Header list of 1cey.pdb file
Complete list - b 16 2 Bytes
HEADER SIGNAL TRANSDUCTION 23-NOV-94 1CEY
TITLE ASSIGNMENTS, SECONDARY STRUCTURE, GLOBAL FOLD, AND DYNAMICS OF
TITLE 2 CHEMOTAXIS Y PROTEIN USING THREE-AND FOUR-DIMENSIONAL HETERONUCLEAR
TITLE 3 (13C,15N) NMR SPECTROSCOPY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHEY;
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_PLASMID: CHEY
KEYWDS SIGNAL TRANSDUCTION
EXPDTA SOLUTION NMR
NUMMDL 46
AUTHOR F.J.MOY,D.F.LOWRY,P.MATSUMURA,F.W.DAHLQUIST,J.E.KRYWKO,P.J.DOMAILLE
REVDAT 4 16-FEB-22 1CEY 1 REMARK
REVDAT 3 24-FEB-09 1CEY 1 VERSN
REVDAT 2 15-MAY-95 1CEY 1 SOURCE REMARK
REVDAT 1 07-FEB-95 1CEY 0
JRNL AUTH F.J.MOY,D.F.LOWRY,P.MATSUMURA,F.W.DAHLQUIST,J.E.KRYWKO,
JRNL AUTH 2 P.J.DOMAILLE
JRNL TITL ASSIGNMENTS, SECONDARY STRUCTURE, GLOBAL FOLD, AND DYNAMICS
JRNL TITL 2 OF CHEMOTAXIS Y PROTEIN USING THREE- AND FOUR-DIMENSIONAL
JRNL TITL 3 HETERONUCLEAR (13C,15N) NMR SPECTROSCOPY.
JRNL REF BIOCHEMISTRY V. 33 10731 1994
JRNL REFN ISSN 0006-2960
JRNL PMID 8075074
JRNL DOI 10.1021/BI00201A022
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CEY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172286.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 46
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 HD21 ASN A 62 H MET A 63 1.31
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 ASP A 3 134.23 62.76
REMARK 500 1 GLU A 5 42.88 -154.63
REMARK 500 1 SER A 15 47.77 -97.96
REMARK 500 1 THR A 16 -34.37 178.23
REMARK 500 1 ASN A 32 89.25 -172.48
REMARK 500 1 ASP A 38 -177.92 -177.23
REMARK 500 1 ALA A 48 -77.26 -52.77
REMARK 500 1 ASP A 57 -120.94 -63.84
REMARK 500 1 TRP A 58 -28.64 -161.89
REMARK 500 1 ASN A 59 34.76 -166.64
REMARK 500 1 PRO A 61 -70.65 -68.83
REMARK 500 1 ASN A 62 -81.07 -154.81
REMARK 500 1 MET A 63 -113.74 -76.00
REMARK 500 1 ASP A 75 -128.03 -67.35
REMARK 500 1 ALA A 77 -14.14 71.79
REMARK 500 1 MET A 78 17.43 -146.82
REMARK 500 1 SER A 79 7.23 -68.78
REMARK 500 1 LEU A 81 107.59 -43.86
REMARK 500 1 LEU A 84 72.03 -110.64
REMARK 500 1 GLU A 89 -152.00 49.33
REMARK 500 1 ALA A 90 115.49 176.76
REMARK 500 1 ILE A 96 -70.01 -80.56
REMARK 500 1 ALA A 101 -115.03 -108.45
REMARK 500 1 ALA A 103 11.15 -59.18
REMARK 500 1 SER A 104 -31.06 -29.20
REMARK 500 1 VAL A 108 -157.53 -64.86
REMARK 500 2 GLU A 5 51.42 -140.96
REMARK 500 2 VAL A 11 40.49 -96.00
REMARK 500 2 SER A 15 34.27 -85.35
REMARK 500 2 THR A 16 -8.76 -165.33
REMARK 500 2 ASN A 31 27.33 -150.10
REMARK 500 2 GLU A 37 13.56 -148.77
REMARK 500 2 ASP A 38 -179.90 178.16
REMARK 500 2 ASP A 57 -97.01 -84.47
REMARK 500 2 TRP A 58 -109.88 -172.40
REMARK 500 2 MET A 60 -50.36 176.62
REMARK 500 2 PRO A 61 -168.87 -64.19
REMARK 500 2 ASN A 62 -84.99 -47.61
