Header list of 1mpe.pdb file
Complete list - t 27 2 Bytes
HEADER PROTEIN BINDING 12-SEP-02 1MPE TITLE ENSEMBLE OF 20 STRUCTURES OF THE TETRAMERIC 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, C, D; COMPND 4 FRAGMENT: B1 DOMAIN, SEQUENCE DATABASE RESIDUES 228-282; 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 STRAND-EXCHANGED TETRAMER, CHANNEL, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 21 MDLTYP MINIMIZED AVERAGE AUTHOR M.K.FRANK,F.DYDA,A.DOBRODUMOV,A.M.GRONENBORN REVDAT 3 27-OCT-21 1MPE 1 REMARK SEQADV REVDAT 2 24-FEB-09 1MPE 1 VERSN REVDAT 1 30-OCT-02 1MPE 0 JRNL AUTH M.KIRSTEN FRANK,F.DYDA,A.DOBRODUMOV,A.M.GRONENBORN JRNL TITL CORE MUTATIONS SWITCH MONOMERIC PROTEIN GB1 INTO AN JRNL TITL 2 INTERTWINED TETRAMER. JRNL REF NAT.STRUCT.BIOL. V. 9 877 2002 JRNL REFN ISSN 1072-8368 JRNL PMID 12379842 JRNL DOI 10.1038/NSB854 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 A.M.GRONENBORN,M.K.FRANK,G.M.CLORE REMARK 1 TITL CORE MUTANTS OF THE IMMUNOGLOBULIN BINDING DOMAIN OF REMARK 1 TITL 2 STREPTOCOCCAL PROTEIN G: STABILITY AND STRUCTURAL INTEGRITY REMARK 1 REF FEBS LETT. V. 398 312 1996 REMARK 1 REFN ISSN 0014-5793 REMARK 1 DOI 10.1016/S0014-5793(96)01262-8 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2.2, X-PLOR 4.0 REMARK 3 AUTHORS : FRANK DELAGLIO (NMRPIPE), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NMR CONSTRAINTS (PER MONOMER) 822 NOE REMARK 3 -DERIVED DISTANCE RESTRAINTS (534 INTRAMONOMER, 288 INTERMONOMER) REMARK 3 42 DISTANCE RESTRAINTS FROM HYDROGEN BONDS (20 INTRAMONOMER, 22 REMARK 3 INTERMONOMER) 30 J-COUPLING RESTRAINTS, 33 RESIDUAL DIPOLAR REMARK 3 COUPLINGS (HN) 66 BACKBONE DIHEDRAL ANGLE RESTRAINTS 31 REMARK 3 SIDECHAIN DIHEDRAL ANGLE RESTRAINTS REMARK 4 REMARK 4 1MPE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-02. REMARK 100 THE DEPOSITION ID IS D_1000017078. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 313 REMARK 210 PH : 5.45 REMARK 210 IONIC STRENGTH : 50 MM SODIUM PHOSPHATE, 0.02% REMARK 210 SODIUM AZIDE REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 3.5 MM (IN MONOMER) U-15N,13C, REMARK 210 50 MM SODIUM PHOSPHATE BUFFER, REMARK 210 0.02% SODIUM AZIDE; 2.89 MM (IN REMARK 210 MONOMER) U-15N, 50 MM SODIUM REMARK 210 PHOSPHATE BUFFER, 0.02% SODIUM REMARK 210 AZIDE; 3.5 MM (IN MONOMER) U-15N, REMARK 210 13C, 50 MM SODIUM PHOSPHATE REMARK 210 BUFFER, 0.02% SODIUM AZIDE; 1.4 REMARK 210 MM (IN MONOMER) 1:1 MIXTURE REMARK 210 UNLABELLED:U-15N,13C, 50 MM REMARK 210 SODIUM PHOSPHATE BUFFER, 0.02% REMARK 210 SODIUM AZIDE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA; REMARK 210 3D_13C-SEPARATED_NOESY; 4D_13C-SEPARATED_NOESY; 4D_13C/15N- REMARK 210 SEPARATED_NOESY; 3D_12C-FILTERED_13C-SEPARATED_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 : PIPP 4.3.2, XWINNMR 2.6, CNS 1.0 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH LEAST RESTRAINT REMARK 210 VIOLATIONS AND PHI, PSI ANGLES REMARK 210 OF RESIDUE 46 IN ALLOWED REGION REMARK 210 OF RAMACHRANDRAN PLOT REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: T1,T2, AND HETERONUCLEAR NOES COLLECTED. DIPOLAR COUPLINGS REMARK 210 (N-H) WERE COLLECTED AS WELL. DIPOLAR COUPLING AND CHEMICAL REMARK 210 SHIFTS FROM RESIDUES WITH HETERONUCLEAR NOE BELOW 0.6 WERE NOT REMARK 210 USED. 