Header list of 1djm.pdb file
Complete list - b 16 2 Bytes
HEADER SIGNALING PROTEIN 03-DEC-99 1DJM
TITLE SOLUTION STRUCTURE OF BEF3-ACTIVATED CHEY FROM ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHEMOTAXIS PROTEIN Y;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS BEFX, CHEY, RESPONSE REGULATOR, CHEMOTAXIS, TWO-COMPONENT, SIGNALING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 27
AUTHOR H.S.CHO,S.Y.LEE,D.YAN,X.PAN,J.S.PARKINSON,S.KUSTU,D.E.WEMMER,
AUTHOR 2 J.G.PELTON
REVDAT 3 16-FEB-22 1DJM 1 REMARK
REVDAT 2 24-FEB-09 1DJM 1 VERSN
REVDAT 1 05-APR-00 1DJM 0
JRNL AUTH H.S.CHO,S.Y.LEE,D.YAN,X.PAN,J.S.PARKINSON,S.KUSTU,
JRNL AUTH 2 D.E.WEMMER,J.G.PELTON
JRNL TITL NMR STRUCTURE OF ACTIVATED CHEY.
JRNL REF J.MOL.BIOL. V. 297 543 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10731410
JRNL DOI 10.1006/JMBI.2000.3595
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.YAN,H.S.CHO,C.A.HASTINGS,M.M.IGO,S.Y.LEE,J.G.PELTON,
REMARK 1 AUTH 2 V.STEWART,D.E.WEMMER,S.KUSTU
REMARK 1 TITL BERYLLOFLUORIDE MIMICS PHOSPHORYLATION OF NTRC AND OTHER
REMARK 1 TITL 2 BACTERIAL RESPONSE REGULATORS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 96 14789 1999
REMARK 1 REFN ISSN 0027-8424
REMARK 1 DOI 10.1073/PNAS.96.26.14789
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, OPAL 2.2
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER, WUTHRICH (DYANA), LUGINBUHL,
REMARK 3 GUNTERT, BILLETER, WUTHRICH (OPAL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 972 NON-TRIVIAL NOE
REMARK 3 RESTRAINTS (213
REMARK 3 INTRA RESIDUE, 271 SEQUENTIAL, 238 MEDIUM-RANGE, AND 250 LONG-
REMARK 3 RANGE). 78 PHI
REMARK 3 TORSION ANGLE RESTRAINTS AND 17 CHI1 RESTRAINTS WERE USED. 47
REMARK 3 HYDROGEN BONDS (
REMARK 3 94 UPPER AND LOWER DISTANCE RESTRAINTS) WERE USED IN LATER STAGES
REMARK 3 OF REFINEMENT.
REMARK 4
REMARK 4 1DJM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-99.
REMARK 100 THE DEPOSITION ID IS D_1000010135.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298
REMARK 210 PH : 6.7; 6.7; 6.7
REMARK 210 IONIC STRENGTH : 16 MM BECL2, 100 MM NAF, 20 MM
REMARK 210 MGCL2; 16 MM BECL2, 100 MM NAF,
REMARK 210 20 MM MGCL2; 16 MM BECL2, 100 MM
REMARK 210 NAF, 20 MM MGCL2
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 4 MM CHEY U-15N, 13C, 16 MM
REMARK 210 BECL2, 100 MM NAF, 20 MM MGCL2,
REMARK 210 PH 6.7; 3 MM U-15N, 16 MM BECL2,
REMARK 210 100 MM NAF, 20 MM MGCL2, PH 6.7;
REMARK 210 3 MM U-10% 13C, 16 MM BECL2, 100
REMARK 210 MM NAF, 20 MM MGCL2, PH 6.7; 2
REMARK 210 MM CHEY, 16 MM BECL2, 100 MM NAF,
REMARK 210 20 MM MGCL2, PH 6.7
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C-SEPARATED_NOESY;
REMARK 210 4D_13C/15N-SEPARATED_NOESY; 3D_
REMARK 210 15N-SEPARATED_NOESY; 15N HMQC-J;
REMARK 210 13C CONSTANT-TIME HMQC-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.7, XEASY 1.3.11
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 27
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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.
