Header list of 2bw2.pdb file
Complete list - y 9 2 Bytes
HEADER SIGNALING PROTEIN 08-JUL-05 2BW2
TITLE BOFC FROM BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BYPASS OF FORESPORE C;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 STRAIN: IG20;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 OTHER_DETAILS: NCIMB11621
KEYWDS SPORULATION, SIGNALING PROTEIN, BOFC, SIGMAK CHECKPOINT
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR H.M.PATTERSON,J.A.BRANNIGAN,S.M.CUTTING,K.S.WILSON,A.J.WILKINSON,
AUTHOR 2 E.AB,T.DIERCKS,G.E.FOLKERS,R.N.DE JONG,V.TRUFFAULT,R.KAPTEIN
REVDAT 4 09-MAY-18 2BW2 1 JRNL REMARK
REVDAT 3 24-FEB-09 2BW2 1 VERSN
REVDAT 2 26-OCT-05 2BW2 1 AUTHOR JRNL
REVDAT 1 15-SEP-05 2BW2 0
JRNL AUTH H.M.PATTERSON,J.A.BRANNIGAN,S.M.CUTTING,K.S.WILSON,
JRNL AUTH 2 A.J.WILKINSON,E.AB,T.DIERCKS,R.N.DE JONG,V.TRUFFAULT,
JRNL AUTH 3 G.E.FOLKERS,R.KAPTEIN
JRNL TITL THE STRUCTURE OF BYPASS OF FORESPORE C, AN
JRNL TITL 2 INTERCOMPARTMENTAL SIGNALING FACTOR DURING SPORULATION IN
JRNL TITL 3 BACILLUS.
JRNL REF J. BIOL. CHEM. V. 280 36214 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 16049010
JRNL DOI 10.1074/JBC.M506910200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-
REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 2BW2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1290024766.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 20
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 95% WATER/5% D20
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY
REMARK 210 METHOD USED : CANDID AND CNS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED BOFC.
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 OE2 GLU A 31 HH TYR A 43 1.59
REMARK 500
REMARK 500 REMARK: NULL
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 12 VAL A 56 CA - CB - CG2 ANGL. DEV. = 11.3 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 SER A 66 153.59 102.95
REMARK 500 1 ASN A 72 -84.38 -92.61
REMARK 500 1 ILE A 83 37.16 -80.96
REMARK 500 1 PHE A 122 147.31 -172.98
REMARK 500 1 SER A 139 17.03 55.40
REMARK 500 2 SER A 66 161.13 160.31
REMARK 500 2 ASN A 72 37.50 -157.91
REMARK 500 2 ILE A 83 36.89 -80.62
REMARK 500 2 PHE A 100 -74.29 -89.81
REMARK 500 2 SER A 110 -64.41 174.31
REMARK 500 2 TYR A 138 -61.65 -93.24
REMARK 500 3 GLU A 4 98.91 -61.20
REMARK 500 3 HIS A 5 -164.03 -106.04
REMARK 500 3 LYS A 53 -76.64 39.13
REMARK 500 3 ILE A 83 36.26 -80.25
REMARK 500 3 PHE A 100 -71.91 -69.63
REMARK 500 3 GLU A 109 -72.80 -65.61
REMARK 500 3 SER A 110 -64.09 -162.46
REMARK 500 3 PHE A 122 143.40 -174.41
REMARK 500 4 ASP A 64 -91.42 -119.86
REMARK 500 4 ASN A 72 -81.51 -98.79
REMARK 500 4 TYR A 74 107.91 -160.05
REMARK 500 4 ILE A 83 38.79 -81.02
REMARK 500 4 PRO A 90 99.49 -64.91
REMARK 500 4 GLN A 98 -168.73 -160.07
REMARK 500 4 PHE A 100 -70.85 -83.46
REMARK 500 5 HIS A 5 -163.39 68.99
