Header list of 1q10.pdb file
Complete list - t 27 2 Bytes
HEADER PROTEIN BINDING 18-JUL-03 1Q10
TITLE ENSEMBLE OF 40 STRUCTURES OF THE DIMERIC MUTANT OF THE B1 DOMAIN OF
TITLE 2 STREPTOCOCCAL PROTEIN G
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMMUNOGLOBULIN G BINDING PROTEIN G;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: B1 DOMAIN;
COMPND 5 SYNONYM: IGG BINDING PROTEIN G;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS SP. 'GROUP G';
SOURCE 3 ORGANISM_TAXID: 1320;
SOURCE 4 GENE: SPG;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HMS174(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS GB1, CORE MUTANTS, DOMAIN-SWAPPING, OLIGOMERIZATION, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 40
MDLTYP MINIMIZED AVERAGE
AUTHOR I.J.BYEON,J.M.LOUIS,A.M.GRONENBORN
REVDAT 3 27-OCT-21 1Q10 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1Q10 1 VERSN
REVDAT 1 14-OCT-03 1Q10 0
JRNL AUTH I.J.BYEON,J.M.LOUIS,A.M.GRONENBORN
JRNL TITL A PROTEIN CONTORTIONIST: CORE MUTATIONS OF GB1 THAT INDUCE
JRNL TITL 2 DIMERIZATION AND DOMAIN SWAPPING
JRNL REF J.MOL.BIOL. V. 333 141 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 14516749
JRNL DOI 10.1016/S0022-2836(03)00928-8
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.M.GRONENBORN,D.R.FILPULA,N.Z.ESSIG,A.ACHARI,M.WHITLOW,
REMARK 1 AUTH 2 P.T.WINGFIELD,G.M.CLORE
REMARK 1 TITL A NOVEL, HIGHLY STABLE FOLD OF THE IMMUNOGLOBULIN BINDING
REMARK 1 TITL 2 DOMAIN OF STREPTOCOCCAL PROTEIN G
REMARK 1 REF SCIENCE V. 253 657 1991
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.K.FRANK,F.DYDA,A.DOBRODUMOV,A.M.GRONENBORN
REMARK 1 TITL CORE MUTATIONS SWITCH MONOMERIC PROTEIN GB1 INTO AN
REMARK 1 TITL 2 INTERTWINED TETRAMER
REMARK 1 REF NAT.STRUCT.BIOL. V. 9 877 2002
REMARK 1 REFN ISSN 1072-8368
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6 AND 3.1, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1311 CONSTRAINTS PER MONOMERIC SUBUNIT: 1035 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 72 HYDROGEN BOND DISTANCE CONSTRAINTS, 148
REMARK 3 DIHEDRAL ANGLE CONSTRAINTS, AND 56 RESIDUAL N-H DIPOLAR COUPLING
REMARK 3 CONSTRAINTS.
REMARK 4
REMARK 4 1Q10 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019780.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 50MM SODIUM PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.7MM (IN MONOMER) U-15N,13C,
REMARK 210 50MM PHOSPHATE BUFFER, 0.02%
REMARK 210 NAN3, 92.5% H2O, 7.5% D2O;
REMARK 210 0.85MM (IN MONOMER) U-15N,13C,
REMARK 210 0.85MM (IN MONOMER) UNLABELED,
REMARK 210 50MM PHOSPHATE BUFFER (PH 5.5),
REMARK 210 0.02 % NAN3, 92.5% H2O, 7.5% D2O;
REMARK 210 0.85MM (IN MONOMER) U-15N,13C,
REMARK 210 0.85MM (IN MONOMER) UNLABELED,
REMARK 210 50MM PHOSPHATE BUFFER, 0.02%
REMARK 210 NAN3, 100% D2O; 1.7MM (IN
REMARK 210 MONOMER) UNLABELED, 50MM
REMARK 210 PHOSPHATE BUFFER, 0.02% NAN3,
REMARK 210 92.5% H2O, 7.5% D2O; 1.7MM (IN
REMARK 210 MONOMER) UNLABELED, 50MM
