HEADER HYDROLASE(ACTING IN CYCLIC AMIDES) 28-MAY-91 4BLM 4BLM 2 COMPND BETA-*LACTAMASE (E.C.3.5.2.6) (PENICILLINASE) 4BLM 3 SOURCE (BACILLUS $LICHENIFORMIS 749(SLASH)*C) 4BLM 4 AUTHOR J.R.KNOX,P.C.MOEWS 4BLM 5 REVDAT 2 15-OCT-94 4BLMA 1 REMARK 4BLMA 1 REVDAT 1 15-JAN-93 4BLM 0 4BLM 6 JRNL AUTH J.R.KNOX,P.C.MOEWS 4BLM 7 JRNL TITL BETA-*LACTAMASE OF BACILLUS LICHENIFORMIS 4BLM 8 JRNL TITL 2 749(SLASH)*C. REFINEMENT AT 2 ANGSTROMS RESOLUTION 4BLM 9 JRNL TITL 3 AND ANALYSIS OF HYDRATION 4BLM 10 JRNL REF J.MOL.BIOL. V. 220 435 1991 4BLM 11 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 4BLM 12 REMARK 1 4BLM 13 REMARK 1 REFERENCE 1 4BLM 14 REMARK 1 AUTH P.C.MOEWS,J.R.KNOX,O.DIDEBERG,P.CHARLIER, 4BLM 15 REMARK 1 AUTH 2 J.-*M.FRERE 4BLM 16 REMARK 1 TITL BETA-*LACTAMASE OF BACILLUS LICHENIFORMIS 4BLM 17 REMARK 1 TITL 2 749(SLASH)C AT 2 ANGSTROMS RESOLUTION 4BLM 18 REMARK 1 REF PROTEINS.STRUCT.,FUNCT., V. 7 156 1990 4BLM 19 REMARK 1 REF 2 GENET. 4BLM 20 REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 867 4BLM 21 REMARK 2 4BLM 22 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. 4BLM 23 REMARK 3 4BLM 24 REMARK 3 REFINEMENT. BY THE RESTRAINED LEAST-SQUARES PROCEDURE OF J. 4BLM 32 REMARK 3 KONNERT AND W. HENDRICKSON (PROGRAM *PROLSQ*). THE R 4BLM 33 REMARK 3 VALUE IS 0.151 FOR 27330 REFLECTIONS IN THE RESOLUTION 4BLM 34 REMARK 3 RANGE 10.0 TO 2.0 ANGSTROMS WITH FOBS .GT. 4BLM 35 REMARK 3 3.0 * SIGMA(FOBS). THE R VALUE IS 0.16 FOR 30090 4BLMA 2 REMARK 3 REFLECTIONS IN THE RESOLUTION RANGE 10.0 TO 2.0 ANGSTROMS 4BLMA 3 REMARK 3 FOBS. GT. 0.0 * SIMA(FOBS). 4BLMA 4 REMARK 3 4BLM 37 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 4BLM 38 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 4BLM 39 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 4BLM 40 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) 4BLM 41 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 4BLM 42 REMARK 3 BOND DISTANCE 0.012(0.014) 4BLM 43 REMARK 3 ANGLE DISTANCE 0.036(0.027) 4BLM 44 REMARK 3 PLANAR 1-4 DISTANCE 0.018(0.013) 4BLM 45 REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.21(0.13) 4BLM 46 REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 4BLM 47 REMARK 3 SINGLE TORSION CONTACT 0.17(0.35) 4BLM 48 REMARK 3 MULTIPLE TORSION CONTACT 0.23(0.35) 4BLM 49 REMARK 3 POSSIBLE HYDROGEN BOND 0.28(0.35) 4BLM 50 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) 