REMARK 500 2 MET A 63 -117.73 -69.76
REMARK 500 2 ASP A 75 -70.23 -52.27
REMARK 500 2 SER A 79 -59.76 75.78
REMARK 500 2 ALA A 80 -54.34 -150.16
REMARK 500 2 LEU A 81 120.30 59.30
REMARK 500 2 LEU A 84 69.48 -108.70
REMARK 500 2 LYS A 91 -125.02 -98.65
REMARK 500 2 LYS A 92 -89.46 -117.17
REMARK 500 2 GLU A 93 -18.74 -47.25
REMARK 500 2 ALA A 101 -103.90 -86.90
REMARK 500 2 ALA A 103 11.40 -58.18
REMARK 500 2 SER A 104 -31.81 -29.40
REMARK 500
REMARK 500 THIS ENTRY HAS 1021 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 1 ARG A 18 0.31 SIDE CHAIN
REMARK 500 1 ARG A 19 0.30 SIDE CHAIN
REMARK 500 1 ARG A 22 0.30 SIDE CHAIN
REMARK 500 1 ARG A 73 0.30 SIDE CHAIN
REMARK 500 2 ARG A 18 0.32 SIDE CHAIN
REMARK 500 2 ARG A 22 0.30 SIDE CHAIN
REMARK 500 2 ARG A 73 0.08 SIDE CHAIN
REMARK 500 3 ARG A 18 0.32 SIDE CHAIN
REMARK 500 3 ARG A 19 0.25 SIDE CHAIN
REMARK 500 3 ARG A 22 0.18 SIDE CHAIN
REMARK 500 3 ARG A 73 0.32 SIDE CHAIN
REMARK 500 4 ARG A 18 0.21 SIDE CHAIN
REMARK 500 4 ARG A 19 0.31 SIDE CHAIN
REMARK 500 4 ARG A 22 0.31 SIDE CHAIN
REMARK 500 4 ARG A 73 0.31 SIDE CHAIN
REMARK 500 5 ARG A 18 0.31 SIDE CHAIN
REMARK 500 5 ARG A 19 0.27 SIDE CHAIN
REMARK 500 5 ARG A 22 0.24 SIDE CHAIN
REMARK 500 5 ARG A 73 0.15 SIDE CHAIN
REMARK 500 6 ARG A 18 0.32 SIDE CHAIN
REMARK 500 6 ARG A 19 0.17 SIDE CHAIN
REMARK 500 6 ARG A 22 0.32 SIDE CHAIN
REMARK 500 6 ARG A 73 0.29 SIDE CHAIN
REMARK 500 7 ARG A 18 0.14 SIDE CHAIN
REMARK 500 7 ARG A 22 0.24 SIDE CHAIN
REMARK 500 7 ARG A 73 0.21 SIDE CHAIN
REMARK 500 8 ARG A 18 0.12 SIDE CHAIN
REMARK 500 8 ARG A 19 0.30 SIDE CHAIN
REMARK 500 8 ARG A 22 0.09 SIDE CHAIN
REMARK 500 8 ARG A 73 0.28 SIDE CHAIN
REMARK 500 9 ARG A 22 0.21 SIDE CHAIN
REMARK 500 9 ARG A 73 0.20 SIDE CHAIN
REMARK 500 10 ARG A 18 0.20 SIDE CHAIN
REMARK 500 10 ARG A 22 0.30 SIDE CHAIN
REMARK 500 10 ARG A 73 0.17 SIDE CHAIN
REMARK 500 11 ARG A 19 0.27 SIDE CHAIN
REMARK 500 11 ARG A 22 0.23 SIDE CHAIN
REMARK 500 11 ARG A 73 0.21 SIDE CHAIN
REMARK 500 12 ARG A 18 0.30 SIDE CHAIN
REMARK 500 12 ARG A 19 0.14 SIDE CHAIN
REMARK 500 12 ARG A 22 0.22 SIDE CHAIN
REMARK 500 12 ARG A 73 0.16 SIDE CHAIN
REMARK 500 13 ARG A 18 0.30 SIDE CHAIN
REMARK 500 13 ARG A 19 0.21 SIDE CHAIN
REMARK 500 13 ARG A 22 0.09 SIDE CHAIN
REMARK 500 13 ARG A 73 0.29 SIDE CHAIN
REMARK 500 14 ARG A 18 0.23 SIDE CHAIN
REMARK 500 14 ARG A 19 0.28 SIDE CHAIN
REMARK 500 14 ARG A 22 0.32 SIDE CHAIN
REMARK 500 14 ARG A 73 0.14 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 167 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CEY A 2 129 UNP P06143 CHEY_ECOLI 1 128
SEQRES 1 A 128 ALA ASP LYS GLU LEU LYS PHE LEU VAL VAL ASP ASP PHE
SEQRES 2 A 128 SER THR MET ARG ARG ILE VAL ARG ASN LEU LEU LYS GLU
