HEADER LECTIN 17-NOV-93 1LEN 1LEN 2 COMPND LECTIN (LENTIL) (MONOCLINIC CRYSTAL FORM) 1LEN 3 SOURCE COMMON LENTIL (LENS CULINARIS) SEED 1LEN 4 AUTHOR D.VAN OVERBERGE,R.LORIS,L.WYNS 1LEN 5 REVDAT 1 31-JAN-94 1LEN 0 1LEN 6 JRNL AUTH R.LORIS,D.VAN OVERBERGE,M.-H.DAO-THI,F.POORTMANS, 1LEN 7 JRNL AUTH 2 N.MAENE,L.WYNS 1LEN 8 JRNL TITL REFINEMENT OF TWO CRYSTAL FORMS OF LENTIL LECTIN 1LEN 9 JRNL TITL 2 AT 1.8 ANGSTROMS RESOLUTION 1LEN 10 JRNL REF TO BE PUBLISHED 1LEN 11 JRNL REFN 353 1LEN 12 REMARK 1 1LEN 13 REMARK 1 REFERENCE 1 1LEN 14 REMARK 1 AUTH R.LORIS,J.STEYAERT,D.MAES,J.LISGARTEN, 1LEN 15 REMARK 1 AUTH 2 R.PICKERSGILL,L.WYNS 1LEN 16 REMARK 1 TITL CRYSTAL STRUCTURE DETERMINATION AND REFINEMENT AT 1LEN 17 REMARK 1 TITL 2 2.3 ANGSTROMS RESOLUTION OF THE LENTIL LECTIN 1LEN 18 REMARK 1 REF BIOCHEMISTRY V. 32 8772 1993 1LEN 19 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 1LEN 20 REMARK 1 REFERENCE 2 1LEN 21 REMARK 1 AUTH R.LORIS,J.LISGARTEN,D.MAES,R.PICKERSGILL,F.KORBER, 1LEN 22 REMARK 1 AUTH 2 C.REYNOLDS,L.WYNS 1LEN 23 REMARK 1 TITL TWO CRYSTAL FORMS OF THE LENTIL LECTIN DIFRACT TO 1LEN 24 REMARK 1 TITL 2 HIGH RESOLUTION 1LEN 25 REMARK 1 REF J.MOL.BIOL. V. 223 579 1992 1LEN 26 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1LEN 27 REMARK 2 1LEN 28 REMARK 2 RESOLUTION. 1.8 ANGSTROMS. 1LEN 29 REMARK 3 1LEN 30 REMARK 3 REFINEMENT. 1LEN 31 REMARK 3 PROGRAM RESTRAIN 1LEN 32 REMARK 3 AUTHORS MOSS,DRIESSEN,HANEEF,HOWLIN, 1LEN 33 REMARK 3 AUTHORS HARRIS 1LEN 34 REMARK 3 R VALUE 0.175 1LEN 35 REMARK 3 RMSD BOND DISTANCES 0.018 ANGSTROMS 1LEN 36 REMARK 3 RMSD BOND ANGLES 7.00 DEGREES 1LEN 37 REMARK 3 RMSD PEPTIDE BOND PLANARITY 3.0 DEG 1LEN 38 REMARK 4 1LEN 39 REMARK 4 THE LENTIL LECTIN MOLECULE NORMALLY EXISTS AS A DIMER. THE 1LEN 40 REMARK 4 TWO MONOMERS IN THIS ENTRY ARE RELATED BY A PSEUDO TWOFOLD 1LEN 41 REMARK 4 AXIS. EACH MONOMER CONSISTS OF TWO SEPARATE POLYPEPTIDE 1LEN 42 REMARK 4 CHAINS, ALPHA AND BETA. THE ALPHA CHAIN CONSISTS OF 181 1LEN 43 REMARK 4 RESIDUES AND THE BETA CHAIN CONSISTS OF 52 RESIDUES. BOTH 1LEN 44 REMARK 4 MONOMERS