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D 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 1 LEU A 12 59.98 -146.42 REMARK 500 1 LYS A 13 -78.02 -153.04 REMARK 500 1 THR A 17 -68.84 68.47 REMARK 500 1 ALA A 20 -54.08 -165.64 REMARK 500 1 THR A 55 -71.76 -152.49 REMARK 500 1 LEU B 12 -76.20 59.87 REMARK 500 1 THR B 17 -73.90 -156.69 REMARK 500 1 ALA B 20 -41.35 -158.87 REMARK 500 1 THR B 55 -71.84 -152.78 REMARK 500 1 THR C 16 36.07 -98.30 REMARK 500 1 THR C 18 -168.17 -76.86 REMARK 500 1 GLU C 19 -49.52 -131.54 REMARK 500 1 ALA C 20 -47.04 75.32 REMARK 500 1 THR C 55 -72.80 -151.99 REMARK 500 1 ASN D 8 71.22 -158.97 REMARK 500 1 LYS D 10 109.97 -44.38 REMARK 500 1 GLU D 15 -33.11 85.85 REMARK 500 1 THR D 16 -176.27 37.84 REMARK 500 1 THR D 17 -74.35 -111.66 REMARK 500 1 ALA D 20 -51.73 -149.12 REMARK 500 1 THR D 55 -71.97 -152.77 REMARK 500 2 ASN A 8 -71.20 -152.11 REMARK 500 2 LYS A 10 86.87 62.44 REMARK 500 2 LEU A 12 -62.91 -142.21 REMARK 500 2 THR A 16 -49.29 -143.96 REMARK 500 2 THR A 17 -68.89 67.60 REMARK 500 2 GLU A 19 99.86 61.44 REMARK 500 2 THR A 55 -67.82 -148.46 REMARK 500 2 ASN B 8 -61.01 -151.98 REMARK 500 2 LEU B 12 146.47 62.89 REMARK 500 2 LYS B 13 96.01 59.24 REMARK 500 2 THR B 55 -67.72 -148.59 REMARK 500 2 ASN C 8 -70.53 -152.05 REMARK 500 2 LYS C 10 163.94 60.63 REMARK 500 2 THR C 11 107.52 61.18 REMARK 500 2 THR C 16 -65.95 -108.47 REMARK 500 2 THR C 17 -65.73 -147.26 REMARK 500 2 THR C 18 73.16 53.11 REMARK 500 2 ALA C 20 -62.27 -169.07 REMARK 500 2 THR C 55 -67.78 -148.54 REMARK 500 2 ASN D 8 -66.72 -152.34 REMARK 500 2 LYS D 10 149.56 63.54 REMARK 500 2 THR D 11 104.08 63.58 REMARK 500 2 LEU D 12 -68.69 -107.85 REMARK 500 2 LYS D 13 96.10 60.65 REMARK 500 2 ALA D 20 56.99 -147.36 REMARK 500 2 THR D 55 -67.84 -148.53 REMARK 500 3 THR A 16 -169.74 45.38 REMARK 500 3 THR A 17 -62.56 -132.29 REMARK 500 3 THR A 18 -173.08 57.03 REMARK 500 REMARK 500 THIS ENTRY HAS 428 RAMACHANDRAN OUTLIERS. 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 DBREF 1MPE A 2 56 UNP P06654 SPG1_STRSG 228 282 DBREF 1MPE B 2 56 UNP P06654 SPG1_STRSG 228 282 DBREF 1MPE C 2 56 UNP P06654 SPG1_STRSG 228 282 DBREF 1MPE D 2 56 UNP P06654 SPG1_STRSG 228 282 SEQADV 1MPE MET A 1 UNP P06654 INITIATING METHIONINE SEQADV 1MPE GLN A 2 UNP P06654 THR 228 ENGINEERED MUTATION SEQADV 1MPE VAL A 5 UNP P06654 LEU 231 ENGINEERED MUTATION SEQADV 1MPE PHE A 26 UNP P06654 ALA 252 ENGINEERED MUTATION SEQADV 1MPE VAL A 30 UNP P06654 