4BLM 51 REMARK 3 PLANAR (OMEGA) 2.6(2.5) 4BLM 52 REMARK 3 STAGGERED 22.2(30.0) 4BLM 53 REMARK 3 ORTHONORMAL 22.7(30.0) 4BLM 54 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) 4BLM 55 REMARK 3 MAIN-CHAIN BOND 1.6(1.500) 4BLM 56 REMARK 3 MAIN-CHAIN ANGLE 2.3(2.000) 4BLM 57 REMARK 3 SIDE-CHAIN BOND 3.0(2.000) 4BLM 58 REMARK 3 SIDE-CHAIN ANGLE 4.6(3.000) 4BLM 59 REMARK 4 4BLM 60 REMARK 4 THE ASYMMETRIC UNIT CONTAINS TWO MOLECULES. THESE HAVE 4BLM 61 REMARK 4 BEEN IDENTIFIED AS MOLECULES 1 AND 4 BY THE DEPOSITORS AND 4BLM 62 REMARK 4 HAVE BEEN ASSIGNED CHAIN IDENTIFIERS *A* AND *B* IN THIS 4BLM 63 REMARK 4 ENTRY. THE TRANSFORMATION PRESENTED ON *MTRIX 1* RECORDS 4BLM 64 REMARK 4 BELOW WILL YIELD APPROXIMATE COORDINATES FOR MOLECULE 4 4BLM 65 REMARK 4 WHEN APPLIED TO MOLECULE 1. 4BLM 66 REMARK 5 4BLM 67 REMARK 5 THE CATALYTIC SITE IS CENTERED AROUND SER 70 AT THE 4BLM 68 REMARK 5 N-TERMINUS OF HELIX A2 AND IS PRESENTED ON *SITE* RECORDS 4BLM 69 REMARK 5 BELOW. STRAND 5 OF SHEET *S1* CONTAINS IMPORTANT RESIDUES 4BLM 70 REMARK 5 LYS 234 AND THR 235. INVARIANT GLUTAMIC ACID 166 IS 4BLM 71 REMARK 5 INVOLVED IN DEACYLATION (SEE ALSO THE E166A MUTANT 4BLM 72 REMARK 5 STRUCTURE PRESENTED IN PROTEIN DATA BANK ENTRY 1MBL). 4BLM 73 REMARK 6 4BLM 74 REMARK 6 RESIDUE NUMBERING IS BASED ON R.P.AMBLER ET AL. (BIOCHEM. 4BLM 75 REMARK 6 J., V. 276, P. 269, 1991). THEREFORE, THERE ARE NO 4BLM 76 REMARK 6 RESIDUES NUMBERED 58, 84, 85, 239, AND 253. 4BLM 77 REMARK 7 4BLM 78 REMARK 7 NO DENSITY WAS OBSERVED FOR THE FIRST FIVE RESIDUES AT THE 4BLM 79 REMARK 7 N-TERMINUS AND FOR THE LAST FOUR RESIDUES AT THE C-TEMRINUS 4BLM 80 REMARK 7 AND, THEREFORE, NO COORDINATES ARE PRESENT FOR THESE 4BLM 81 REMARK 7 RESIDUES IN THIS ENTRY. 4BLM 82 REMARK 8 4BLMA 5 REMARK 8 CORRECTION. REVISE REMARK 3. 15-OCT-94. 4BLMA 6 SEQRES 1 A 265 LYS THR GLU MET LYS ASP ASP PHE ALA LYS LEU GLU GLU 4BLM 83 SEQRES 2 A 265 GLN PHE ASP ALA LYS LEU GLY ILE PHE ALA LEU ASP THR 4BLM 84 SEQRES 3 A 265 GLY THR ASN ARG THR VAL ALA TYR ARG PRO ASP GLU ARG 4BLM 85 SEQRES 4 A 265 PHE ALA PHE ALA SER THR ILE LYS ALA LEU THR VAL GLY 4BLM 86 SEQRES 5 A 265 VAL LEU LEU GLN GLN LYS SER ILE GLU ASP LEU ASN GLN 4BLM 87 SEQRES 6 A 265 ARG ILE THR TYR THR ARG ASP ASP LEU VAL ASN TYR ASN 4BLM 88 SEQRES 7 A 265 PRO ILE THR GLU LYS HIS VAL ASP THR GLY MET THR LEU 4BLM 89 SEQRES 8 A 265 LYS GLU LEU ALA ASP ALA SER LEU ARG TYR