ARE RELATED BY A NON-CRYSTALLOGRAPHIC 1LEN 45 REMARK 4 2-FOLD AXIS PARALLEL TO THE CRYSTALLOGRAPHIC B-AXIS. THE 1LEN 46 REMARK 4 RMS BETWEEN THE BACKBONE COORDINATES IS 0.17 A. THE 1LEN 47 REMARK 4 ALPHA AND BETA CHAINS OF MONOMER 1 HAVE BEEN ASSIGNED CHAIN 1LEN 48 REMARK 4 IDENTIFIERS *A* AND *B*, RESPECTIVELY, IN THIS ENTRY. THE 1LEN 49 REMARK 4 ALPHA AND BETA CHAINS OF MONOMER 2 HAVE BEEN ASSIGNED CHAIN 1LEN 50 REMARK 4 IDENTIFIERS *C* AND *D*, RESPECTIVELY, IN THIS ENTRY. THIS 1LEN 51 REMARK 4 NUMBERING SCHEME IS THE SAME AS THAT USED FOR PEA LECTIN 1LEN 52 REMARK 4 BY EINSPAHR ET AL. (ENTRY 2LTN) 1LEN 53 REMARK 5 1LEN 54 REMARK 5 NO DENSITY WAS OBSERVED FOR RESIDUES 48 - 52 IN CHAINS B 1LEN 55 REMARK 5 AND D AND, THEREFORE, NO COORDINATES ARE PRESENT IN THIS 1LEN 56 REMARK 5 ENTRY FOR THESE RESIDUES. 1LEN 57 REMARK 6 1LEN 58 REMARK 6 EACH MONOMER HAS A BOUND CALCIUM, MANGANESE AMD PHOSPHATE 1LEN 59 REMARK 6 ION. THE CALCIUM AND MANGANESE IONS ARE ESSENTIAL FOR 1LEN 60 REMARK 6 STABILIZING AN UNUSUAL ALA-ASP CIS PEPTIDE BOND, THAT IS 1LEN 61 REMARK 6 AN ESSENTIAL FEATURE OF THE CARBOHYDRATE RECOGNITION SITE 1LEN 62 REMARK 6 OF THIS LECTIN. THE PHOSPHATE IS BOUND IN THE CARBOHYDRATE 1LEN 63 REMARK 6 RECOGNITION SITE. 1LEN 64 REMARK 7 1LEN 65 REMARK 7 A POSSIBLE SECOND CONFORMATION FOR RESIDUES SER A 5, 1LEN 66 REMARK 7 VAL A 37,TYR A 77, GLN B 35, TYR C 77, ASP C 91, AND 1LEN 67 REMARK 7 GLN D 35 IS GIVEN IN THIS ENTRY. 1LEN 68 SEQRES 1 A 181 THR GLU THR THR SER PHE SER ILE THR LYS PHE SER PRO 1LEN 69 SEQRES 2 A 181 ASP GLN GLN ASN LEU ILE PHE GLN GLY ASP GLY TYR THR 1LEN 70 SEQRES 3 A 181 THR LYS GLY LYS LEU THR LEU THR LYS ALA VAL LYS SER 1LEN 71 SEQRES 4 A 181 THR VAL GLY ARG ALA LEU TYR SER THR PRO ILE HIS ILE 1LEN 72 SEQRES 5 A 181 TRP ASP ARG ASP THR GLY ASN VAL ALA ASN PHE VAL THR 1LEN 73 SEQRES 6 A 181 SER PHE THR PHE VAL ILE ASP ALA PRO SER SER TYR ASN 1LEN 74 SEQRES 7 A 181 VAL ALA ASP GLY PHE THR PHE PHE ILE ALA PRO VAL ASP 1LEN 75 SEQRES 8 A 181 THR LYS PRO GLN THR GLY GLY GLY TYR LEU GLY VAL PHE 1LEN 76 SEQRES 9 A 181 ASN SER LYS