING PROTEIN OF KLEBSIELLA
TITLE 2 PNEUMONIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE COA-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 573;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET-22B(+)
KEYWDS KLEBSIELLA PNEUMONIAE, PUTATIVE COA-BINDING PROTEIN, LIGAND BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.W.HUNG,Y.C.LIN,C.C.CHENG,C.F.CHANG,S.F.TSAI,T.H.HUANG
REVDAT 3 09-MAR-22 2DUW 1 REMARK
REVDAT 2 24-FEB-09 2DUW 1 VERSN
REVDAT 1 14-AUG-07 2DUW 0
JRNL AUTH K.W.HUNG,Y.C.LIN,C.C.CHENG,P.J.FANG,C.F.CHANG,S.F.TSAI,
JRNL AUTH 2 T.H.HUANG
JRNL TITL SOLUTION STRUCTURE OF PUTATIVE COA-BINDING PROTEIN OF
JRNL TITL 2 KLEBSIELLA PNEUMONIAE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), PETER GUNTERT (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1912
REMARK 3 DISTANCE CONSTRAINTS AND 150 ANGLE CONSTRAINTS
REMARK 4
REMARK 4 2DUW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1000025872.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 20MM TRIS-HCL BUFFER CONTAINING
REMARK 210 50MM NACL, 50MM GLU AND 50MM ARG
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM PUTATIVE COA BINDING
REMARK 210 PROTEIN, U-15N, 13C; 20MM TRIS-
REMARK 210 HCL BUFFER CONTAINING 50MM NACL,
REMARK 210 50MM GLU AND 50MM ARG, 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, SPARKY 3.112, CYANA
REMARK 210 2.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 LEU A 138
REMARK 465 GLU A 139
REMARK 465 HIS A 140
REMARK 465 HIS A 141
REMARK 465 HIS A 142
REMARK 465 HIS A 143
REMARK 465 HIS A 144
REMARK 465 HIS A 145
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 LYS A 2 41.96 -95.36
REMARK 500 1 ASN A 4 71.68 -110.06
REMARK 500 1 SER A 22 -169.10 -106.33
REMARK 500 1 ASP A 23 44.56 -94.85
REMARK 500 1 ALA A 51 99.39 -57.17
REMARK 500 1 ALA A 95 -178.34 -68.91
REMARK 500 1 LYS A 96 -40.75 -133.60
REMARK 500 1 LEU A 100 -169.97 -104.86
REMARK 500 2 SER A 22 -168.69 -106.92
REMARK 500 2 ASP A 23 43.27 -92.66
REMARK 500 2 ALA A 51 103.50 -54.70
REMARK 500 2 ALA A 95 -179.73 -57.90
REMARK 500 3 SER A 22 -169.58 -102.69
REMARK 500 3 ASP A 23 44.10 -94.80
REMARK 500 3 ALA A 51 102.90 -54.31
REMARK 500 3 VAL A 67 108.52 -50.36
REMARK 500 3 ARG A 78 -72.08 -51.61
REMARK 500 3 LYS A 96 -43.93 -130.42
REMARK 500 4 ASP A 23 43.36 -93.54
REMARK 500 4 ALA A 51 103.24 -54.60
REMARK 500 4 VAL A 67 108.47 -50.40
REMARK 500 4 ALA A 95 177.97 -59.57
REMARK 500 5 ASP A 5 -75.30 -110.15
REMARK 500 5 ASP A 23 43.26 -93.38
REMARK 500 5 ALA A 51 104.28 -54.32
