Header list of 1sr2.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 22-MAR-04 1SR2
TITLE SOLUTION STRUCTURE OF THE ESCHERICHIA COLI YOJN HISTIDINE-
TITLE 2 PHOSPHOTRANSFERASE (HPT) DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE SENSOR-LIKE HISTIDINE KINASE YOJN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (RESIDUES 775-890);
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 STRAIN: XL1 BLUE;
SOURCE 5 GENE: YOJN, B2216;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS FOUR-HELICAL BUNDLE, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR V.V.ROGOV,F.BERNHARD,F.LOEHR,V.DOETSCH
REVDAT 3 02-MAR-22 1SR2 1 REMARK
REVDAT 2 24-FEB-09 1SR2 1 VERSN
REVDAT 1 26-OCT-04 1SR2 0
JRNL AUTH V.V.ROGOV,F.BERNHARD,F.LOEHR,V.DOETSCH
JRNL TITL SOLUTION STRUCTURE OF THE ESCHERICHIA COLI YOJN
JRNL TITL 2 HISTIDINE-PHOSPHOTRANSFERASE DOMAIN AND ITS INTERACTION WITH
JRNL TITL 3 COGNATE PHOSPHORYL RECEIVER DOMAINS
JRNL REF J.MOL.BIOL. V. 343 1035 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15476819
JRNL DOI 10.1016/J.JMB.2004.08.096
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SR2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021938.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 15 MM BIS-TRIS, 15 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM YOJN-HPT U-15N, 15 MM BIS
REMARK 210 -TRIS, 15 MM NACL, 95% H2O, 5%
REMARK 210 D2O; 1 MM YOJN-HPT U-15N,13C, 15
REMARK 210 MM BIS-TRIS, 15 MM NACL, 95% H2O,
REMARK 210 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 700 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, AURELIA 2.7.5,
REMARK 210 DYANA 1.5
REMARK 210 METHOD USED : ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE 3D_13C-SEPARATED_NOESY WAS RECORDED IN THREE
REMARK 210 MODIFICATIONS
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 HB ILE A 783 H GLU A 784 1.27
REMARK 500 HG LEU A 782 HG12 ILE A 783 1.31
REMARK 500 HG12 VAL A 779 H LEU A 780 1.33
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 GLU A 777 -77.39 -102.34
REMARK 500 1 VAL A 779 -90.58 41.70
REMARK 500 1 ILE A 783 -126.10 -163.39
REMARK 500 1 GLU A 784 -39.78 -142.38
REMARK 500 1 GLN A 786 73.19 62.98
REMARK 500 1 VAL A 792 49.29 -93.76
REMARK 500 1 SER A 795 97.54 59.10
REMARK 500 1 PRO A 796 -144.26 -79.96
REMARK 500 1 ASP A 800 40.34 -165.95
REMARK 500 1 ASP A 816 -81.25 -97.43
REMARK 500 2 GLN A 781 -44.83 173.90
REMARK 500 2 LEU A 782 -83.74 66.17
REMARK 500 2 GLU A 784 -19.45 71.84
REMARK 500 2 VAL A 785 -61.90 -92.04
REMARK 500 2 LEU A 787 -48.12 -168.73
REMARK 500 2 GLU A 790 -174.06 62.95
REMARK 500 2 VAL A 792 -144.46 34.07
REMARK 500 2 GLU A 794 -83.05 64.83
REMARK 500 2 LEU A 797 -131.44 57.61
REMARK 500 2 ASP A 816 -61.68 -92.24
REMARK 500 2 ASN A 852 34.67 70.90
REMARK 500 3 ILE A 783 42.38 -88.46
REMARK 500 3 VAL A 785 -47.76 -147.39
REMARK 500 3 GLN A 786 -114.01 53.80
REMARK 500 3 GLU A 791 -149.60 53.61
REMARK 500 3 SER A 795 118.38 -161.93
REMARK 500 3 ASP A 816 -70.48 -95.13
REMARK 500 3 ASN A 852 39.16 72.91
REMARK 500 4 GLN A 776 -53.85 -141.53
REMARK 500 4 LEU A 780 -101.07 55.43
REMARK 500 4 ILE A 783 -136.04 -157.46
REMARK 500 4 VAL A 785 78.03 -103.87
REMARK 500 4 LEU A 787 -95.24 -176.21
REMARK 500 4 GLN A 789 -109.04 -116.93
REMARK 500 4 VAL A 792 57.80 -90.35
REMARK 500 4 GLU A 794 -137.16 49.04
REMARK 500 4 SER A 795 -55.80 -121.27
REMARK 500 4 ASN A 852 9.48 85.75
REMARK 500 5 GLU A 777 -56.89 170.78
REMARK 500 5 VAL A 779 -71.87 -52.74
REMARK 500 5 LEU A 780 -80.44 -169.52
REMARK 500 5 ILE A 783 -90.51 -149.72
REMARK 500 5 GLU A 784 -69.21 -151.46
REMARK 500 5 LEU A 787 45.79 -100.56
REMARK 500 5 GLU A 791 114.27 -179.17
REMARK 500 5 PRO A 796 45.13 -79.71
REMARK 500 5 LEU A 797 -52.78 70.86
REMARK 500 5 ASP A 816 -63.94 -95.62
REMARK 500 6 ALA A 778 -67.42 -147.39
REMARK 500 6 VAL A 779 -97.76 60.97
REMARK 500
REMARK 500 THIS ENTRY HAS 247 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6133 RELATED DB: BMRB
REMARK 900 THE CHEMICAL SHIFT VALUES FOR THE YOJN-HPT PROTEIN
DBREF 1SR2 A 775 890 UNP P39838 YOJN_ECOLI 775 890
SEQRES 1 A 116 MET GLN GLU ALA VAL LEU GLN LEU ILE GLU VAL GLN LEU
SEQRES 2 A 116 ALA GLN GLU GLU VAL THR GLU SER PRO LEU GLY GLY ASP
SEQRES 3 A 116 GLU ASN ALA GLN LEU HIS ALA SER GLY TYR TYR ALA LEU
SEQRES 4 A 116 PHE VAL ASP THR VAL PRO ASP ASP VAL LYS ARG LEU TYR
SEQRES 5 A 116 THR GLU ALA ALA THR SER ASP PHE ALA ALA LEU ALA GLN
SEQRES 6 A 116 THR ALA HIS ARG LEU LYS GLY VAL PHE ALA MET LEU ASN
SEQRES 7 A 116 LEU VAL PRO GLY LYS GLN LEU CYS GLU THR LEU GLU HIS
SEQRES 8 A 116 LEU ILE ARG GLU LYS ASP VAL PRO GLY ILE GLU LYS TYR
SEQRES 9 A 116 ILE SER ASP ILE ASP SER TYR VAL LYS SER LEU LEU
HELIX 1 1 ASP A 800 GLY A 809 1 10
HELIX 2 2 TYR A 810 VAL A 815 1 6
HELIX 3 3 THR A 817 SER A 832 1 16
HELIX 4 4 ASP A 833 ASN A 852 1 20
HELIX 5 5 LEU A 853 GLU A 869 1 17
HELIX 6 6 ASP A 871 LEU A 890 1 20
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 - r 2 2 Bytes