HEADER OXYGEN TRANSPORT 11-FEB-91 2HBG 2HBG 2 COMPND HEMOGLOBIN (DEOXY) 2HBG 3 SOURCE MARINE BLOODWORM (GLYCERA $DIBRANCHIATA) 2HBG 4 AUTHOR G.A.ARENTS,W.E.LOVE 2HBG 5 REVDAT 1 15-JUL-92 2HBG 0 2HBG 6 REMARK 1 2HBG 7 REMARK 1 REFERENCE 1 2HBG 8 REMARK 1 AUTH G.A.ARENTS,W.E.LOVE 2HBG 9 REMARK 1 TITL GLYCERA $DIBRANCHIATA HEMOGLOBIN. STRUCTURE AND 2HBG 10 REMARK 1 TITL 2 REFINEMENT AT 1.5 ANGSTROMS RESOLUTION 2HBG 11 REMARK 1 REF J.MOL.BIOL. V. 210 149 1989 2HBG 12 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 2HBG 13 REMARK 2 2HBG 14 REMARK 2 RESOLUTION. 1.5 ANGSTROMS. 2HBG 15 REMARK 3 2HBG 16 REMARK 3 REFINEMENT. BY THE RESTRAINED LEAST SQUARES PROCEDURE OF J. 2HBG 17 REMARK 3 KONNERT AND W. HENDRICKSON (PROGRAM *PROLSQ*). THE R 2HBG 18 REMARK 3 VALUE IS 0.127. THE RMS DEVIATION FROM IDEALITY OF THE 2HBG 19 REMARK 3 BOND LENGTHS IS 0.015 ANGSTROMS. THE RMS DEVIATION FROM 2HBG 20 REMARK 3 IDEALITY OF THE BOND ANGLE DISTANCES IS 0.04 ANGSTROMS. 2HBG 21 REMARK 3 THE RMS DEVIATION FROM IDEALITY OF THE PLANAR GROUPS IS 2HBG 22 REMARK 3 0.007 ANGSTROMS. AN OCCUPANCY OF 0.01 DENOTES AN ATOM 2HBG 23 REMARK 3 THAT WAS NOT OBSERVED IN THE ELECTRON DENSITY MAPS. 2HBG 24 REMARK 4 2HBG 25 REMARK 4 ERROR IN ATOMIC POSITIONS IS ESTIMATED TO BE 0.13 2HBG 26 REMARK 4 ANGSTROMS BY THE METHOD OF LUZZATI AND 0.11 ANGSTROMS BY 2HBG 27 REMARK 4 THE METHOD OF CRUICKSHANK. 2HBG 28 REMARK 5 2HBG 29 REMARK 5 THERE ARE A NUMBER OF SEQUENCE DIFFERENCES BETWEEN THE 2HBG 30 REMARK 5 SEQUENCE PRESENTED IN THIS ENTRY AND THAT IN PROTEIN 2HBG 31 REMARK 5 IDENTIFICATION RESOURCE (PIR) ENTRY GGNW1B WHICH IS BASED 2HBG 32 REMARK 5 ON THE SEQUENCE OF T.IMAMURA,T.O.BALDWIN,A.RIGGS, 2HBG 33 REMARK 5 J.BIOL.CHEM., V. 247, P. 2785 (1972). THE SUBSTITUTION OF 2HBG 34 REMARK 5 ALA FOR ASP AT RESIDUE 20 AND PHE FOR HIS AT RESIDUE 34 2HBG 35 REMARK 5 AGREE WITH THE PARTIAL SEQUENCE OF S.L.LI,A.F.RIGGS, 2HBG 36 REMARK 5 BIOCHIM.BIOPHYS.ACTA, V. 236, P. 208 (1971)). RESIDUE 29 2HBG 37 REMARK 5 IS ASP IN THE SEQUENCE OF IMAMURA ET AL. AND GLU IN THE 2HBG 38 REMARK 5 SEQUENCE OF LI AND RIGGS. RESIDUE 29 HAS BEEN MODELED AS 2HBG 39 REMARK 5 LYS IN THIS ENTRY DUE TO THE ABSENCE OF SIDE CHAIN 2HBG 40 REMARK 5 BRANCHING IN THE ELECTRON DENSITY MAP. RESIDUE 54 WAS 2HBG 41 REMARK 5 CHANGED FROM ALA TO GLY AND RESIDUE 100 WAS CHANGED FROM 2HBG 42 REMARK 5 GLY TO ALA; THE CORRESPONDING NEGATIVE AND POSITIVE 2HBG 43 REMARK 5 DIFFERENCE ELECTRON DENSITY PEAKS IMMEDIATELY DISAPPEARED. 