HEADER OXYGEN TRANSPORT 29-SEP-94 2HHD 2HHD 2 COMPND HEMOGLOBIN (DEOXY) (HBA) 2HHD 3 SOURCE HUMAN (HOMO SAPIENS) PLASMA 2HHD 4 AUTHOR G.L.GILLILAND,I.PECHIK,C.FRONTICELLI,X.JI 2HHD 5 REVDAT 1 26-JAN-95 2HHD 0 2HHD 6 JRNL AUTH C.FRONTICELLI,I.PECHIK,W.S.BRINIGAR,Z.GRYCZYNSKI, 2HHD 7 JRNL AUTH 2 G.L.GILLILAND 2HHD 8 JRNL TITL OXYGEN AFFINITY MODULATION BY THE N-TERMINI OF 2HHD 9 JRNL TITL 2 THE BETA- CHAINS IN HUMAN AND BOVINE HEMOGLOBIN 2HHD 10 JRNL REF TO BE PUBLISHED 2HHD 11 JRNL REFN ASTM 0353 2HHD 12 REMARK 1 2HHD 13 REMARK 2 2HHD 14 REMARK 2 RESOLUTION. 2.2 ANGSTROMS. 2HHD 15 REMARK 3 2HHD 16 REMARK 3 REFINEMENT. 2HHD 17 REMARK 3 PROGRAM PROLSQ 2HHD 18 REMARK 3 AUTHORS KONNERT,HENDRICKSON 2HHD 19 REMARK 3 R VALUE 0.137 2HHD 20 REMARK 3 MEAN B VALUE 16.05 ANGSTROMS**2 2HHD 21 REMARK 3 NUMBER OF REFLECTIONS 21076 2HHD 22 REMARK 3 RESOLUTION RANGE 6.0 - 2.2 ANGSTROMS 2HHD 23 REMARK 3 DATA CUTOFF 2. SIGMA(F) 2HHD 24 REMARK 3 2HHD 25 REMARK 3 DATA COLLECTION. 2HHD 26 REMARK 3 NUMBER OF UNIQUE REFLECTIONS 27357 2HHD 27 REMARK 3 COMPLETENESS OF DATA 93. % 2HHD 28 REMARK 3 2HHD 29 REMARK 3 SOLVENT CONTENT (VS) 39.0 % 2HHD 30 REMARK 3 2HHD 31 REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 2HHD 32 REMARK 3 NUMBER OF PROTEIN ATOMS 4384 2HHD 33 REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 2HHD 34 REMARK 3 NUMBER OF HETEROGEN ATOMS 172 2HHD 35 REMARK 3 NUMBER OF SOLVENT ATOMS 474 2HHD 36 REMARK 3 2HHD 37 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 2HHD 38 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 2HHD 39 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 2HHD 40 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS). 2HHD 41 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS). 2HHD 42 REMARK 3 BOND DISTANCE 0.016(0.020) 2HHD 43 REMARK 3 ANGLE DISTANCE 0.038(0.036) 2HHD 44 REMARK 3 PLANAR 1-4 DISTANCE 0.038(0.040) 2HHD 45 REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.023(0.030) 2HHD 46 REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.190(0.200) 2HHD 47 REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS). 2HHD 48 REMARK 3 SINGLE TORSION CONTACT 0.195(0.300) 2HHD 49 REMARK 3 MULTIPLE TORSION CONTACT 0.207(0.300) 2HHD 50 REMARK 3 POSSIBLE HYDROGEN BOND 0.175(0.300) 2HHD 51 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES). 2HHD 52 REMARK 3 PLANAR 3.5(5.0) 2HHD 53 REMARK 3 STAGGERED 18.5(15.0) 2HHD 54 REMARK 3 ORTHONORMAL 32.0(15.0) 2HHD 55 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2). 2HHD 56 REMARK 3 MAIN-CHAIN BOND 0.787(1.000) 2HHD 57 REMARK 3 MAIN-CHAIN ANGLE 1.310(1.500) 2HHD 58 REMARK 3 SIDE-CHAIN BOND 1.398(1.500) 2HHD 59 REMARK 3 SIDE-CHAIN ANGLE 2.193(2.000) 2HHD 60 REMARK 4 2HHD 61 REMARK 4 COMPND 2HHD 62 REMARK 5 ALPHA-BETA-ALPHA-BETA TETRAMER. 2HHD 63 REMARK 5 2HHD 64 REMARK 5 SOURCE 2HHD 65 REMARK 5 PURIFIED FROM OUTDATED BLOOD OBTAINED FROM THE BLOOD 2HHD 66 REMARK 5 BANK OF THE UNIVERSITY OF MARYLAND. 2HHD 67 REMARK 6 2HHD 68 REMARK 6 CROSS REFERENCE TO SEQUENCE DATABASE 2HHD 69 REMARK 6 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 2HHD 70 REMARK 6 HBA_HUMAN A 2HHD 71 REMARK 6 HBA_HUMAN C 2HHD 72 REMARK 6 2HHD 73 REMARK 6 CROSS REFERENCE TO SEQUENCE DATABASE 2HHD 74 REMARK 6 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 2HHD 75 REMARK 6 HBB_HUMAN B 2HHD 76 REMARK 6 HBB_HUMAN D 2HHD 77 SEQRES 1 A 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA 2HHD 78 SEQRES 2 A 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA 2HHD 79 SEQRES 3 A 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR 2HHD 80 SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER 2HHD 81 SEQRES 5 A 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA 2HHD 82 SEQRES 6 A 