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
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 4 ARG A 18 CD - NE - CZ ANGL. DEV. = 9.4 DEGREES
REMARK 500 4 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 18 TYR A 51 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 22 ARG A 73 NE - CZ - NH2 ANGL. DEV. = -3.2 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 LEU A 6 108.56 -58.60
REMARK 500 1 ASN A 32 82.34 65.15
REMARK 500 1 ASP A 57 -158.25 -73.46
REMARK 500 1 TRP A 58 -30.27 -134.08
REMARK 500 1 MET A 60 154.33 -44.69
REMARK 500 1 ASN A 62 -99.57 -119.98
REMARK 500 1 ARG A 73 4.16 -68.79
REMARK 500 1 ASP A 75 -176.35 64.34
REMARK 500 1 ALA A 77 -72.02 -125.41
REMARK 500 2 GLU A 5 47.48 37.92
REMARK 500 2 ASN A 32 77.17 64.39
REMARK 500 2 ASP A 57 -176.13 -46.93
REMARK 500 2 PRO A 61 26.67 -61.12
REMARK 500 2 ASN A 62 -71.89 -161.33
REMARK 500 2 ASP A 64 153.55 -47.07
REMARK 500 2 ASP A 75 30.49 89.54
REMARK 500 2 LYS A 126 -70.41 -68.49
REMARK 500 3 LEU A 6 106.37 -54.98
REMARK 500 3 PHE A 30 64.76 35.92
REMARK 500 3 ASN A 31 1.48 -68.41
REMARK 500 3 ASN A 62 -89.95 -139.88
REMARK 500 3 ASP A 75 175.08 63.40
REMARK 500 3 ALA A 77 -28.01 -148.10
REMARK 500 4 LEU A 6 109.43 -53.22
REMARK 500 4 SER A 15 -47.27 70.64
REMARK 500 4 LEU A 28 28.53 -146.67
REMARK 500 4 ASN A 32 74.29 60.05
REMARK 500 4 ASP A 75 163.15 68.59
REMARK 500 4 ALA A 77 82.02 -165.85
REMARK 500 4 MET A 78 17.31 103.81
REMARK 500 4 ALA A 90 -95.80 -81.34
REMARK 500 4 LYS A 91 112.16 59.15
REMARK 500 5 ALA A 2 -163.54 -77.93
REMARK 500 5 ASP A 57 -157.60 -78.98
REMARK 500 5 ASN A 59 43.74 -84.63
REMARK 500 5 ASN A 62 -78.13 53.82
REMARK 500 5 ASP A 75 -161.92 -175.16
REMARK 500 5 ALA A 77 -37.33 69.74
REMARK 500 6 SER A 15 -60.18 62.31
REMARK 500 6 LEU A 28 47.37 -156.79
REMARK 500 6 ASN A 32 79.25 60.78
REMARK 500 6 ASN A 62 -99.36 -92.65
REMARK 500 7 ASP A 3 86.68 58.91
REMARK 500 7 LYS A 4 32.53 -76.94
REMARK 500 7 LEU A 6 108.22 -55.07
REMARK 500 7 VAL A 11 70.12 -114.37
REMARK 500 7 PHE A 30 60.23 64.86
REMARK 500 7 ASN A 62 -101.91 -83.54
REMARK 500 7 ALA A 74 -79.40 -59.25
REMARK 500 7 ASP A 75 8.40 -168.79
REMARK 500
REMARK 500 THIS ENTRY HAS 229 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 MET A 1 ALA A 2 6 147.42
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 1 ARG A 22 0.08 SIDE CHAIN
REMARK 500 3 ARG A 73 0.09 SIDE CHAIN
REMARK 500 6 ARG A 19 0.14 SIDE CHAIN
REMARK 500 7 ARG A 22 0.12 SIDE CHAIN
REMARK 500 7 TYR A 51 0.08 SIDE CHAIN
REMARK 500 8 ARG A 18 0.14 SIDE CHAIN
REMARK 500 8 ARG A 19 0.14 SIDE CHAIN
REMARK 500 8 TYR A 51 0.07 SIDE CHAIN
REMARK 500 9 TYR A 51 0.09 SIDE CHAIN
REMARK 500 10 ARG A 73 0.12 SIDE CHAIN
REMARK 500 13 ARG A 22 0.11 SIDE CHAIN
REMARK 500 15 ARG A 18 0.09 SIDE CHAIN
