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HEADER OXYGEN STORAGE/TRANSPORT 27-SEP-02 1MWB TITLE SOLUTION STRUCTURE OF THE RECOMBINANT HEMOGLOBIN FROM THE TITLE 2 CYANOBACTERIUM SYNECHOCYSTIS SP. PCC 6803 IN ITS TITLE 3 HEMICHROME STATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYANOGLOBIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: HEMOGLOBIN, HB; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP.; SOURCE 3 ORGANISM_COMMON: CYANOBACTERIA; SOURCE 4 STRAIN: PCC 6803; SOURCE 5 GENE: SLR2097 (GLBN); SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3C KEYWDS GLOBIN, CYANOGLOBIN EXPDTA NMR, 20 STRUCTURES AUTHOR C.J.FALZONE,B.C.VU,N.L.SCOTT,J.T.LECOMTE REVDAT 1 04-DEC-02 1MWB 0 JRNL AUTH C.J.FALZONE,B.C.VU,N.L.SCOTT,J.T.LECOMTE JRNL TITL THE SOLUTION STRUCTURE OF THE RECOMBINANT JRNL TITL 2 HEMOGLOBIN FROM THE CYANOBACTERIUM SYNECHOCYSTIS JRNL TITL 3 SP. PCC 6803 IN ITS HEMICHROME STATE JRNL REF J.MOL.BIOL. V. 324 1015 2002 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.J.FALZONE,J.T.LECOMTE REMARK 1 TITL ASSIGNMENT OF THE 1H, 13C, AND 15N SIGNALS OF REMARK 1 TITL 2 SYNECHOCYSTIS SP. PCC 6803 METHEMOGLOBIN REMARK 1 REF J.BIOMOL.NMR V. 23 71 2002 REMARK 1 REFN ASTM JBNME9 NE ISSN 0925-2738 REMARK 1 REFERENCE 2 REMARK 1 AUTH N.L.SCOTT,J.T.LECOMTE REMARK 1 TITL CLONING, EXPRESSION, PURIFICATION, AND PRELIMINARY REMARK 1 TITL 2 CHARACTERIZATION OF A PUTATIVE HEMOGLOBIN FROM THE REMARK 1 TITL 3 CYANOBACTERIUM SYNECHOCYSTIS SP. PCC 6803 REMARK 1 REF PROTEIN SCI. V. 9 587 2000 REMARK 1 REFN ASTM PRCIEI US ISSN 0961-8368 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR-NIH 1.2.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1MWB COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB017245. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.5 REMARK 210 IONIC STRENGTH : 50 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.6 - 2 MM PROTEIN, 20 MM K REMARK 210 OR NA PHOSPHATE; 0.6 - 2 MM REMARK 210 PROTEIN, 20 MM K OR NA REMARK 210 PHOSPHATE; 1 MM U-15N PROTEIN, REMARK 210 20 MM K OR NA PHOSPHATE; 1 MM REMARK 210 U-15N, 13C PROTEIN, 20 MM K OR REMARK 210 NA PHOSPHATE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY, 3D_13C-SEPARATED_ REMARK 210 NOESY, 3D_15N-SEPARATED_NOESY, REMARK 210 J-MODULATED 1H-15N HSQC, 2D REMARK 210 TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ, 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX, INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER, VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.851, FELIX 2000, REMARK 210 XWINNMR 2.5, NMRPIPE 2.1 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING, MOLECULAR DYNAMICS, REMARK 210 TORSIONAL ANGLE DATABASE REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH LOWEST ENERGY REMARK 210 AND LEAST RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS IS A LOW-SPIN FE(+3) COMPLEX. STANDARD METHODS AS REMARK 210 APPLIED TO DIMAGNETIC PROTEINS WERE USED TO DETERMINE THE REMARK 210 STRUCTURE. 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 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 M RES CSSEQI PSI PHI REMARK 500 11 THR A 11 -89.29 44.83 REMARK 500 12 THR A 11 -101.69 39.75 REMARK 500 15 ASP A 59 127.36 59.43 REMARK 500 17 ASN A 123 -68.56 59.29 REMARK 999 REMARK 999 SEQUENCE REMARK 999 AUTHORS INFORMED THAT MET 1 IN SWISSPROT P73925 REMARK 999 WAS CLEAVED POST-TRANSLATIONALLY DBREF 1MWB A 2 124 UNP P73925 GLBN_SYNY3 2 124 SEQRES 1 A 123 SER THR LEU TYR GLU LYS LEU GLY GLY THR THR ALA VAL SEQRES 2 A 123 ASP LEU ALA VAL ASP LYS PHE TYR GLU ARG VAL LEU GLN SEQRES 3 A 123 ASP ASP ARG ILE LYS HIS PHE PHE ALA ASP VAL ASP MET SEQRES 4 A 123 ALA LYS GLN ARG ALA HIS GLN LYS ALA PHE LEU THR TYR SEQRES 5 A 123 ALA PHE GLY GLY THR ASP LYS TYR ASP GLY ARG TYR MET SEQRES 6 A 123 ARG GLU ALA HIS LYS GLU LEU VAL GLU ASN HIS GLY LEU SEQRES 7 A 123 ASN GLY GLU HIS PHE ASP ALA VAL ALA GLU ASP LEU LEU SEQRES 8 A 123 ALA THR LEU LYS GLU MET GLY VAL PRO GLU ASP LEU ILE SEQRES 9 A 123 ALA GLU VAL ALA ALA VAL ALA GLY ALA PRO ALA HIS LYS SEQRES 10 A 123 ARG ASP VAL LEU ASN GLN HET HEM A 125 73 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 2 HEM C34 H32 FE N4 O4 HELIX 1 1 SER A 2 LYS A 7 5 6 HELIX 2 2 GLY A 10 ASP A 28 1 19 HELIX 3 3 ASP A 28 ALA A 36 1 9 HELIX 4 4 ASP A 39 GLY A 56 1 18 HELIX 5 5 GLY A 63 HIS A 77 1 15 HELIX 6 6 ASN A 80 GLY A 99 1 20 HELIX 7 7 PRO A 101 ALA A 114 1 14 HELIX 8 8 ALA A 114 ASN A 123 1 10 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