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN 2HHD 83 SEQRES 7 A 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU 2HHD 84 SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS 2HHD 85 SEQRES 9 A 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE 2HHD 86 SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA 2HHD 87 SEQRES 11 A 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG 2HHD 88 SEQRES 1 B 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA 2HHD 89 SEQRES 2 B 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU 2HHD 90 SEQRES 3 B 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN 2HHD 91 SEQRES 4 B 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP 2HHD 92 SEQRES 5 B 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS 2HHD 93 SEQRES 6 B 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU 2HHD 94 SEQRES 7 B 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU 2HHD 95 SEQRES 8 B 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG 2HHD 96 SEQRES 9 B 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS 2HHD 97 SEQRES 10 B 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR 2HHD 98 SEQRES 11 B 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS 2HHD 99 SEQRES 12 B 146 LYS TYR HIS 2HHD 100 SEQRES 1 C 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA 2HHD 101 SEQRES 2 C 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA 2HHD 102 SEQRES 3 C 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR 2HHD 103 SEQRES 4 C 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER 2HHD 104 SEQRES 5 C 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA 2HHD 105 SEQRES 6 C 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN 2HHD 106 SEQRES 7 C 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU 2HHD 107 SEQRES 8 C 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS 2HHD 108 SEQRES 9 C 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE 2HHD 109 SEQRES 10 C 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA 2HHD 110 SEQRES 11 C 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG 2HHD 111 SEQRES 1 D 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA 2HHD 112 SEQRES 2 D 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU 2HHD 113 SEQRES 3 D 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN 2HHD 114 SEQRES 4 D 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP 2HHD 115 SEQRES 5 D 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS 2HHD 116 SEQRES 6 D 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU 2HHD 117 SEQRES 7 D 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU 2HHD 118 SEQRES 8 D 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG 2HHD 119 SEQRES 9 D 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS 2HHD 120 SEQRES 10 D 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR 2HHD 121 SEQRES 11 D 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS 2HHD 122 SEQRES 12 D 146 LYS TYR HIS 2HHD 123 HET HEM A 142 43 PROTOPORPHYRIN IX CONTAINS FE(II) 2HHD 124 HET HEM B 147 43 PROTOPORPHYRIN IX CONTAINS FE(II) 2HHD 125 HET HEM C 142 43 PROTOPORPHYRIN IX CONTAINS FE(II) 2HHD 126 HET HEM D 147 43 PROTOPORPHYRIN IX CONTAINS FE(II) 2HHD 127 HET SO4 1 5 SULFATE 2HHD 128 HET SO4 2 5 SULFATE 2HHD 129 FORMUL 5 HEM 4(C34 H32 N4 O4 FE1 ++) 2HHD 130 FORMUL 6 SO4 2(O4 S1 --) 2HHD 131 FORMUL 7 HOH *474(H2 O1) 2HHD 132 CRYST1 62.450 82.130 53.760 90.00 98.87 90.00 P 21 4 2HHD 133 ORIGX1 1.000000 0.000000 0.000000 0.00000 2HHD 134 ORIGX2 0.000000 1.000000 0.000000 0.00000 2HHD 135 ORIGX3 0.000000 0.000000 1.000000 0.00000 2HHD 136 SCALE1 0.016013 0.000000 0.002499 0.00000 2HHD 137 SCALE2 0.000000 0.012176 0.000000 0.00000 2HHD 138 SCALE3 0.000000 0.000000 0.018826 0.00000 2HHD 139