GLU TYR ASP LYS THR SER GLN THR VAL ALA 1LEN 77 SEQRES 10 A 181 VAL GLU PHE ASP THR PHE TYR ASN ALA ALA TRP ASP PRO 1LEN 78 SEQRES 11 A 181 SER ASN LYS GLU ARG HIS ILE GLY ILE ASP VAL ASN SER 1LEN 79 SEQRES 12 A 181 ILE LYS SER VAL ASN THR LYS SER TRP ASN LEU GLN ASN 1LEN 80 SEQRES 13 A 181 GLY GLU ARG ALA ASN VAL VAL ILE ALA PHE ASN ALA ALA 1LEN 81 SEQRES 14 A 181 THR ASN VAL LEU THR VAL THR LEU THR TYR PRO ASN 1LEN 82 SEQRES 1 B 52 VAL THR SER TYR THR LEU ASN GLU VAL VAL PRO LEU LYS 1LEN 83 SEQRES 2 B 52 ASP VAL VAL PRO GLU TRP VAL ARG ILE GLY PHE SER ALA 1LEN 84 SEQRES 3 B 52 THR THR GLY ALA GLU PHE ALA ALA GLN GLU VAL HIS SER 1LEN 85 SEQRES 4 B 52 TRP SER PHE ASN SER GLN LEU GLY HIS THR SER LYS SER 1LEN 86 SEQRES 1 C 181 THR GLU THR THR SER PHE SER ILE THR LYS PHE SER PRO 1LEN 87 SEQRES 2 C 181 ASP GLN GLN ASN LEU ILE PHE GLN GLY ASP GLY TYR THR 1LEN 88 SEQRES 3 C 181 THR LYS GLY LYS LEU THR LEU THR LYS ALA VAL LYS SER 1LEN 89 SEQRES 4 C 181 THR VAL GLY ARG ALA LEU TYR SER THR PRO ILE HIS ILE 1LEN 90 SEQRES 5 C 181 TRP ASP ARG ASP THR GLY ASN VAL ALA ASN PHE VAL THR 1LEN 91 SEQRES 6 C 181 SER PHE THR PHE VAL ILE ASP ALA PRO SER SER TYR ASN 1LEN 92 SEQRES 7 C 181 VAL ALA ASP GLY PHE THR PHE PHE ILE ALA PRO VAL ASP 1LEN 93 SEQRES 8 C 181 THR LYS PRO GLN THR GLY GLY GLY TYR LEU GLY VAL PHE 1LEN 94 SEQRES 9 C 181 ASN SER LYS GLU TYR ASP LYS THR SER GLN THR VAL ALA 1LEN 95 SEQRES 10 C 181 VAL GLU PHE ASP THR PHE TYR ASN ALA ALA TRP ASP PRO 1LEN 96 SEQRES 11 C 181 SER ASN LYS GLU ARG HIS ILE GLY ILE ASP VAL ASN SER 1LEN 97 SEQRES 12 C 181 ILE LYS SER VAL ASN THR LYS SER TRP ASN LEU GLN ASN 1LEN 98 SEQRES 13 C 181 GLY GLU ARG ALA ASN VAL VAL ILE ALA PHE ASN ALA ALA 1LEN 99 SEQRES 14 C 181 THR ASN VAL LEU THR VAL THR LEU THR TYR PRO ASN 1LEN 100 SEQRES 1 D 52 VAL THR SER TYR THR LEU ASN GLU VAL VAL PRO LEU LYS 1LEN 101 SEQRES 2 D 52 ASP VAL VAL PRO GLU TRP VAL ARG ILE GLY PHE SER ALA 1LEN 102 SEQRES 3 D 52 THR THR GLY ALA GLU PHE ALA ALA GLN GLU VAL HIS SER 1LEN 103 SEQRES 4 D 52 TRP SER PHE ASN SER GLN LEU GLY HIS THR SER LYS SER 1LEN 104 FTNOTE 1 