REMARK 210 PHOSPHATE BUFFER, 0.02% NAN3,
REMARK 210 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-SEPARATED/12C-FILTERED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 750 MHZ; 600 MHZ; 500
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.2, PIPP 4.3.2, CNS 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY,TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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: 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 H ILE A 6 O PHE B 52 1.57
REMARK 500 O PHE A 52 H ILE B 6 1.57
REMARK 500 OD1 ASP B 22 H THR B 25 1.58
REMARK 500 OD1 ASP A 22 H THR A 25 1.58
REMARK 500 O PHE A 34 H GLY A 38 1.60
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 27 PHE A 33 -72.21 -51.61
REMARK 500 27 PHE B 33 -72.32 -51.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GB1 RELATED DB: PDB
REMARK 900 THE MONOMERIC WILDTYPE PROTEIN
REMARK 900 RELATED ID: 1MPE RELATED DB: PDB
REMARK 900 THE TETRAMERIC MUTANT PROTEIN
DBREF 1Q10 A 2 56 UNP P06654 SPG1_STRSG 228 282
DBREF 1Q10 B 2 56 UNP P06654 SPG1_STRSG 228 282
SEQADV 1Q10 MET A 1 UNP P06654 INITIATING METHIONINE
SEQADV 1Q10 GLN A 2 UNP P06654 THR 228 ENGINEERED MUTATION
SEQADV 1Q10 VAL A 5 UNP P06654 LEU 231 ENGINEERED MUTATION
SEQADV 1Q10 VAL A 30 UNP P06654 PHE 256 ENGINEERED MUTATION
SEQADV 1Q10 PHE A 33 UNP P06654 TYR 259 ENGINEERED MUTATION
SEQADV 1Q10 PHE A 34 UNP P06654 ALA 260 ENGINEERED MUTATION
SEQADV 1Q10 MET B 1 UNP P06654 INITIATING METHIONINE
SEQADV 1Q10 GLN B 2 UNP P06654 THR 228 ENGINEERED MUTATION
SEQADV 1Q10 VAL B 5 UNP P06654 LEU 231 ENGINEERED MUTATION
SEQADV 1Q10 VAL B 30 UNP P06654 PHE 256 ENGINEERED MUTATION
SEQADV 1Q10 PHE B 33 UNP P06654 TYR 259 ENGINEERED MUTATION
SEQADV 1Q10 PHE B 34 UNP P06654 ALA 260 ENGINEERED MUTATION
SEQRES 1 A 56 MET GLN TYR LYS VAL ILE LEU ASN GLY LYS THR LEU LYS
SEQRES 2 A 56 GLY GLU THR THR THR GLU ALA VAL ASP ALA ALA THR ALA
SEQRES 3 A 56 GLU LYS VAL VAL LYS GLN PHE PHE ASN ASP ASN GLY VAL
SEQRES 4 A 56 ASP GLY GLU TRP THR TYR ASP ASP ALA THR LYS THR PHE
SEQRES 5 A 56 THR VAL THR GLU
SEQRES 1 B 56 MET GLN TYR LYS VAL ILE LEU ASN GLY LYS THR LEU LYS
SEQRES 2 B 56 GLY GLU THR THR THR GLU ALA VAL ASP ALA ALA THR ALA
SEQRES 3 B 56 GLU LYS VAL VAL LYS GLN PHE PHE ASN ASP ASN GLY VAL
SEQRES 4 B 56 ASP GLY GLU TRP THR TYR ASP ASP ALA THR LYS THR PHE
SEQRES 5 B 56 THR VAL THR GLU
HELIX 1 1 ASP A 22 GLY A 38 1 17
HELIX 2 2 ASP A 47 THR A 49 5 3
HELIX 3 3 ASP B 22 GLY B 38 1 17
HELIX 4 4 ASP B 47 THR B 49 5 3
SHEET 1 A 8 GLU A 42 ASP A 46 0
SHEET 2 A 8 THR A 51 THR A 55 -1 O THR A 53 N THR A 44
SHEET 3 A 8 GLN B 2 ASN B 8 1 O ILE B 6 N PHE A 52
SHEET 4 A 8 LEU B 12 GLU B 19 -1 O THR B 16 N VAL B 5
SHEET 5 A 8 LEU A 12 GLU A 19 -1 N THR A 17 O LYS B 13
SHEET 6 A 8 GLN A 2 ASN A 8 -1 N VAL A 5 O THR A 16
SHEET 7 A 8 THR B 51 THR B 55 1 O PHE B 52 N ILE A 6
SHEET 8 A 8 GLU B 42 ASP B 46 -1 N THR B 44 O THR B 53
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 - t 27 2 Bytes