Header list of 1joy.pdb file
Complete list - b 12 2 Bytes
HEADER TRANSFERASE 28-DEC-98 1JOY
TITLE SOLUTION STRUCTURE OF THE HOMODIMERIC DOMAIN OF ENVZ FROM ESCHERICHIA
TITLE 2 COLI BY MULTI-DIMENSIONAL NMR.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (ENVZ_ECOLI);
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 223-289;
COMPND 5 EC: 2.7.3.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS HISTIDINE KINASE, SENSORY TRANSDUCTION, OSMOLARITY SENSOR PROTEIN,
KEYWDS 2 INNER MEMBRANE, PHOSPHORYLATION, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR C.TOMOMORI,T.TANAKA,R.DUTTA,H.PARK,S.K.SAHA,Y.ZHU,R.ISHIMA,D.LIU,
AUTHOR 2 K.I.TONG,H.KUROKAWA,H.QIAN,M.INOUYE,M.IKURA
REVDAT 4 06-NOV-13 1JOY 1 ATOM
REVDAT 3 24-FEB-09 1JOY 1 VERSN
REVDAT 2 01-APR-03 1JOY 1 JRNL
REVDAT 1 12-JAN-00 1JOY 0
JRNL AUTH C.TOMOMORI,T.TANAKA,R.DUTTA,H.PARK,S.K.SAHA,Y.ZHU,R.ISHIMA,
JRNL AUTH 2 D.LIU,K.I.TONG,H.KUROKAWA,H.QIAN,M.INOUYE,M.IKURA
JRNL TITL SOLUTION STRUCTURE OF THE HOMODIMERIC CORE DOMAIN OF
JRNL TITL 2 ESCHERICHIA COLI HISTIDINE KINASE ENVZ.
JRNL REF NAT.STRUCT.BIOL. V. 6 729 1999
JRNL REFN ISSN 1072-8368
JRNL PMID 10426948
JRNL DOI 10.1038/11495
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 TITL NMR STRUCTURE OF THE HISTIDINE KINASE DOMAIN OF THE E.COLI
REMARK 1 TITL 2 OSMOSENSOR ENVZ.
REMARK 1 REF NATURE V. 396 88 1998
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JOY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-99.
REMARK 100 THE RCSB ID CODE IS RCSB007119.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY-PLUS 500; UNITY 600
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C- LABELED OR 13C/15N-LABELED ENVZ (223-289).
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 ALA A 225 -44.01 -170.28
REMARK 500 1 ALA A 231 -166.47 177.03
REMARK 500 1 HIS A 243 -38.19 -33.77
REMARK 500 1 ASP A 263 56.38 -174.46
REMARK 500 1 ALA B 225 -44.15 -170.27
REMARK 500 1 ALA B 231 -166.50 177.04
REMARK 500 1 HIS B 243 -38.17 -33.78
REMARK 500 1 ASP B 263 56.38 -174.45
REMARK 500 2 LYS A 228 40.35 -108.63
REMARK 500 2 LEU A 230 38.81 -89.83
REMARK 500 2 ASP A 233 -36.15 -139.80
REMARK 500 2 SER A 242 -27.28 -36.38
REMARK 500 2 ILE A 270 -70.57 -86.37
REMARK 500 2 LYS B 228 40.37 -108.61
REMARK 500 2 LEU B 230 38.81 -89.88
REMARK 500 2 ASP B 233 -36.14 -139.86
REMARK 500 2 SER B 242 -27.35 -36.42
REMARK 500 2 ILE B 270 -70.68 -86.38
REMARK 500 3 ALA A 225 -52.23 -126.78
REMARK 500 3 GLN A 229 53.04 -157.75
REMARK 500 3 ASP A 232 30.56 -179.07
REMARK 500 3 ASP A 263 57.97 -162.01
REMARK 500 3 ASN A 271 -28.62 -39.94
REMARK 500 3 TYR A 287 41.11 -162.78
REMARK 500 3 ALA B 225 -52.30 -126.74
REMARK 500 3 GLN B 229 52.97 -157.77
REMARK 500 3 ASP B 232 30.56 -179.12
REMARK 500 3 ASP B 263 57.99 -162.06
REMARK 500 3 ASN B 271 -28.68 -39.93
REMARK 500 3 TYR B 287 41.17 -162.77
REMARK 500 4 GLN A 229 32.06 -157.26
REMARK 500 4 LEU A 230 -38.09 -151.49
REMARK 500 4 ALA A 231 39.74 -156.39
REMARK 500 4 ASP A 232 30.35 -162.59
REMARK 500 4 ASP A 233 -61.45 -143.78
REMARK 500 4 MET A 238 -75.01 -65.93
REMARK 500 4 SER A 242 -28.86 -35.21
REMARK 500 4 ASP A 263 59.43 -152.94
REMARK 500 4 ILE A 270 -71.76 -84.21
REMARK 500 4 LEU A 288 47.26 -85.72
REMARK 500 4 GLN B 229 32.00 -157.25
REMARK 500 4 LEU B 230 -38.13 -151.44
REMARK 500 4 ALA B 231 39.80 -156.34
REMARK 500 4 ASP B 232 30.37 -162.63
REMARK 500 4 ASP B 233 -61.43 -143.79
REMARK 500 4 MET B 238 -74.99 -66.01
REMARK 500 4 SER B 242 -28.93 -35.14