PHE 256 ENGINEERED MUTATION SEQADV 1MPE PHE A 33 UNP P06654 TYR 259 ENGINEERED MUTATION SEQADV 1MPE PHE A 34 UNP P06654 ALA 260 ENGINEERED MUTATION SEQADV 1MPE MET B 1 UNP P06654 INITIATING METHIONINE SEQADV 1MPE GLN B 2 UNP P06654 THR 228 ENGINEERED MUTATION SEQADV 1MPE VAL B 5 UNP P06654 LEU 231 ENGINEERED MUTATION SEQADV 1MPE PHE B 26 UNP P06654 ALA 252 ENGINEERED MUTATION SEQADV 1MPE VAL B 30 UNP P06654 PHE 256 ENGINEERED MUTATION SEQADV 1MPE PHE B 33 UNP P06654 TYR 259 ENGINEERED MUTATION SEQADV 1MPE PHE B 34 UNP P06654 ALA 260 ENGINEERED MUTATION SEQADV 1MPE MET C 1 UNP P06654 INITIATING METHIONINE SEQADV 1MPE GLN C 2 UNP P06654 THR 228 ENGINEERED MUTATION SEQADV 1MPE VAL C 5 UNP P06654 LEU 231 ENGINEERED MUTATION SEQADV 1MPE PHE C 26 UNP P06654 ALA 252 ENGINEERED MUTATION SEQADV 1MPE VAL C 30 UNP P06654 PHE 256 ENGINEERED MUTATION SEQADV 1MPE PHE C 33 UNP P06654 TYR 259 ENGINEERED MUTATION SEQADV 1MPE PHE C 34 UNP P06654 ALA 260 ENGINEERED MUTATION SEQADV 1MPE MET D 1 UNP P06654 INITIATING METHIONINE SEQADV 1MPE GLN D 2 UNP P06654 THR 228 ENGINEERED MUTATION SEQADV 1MPE VAL D 5 UNP P06654 LEU 231 ENGINEERED MUTATION SEQADV 1MPE PHE D 26 UNP P06654 ALA 252 ENGINEERED MUTATION SEQADV 1MPE VAL D 30 UNP P06654 PHE 256 ENGINEERED MUTATION SEQADV 1MPE PHE D 33 UNP P06654 TYR 259 ENGINEERED MUTATION SEQADV 1MPE PHE D 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 PHE 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 PHE 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 SEQRES 1 C 56 MET GLN TYR LYS VAL ILE LEU ASN GLY LYS THR LEU LYS SEQRES 2 C 56 GLY GLU THR THR THR GLU ALA VAL ASP ALA ALA THR PHE SEQRES 3 C 56 GLU LYS VAL VAL LYS GLN PHE PHE ASN ASP ASN GLY VAL SEQRES 4 C 56 ASP GLY GLU TRP THR TYR ASP ASP ALA THR LYS THR PHE SEQRES 5 C 56 THR VAL THR GLU SEQRES 1 D 56 MET GLN TYR LYS VAL ILE LEU ASN GLY LYS THR LEU LYS SEQRES 2 D 56 GLY GLU THR THR THR GLU ALA VAL ASP ALA ALA THR PHE SEQRES 3 D 56 GLU LYS VAL VAL LYS GLN PHE PHE ASN ASP ASN GLY VAL SEQRES 4 D 56 ASP GLY GLU TRP THR TYR ASP ASP ALA THR LYS THR PHE SEQRES 5 D 56 THR VAL THR GLU HELIX 1 1 ASP A 22 ASP A 36 1 15 HELIX 2 2 ASP B 22 ASP B 36 1 15 HELIX 3 3 ASP C 22 ASP C 36 1 15 HELIX 4 4 ASP D 22 ASP D 36 1 15 SHEET 1 A 6 GLY A 41 TYR A 45 0 SHEET 2 A 6 THR C 49 VAL C 54 -1 O THR C 51 N THR A 44 SHEET 3 A 6 GLN B 2 ILE B 6 1 N LYS B 4 O LYS C 50 SHEET 4 A 6 GLN A 2 ILE A 6 -1 N VAL A 5 O TYR B 3 SHEET 5 A 6 THR D 49 VAL D 54 1 O LYS D 50 N LYS A 4 SHEET 6 A 6 GLY B 41 TYR B 45 -1 N THR B 44 O THR D 51 SHEET 1 B 6 GLY C 41 TYR C 45 0 SHEET 2 B 6 THR A 49 VAL A 54 -1 N THR A 51 O THR C 44 SHEET 3 B 6 GLN D 2 ILE D 6 1 O LYS D 4 N LYS A 50 SHEET 4 B 6 GLN C 2 ILE C 6 -1 N VAL C 5 O TYR D 3 SHEET 5 B 6 THR B 49 VAL B 54 1 N LYS B 50 O LYS C 4 SHEET 6 B 6 GLY D 41 TYR D 45 -1 O THR D 44 N THR B 51 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