SEQRES 3 A 128 LEU GLY PHE ASN ASN VAL GLU GLU ALA GLU ASP GLY VAL
SEQRES 4 A 128 ASP ALA LEU ASN LYS LEU GLN ALA GLY GLY TYR GLY PHE
SEQRES 5 A 128 VAL ILE SER ASP TRP ASN MET PRO ASN MET ASP GLY LEU
SEQRES 6 A 128 GLU LEU LEU LYS THR ILE ARG ALA ASP GLY ALA MET SER
SEQRES 7 A 128 ALA LEU PRO VAL LEU MET VAL THR ALA GLU ALA LYS LYS
SEQRES 8 A 128 GLU ASN ILE ILE ALA ALA ALA GLN ALA GLY ALA SER GLY
SEQRES 9 A 128 TYR VAL VAL LYS PRO PHE THR ALA ALA THR LEU GLU GLU
SEQRES 10 A 128 LYS LEU ASN LYS ILE PHE GLU LYS LEU GLY MET
HELIX 1 1 THR A 16 LEU A 28 1 13
HELIX 2 2 ASP A 38 GLN A 47 1 10
HELIX 3 3 GLY A 65 ASP A 75 1 11
HELIX 4 4 LYS A 91 GLN A 100 1 10
HELIX 5 5 THR A 112 GLY A 128 1 17
SHEET 1 A 3 VAL A 33 GLU A 35 0
SHEET 2 A 3 PHE A 8 VAL A 10 1 O PHE A 8 N GLU A 34
SHEET 3 A 3 PHE A 53 ILE A 55 1 O PHE A 53 N LEU A 9
SHEET 1 B 2 LEU A 84 VAL A 86 0
SHEET 2 B 2 GLY A 105 VAL A 107 1 O GLY A 105 N MET A 85
CISPEP 1 LYS A 109 PRO A 110 1 -2.03
CISPEP 2 LYS A 109 PRO A 110 2 -2.02
CISPEP 3 LYS A 109 PRO A 110 3 -2.09
CISPEP 4 LYS A 109 PRO A 110 4 -1.98
CISPEP 5 LYS A 109 PRO A 110 5 -1.34
CISPEP 6 LYS A 109 PRO A 110 6 -1.98
CISPEP 7 LYS A 109 PRO A 110 7 -2.07
CISPEP 8 LYS A 109 PRO A 110 8 -1.89
CISPEP 9 LYS A 109 PRO A 110 9 -1.37
CISPEP 10 LYS A 109 PRO A 110 10 -1.94
CISPEP 11 LYS A 109 PRO A 110 11 -2.14
CISPEP 12 LYS A 109 PRO A 110 12 -1.89
CISPEP 13 LYS A 109 PRO A 110 13 -2.06
CISPEP 14 LYS A 109 PRO A 110 14 -1.41
CISPEP 15 LYS A 109 PRO A 110 15 -2.15
CISPEP 16 LYS A 109 PRO A 110 16 -1.91
CISPEP 17 LYS A 109 PRO A 110 17 -2.14
CISPEP 18 LYS A 109 PRO A 110 18 -1.80
CISPEP 19 LYS A 109 PRO A 110 19 -1.68
CISPEP 20 LYS A 109 PRO A 110 20 -2.03
CISPEP 21 LYS A 109 PRO A 110 21 -2.58
CISPEP 22 LYS A 109 PRO A 110 22 -1.64
CISPEP 23 LYS A 109 PRO A 110 23 -1.97
CISPEP 24 LYS A 109 PRO A 110 24 -1.96
CISPEP 25 LYS A 109 PRO A 110 25 -2.39
CISPEP 26 LYS A 109 PRO A 110 26 -1.66
CISPEP 27 LYS A 109 PRO A 110 27 -2.18
CISPEP 28 LYS A 109 PRO A 110 28 -3.18
CISPEP 29 LYS A 109 PRO A 110 29 -2.33
CISPEP 30 LYS A 109 PRO A 110 30 -2.03
CISPEP 31 LYS A 109 PRO A 110 31 -2.52
CISPEP 32 LYS A 109 PRO A 110 32 -1.35
CISPEP 33 LYS A 109 PRO A 110 33 -2.49
CISPEP 34 LYS A 109 PRO A 110 34 -2.35
CISPEP 35 LYS A 109 PRO A 110 35 -2.33
CISPEP 36 LYS A 109 PRO A 110 36 -2.09
CISPEP 37 LYS A 109 PRO A 110 37 -2.69
CISPEP 38 LYS A 109 PRO A 110 38 -2.26
CISPEP 39 LYS A 109 PRO A 110 39 -2.25
CISPEP 40 LYS A 109 PRO A 110 40 -2.30
CISPEP 41 LYS A 109 PRO A 110 41 -2.45
CISPEP 42 LYS A 109 PRO A 110 42 -2.04
CISPEP 43 LYS A 109 PRO A 110 43 -2.18
CISPEP 44 LYS A 109 PRO A 110 44 -2.06
CISPEP 45 LYS A 109 PRO A 110 45 -2.19
CISPEP 46 LYS A 109 PRO A 110 46 -1.62
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