Header list of 1gdf.pdb file
Complete list - 23 20 Bytes
HEADER RHO-GTPASE INHIBITOR 11-MAY-97 1GDF
TITLE STRUCTURE OF RHOGDI: A C-TERMINAL BINDING DOMAIN TARGETS AN N-TERMINAL
TITLE 2 INHIBITORY PEPTIDE TO GTPASES, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RHOGDI;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ISOPRENE BINDING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS RHO-GTPASE INHIBITOR, NUCLEOTIDE EXCHANGE, ISOPRENE BINDING
EXPDTA SOLUTION NMR
AUTHOR M.K.ROSEN,Y.Q.GOSSER
REVDAT 3 23-FEB-22 1GDF 1 REMARK
REVDAT 2 24-FEB-09 1GDF 1 VERSN
REVDAT 1 19-NOV-97 1GDF 0
JRNL AUTH Y.Q.GOSSER,T.K.NOMANBHOY,B.AGHAZADEH,D.MANOR,C.COMBS,
JRNL AUTH 2 R.A.CERIONE,M.K.ROSEN
JRNL TITL C-TERMINAL BINDING DOMAIN OF RHO GDP-DISSOCIATION INHIBITOR
JRNL TITL 2 DIRECTS N-TERMINAL INHIBITORY PEPTIDE TO GTPASES.
JRNL REF NATURE V. 387 814 1997
JRNL REFN ISSN 0028-0836
JRNL PMID 9194563
JRNL DOI 10.1038/42961
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.0
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GDF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173529.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCACB; CBCACONNH; HNCO; CCC
REMARK 210 -TOCSY-NNH; HCC-TOCSY-NNH; 15N-
REMARK 210 TOCSY; HCCH-TOCSY; HCCH-COSY;
REMARK 210 15N-NOESY; 15N/13C-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW, X-PLOR
REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY/
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO DISTANCE VIOLATIONS 0.3
REMARK 210 ANGSTROMS, THEN LOWEST OVERALL
REMARK 210 ENERGY
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: 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 64 85.99 52.68
REMARK 500 CYS A 79 -166.34 -160.30
REMARK 500 GLU A 106 105.74 -50.27
REMARK 500 ARG A 120 -66.94 -149.45
REMARK 500 GLN A 130 119.26 -162.12
REMARK 500 ASP A 140 132.81 -170.09
REMARK 500 ARG A 152 -39.47 -167.10
REMARK 500 ALA A 153 -75.20 -136.37
REMARK 500 GLU A 154 -145.00 -143.37
REMARK 500 ASP A 183 -151.18 -121.45
REMARK 500 ASP A 185 -15.58 -171.25
REMARK 500 THR A 187 -166.29 -175.93
REMARK 500 LYS A 199 -154.24 -154.93
REMARK 500 GLU A 201 51.56 -143.19
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 ARG A 74 0.26 SIDE CHAIN
REMARK 500 ARG A 111 0.29 SIDE CHAIN
REMARK 500 ARG A 117 0.27 SIDE CHAIN
REMARK 500 ARG A 120 0.22 SIDE CHAIN
REMARK 500 ARG A 134 0.23 SIDE CHAIN
REMARK 500 ARG A 152 0.32 SIDE CHAIN
REMARK 500 ARG A 172 0.24 SIDE CHAIN
REMARK 500 ARG A 180 0.21 SIDE CHAIN
REMARK 500 ARG A 186 0.24 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AJW RELATED DB: PDB
DBREF 1GDF A 60 204 UNP P19803 GDIR_BOVIN 60 204
SEQRES 1 A 145 ALA VAL SER ALA ASP PRO ASN VAL PRO ASN VAL VAL VAL
SEQRES 2 A 145 THR ARG LEU THR LEU VAL CYS SER THR ALA PRO GLY PRO
SEQRES 3 A 145 LEU GLU LEU ASP LEU THR GLY ASP LEU GLU SER PHE LYS
SEQRES 4 A 145 LYS GLN SER PHE VAL LEU LYS GLU GLY VAL GLU TYR ARG
SEQRES 5 A 145 ILE LYS ILE SER PHE ARG VAL ASN ARG GLU ILE VAL SER
SEQRES 6 A 145 GLY MET LYS TYR ILE GLN HIS THR TYR ARG LYS GLY VAL
SEQRES 7 A 145 LYS ILE ASP LYS THR ASP TYR MET VAL GLY SER TYR GLY
SEQRES 8 A 145 PRO ARG ALA GLU GLU TYR GLU PHE LEU THR PRO MET GLU
SEQRES 9 A 145 GLU ALA PRO LYS GLY MET LEU ALA ARG GLY SER TYR ASN
SEQRES 10 A 145 ILE LYS SER ARG PHE THR ASP ASP ASP ARG THR ASP HIS
SEQRES 11 A 145 LEU SER TRP GLU TRP ASN LEU THR ILE LYS LYS GLU TRP
SEQRES 12 A 145 LYS ASP
HELIX 1 1 GLU A 95 LYS A 99 3 5
SHEET 1 A 3 SER A 101 VAL A 103 0
SHEET 2 A 3 ASP A 188 THR A 197 1 N ASN A 195 O PHE A 102
SHEET 3 A 3 ASN A 176 THR A 182 -1 N PHE A 181 O HIS A 189
SHEET 1 B 3 GLU A 155 GLU A 157 0
SHEET 2 B 3 ARG A 111 VAL A 118 -1 N PHE A 116 O TYR A 156
SHEET 3 B 3 VAL A 70 VAL A 78 -1 N VAL A 78 O ARG A 111
SHEET 1 C 2 MET A 126 THR A 132 0
SHEET 2 C 2 ASP A 140 GLY A 147 -1 N GLY A 147 O MET A 126
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 - 23 20 Bytes