1LEN 105 FTNOTE 1 ALA A 80 - ASP A 81 OMEGA =356.62 1LEN 106 FTNOTE 1 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1LEN 107 FTNOTE 2 1LEN 108 FTNOTE 2 ALA C 80 - ASP C 81 OMEGA =358.29 1LEN 109 FTNOTE 2 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1LEN 110 HET PO4 1 5 PHOSPHATE GROUP 1LEN 111 HET PO4 2 5 PHOSPHATE GROUP 1LEN 112 HET MN 1 1 MANGANESE ++ 1LEN 113 HET MN 2 1 MANGANESE ++ 1LEN 114 HET CA 3 1 CALCIUM +2 COUNTER ION 1LEN 115 HET CA 4 1 CALCIUM +2 COUNTER ION 1LEN 116 FORMUL 5 PO4 2(O4 P1) 1LEN 117 FORMUL 6 MN 2(MN1 ++) 1LEN 118 FORMUL 7 CA 2(CA1) 1LEN 119 FORMUL 8 HOH *231(H2 O1) 1LEN 120 HELIX 1 HA1 GLY A 99 LEU A 101 5 1LEN 121 HELIX 2 HB1 PRO B 11 ASP B 14 1 1LEN 122 HELIX 3 HC1 GLY C 99 LEU C 101 5 1LEN 123 HELIX 4 HD2 PRO D 11 ASP D 14 1 1LEN 124 SHEET 1 AS1 6 THR B 2 GLU B 8 0 1LEN 125 SHEET 2 AS1 6 LEU A 173 TYR A 179 -1 O TYR A 179 N THR B 2 1LEN 126 SHEET 3 AS1 6 GLU A 158 PHE A 166 -1 N ASN A 161 O THR A 178 1LEN 127 SHEET 4 AS1 6 ASN A 62 PHE A 69 -1 N PHE A 69 O ALA A 160 1LEN 128 SHEET 5 AS1 6 SER B 39 LEU B 46 -1 N SER B 39 O THR A 68 1LEN 129 SHEET 6 AS1 6 GLU A 2 ILE A 8 -1 N GLU A 2 O LEU B 46 1LEN 130 SHEET 1 AS2 7 LEU A 18 ASP A 23 0 1LEN 131 SHEET 2 AS2 7 VAL A 41 TYR A 46 -1 O VAL A 41 N ASP A 23 1LEN 132 SHEET 3 AS2 7 ILE B 22 THR B 27 -1 O ALA B 26 N GLY A 42 1LEN 133 SHEET 4 AS2 7 GLY A 82 ILE A 87 -1 N GLY A 82 O THR B 27 1LEN 134 SHEET 5 AS2 7 VAL A 116 ASP A 121 -1 O PHE A 120 N PHE A 83 1LEN 135 SHEET 6 AS2 7 HIS A 136 VAL A 141 -1 N HIS A 136 O ASP A 121 1LEN 136 SHEET 7 AS2 7 SER A 146 SER A 151 -1 O LYS A 150 N ILE A 137 1LEN 137 SHEET 1 BS1 6 THR D 2 GLU D 8 0 1LEN 138 SHEET 2 BS1 6 LEU C 173 TYR C 179 -1 O TYR C 179 N THR D 2 1LEN 139 SHEET 3 BS1 6 GLU C 158 PHE C 166 -1 N ASN C 161 O THR C 178 1LEN 140 SHEET 4 BS1 6 ASN C 62 PHE C 69 -1 N PHE C 69 O ALA C 160 1LEN 141 SHEET 5 BS1 6 SER D 39 LEU D 46 -1 N SER D 39 O THR C 68 1LEN 142 SHEET 6 BS1 6 GLU C 2 ILE C 8 -1 N GLU C 2 O LEU D 46 1LEN 143 SHEET 1 BS2 7 LEU C 18 ASP C 23 0 1LEN 144 SHEET 2 BS2 7 VAL C 41 TYR C 46 -1 O VAL C 41 N ASP