2HBG 44 REMARK 5 THE SUBSTITUTION OF ALA FOR ASP AT RESIDUE 57 AGREES WELL 2HBG 45 REMARK 5 WITH THE X-RAY DATA BUT MAY NOT REPRESENT THE TRUTH. THE 2HBG 46 REMARK 5 SIDE-CHAIN OF RESIDUE 57 IS COMPLETELY EXPOSED TO THE 2HBG 47 REMARK 5 SOLVENT; THEREFORE IT IS POSSIBLE THAT THE CG AND OD ATOMS 2HBG 48 REMARK 5 ARE PRESENT BUT EXIST IN TOO MANY CONFORMATIONS IN THE 2HBG 49 REMARK 5 CRYSTAL FOR ANY CORRESPONDING ELECTRON DENSITY TO BE 2HBG 50 REMARK 5 VISIBLE. NEVERTHELESS, ALA WAS SUBSTITUTED AT RESIDUE 57 2HBG 51 REMARK 5 BECAUSE THERE IS NO ELECTRON DENSITY TO WHICH THE 2HBG 52 REMARK 5 ASPARTATE ATOMS COULD BE FITTED. 2HBG 53 REMARK 6 2HBG 54 REMARK 6 LEUCINE 31 SHOWS THREE POSSIBLE GAUCHE CONFORMATIONS OF 2HBG 55 REMARK 6 ATOMS CD1 AND CD2. THESE ARE PRESENTED AS THREE ALTERNATE 2HBG 56 REMARK 6 CONFORMATIONS. NOTE THAT ONLY THREE SETS OF COORDINATES 2HBG 57 REMARK 6 WERE USED TO MODEL THIS DISORDER AND, THEREFORE, THE SIX 2HBG 58 REMARK 6 ATOMS APPEAR AS THREE ATOMS IN A GRAPHICAL VIEW OF THE 2HBG 59 REMARK 6 ENTRY. 2HBG 60 SEQRES 1 147 GLY LEU SER ALA ALA GLN ARG GLN VAL ILE ALA ALA THR 2HBG 61 SEQRES 2 147 TRP LYS ASP ILE ALA GLY ALA ASP ASN GLY ALA GLY VAL 2HBG 62 SEQRES 3 147 GLY LYS LYS CYS LEU ILE LYS PHE LEU SER ALA HIS PRO 2HBG 63 SEQRES 4 147 GLN MET ALA ALA VAL PHE GLY PHE SER GLY ALA SER ASP 2HBG 64 SEQRES 5 147 PRO GLY VAL ALA ALA LEU GLY ALA LYS VAL LEU ALA GLN 2HBG 65 SEQRES 6 147 ILE GLY VAL ALA VAL SER HIS LEU GLY ASP GLU GLY LYS 2HBG 66 SEQRES 7 147 MET VAL ALA GLN MET LYS ALA VAL GLY VAL ARG HIS LYS 2HBG 67 SEQRES 8 147 GLY TYR GLY ASN LYS HIS ILE LYS ALA GLN TYR PHE GLU 2HBG 68 SEQRES 9 147 PRO LEU GLY ALA SER LEU LEU SER ALA MET GLU HIS ARG 2HBG 69 SEQRES 10 147 ILE GLY GLY LYS MET ASN ALA ALA ALA LYS ASP ALA TRP 2HBG 70 SEQRES 11 147 ALA ALA ALA TYR ALA ASP ILE SER GLY ALA LEU ILE SER 2HBG 71 SEQRES 12 147 GLY LEU GLN SER 2HBG 72 FTNOTE 1 2HBG 73 FTNOTE 1 SIX RESIDUES HAVE THEIR SIDE CHAINS MODELED IN MORE THAN 2HBG 74 FTNOTE 1 ONE CONFORMATION. THEY ARE LEU 31, LYS 84, ASN 95, 2HBG 75 FTNOTE 1 SER 109, SER 112, AND SER 143. 2HBG 76 HET HEM 148 43 PROTOPORPHYRIN IX 2HBG 77 FORMUL 2 HEM C34 H32 N4 O4 FE1 ++ 2HBG 78 FORMUL 3 HOH *146(H2 O1) 2HBG 79 HELIX 1 HA SER 3 ALA 18 1 2HBG 80 HELIX 2 HB GLY 23 ALA 37 1 2HBG 81 HELIX 3 HC PRO 39 GLY 46 1 IRREGULAR 2HBG 82 HELIX 4 HE PRO 53 HIS 72 1 2HBG 83 HELIX 5 HF GLU 76 GLY 92 1 89-92 DISTORTED 2HBG 84 HELIX 6 HG ALA 100 GLY 119 1 2HBG 85 HELIX 7 HH ALA 124 SER 147 1 2HBG 86 TURN 1 AB ASP 21 ALA 24 TYPE I' 2HBG 87 TURN 2 EF HIS 72 ASP 75 TYPE I 2HBG 88 CRYST1 42.750 83.150 38.660 90.00 90.00 90.00 P 21 21 21 4 2HBG 89 ORIGX1 1.000000 0.000000 0.000000 0.00000 2HBG 90 ORIGX2 0.000000 1.000000 0.000000 0.00000 2HBG 91 ORIGX3 0.000000 0.000000 1.000000 0.00000 2HBG 92 SCALE1 0.023392 0.000000 0.000000 0.00000 2HBG 93 SCALE2 0.000000 0.012026 0.000000 0.00000 2HBG 94 SCALE3 0.000000 0.000000 0.025867 0.00000 2HBG 95