Header list of 1q5f.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 07-AUG-03 1Q5F
TITLE NMR STRUCTURE OF TYPE IVB PILIN (PILS) FROM SALMONELLA TYPHI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PILS;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 26-181;
COMPND 5 SYNONYM: TYPE IVB PILIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHI;
SOURCE 3 ORGANISM_TAXID: 601;
SOURCE 4 GENE: PILS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-H
KEYWDS TYPE IVB PILIN, ALPHA-BETA ROLL, MONOMER, CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR X.F.XU,Y.W.TAN,J.HACKETT,M.ZHANG,Y.K.MOK
REVDAT 3 02-MAR-22 1Q5F 1 REMARK
REVDAT 2 24-FEB-09 1Q5F 1 VERSN
REVDAT 1 27-JUL-04 1Q5F 0
JRNL AUTH X.F.XU,Y.W.TAN,L.LAM,J.HACKETT,M.ZHANG,Y.K.MOK
JRNL TITL NMR STRUCTURE OF A TYPE IVB PILIN FROM SALMONELLA TYPHI AND
JRNL TITL 2 ITS ASSEMBLY INTO PILUS
JRNL REF J.BIOL.CHEM. V. 279 31599 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15159389
JRNL DOI 10.1074/JBC.M404727200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, AMBER 7.0
REMARK 3 AUTHORS : CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Q5F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000019938.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 0.55
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM PILS U-15N, 13C; 50MM
REMARK 210 PHOSPHATE BUFFER; 0.5M SODIUM
REMARK 210 SULFATE; 90% H2O, 10% D2O; 1MM
REMARK 210 PILS 10% 13C; 50MM PHOSPHATE
REMARK 210 BUFFER; 0.5M SODIUM SULFATE; 90%
REMARK 210 H2O, 10% D2O; 1MM PILS U-15N;
REMARK 210 50MM PHOSPHATE BUFFER; 0.5M
REMARK 210 SODIUM SULFATE; 90% H2O, 10% D2O;
REMARK 210 1MM PILS U-15N; 50MM PHOSPHATE
REMARK 210 BUFFER; 0.5M SODIUM SULFATE; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; AMIDE
REMARK 210 PROTON EXCHANGE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW, DYANA, CYANA
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 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: THE STRUCTURES ARE BASED ON A TOTAL OF 2315 RESTRAINTS,
REMARK 210 2033 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 206 DIHEDRAL ANGLE
REMARK 210 RESTRAINTS, 76 DISTANCE RESTRAINTS FROM HYDROGEN BONDS.
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 TRP A 27 -66.13 -128.96
REMARK 500 1 LYS A 29 -62.10 69.11
REMARK 500 1 MET A 50 34.32 -153.44
REMARK 500 1 LYS A 51 31.48 -80.18
REMARK 500 1 ASP A 54 -50.02 -160.96
REMARK 500 1 PHE A 58 166.25 58.66
REMARK 500 1 ALA A 62 -62.75 -107.17
REMARK 500 1 ALA A 73 -76.90 -82.11
REMARK 500 1 ASP A 82 115.79 -35.92
REMARK 500 1 SER A 85 86.42 52.48
REMARK 500 1 THR A 108 -43.95 -142.10
REMARK 500 1 LYS A 120 -36.57 -174.89
REMARK 500 1 VAL A 121 101.95 -48.61
REMARK 500 1 SER A 136 46.94 -150.08
REMARK 500 1 SER A 140 -33.49 -172.21
REMARK 500 1 ASN A 148 98.96 -36.62
