Ligand Migration and Protein Fluctuations in Myoglobin Mutant L29W
VLSEGEWQLVLHVWAKVEADVAGHGQDIWIRLFKSHPETLEKFDRFKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKG HHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGNFGADAQGAMNKALELFRKDIAAKYKELGYQG
2.8 M AMMONIUM SULFATE, 25 MM TRIS, 1 MM EDTA, PH 8.0
SPERM WHALE MYOGLOBIN F46V N-BUTYL ISOCYANIDE AT PH 9.0
SPERM WHALE MYOGLOBIN H64A AQUOMET AT PH 9.0
SPERM WHALE MYOGLOBIN H64A N-BUTYL ISOCYANIDE AT PH 9.0
SPERM WHALE MYOGLOBIN N-BUTYL ISOCYANIDE AT PH 7.0
SPERM WHALE MYOGLOBIN N-BUTYL ISOCYANIDE AT PH 9.0
SPERM WHALE MYOGLOBIN V68F ETHYL ISOCYANIDE AT PH 9.0
SPERM WHALE MYOGLOBIN V68F N-BUTYL ISOCYANIDE AT PH 9.0
SPERM WHALE MYOGLOBIN V68F N-BUTYL ISOCYANIDE AT PH 7.0
SPERM WHALE MYOGLOBIN D122N ETHYL ISOCYANIDE AT PH 9.0
SPERM WHALE MYOGLOBIN D122N METHYL ISOCYANIDE AT PH 9.0
SPERM WHALE MYOGLOBIN D112N N-BUTYL ISOCYANIDE AT PH 9.0
SPERM WHALE MYOGLOBIN D122N N-PROPYL ISOCYANIDE AT PH 9.0
CARBONMONOXY-MYOGLOBIN, ATOMIC RESOLUTION
PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20K
PHOTOPRODUCT OF CARBONMONOXY MYOGLOBIN AT 40K
STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM D) AT 118 K
STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM B) AT 98 K
ATOMIC RESOLUTION CRYSTAL STRUCTURE AQUOMET- MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE
ATOMIC RESOLUTION CRYSTAL STRUCTURE ANALYSIS OF NATIVE DEOXY AND CO MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE
RECOMBINANT SPERM WHALE MYOGLOBIN L89G MUTANT (MET)
RECOMBINANT SPERM WHALE MYOGLOBIN L89F MUTANT (MET)
RECOMBINANT SPERM WHALE MYOGLOBIN L89W MUTANT (MET)
RECOMBINANT SPERM WHALE MYOGLOBIN H97V MUTANT (MET)
RECOMBINANT SPERM WHALE MYOGLOBIN H97F MUTANT (MET)
RECOMBINANT SPERM WHALE MYOGLOBIN H97Q MUTANT (MET)
RECOMBINANT SPERM WHALE MYOGLOBIN I99A MUTANT (MET)
RECOMBINANT SPERM WHALE MYOGLOBIN I99V MUTANT (MET)
RECOMBINANT SPERM WHALE MYOGLOBIN L104A MUTANT (MET)
RECOMBINANT SPERM WHALE MYOGLOBIN L104V MUTANT (MET)
RECOMBINANT SPERM WHALE MYOGLOBIN L104N MUTANT (MET)
RECOMBINANT SPERM WHALE MYOGLOBIN L104F MUTANT (MET)
RECOMBINANT SPERM WHALE MYOGLOBIN L104W MUTANT (MET)
NEUTRON STRUTURE OF FULLY DEUTERATED SPERM WHALE MYOGLOBIN AT 2.0 ANGSTROM
CARBONMONOXY-MYOGLOBIN MUTANT L29W AT 105K
CARBONMONOXY-MYOGLOBIN (MUTANT L29W) AFTER PHOTOLYSIS AT T>180K
CARBONMONOXY-MYOGLOBIN (MUTANT L29W) AFTER PHOTOLYSIS AT T<180K
CARBONMONOXY-MYOGLOBIN (MUTANT L29W) REBINDING STRUCTURE AFTER PHOTOLYSIS AT T< 180K
RECOMBINANT SPERM WHALE MYOGLOBIN H97D, D122N MUTANT (MET)
CRYSTAL STRUCTURE OF THE SPERM-WHALE MYOGLOBIN MUTANT H93G COMPLEXED WITH 4- METHYLIMIDAZOLE, METAQUO FORM
WILD-TYPE RECOMBINANT SPERM WHALE METAQUOMYOGLOBIN
SPERM WHALE METAQUOMYOGLOBIN PROXIMAL HISTIDINE MUTANT H93G WITH 1-METHYLIMIDAZOLE AS PROXIMAL LIGAND.