REMARK 500 15 ARG A 19 0.09 SIDE CHAIN
REMARK 500 16 ARG A 73 0.12 SIDE CHAIN
REMARK 500 16 TYR A 106 0.07 SIDE CHAIN
REMARK 500 18 ARG A 19 0.08 SIDE CHAIN
REMARK 500 18 ARG A 73 0.09 SIDE CHAIN
REMARK 500 19 ARG A 18 0.08 SIDE CHAIN
REMARK 500 20 ARG A 19 0.09 SIDE CHAIN
REMARK 500 21 ARG A 22 0.10 SIDE CHAIN
REMARK 500 22 ARG A 18 0.12 SIDE CHAIN
REMARK 500 22 ARG A 19 0.10 SIDE CHAIN
REMARK 500 24 ARG A 73 0.08 SIDE CHAIN
REMARK 500 25 ARG A 18 0.09 SIDE CHAIN
REMARK 500 25 ARG A 73 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1DJM A 1 129 UNP P06143 CHEY_ECOLI 1 129
SEQRES 1 A 129 MET ALA ASP LYS GLU LEU LYS PHE LEU VAL VAL ASP ASP
SEQRES 2 A 129 PHE SER THR MET ARG ARG ILE VAL ARG ASN LEU LEU LYS
SEQRES 3 A 129 GLU LEU GLY PHE ASN ASN VAL GLU GLU ALA GLU ASP GLY
SEQRES 4 A 129 VAL ASP ALA LEU ASN LYS LEU GLN ALA GLY GLY TYR GLY
SEQRES 5 A 129 PHE VAL ILE SER ASP TRP ASN MET PRO ASN MET ASP GLY
SEQRES 6 A 129 LEU GLU LEU LEU LYS THR ILE ARG ALA ASP GLY ALA MET
SEQRES 7 A 129 SER ALA LEU PRO VAL LEU MET VAL THR ALA GLU ALA LYS
SEQRES 8 A 129 LYS GLU ASN ILE ILE ALA ALA ALA GLN ALA GLY ALA SER
SEQRES 9 A 129 GLY TYR VAL VAL LYS PRO PHE THR ALA ALA THR LEU GLU
SEQRES 10 A 129 GLU LYS LEU ASN LYS ILE PHE GLU LYS LEU GLY MET
HELIX 1 1 PHE A 14 GLY A 29 1 16
HELIX 2 2 ASP A 38 GLN A 47 1 10
HELIX 3 3 ASP A 64 ARG A 73 1 10
HELIX 4 4 LYS A 91 GLY A 102 1 12
HELIX 5 5 THR A 112 LYS A 126 1 15
SHEET 1 A 5 VAL A 33 GLU A 34 0
SHEET 2 A 5 PHE A 8 VAL A 11 1 O PHE A 8 N GLU A 34
SHEET 3 A 5 PHE A 53 SER A 56 1 O PHE A 53 N LEU A 9
SHEET 4 A 5 VAL A 83 THR A 87 1 N LEU A 84 O VAL A 54
SHEET 5 A 5 GLY A 105 VAL A 108 1 O GLY A 105 N MET A 85
CISPEP 1 LYS A 109 PRO A 110 1 -16.26
CISPEP 2 LYS A 109 PRO A 110 2 -3.38
CISPEP 3 LYS A 109 PRO A 110 3 -10.45
CISPEP 4 LYS A 109 PRO A 110 4 -12.22
CISPEP 5 LYS A 109 PRO A 110 5 -8.74
CISPEP 6 LYS A 109 PRO A 110 6 -8.04
CISPEP 7 LYS A 109 PRO A 110 7 -12.36
CISPEP 8 LYS A 109 PRO A 110 8 -9.53
CISPEP 9 LYS A 109 PRO A 110 9 -12.97
CISPEP 10 LYS A 109 PRO A 110 10 -20.47
CISPEP 11 LYS A 109 PRO A 110 11 8.51
CISPEP 12 LYS A 109 PRO A 110 12 -7.55
CISPEP 13 LYS A 109 PRO A 110 13 -16.78
CISPEP 14 LYS A 109 PRO A 110 14 -14.35
CISPEP 15 LYS A 109 PRO A 110 15 -3.47
CISPEP 16 LYS A 109 PRO A 110 16 -1.41
CISPEP 17 LYS A 109 PRO A 110 17 -11.43
CISPEP 18 LYS A 109 PRO A 110 18 -15.63
CISPEP 19 LYS A 109 PRO A 110 19 -15.18
CISPEP 20 LYS A 109 PRO A 110 20 -10.44
CISPEP 21 LYS A 109 PRO A 110 21 -6.54
CISPEP 22 LYS A 109 PRO A 110 22 -21.06
CISPEP 23 LYS A 109 PRO A 110 23 -14.49
CISPEP 24 LYS A 109 PRO A 110 24 -16.35
CISPEP 25 LYS A 109 PRO A 110 25 -6.33
CISPEP 26 LYS A 109 PRO A 110 26 -6.52
CISPEP 27 LYS A 109 PRO A 110 27 -20.73
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 - b 16 2 Bytes