Header list of 1dc8.pdb file
Complete list - 21 20 Bytes
HEADER SIGNALING PROTEIN 04-NOV-99 1DC8
TITLE STRUCTURE OF A TRANSIENTLY PHOSPHORYLATED "SWITCH" IN BACTERIAL SIGNAL
TITLE 2 TRANSDUCTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITROGEN REGULATION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL RECEIVER DOMAIN(1-124);
COMPND 5 SYNONYM: NTRC;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 602;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PJES592
KEYWDS RECEIVER DOMAIN, PHOSPHORYLATION, SIGNAL TRANSDUCTION, CONFORMATIONAL
KEYWDS 2 REARRANGEMENT, TWO-COMPONENT SYSTEM, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR D.KERN,B.F.VOLKMAN,P.LUGINBUHL,M.J.NOHAILE,S.KUSTU,D.E.WEMMER
REVDAT 4 21-DEC-22 1DC8 1 SEQADV
REVDAT 3 16-FEB-22 1DC8 1 REMARK LINK
REVDAT 2 24-FEB-09 1DC8 1 VERSN
REVDAT 1 05-JAN-00 1DC8 0
JRNL AUTH D.KERN,B.F.VOLKMAN,P.LUGINBUHL,M.J.NOHAILE,S.KUSTU,
JRNL AUTH 2 D.E.WEMMER
JRNL TITL STRUCTURE OF A TRANSIENTLY PHOSPHORYLATED SWITCH IN
JRNL TITL 2 BACTERIAL SIGNAL TRANSDUCTION.
JRNL REF NATURE V. 402 894 1999
JRNL REFN ISSN 0028-0836
JRNL PMID 10622255
JRNL DOI 10.1038/47273
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.F.VOLKMAN,M.J.NOHAILE,N.K.AMY,S.KUSTU,D.E.WEMMER
REMARK 1 TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE N-TERMINAL
REMARK 1 TITL 2 RECEIVER DOMAIN OF NTRC
REMARK 1 REF BIOCHEMISTRY V. 34 1413 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5
REMARK 3 AUTHORS : PETER GUENTERT (DYANA), PETER GUENTERT (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 STRUCTURE BASED ON A TOTAL OF 1301 UNIQUE DISTANCE CONSTRAINTS
REMARK 3 (OBTAINED FROM
REMARK 3 3095 NOE CROSSPEAKS), INCLUDING 374 INTRARESIDUE, 405 SHORT-RANGE,
REMARK 3 228 MEDIUM
REMARK 3 RANGE AND 294 LONG-RANGE CONSTRAINTS. DYANA 1.5 ANNEAL COMMAND
REMARK 3 (10000 STEPS)
REMARK 3 USED TO GENERATE 40 CONFORMERS. 20 LOWEST TARGET FUNCTION
REMARK 3 STRUCTURES ANALYZED.
REMARK 3 CONFORMER 4 CHOSEN FOR DEPOSITION AS CLOSEST TO MEAN COORDINATES
REMARK 3 OF THE
REMARK 3 ENSEMBLE.
REMARK 4
REMARK 4 1DC8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1000009966.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.75
REMARK 210 IONIC STRENGTH : 250-500 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.3 MM NTRC(1-124) U-15N; 200 MM
REMARK 210 SODIUM PHOSPHATE, PH 6.75; 50 MM
REMARK 210 MAGNESIUM CHLORIDE; 200 MM
REMARK 210 CARBAMOYLPHOSPHATE; 0.3 MM
REMARK 210 NTRC(1-124) U-15N,13C; 200 MM
REMARK 210 SODIUM PHOSPHATE, PH 6.75; 50 MM
REMARK 210 MAGNESIUM CHLORIDE; 200 MM
REMARK 210 CARBAMOYLPHOSPHATE; 0.3 MM
REMARK 210 NTRC(1-124) U-15N; 200 MM SODIUM
REMARK 210 PHOSPHATE, PH 6.75; 50 MM
REMARK 210 MAGNESIUM CHLORIDE; 200 MM
REMARK 210 CARBAMOYLPHOSPHATE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 95.0, XWINNMR 1.5, DYANA
REMARK 210 1.5, XEASY 1.3.13
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK:
REMARK 210 PHOSPHORYLATION (>95%) COULD BE MAINTAINED FOR 36 HR. TO OBTAIN
REMARK 210 SUFFICIENT S/N
REMARK 210 IN 3D NOESY EXPERIMENTS, MULTIPLE (TYPICALLY 4) COMPLETE 3D
REMARK 210 DATASETS WERE
REMARK 210 ACQUIRED ON FRESHLY PREPARED SAMPLES AND THEN COADDED TO YIELD
REMARK 210 HIGH-QUALITY
REMARK 210 DATASETS FOR STRUCTURE DETERMINATION.
