Header list of 1ezt.pdb file
Complete list - 16 20 Bytes
HEADER SIGNALING PROTEIN INHIBITOR 11-MAY-00 1EZT
TITLE HIGH-RESOLUTION SOLUTION STRUCTURE OF FREE RGS4 BY NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REGULATOR OF G-PROTEIN SIGNALING 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CORE RGS DOMAIN;
COMPND 5 SYNONYM: RGS4;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: SIX RESIDUE HISTIDINE TAG AT C-TERMINUS
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PRGS4
KEYWDS 4-HELIX-BUNDLE, FREE FORM OF PROTEIN, SIGNALING PROTEIN INHIBITOR
EXPDTA SOLUTION NMR
AUTHOR F.J.MOY,P.K.CHANDA,M.I.COCKETT,W.EDRIS,P.G.JONES,K.MASON,S.SEMUS,
AUTHOR 2 R.POWERS
REVDAT 4 16-FEB-22 1EZT 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1EZT 1 VERSN
REVDAT 2 01-APR-03 1EZT 1 JRNL
REVDAT 1 15-JAN-01 1EZT 0
JRNL AUTH F.J.MOY,P.K.CHANDA,M.I.COCKETT,W.EDRIS,P.G.JONES,K.MASON,
JRNL AUTH 2 S.SEMUS,R.POWERS
JRNL TITL NMR STRUCTURE OF FREE RGS4 REVEALS AN INDUCED CONFORMATIONAL
JRNL TITL 2 CHANGE UPON BINDING GALPHA.
JRNL REF BIOCHEMISTRY V. 39 7063 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10852703
JRNL DOI 10.1021/BI992760W
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.J.MOY,P.K.CHANDA,M.I.COCKETT,W.EDRIS,P.G.JONES,R.POWERS
REMARK 1 TITL 1H, 15N, 13C, AND 13CO ASSIGNMENTS AND SECONDARY STRUCTURE
REMARK 1 TITL 2 DETERMINATION OF RGS4
REMARK 1 REF J.BIOMOL.NMR V. 15 339 1999
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1008343609739
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.840, X-PLOR 3.840
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON A TOTAL OF
REMARK 3 2871 RESTRAINTS, 1960 APPROXIMATE INTERPROTON DISTANCE
REMARK 3 RESTRAINTS, 78 DISTANCE RESTRAINTS FOR 39 BACKBONE HYDROGEN
REMARK 3 BONDS, 431 TORSION ANGLE RESTRAINTS, 132 3JHNA RESTRAINTS, 136
REMARK 3 CA AND 134 CB CHEMICAL SHIFT RESTRAINTS. STRUCTURE ALSO REFINED
REMARK 3 WITH CONFORMATIONAL DATABASE TARGET FUNCTION.
REMARK 4
REMARK 4 1EZT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-00.
REMARK 100 THE DEPOSITION ID IS D_1000011069.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 50 MM K
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM RGS4 U-15N,13C; 50MM
REMARK 210 PHOSPHATE BUFFER, 2 MM NAN3, 50
REMARK 210 MM DEUTERATED DTT, PH 6.0; 1 MM
REMARK 210 RGS4 U-15N,13C; 50MM PHOSPHATE
REMARK 210 BUFFER, 2 MM NAN3, 50 MM
REMARK 210 DEUTERATED DTT, PH 6.0; 1 MM
REMARK 210 RGS4 U-15N; 50MM PHOSPHATE
REMARK 210 BUFFER, 2 MM NAN3, 50 MM
REMARK 210 DEUTERATED DTT, PH 6.0
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
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, PIPP 4.2.8, XWINNMR
REMARK 210 2.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ARG A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 PRO A 134
REMARK 465 SER A 135
REMARK 465 SER A 136
REMARK 465 CYS A 137
REMARK 465 GLY A 138
REMARK 465 ALA A 139