PHOTOLYZED CO COMPLEX OF MYOGLOBIN MB-YQR AT 20K
SPERM WHALE MET-MYOGLOBIN:CYANIDE COMPLEX
CRYSTAL STRUCTURE OF DEOXY SPERM WHALE MYOGLOBIN MUTANTY(B10)Q(E7)R(E10)
CRYSTAL STRUCTURE OF OXY SPERM WHALE MYOGLOBIN MUTANT Y(B10)Q(E7)R(E10)
COMBINED RIETVELD AND STEREOCHEMICAL RESTRAINT REFINEMENTOF A PROTEIN
MYOGLOBIN MUTANT WITH HIS 64 REPLACED BY VAL AND THR 67 REPLACED BY ARG (H64V, T67R)
SPERM WHALE MYOGLOBIN (FERROUS, NITRIC OXIDE BOUND)
INCORPORATION OF A HEMIN WITH THE SHORTEST ACID SIDE-CHAINS INTO MYOGLOBIN
CRYSTAL STRUCTURE OF AN ARTIFICIAL METALLOPROTEIN:CR(III)(3,3'-ME2-SALOPHEN)/ APO-A71G MYOGLOBIN
RECOMBINANT SPERM WHALE MYOGLOBIN IN THE PRESENCE OF 7ATMXENON
SPERM WHALE MET-MYOGLOBIN (ROOM TEMPERATURE; ROOM PRESSURE)
SPERM WHALE MET-MYOGLOBIN (ROOM TEMPERATURE; HIGH PRESSURE)
SPERM WHALE MET-MYOGLOBIN (LOW TEMPERATURE; HIGH PRESSURE)
1.3 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF P6 FORM OFMYOGLOBIN
NEUTRON STRUCTURE DETERMINATION OF SPERM WHALE MET-MYOGLOBIN AT 1.5A RESOLUTION.
RECOMBINANT SPERM WHALE MYOGLOBIN 29W MUTANT (OXY)
RECOMBINANT SPERM WHALE MYOGLOBIN H64D/V68A/ D122N MUTANT(MET)
MYOGLOBIN (FE II, CARBONMONOXY, 260 DEGREES K)
MYOGLOBIN (FERRIC) COMPLEX WITH IMIDAZOLE
SPERM WHALE MYOGLOBIN (MUTANT WITH INITIATOR MET AND WITH HIS 64 REPLACED BY GLN, LEU 29 REPLACED BY PHE
METMYOGLOBIN MUTANT WITH INITIATOR MET, ASP 122 REPLACED BY ASN, AND HIS 64 REPLACED BY TYR (INS(M-V1),D122N,H64Y)
MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET, VAL 68 REPLACED BY ALA, ASP 122 REPLACED BY ASN (M0,V68A,D122N)
MYOGLOBIN (DEOXY) MUTANT WITH INITIATOR MET, VAL 68 REPLACED BY ALA, ASP 122 REPLACED BY ASN (M0,V68A,D122N)
MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, VAL 68 REPLACED BY ALA, ASP 122 REPLACED BY ASN (M0,V68A,D122N)
MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET, VAL 68 REPLACED BY PHE, ASP 122 REPLACED BY ASN (M0,V68F,D122N)
MYOGLOBIN (DEOXY) MUTANT WITH INITIATOR MET, VAL 68 REPLACED BY PHE, ASP 122 REPLACED BY ASN (M0,V68F,D122N)
MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, VAL 68 REPLACED BY PHE, ASP 122 REPLACED BY ASN (M0,V68F,D122N)
MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET, VAL 68 REPLACED BY ILE, ASP 122 REPLACED BY ASN (M0,V68I,D122N)
MYOGLOBIN (DEOXY) MUTANT WITH INITIATOR MET, VAL 68 REPLACED BY ILE, ASP 122 REPLACED BY ASN (M0,V68I,D122N)
MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, VAL 68 REPLACED BY ILE, ASP 122 REPLACED BY ASN (M0,V68I,D122N)
MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET, VAL 68 REPLACED BY LEU, ASP 122 REPLACED BY ASN (INS(M0),V68L,D122N)
MYOGLOBIN (DEOXY) MUTANT WITH INITIATOR MET, VAL 68 REPLACED BY LEU, ASP 122 REPLACED BY ASN (M0,V68L,D122N)
MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, VAL 68 REPLACED BY LEU, ASP 122 REPLACED BY ASN (M0,V68L,D122N)
MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET, HIS 64 REPLACED BY GLY, VAL 68 REPLACED BY ALA, ASP 122 REPLACED BY ASN (M0,H64G,V68A,D122N)
MYOGLOBIN (DEOXY) MUTANT WITH INITIATOR MET, LEU 29 REPLACED BY PHE, ASP 122 REPLACED BY ASN (INS(M0),L29F,D122N)
MYOGLOBIN (DEOXY) MUTANT WITH INITIATOR MET, HIS 64 REPLACED BY GLY, ASP 122 REPLACED BY ASN (INS(M0,H64G,D122N)
MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET, HIS 64 REPLACED BY THR, ASP 122 REPLACED BY ASN (INS(M0),H64T,D122N)
MYOGLOBIN (DEOXY) MUTANT WITH INITIATOR MET, HIS 64 REPLACED BY THR, ASP 122 REPLACED BY ASN (INS(M0),H64T,D122N)
MOL_ID: 1; MOLECULE: MYOGLOBIN; CHAIN: NULL; ENGINEERED: YES; MUTATION: INITIATOR MET, PHE 46 REPLACED BY LEU AND ASP 122 REPLACED BY ASN (INS(MET 0), F46L, D122N); OTHER_DETAILS: FERRIC
MOL_ID: 1; MOLECULE: MYOGLOBIN; CHAIN: NULL; ENGINEERED: YES; MUTATION: INITIATOR MET, PHE 46 REPLACED BY VAL AND ASP 122 REPLACED BY ASN (INS(MET 0), F46V, D122N); OTHER_DETAILS: DEOXY
MOL_ID: 1; MOLECULE: MYOGLOBIN; CHAIN: NULL; ENGINEERED: YES; MUTATION: INITIATOR MET, PHE 46 REPLACED BY VAL AND ASP 122 REPLACED BY ASN (INS(MET 0), F46V, D122N); OTHER_DETAILS: FERRIC
MYOGLOBIN (FE II, CARBONMONOXY) (NMR, 12 STRUCTURES)
MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET, ASP 122 REPLACED BY ASN, AND PHE 46 REPLACED BY VAL (INS(M-V1),D122N,F46V)
CO COMPLEX OF MYOGLOBIN MB-YQR AT RT SOLVED FROM LAUE DATA.
STRUCTURE OF MYOGLOBIN MB-YQR 316 NS AFTER PHOTOLYSIS OFCARBON MONOXIDE SOLVED FROM LAUE DATA AT RT.