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 RES CSSEQI ATOMS
REMARK 470 PHD A 54 P OP1 OP2 OP3
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 O ILE A 108 H VAL A 112 1.49
REMARK 500 O ILE A 15 H LEU A 19 1.54
REMARK 500 O ASP A 109 H ALA A 113 1.57
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 ASP A 11 31.46 -166.49
REMARK 500 ASP A 12 -79.73 -62.13
REMARK 500 SER A 13 -44.69 -154.99
REMARK 500 SER A 14 41.73 -174.95
REMARK 500 LEU A 28 147.88 174.95
REMARK 500 THR A 29 109.33 55.61
REMARK 500 GLU A 34 -76.87 -95.82
REMARK 500 ASN A 37 -74.16 -59.81
REMARK 500 LYS A 46 -78.25 -97.65
REMARK 500 THR A 47 103.78 71.31
REMARK 500 PRO A 48 -162.46 -75.00
REMARK 500 LEU A 52 -157.62 -104.78
REMARK 500 SER A 53 89.73 167.01
REMARK 500 ILE A 55 -146.17 -176.04
REMARK 500 ARG A 56 38.98 175.50
REMARK 500 MET A 60 -82.26 -139.57
REMARK 500 ASP A 61 165.04 50.41
REMARK 500 ALA A 64 -139.33 34.23
REMARK 500 LEU A 65 -89.98 -46.19
REMARK 500 LEU A 66 -25.20 154.84
REMARK 500 LYS A 67 -72.39 -80.13
REMARK 500 LYS A 70 -91.81 -52.23
REMARK 500 HIS A 73 84.00 -165.39
REMARK 500 ILE A 79 -147.73 35.37
REMARK 500 THR A 82 120.67 161.85
REMARK 500 ALA A 83 -143.94 -83.93
REMARK 500 HIS A 84 -156.80 45.96
REMARK 500 ASP A 86 55.69 179.30
REMARK 500 VAL A 91 -60.26 -137.62
REMARK 500 GLN A 95 44.94 -179.06
REMARK 500 GLN A 96 -89.93 -174.47
REMARK 500 ALA A 98 131.98 93.97
REMARK 500 TYR A 101 140.97 -176.29
REMARK 500 LYS A 104 171.30 55.52
REMARK 500 PHE A 106 -171.52 -51.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NTR RELATED DB: PDB
REMARK 900 THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE N-TERMINAL RECEIVER
REMARK 900 DOMAIN OF NTRC
REMARK 900 RELATED ID: 1DC7 RELATED DB: PDB
REMARK 900 UNPHOSPHORYLATED NTRC RECEIVER DOMAIN
DBREF 1DC8 A 1 124 UNP P41789 NTRC_SALTY 1 124
SEQADV 1DC8 PHD A 54 UNP P41789 ASP 54 MODIFIED RESIDUE
SEQRES 1 A 124 MET GLN ARG GLY ILE VAL TRP VAL VAL ASP ASP ASP SER
SEQRES 2 A 124 SER ILE ARG TRP VAL LEU GLU ARG ALA LEU ALA GLY ALA
SEQRES 3 A 124 GLY LEU THR CYS THR THR PHE GLU ASN GLY ASN GLU VAL
SEQRES 4 A 124 LEU ALA ALA LEU ALA SER LYS THR PRO ASP VAL LEU LEU
SEQRES 5 A 124 SER PHD ILE ARG MET PRO GLY MET ASP GLY LEU ALA LEU
SEQRES 6 A 124 LEU LYS GLN ILE LYS GLN ARG HIS PRO MET LEU PRO VAL
SEQRES 7 A 124 ILE ILE MET THR ALA HIS SER ASP LEU ASP ALA ALA VAL
SEQRES 8 A 124 SER ALA TYR GLN GLN GLY ALA PHE ASP TYR LEU PRO LYS
SEQRES 9 A 124 PRO PHE ASP ILE ASP GLU ALA VAL ALA LEU VAL GLU ARG
SEQRES 10 A 124 ALA ILE SER HIS TYR GLN GLU
MODRES 1DC8 PHD A 54 ASP ASPARTYL PHOSPHATE
HET PHD A 54 12
HETNAM PHD ASPARTYL PHOSPHATE
FORMUL 1 PHD C4 H8 N O7 P
HELIX 1 1 ILE A 15 ALA A 24 1 10
HELIX 2 2 GLY A 25 GLY A 27 5 3
HELIX 3 3 GLY A 36 ALA A 42 1 7
HELIX 4 4 GLN A 68 HIS A 73 1 6
HELIX 5 5 ILE A 108 SER A 120 1 13
HELIX 6 6 HIS A 121 GLN A 123 5 3
LINK C SER A 53 N PHD A 54 1555 1555 1.33
LINK C PHD A 54 N ILE A 55 1555 1555 1.33
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
Complete list - 21 20 Bytes