REMARK 500 4 ASP B 263 59.45 -152.91
REMARK 500 4 ILE B 270 -71.76 -84.21
REMARK 500 4 LEU B 288 47.25 -85.73
REMARK 500
REMARK 500 THIS ENTRY HAS 322 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 234 0.14 SIDE CHAIN
REMARK 500 1 ARG A 246 0.17 SIDE CHAIN
REMARK 500 1 ARG A 251 0.27 SIDE CHAIN
REMARK 500 1 ARG A 253 0.32 SIDE CHAIN
REMARK 500 1 ARG A 289 0.31 SIDE CHAIN
REMARK 500 1 ARG B 234 0.14 SIDE CHAIN
REMARK 500 1 ARG B 246 0.17 SIDE CHAIN
REMARK 500 1 ARG B 251 0.27 SIDE CHAIN
REMARK 500 1 ARG B 253 0.32 SIDE CHAIN
REMARK 500 1 ARG B 289 0.31 SIDE CHAIN
REMARK 500 2 ARG A 234 0.31 SIDE CHAIN
REMARK 500 2 ARG A 246 0.32 SIDE CHAIN
REMARK 500 2 ARG A 251 0.31 SIDE CHAIN
REMARK 500 2 ARG A 253 0.08 SIDE CHAIN
REMARK 500 2 ARG A 289 0.21 SIDE CHAIN
REMARK 500 2 ARG B 234 0.31 SIDE CHAIN
REMARK 500 2 ARG B 246 0.32 SIDE CHAIN
REMARK 500 2 ARG B 251 0.31 SIDE CHAIN
REMARK 500 2 ARG B 253 0.08 SIDE CHAIN
REMARK 500 2 ARG B 289 0.21 SIDE CHAIN
REMARK 500 3 ARG A 234 0.29 SIDE CHAIN
REMARK 500 3 ARG A 246 0.26 SIDE CHAIN
REMARK 500 3 ARG A 251 0.12 SIDE CHAIN
REMARK 500 3 ARG A 253 0.13 SIDE CHAIN
REMARK 500 3 ARG A 289 0.31 SIDE CHAIN
REMARK 500 3 ARG B 234 0.29 SIDE CHAIN
REMARK 500 3 ARG B 246 0.26 SIDE CHAIN
REMARK 500 3 ARG B 251 0.12 SIDE CHAIN
REMARK 500 3 ARG B 253 0.13 SIDE CHAIN
REMARK 500 3 ARG B 289 0.31 SIDE CHAIN
REMARK 500 4 ARG A 234 0.32 SIDE CHAIN
REMARK 500 4 ARG A 246 0.13 SIDE CHAIN
REMARK 500 4 ARG A 251 0.23 SIDE CHAIN
REMARK 500 4 ARG A 253 0.27 SIDE CHAIN
REMARK 500 4 ARG A 289 0.32 SIDE CHAIN
REMARK 500 4 ARG B 234 0.32 SIDE CHAIN
REMARK 500 4 ARG B 246 0.13 SIDE CHAIN
REMARK 500 4 ARG B 251 0.23 SIDE CHAIN
REMARK 500 4 ARG B 253 0.27 SIDE CHAIN
REMARK 500 4 ARG B 289 0.32 SIDE CHAIN
REMARK 500 5 ARG A 234 0.20 SIDE CHAIN
REMARK 500 5 ARG A 246 0.17 SIDE CHAIN
REMARK 500 5 ARG A 251 0.32 SIDE CHAIN
REMARK 500 5 ARG A 253 0.25 SIDE CHAIN
REMARK 500 5 ARG A 289 0.22 SIDE CHAIN
REMARK 500 5 ARG B 234 0.20 SIDE CHAIN
REMARK 500 5 ARG B 246 0.17 SIDE CHAIN
REMARK 500 5 ARG B 251 0.32 SIDE CHAIN
REMARK 500 5 ARG B 253 0.25 SIDE CHAIN
REMARK 500 5 ARG B 289 0.22 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 202 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: APH
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: AUTOPHOSPHORYLATION SITE
DBREF 1JOY A 223 289 UNP P02933 ENVZ_ECOLI 223 289
DBREF 1JOY B 223 289 UNP P02933 ENVZ_ECOLI 223 289
SEQRES 1 A 67 MET ALA ALA GLY VAL LYS GLN LEU ALA ASP ASP ARG THR
SEQRES 2 A 67 LEU LEU MET ALA GLY VAL SER HIS ASP LEU ARG THR PRO
SEQRES 3 A 67 LEU THR ARG ILE ARG LEU ALA THR GLU MET MET SER GLU
SEQRES 4 A 67 GLN ASP GLY TYR LEU ALA GLU SER ILE ASN LYS ASP ILE
SEQRES 5 A 67 GLU GLU CYS ASN ALA ILE ILE GLU GLN PHE ILE ASP TYR
SEQRES 6 A 67 LEU ARG
SEQRES 1 B 67 MET ALA ALA GLY VAL LYS GLN LEU ALA ASP ASP ARG THR
SEQRES 2 B 67 LEU LEU MET ALA GLY VAL SER HIS ASP LEU ARG THR PRO
SEQRES 3 B 67 LEU THR ARG ILE ARG LEU ALA THR GLU MET MET SER GLU
SEQRES 4 B 67 GLN ASP GLY TYR LEU ALA GLU SER ILE ASN LYS ASP ILE
SEQRES 5 B 67 GLU GLU CYS ASN ALA ILE ILE GLU GLN PHE ILE ASP TYR
SEQRES 6 B 67 LEU ARG
HELIX 1 1 ARG A 234 MET A 238 1 5
HELIX 2 2 SER A 242 LEU A 245 1 4
HELIX 3 3 THR A 247 ASP A 263 1 17
HELIX 4 4 TYR A 265 ILE A 285 1 21
HELIX 5 5 ARG B 234 MET B 238 1 5
HELIX 6 6 SER B 242 LEU B 245 1 4
HELIX 7 7 THR B 247 ASP B 263 1 17
HELIX 8 8 TYR B 265 ILE B 285 1 21
SITE 1 APH 1 HIS A 243
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 12 2 Bytes