STRUCTURE OF EARTH-GROWN OXIDIZED MYOGLOBIN MUTANT YQR(ISS6A)
STRUCTURE OF MICROGRAVITY-GROWN OXIDIZED MYOGLOBIN MUTANTYQR (ISS6A)
STRUCTURE OF EARTH-GROWN OXIDIZED MYOGLOBIN MUTANT YQR(ISS8A)
STRUCTURE OF MICROGRAVITY-GROWN OXIDIZED MYOGLOBIN MUTANTYQR (ISS8A)
RECOMBINANT SPERM WHALE MYOGLOBIN H64D/V68S/ D122N MUTANT(MET)
RECOMBINANT SPERM WHALE MYOGLOBIN 29F/64Q/ 68F/122N MUTANT (MET)
RECOMBINANT SPERM WHALE MYOGLOBIN L29H/H64L/ D122N MUTANT (WITH INITIATOR MET)
RECOMBINANT SPERM WHALE MYOGLOBIN F43H, H64L MUTANT (MET)
SPERM WHALE NATIVE CO MYOGLOBIN AT PH 4. 0, TEMP 4C
CRYSTAL STRUCTURE OF AN ARTIFICIAL METALLOPROTEIN:FE(III)(3,3'-ME2-SALOPHEN)/ APO-A71G MYOGLOBIN
CRYSTAL STRUCTURE OF AN ARTIFICIAL METALLOPROTEIN:FE(III)(3,3'-ME2-SALOPHEN)/ APO-WILD TYPE MYOGLOBIN
STRUCTURE OF CHEMICALLY MODIFIED MYOGLOBIN WITH DISTAL N-TETRAZOLYL-HISTIDINE E7(64)
MYOGLOBIN (CYANO,MET) RECONSTITUTED WITH IRON (III) COMPLEXES OF PORPHYRIN
MYOGLOBIN (CARBONMONOXYMYOGLOBIN) (NEUTRON STUDY)
MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET, HIS 64 REPLACED BY GLY, AND ASP 122 REPLACED BY ASN (MET,H64G,D122N)
MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, HIS 64 REPLACED BY GLY, AND ASP 122 REPLACED BY ASN (MET,H64G,D122N)
MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET, HIS 64 REPLACED BY LEU, AND ASP 122 REPLACED BY ASN (MET,H64L,D122N)
MYOGLOBIN (DEOXY) MUTANT WITH INITIATOR MET, ASP 122 REPLACED BY ASN, AND HIS 64 REPLACED BY LEU (MET,D122N,H64L)
MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, ASP 122 REPLACED BY ASN, AND HIS 64 REPLACED BY LEU (MET,D122N,H64L)
MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET, ASP 122 REPLACED BY ASN, AND HIS 64 REPLACED BY GLN (MET,D122N,H64Q)
MYOGLOBIN (DEOXY) MUTANT WITH INITIATOR MET AND WITH ASP 122 REPLACED BY ASN AND HIS 64 REPLACED BY GLN (INS(M-V1,D122N, H64Q)
MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, HIS 64 REPLACED BY GLN, AND ASP 122 REPLACED BY ASN (MET,H64Q,D122N)
MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, ASP 122 REPLACED BY ASN, AND HIS 64 REPLACED BY THR (MET,D122N,H64T)
MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, ASP 122 REPLACED BY ASN, AND HIS 64 REPLACED BY VAL (MET,D122N,H64V)
MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET AND ASP 122 REPLACED BY ASN (MET, D122N)
MYOGLOBIN (DEOXY) MUTANT WITH INITIATOR MET AND ASP 122 REPLACED BY ASN (MET,D122N)
MYOGLOBIN (OXY) MUTANT WITH INITIATOR MET AND ASP 122 REPLACED BY ASN (MET,D122N)
MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET, ASP 122 REPLACED BY ASN, AND LEU 29 REPLACED BY PHE (MET,D122N,L29F)
MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, ASP 122 REPLACED BY ASN, AND LEU 29 REPLACED BY PHE (MET,D122N,L29F)
MYOGLOBIN (OXY) MUTANT WITH INITIATOR MET, LEU 29 REPLACED BY PHE, AND ASP 122 REPLACED BY ASN (MET,L29F,D122N)
MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, LEU 29 REPLACED BY VAL, AND ASP 122 REPLACED BY ASN (MET,L29V,D122N)
ENGINEERED RESIDUE IN CHAIN A, LEU 29 TO TRP
SEQUENCE REVISION TO CHAIN A 122, ASP TO ASN. REFERENCE: ROMERO-HERRERA A.E., LEHMANN H. RESIDUE 122 OF SPERM WHALE AND HORSE MYOGLOBIN. BIOCHIM. BIOPHYS. ACTA 336:318-323(1974).
MYOGLOBIN, MUTANT, OXYGEN TRANSPORT, HEME