REMARK 500 5 ARG A 78 -73.91 -64.77
REMARK 500 5 ALA A 95 -176.68 -69.68
REMARK 500 5 ALA A 136 172.07 -53.32
REMARK 500 6 ASP A 23 43.30 -92.29
REMARK 500 6 ALA A 51 100.82 -55.22
REMARK 500 6 ARG A 78 -70.60 -51.55
REMARK 500 6 ALA A 95 -169.82 -70.25
REMARK 500 7 SER A 22 -169.62 -168.62
REMARK 500 7 ASP A 23 44.48 -95.00
REMARK 500 7 ALA A 51 82.76 -69.41
REMARK 500 7 ARG A 78 -74.09 -51.32
REMARK 500 8 ASN A 4 -65.73 -95.03
REMARK 500 8 SER A 22 -168.82 -107.38
REMARK 500 8 ASP A 23 43.09 -92.43
REMARK 500 8 ILE A 44 77.61 -113.99
REMARK 500 8 ALA A 51 82.39 -69.30
REMARK 500 8 LEU A 100 -169.92 -112.13
REMARK 500 9 ASN A 4 54.37 -102.99
REMARK 500 9 ASP A 23 41.73 -93.12
REMARK 500 9 ALA A 51 90.71 -63.65
REMARK 500 9 ARG A 78 -74.51 -51.10
REMARK 500 9 ALA A 136 -178.79 -56.52
REMARK 500 10 ASP A 23 43.34 -92.96
REMARK 500 10 ALA A 51 104.75 -54.35
REMARK 500 10 ALA A 136 174.38 -53.47
REMARK 500
REMARK 500 THIS ENTRY HAS 105 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 A SEQUENCE DATABASE REFERENCE FOR THIS PROTEIN
REMARK 999 DOES NOT CURRENTLY EXIST.
REMARK 999 8 RESIDUES IN THE C TERMINUS WERE CLONING ARTIFACTS.
DBREF 2DUW A 1 137 UNP A6T758 A6T758_KLEP7 1 137
SEQRES 1 A 145 MET LYS GLU ASN ASP ILE ALA GLY ILE LEU THR SER THR
SEQRES 2 A 145 ARG THR ILE ALA LEU VAL GLY ALA SER ASP LYS PRO ASP
SEQRES 3 A 145 ARG PRO SER TYR ARG VAL MET LYS TYR LEU LEU ASP GLN
SEQRES 4 A 145 GLY TYR HIS VAL ILE PRO VAL SER PRO LYS VAL ALA GLY
SEQRES 5 A 145 LYS THR LEU LEU GLY GLN GLN GLY TYR ALA THR LEU ALA
SEQRES 6 A 145 ASP VAL PRO GLU LYS VAL ASP MET VAL ASP VAL PHE ARG
SEQRES 7 A 145 ASN SER GLU ALA ALA TRP GLY VAL ALA GLN GLU ALA ILE
SEQRES 8 A 145 ALA ILE GLY ALA LYS THR LEU TRP LEU GLN LEU GLY VAL
SEQRES 9 A 145 ILE ASN GLU GLN ALA ALA VAL LEU ALA ARG GLU ALA GLY
SEQRES 10 A 145 LEU SER VAL VAL MET ASP ARG CYS PRO ALA ILE GLU LEU
SEQRES 11 A 145 PRO ARG LEU GLY LEU ALA LYS LEU GLU HIS HIS HIS HIS
SEQRES 12 A 145 HIS HIS
HELIX 1 1 ASP A 5 THR A 13 1 9
HELIX 2 2 ARG A 27 GLY A 40 1 14
HELIX 3 3 GLU A 81 GLY A 94 1 14
HELIX 4 4 ASN A 106 GLU A 115 1 10
HELIX 5 5 CYS A 125 LEU A 130 1 6
SHEET 1 A 5 VAL A 43 VAL A 46 0
SHEET 2 A 5 ILE A 16 VAL A 19 1 N LEU A 18 O VAL A 46
SHEET 3 A 5 MET A 73 ASP A 75 1 O ASP A 75 N ALA A 17
SHEET 4 A 5 THR A 97 TRP A 99 1 O TRP A 99 N VAL A 74
SHEET 5 A 5 SER A 119 VAL A 121 1 O SER A 119 N LEU A 98
SHEET 1 B 2 THR A 54 LEU A 55 0
SHEET 2 B 2 GLN A 58 GLN A 59 -1 O GLN A 58 N LEU A 55
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