REMARK 500 1 THR A 150 -46.48 -147.98
REMARK 500 1 ASP A 166 117.05 -177.21
REMARK 500 1 ARG A 169 79.89 -100.68
REMARK 500 2 LYS A 29 -66.96 -135.74
REMARK 500 2 MET A 49 -71.49 -136.64
REMARK 500 2 ASP A 54 110.74 65.00
REMARK 500 2 THR A 59 86.16 57.17
REMARK 500 2 ALA A 73 -81.16 -123.21
REMARK 500 2 SER A 87 57.80 -175.43
REMARK 500 2 PHE A 110 33.55 -163.02
REMARK 500 2 LYS A 120 -31.92 -171.43
REMARK 500 2 VAL A 121 107.06 -53.50
REMARK 500 2 PRO A 122 -169.47 -74.85
REMARK 500 2 SER A 136 48.44 -150.61
REMARK 500 2 THR A 139 -88.62 -69.55
REMARK 500 2 SER A 140 -40.36 172.86
REMARK 500 2 ASN A 147 34.34 -84.59
REMARK 500 2 ASN A 148 93.36 -46.32
REMARK 500 2 HIS A 149 -168.22 -113.94
REMARK 500 2 THR A 150 -49.71 -138.70
REMARK 500 2 LYS A 153 70.62 -117.91
REMARK 500 2 ALA A 165 -174.91 65.08
REMARK 500 2 ARG A 169 59.50 -174.39
REMARK 500 3 LYS A 29 -64.92 -135.92
REMARK 500 3 MET A 50 60.42 -154.74
REMARK 500 3 TYR A 56 165.95 59.78
REMARK 500 3 THR A 59 56.59 -102.38
REMARK 500 3 SER A 60 83.25 -56.64
REMARK 500 3 ALA A 73 -83.86 -110.34
REMARK 500 3 SER A 85 -33.59 160.36
REMARK 500 3 SER A 87 61.62 -179.80
REMARK 500 3 PHE A 110 29.09 -166.49
REMARK 500 3 LYS A 120 -42.90 160.38
REMARK 500 3 VAL A 121 103.64 -45.87
REMARK 500
REMARK 500 THIS ENTRY HAS 211 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5879 RELATED DB: BMRB
DBREF 1Q5F A 26 181 UNP Q9ZIU9 Q9ZIU9_SALTI 51 206
SEQRES 1 A 156 MET TRP GLY LYS LYS ASP ALA GLY THR GLU LEU THR ASN
SEQRES 2 A 156 TYR GLN THR LEU ALA THR ASN THR ILE GLY MET MET LYS
SEQRES 3 A 156 GLY VAL ASP GLY TYR ALA PHE THR SER GLY ALA LYS MET
SEQRES 4 A 156 THR ASP THR LEU ILE GLN ALA GLY ALA ALA LYS GLY MET
SEQRES 5 A 156 THR VAL SER GLY ASP PRO ALA SER GLY SER ALA THR LEU
SEQRES 6 A 156 TRP ASN SER TRP GLY GLY GLN ILE VAL VAL ALA PRO ASP
SEQRES 7 A 156 THR ALA GLY GLY THR GLY PHE ASN ASN GLY PHE THR ILE
SEQRES 8 A 156 THR THR ASN LYS VAL PRO GLN SER ALA CYS VAL SER ILE
SEQRES 9 A 156 SER THR GLY MET SER ARG SER GLY GLY THR SER GLY ILE
SEQRES 10 A 156 LYS ILE ASN GLY ASN ASN HIS THR ASP ALA LYS VAL THR
SEQRES 11 A 156 ALA GLU ILE ALA SER SER GLU CYS THR ALA ASP ASN GLY
SEQRES 12 A 156 ARG THR GLY THR ASN THR LEU VAL PHE ASN TYR ASN GLY
HELIX 1 1 ALA A 32 ILE A 47 1 16
HELIX 2 2 ALA A 62 ALA A 71 1 10
HELIX 3 3 PRO A 122 ARG A 135 1 14
HELIX 4 4 THR A 155 CYS A 163 1 9
SHEET 1 A 6 VAL A 79 SER A 80 0
SHEET 2 A 6 ALA A 88 TRP A 91 -1 O THR A 89 N SER A 80
SHEET 3 A 6 GLN A 97 PRO A 102 -1 O ILE A 98 N LEU A 90
SHEET 4 A 6 GLY A 113 ASN A 119 -1 O THR A 115 N ALA A 101
SHEET 5 A 6 THR A 174 ASN A 180 -1 O PHE A 177 N ILE A 116
SHEET 6 A 6 LYS A 143 ILE A 144 -1 N LYS A 143 O VAL A 176
SSBOND 1 CYS A 126 CYS A 163 1555 1555 2.02
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
Complete list - r 2 2 Bytes