C 23 1LEN 145 SHEET 3 BS2 7 ILE D 22 THR D 27 -1 O ALA D 26 N GLY C 42 1LEN 146 SHEET 4 BS2 7 GLY C 82 ILE C 87 -1 N GLY C 82 O THR D 27 1LEN 147 SHEET 5 BS2 7 VAL C 116 ASP C 121 -1 O PHE C 120 N PHE C 83 1LEN 148 SHEET 6 BS2 7 HIS C 136 VAL C 141 -1 N HIS C 136 O ASP C 121 1LEN 149 SHEET 7 BS2 7 SER C 146 SER C 151 -1 O LYS C 150 N ILE C 137 1LEN 150 TURN 1 A1 SER A 12 GLN A 15 1LEN 151 TURN 2 A2 GLN A 15 LEU A 18 1LEN 152 TURN 3 A3 GLN A 21 GLY A 24 1LEN 153 TURN 4 A4 THR A 27 LYS A 30 1LEN 154 TURN 5 A5 ASP A 54 THR A 57 1LEN 155 TURN 6 A6 SER A 75 ASN A 78 1LEN 156 TURN 7 A7 PRO A 89 THR A 92 1LEN 157 TURN 8 A8 LEU A 101 PHE A 104 1LEN 158 TURN 9 A9 ASP A 110 SER A 113 1LEN 159 TURN 10 A10 ASN A 125 TRP A 128 1LEN 160 TURN 11 A11 PRO A 130 LYS A 133 1LEN 161 TURN 12 A12 GLN A 155 GLU A 158 1LEN 162 TURN 13 A13 ASN A 167 THR A 170 1LEN 163 TURN 14 B1 SER C 12 GLN C 15 1LEN 164 TURN 15 B2 GLN C 15 LEU C 18 1LEN 165 TURN 16 B3 GLN C 21 GLY C 24 1LEN 166 TURN 17 B4 THR C 27 LYS C 30 1LEN 167 TURN 18 B5 ASP C 54 THR C 57 1LEN 168 TURN 19 B6 SER C 75 ASN C 78 1LEN 169 TURN 20 B7 PRO C 89 THR C 92 1LEN 170 TURN 21 B8 LEU C 101 PHE C 104 1LEN 171 TURN 22 B9 ASP C 110 SER C 113 1LEN 172 TURN 23 B10 ASN C 125 TRP C 128 1LEN 173 TURN 24 B11 PRO C 130 LYS C 133 1LEN 174 TURN 25 B12 GLN C 155 GLU C 158 1LEN 175 TURN 26 B13 ASN C 167 THR C 170 1LEN 176 SITE 1 MN1 4 GLU A 119 ASP A 121 ASP A 129 HIS A 136 1LEN 177 SITE 1 CA1 4 ASP A 121 PHE A 123 ASN A 125 ASP A 129 1LEN 178 SITE 1 MN2 4 GLU C 119 ASP C 121 ASP C 129 HIS C 136 1LEN 179 SITE 1 CA2 4 ASP C 121 PHE C 123 ASN C 125 ASP C 129 1LEN 180 SITE 1 PO1 3 ASP A 81 GLY A 99 ASN A 125 1LEN 181 SITE 1 PO2 3 ASP C 81 GLY C 99 ASN C 125 1LEN 182 CRYST1 58.490 56.370 82.730 90.00 104.40 90.00 P 21 4 1LEN 183 ORIGX1 1.000000 0.000000 0.000000 0.00000 1LEN 184 ORIGX2 0.000000 1.000000 0.000000 0.00000 1LEN 185 ORIGX3 0.000000 0.000000 1.000000 0.00000 1LEN 186 SCALE1 0.017097 0.000000 0.004390 0.00000 1LEN 187 SCALE2 0.000000 0.017740 0.000000 0.00000 1LEN 188 SCALE3 0.000000 0.000000 0.012480 0.00000 1LEN 189