REMARK 465 GLU A 140
REMARK 465 LYS A 141
REMARK 465 GLN A 142
REMARK 465 LYS A 143
REMARK 465 GLY A 144
REMARK 465 ALA A 145
REMARK 465 LYS A 146
REMARK 465 SER A 147
REMARK 465 SER A 148
REMARK 465 ALA A 149
REMARK 465 ASP A 150
REMARK 465 CYS A 151
REMARK 465 THR A 152
REMARK 465 SER A 153
REMARK 465 LEU A 154
REMARK 465 VAL A 155
REMARK 465 PRO A 156
REMARK 465 GLN A 157
REMARK 465 CYS A 158
REMARK 465 ALA A 159
REMARK 465 HIS A 160
REMARK 465 HIS A 161
REMARK 465 HIS A 162
REMARK 465 HIS A 163
REMARK 465 HIS A 164
REMARK 465 HIS A 165
REMARK 465 PRO A 166
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 HD22 ASN A 42 HD22 ASN A 82 1.24
REMARK 500 HD1 HIS A 23 H GLY A 26 1.35
REMARK 500 O TYR A 128 HG1 THR A 132 1.43
REMARK 500 O SER A 118 H PHE A 122 1.47
REMARK 500 O GLY A 26 H PHE A 30 1.48
REMARK 500 O ILE A 68 H PHE A 72 1.58
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 SER A 16 142.37 -173.97
REMARK 500 ASP A 117 -57.88 -124.88
REMARK 500 THR A 132 73.95 -117.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EZY RELATED DB: PDB
REMARK 900 1EZY IS THE ENSEMBLE STRUCTURE OF FREE RGS4
DBREF 1EZT A 5 159 UNP P49799 RGS4_RAT 51 205
SEQADV 1EZT MET A 1 UNP P49799 CLONING ARTIFACT
SEQADV 1EZT ARG A 2 UNP P49799 CLONING ARTIFACT
SEQADV 1EZT GLY A 3 UNP P49799 CLONING ARTIFACT
SEQADV 1EZT SER A 4 UNP P49799 CLONING ARTIFACT
SEQADV 1EZT HIS A 160 UNP P49799 EXPRESSION TAG
SEQADV 1EZT HIS A 161 UNP P49799 EXPRESSION TAG
SEQADV 1EZT HIS A 162 UNP P49799 EXPRESSION TAG
SEQADV 1EZT HIS A 163 UNP P49799 EXPRESSION TAG
SEQADV 1EZT HIS A 164 UNP P49799 EXPRESSION TAG
SEQADV 1EZT HIS A 165 UNP P49799 EXPRESSION TAG
SEQADV 1EZT PRO A 166 UNP P49799 CLONING ARTIFACT
SEQRES 1 A 166 MET ARG GLY SER VAL SER GLN GLU GLU VAL LYS LYS TRP
SEQRES 2 A 166 ALA GLU SER LEU GLU ASN LEU ILE ASN HIS GLU CYS GLY
SEQRES 3 A 166 LEU ALA ALA PHE LYS ALA PHE LEU LYS SER GLU TYR SER
SEQRES 4 A 166 GLU GLU ASN ILE ASP PHE TRP ILE SER CYS GLU GLU TYR
SEQRES 5 A 166 LYS LYS ILE LYS SER PRO SER LYS LEU SER PRO LYS ALA
SEQRES 6 A 166 LYS LYS ILE TYR ASN GLU PHE ILE SER VAL GLN ALA THR
SEQRES 7 A 166 LYS GLU VAL ASN LEU ASP SER CYS THR ARG GLU GLU THR
SEQRES 8 A 166 SER ARG ASN MET LEU GLU PRO THR ILE THR CYS PHE ASP
SEQRES 9 A 166 GLU ALA GLN LYS LYS ILE PHE ASN LEU MET GLU LYS ASP
SEQRES 10 A 166 SER TYR ARG ARG PHE LEU LYS SER ARG PHE TYR LEU ASP
SEQRES 11 A 166 LEU THR ASN PRO SER SER CYS GLY ALA GLU LYS GLN LYS
SEQRES 12 A 166 GLY ALA LYS SER SER ALA ASP CYS THR SER LEU VAL PRO
SEQRES 13 A 166 GLN CYS ALA HIS HIS HIS HIS HIS HIS PRO
HELIX 1 1 SER A 6 SER A 16 1 11
HELIX 2 2 SER A 16 HIS A 23 1 8
HELIX 3 3 HIS A 23 GLU A 37 1 15
HELIX 4 4 SER A 39 ILE A 55 1 17
HELIX 5 5 SER A 57 ILE A 73 1 17
HELIX 6 6 ASP A 84 MET A 95 1 12
HELIX 7 7 PHE A 103 SER A 125 1 23
HELIX 8 8 SER A 125 THR A 132 1 8
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 - 16 20 Bytes