REMARK 500 5 LYS A 53 94.98 -67.01
REMARK 500 5 ASN A 72 -72.60 -79.27
REMARK 500 5 ILE A 83 36.28 -80.42
REMARK 500 5 GLN A 98 -160.67 -162.52
REMARK 500 5 PHE A 100 -73.16 -108.74
REMARK 500 5 GLU A 109 -73.16 -64.41
REMARK 500 5 SER A 110 -80.97 -162.92
REMARK 500 5 PHE A 122 141.38 -175.07
REMARK 500 5 SER A 139 17.13 49.86
REMARK 500 6 PRO A 8 -168.97 -73.70
REMARK 500 6 SER A 66 145.55 141.98
REMARK 500 6 ASN A 72 75.56 -151.58
REMARK 500 6 ILE A 83 37.92 -81.43
REMARK 500 7 HIS A 5 -171.12 76.28
REMARK 500 7 LYS A 53 98.77 -68.14
REMARK 500 7 ASN A 72 -73.91 -85.79
REMARK 500 7 ILE A 83 36.49 -81.68
REMARK 500 7 PHE A 100 -91.71 -97.11
REMARK 500 7 GLU A 109 -75.26 -59.86
REMARK 500 7 SER A 110 -69.12 -172.81
REMARK 500 7 PHE A 122 139.34 -178.65
REMARK 500 7 SER A 139 7.89 55.05
REMARK 500 8 LYS A 53 97.80 -68.84
REMARK 500
REMARK 500 THIS ENTRY HAS 200 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 2 ARG A 123 0.09 SIDE CHAIN
REMARK 500 5 ARG A 123 0.07 SIDE CHAIN
REMARK 500 11 ARG A 107 0.07 SIDE CHAIN
REMARK 500 12 ARG A 107 0.07 SIDE CHAIN
REMARK 500 16 ARG A 107 0.07 SIDE CHAIN
REMARK 500 19 ARG A 107 0.08 SIDE CHAIN
REMARK 500 20 ARG A 123 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6731 RELATED DB: BMRB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE PROTEIN PRECURSOR FOR BOFC HAS 170 RESIDUES. THE NMR
REMARK 999 STRUCTURE IS FOR MATURE BOFC, WITH THE N-TERMINAL 30
REMARK 999 RESIDUE TRANSLOCATION SEQUENCE CLEAVED. THE NMR STRUCTURE
REMARK 999 REFERS TO RESIDUE NUMBERS FOR THE MATURE PROTEIN, IE
REMARK 999 RESIDUES A1-G140 (NOT A31-G170)
DBREF 2BW2 A 1 140 UNP O05391 BOFC_BACSU 31 170
SEQRES 1 A 140 ALA GLU VAL GLU HIS TYR GLU PRO LEU GLN VAL HIS VAL
SEQRES 2 A 140 GLN LEU GLU LYS VAL TYR LEU ASP GLY ASP VAL SER ILE
SEQRES 3 A 140 GLU HIS LYS HIS GLU LYS VAL PHE SER MET ASP ASP PHE
SEQRES 4 A 140 TRP ALA ALA TYR ALA GLY TRP THR LEU VAL GLU GLN LYS
SEQRES 5 A 140 LYS GLY TYR VAL LEU PHE ARG LYS GLN MET ASP ASP ILE
SEQRES 6 A 140 SER PRO LEU SER LYS VAL ASN GLY TYR ILE GLY VAL SER
SEQRES 7 A 140 ASP ASN GLY VAL ILE SER THR PHE HIS GLY ARG PRO GLU
SEQRES 8 A 140 PRO ALA SER GLU PRO ILE GLN SER PHE PHE GLN ILE ASP
SEQRES 9 A 140 LEU GLU ARG LEU GLU SER HIS MET GLN LYS ASN LEU LEU
SEQRES 10 A 140 LYS GLY ILE PRO PHE ARG THR LYS ALA GLU PHE GLU ASP
SEQRES 11 A 140 VAL ILE GLU HIS MET LYS THR TYR SER GLY
HELIX 1 1 MET A 36 TYR A 43 1 8
HELIX 2 2 PRO A 67 VAL A 71 5 5
HELIX 3 3 GLU A 109 GLY A 119 1 11
HELIX 4 4 THR A 124 SER A 139 1 16
SHEET 1 AA 4 VAL A 24 SER A 35 0
SHEET 2 AA 4 GLU A 4 VAL A 18 -1 N HIS A 5 O PHE A 34
SHEET 3 AA 4 TYR A 55 GLN A 61 1 O VAL A 56 N GLN A 14
SHEET 4 AA 4 THR A 47 LYS A 52 -1 O THR A 47 N ARG A 59
SHEET 1 AB 2 ILE A 75 SER A 78 0
SHEET 2 AB 2 VAL A 82 THR A 85 -1 N VAL A 82 O SER A 78
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 - y 9 2 Bytes