Header list of 1p7f.pdb file
Complete list - 23 202 Bytes
HEADER IMMUNE SYSTEM 01-MAY-03 1P7F
TITLE GB3 SOLUTION STRUCTURE OBTAINED BY REFINEMENT OF X-RAY STRUCTURE WITH
TITLE 2 DIPOLAR COUPLINGS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMMUNOGLOBULIN G BINDING PROTEIN G;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THIRD IGG-BINDING DOMAIN;
COMPND 5 SYNONYM: IGG BINDING PROTEIN G, GB3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS SP. 'GROUP G';
SOURCE 3 ORGANISM_TAXID: 1320;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: HMS174;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-11A
KEYWDS IMMUNE SYSTEM
EXPDTA SOLUTION NMR
AUTHOR T.S.ULMER,B.E.RAMIREZ,F.DELAGLIO,A.BAX
REVDAT 3 23-FEB-22 1P7F 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1P7F 1 VERSN
REVDAT 1 05-AUG-03 1P7F 0
JRNL AUTH T.S.ULMER,B.E.RAMIREZ,F.DELAGLIO,A.BAX
JRNL TITL EVALUATION OF BACKBONE PROTON POSITIONS AND DYNAMICS IN A
JRNL TITL 2 SMALL PROTEIN BY LIQUID CRYSTAL NMR SPECTROSCOPY.
JRNL REF J.AM.CHEM.SOC. V. 125 9179 2003
JRNL REFN ISSN 0002-7863
JRNL PMID 15369375
JRNL DOI 10.1021/JA0350684
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.P.DERRICK,D.B.WIGLEY
REMARK 1 TITL THE THIRD IGG-BINDING DOMAIN FROM STREPTOCOCCAL PROTEIN G.
REMARK 1 TITL 2 AN ANALYSIS BY X-RAY CRYSTALLOGRAPHY OF THE STRUCTURE ALONE
REMARK 1 TITL 3 AND IN A COMPLEX WITH FAB.
REMARK 1 REF J.MOL.BIOL. V. 243 906 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1994.1691
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYNAMO 2.1, DYNAMO 2.1
REMARK 3 AUTHORS : DELAGLIO, F. (DYNAMO), DELAGLIO, F. (DYNAMO)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 GB3 SOLUTION STRUCTURE OBTAINED BY REFINEMENT OF THE X-RAY
REMARK 3 STRUCTURE OF GB3 (1IGD) WITH C(ALPHA)-C', C'-N AND N-H DIPOLAR
REMARK 3 COUPLINGS MEASURED IN FIVE ALIGNING MEDIA (BICELLE, PEG, PF1 PHAGE,
REMARK 3 NEGATIVELY AND POSITIVELY CHARGED POLYACRYLAMIDE GELS). HA IS
REMARK 3 PLACED AT THE POSITION THAT YIELDS BEST AGREEMENT WITH THE C(ALPHA)
REMARK 3 -H(ALPHA) DIPOLAR COUPLINGS. THE HA POSITIONS OF V42 AND T55 ARE
REMARK 3 EXTREME AND MAY REFLECT DYNAMIC EFFECTS OR ERRORS IN THE BACKBONE
REMARK 3 POSITION OF CA. DIPOLAR COUPLINGS ORIGINATING ON RESIDUES 10-11,
REMARK 3 24-26, 39-41 AND THE N- AND C-TERMINAL RESIDUES WERE EXCLUDED,
REMARK 3 RESULTING IN IDENTITY
REMARK 3 WITH THE X-RAY STRUCTURE FOR THESE RESIDUES.
REMARK 4
REMARK 4 1P7F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019101.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 0.05
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 25 MM NAH2PO4/NA2HPO4, 0.2 MG/ML
REMARK 210 NAN3, 1.5 MM GB3 PROTEIN AND
REMARK 210 ALIGNING MEDIA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D IPAP [15N,1H]-HSQC; 3D
REMARK 210 CT(H)CA(CO)NH; 13C-COUPLED 3D
REMARK 210 HNCO; QUANTITATIVE J-CORRELATION
REMARK 210 3D TROSY-HNCO
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : BEST AGREEMENT WITH DIPOLAR
REMARK 210 CONSTRAINTS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 ASN A 8 70.44 -113.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IGD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE THIRD IGG-BINDING DOMAIN FROM
REMARK 900 STREPTOCOCCAL PROTEIN G
REMARK 900 RELATED ID: 1P7E RELATED DB: PDB
REMARK 900 GB3 SOLUTION STRUCTURE OBTAINED BY REFINEMENT OF X-RAY STRUCTURE
REMARK 900 WITH DIPOLAR COUPLINGS
DBREF 1P7F A 3 56 UNP P19909 SPG2_STRSG 444 497
SEQADV 1P7F MET A 1 UNP P19909 CLONING ARTIFACT
SEQADV 1P7F GLN A 2 UNP P19909 CLONING ARTIFACT
SEQRES 1 A 56 MET GLN TYR LYS LEU VAL ILE ASN GLY LYS THR LEU LYS
SEQRES 2 A 56 GLY GLU THR THR THR LYS ALA VAL ASP ALA GLU THR ALA
SEQRES 3 A 56 GLU LYS ALA PHE LYS GLN TYR ALA ASN ASP ASN GLY VAL
SEQRES 4 A 56 ASP GLY VAL TRP THR TYR ASP ASP ALA THR LYS THR PHE
SEQRES 5 A 56 THR VAL THR GLU
HELIX 1 1 ASP A 22 ASN A 37 1 16
SHEET 1 A 4 LYS A 13 LYS A 19 0
SHEET 2 A 4 GLN A 2 ASN A 8 -1 N TYR A 3 O THR A 18
SHEET 3 A 4 THR A 51 THR A 55 1 O VAL A 54 N ASN A 8
SHEET 4 A 4 VAL A 42 ASP A 46 -1 N VAL A 42 O THR A 55
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 - 23 202 Bytes