SER ASP ASN 4BLM 90 SEQRES 9 A 265 ALA ALA GLN ASN LEU ILE LEU LYS GLN ILE GLY GLY PRO 4BLM 91 SEQRES 10 A 265 GLU SER LEU LYS LYS GLU LEU ARG LYS ILE GLY ASP GLU 4BLM 92 SEQRES 11 A 265 VAL THR ASN PRO GLU ARG PHE GLU PRO GLU LEU ASN GLU 4BLM 93 SEQRES 12 A 265 VAL ASN PRO GLY GLU THR GLN ASP THR SER THR ALA ARG 4BLM 94 SEQRES 13 A 265 ALA LEU VAL THR SER LEU ARG ALA PHE ALA LEU GLU ASP 4BLM 95 SEQRES 14 A 265 LYS LEU PRO SER GLU LYS ARG GLU LEU LEU ILE ASP TRP 4BLM 96 SEQRES 15 A 265 MET LYS ARG ASN THR THR GLY ASP ALA LEU ILE ARG ALA 4BLM 97 SEQRES 16 A 265 GLY VAL PRO ASP GLY TRP GLU VAL ALA ASP LYS THR GLY 4BLM 98 SEQRES 17 A 265 ALA ALA SER TYR GLY THR ARG ASN ASP ILE ALA ILE ILE 4BLM 99 SEQRES 18 A 265 TRP PRO PRO LYS GLY ASP PRO VAL VAL LEU ALA VAL LEU 4BLM 100 SEQRES 19 A 265 SER SER ARG ASP LYS LYS ASP ALA LYS TYR ASP ASP LYS 4BLM 101 SEQRES 20 A 265 LEU ILE ALA GLU ALA THR LYS VAL VAL MET LYS ALA LEU 4BLM 102 SEQRES 21 A 265 ASN MET ASN GLY LYS 4BLM 103 SEQRES 1 B 265 LYS THR GLU MET LYS ASP ASP PHE ALA LYS LEU GLU GLU 4BLM 104 SEQRES 2 B 265 GLN PHE ASP ALA LYS LEU GLY ILE PHE ALA LEU ASP THR 4BLM 105 SEQRES 3 B 265 GLY THR ASN ARG THR VAL ALA TYR ARG PRO ASP GLU ARG 4BLM 106 SEQRES 4 B 265 PHE ALA PHE ALA SER THR ILE LYS ALA LEU THR VAL GLY 4BLM 107 SEQRES 5 B 265 VAL LEU LEU GLN GLN LYS SER ILE GLU ASP LEU ASN GLN 4BLM 108 SEQRES 6 B 265 ARG ILE THR TYR THR ARG ASP ASP LEU VAL ASN TYR ASN 4BLM 109 SEQRES 7 B 265 PRO ILE THR GLU LYS HIS VAL ASP THR GLY MET THR LEU 4BLM 110 SEQRES 8 B 265 LYS GLU LEU ALA ASP ALA SER LEU ARG TYR SER ASP ASN 4BLM 111 SEQRES 9 B 265 ALA ALA GLN ASN LEU ILE LEU LYS GLN ILE GLY GLY PRO 4BLM 112 SEQRES 10 B 265 GLU SER LEU LYS LYS GLU LEU ARG LYS ILE GLY ASP GLU 4BLM 113 SEQRES 11 B 265 VAL THR ASN PRO GLU ARG PHE GLU PRO GLU LEU ASN GLU 4BLM 114 SEQRES 12 B 265 VAL ASN PRO GLY GLU THR GLN ASP THR SER THR ALA ARG 4BLM 115 SEQRES 13 B 265 ALA LEU VAL THR SER LEU ARG ALA PHE ALA LEU GLU ASP 4BLM 116 SEQRES 14 B 265 LYS LEU PRO SER GLU LYS ARG GLU LEU LEU ILE ASP TRP 4BLM 117 SEQRES 15 B 265 MET LYS ARG ASN THR THR GLY ASP ALA LEU ILE ARG ALA 4BLM 118 SEQRES 16 B 265 GLY VAL PRO ASP GLY TRP GLU VAL ALA ASP LYS THR GLY 4BLM 119 SEQRES 17 B 265 ALA ALA SER TYR GLY THR ARG ASN ASP ILE ALA ILE ILE 4BLM 120 SEQRES 18 B 265 TRP PRO PRO LYS GLY ASP PRO VAL VAL LEU ALA VAL LEU 4BLM 121 SEQRES 19 B 265 SER SER ARG ASP LYS LYS ASP ALA LYS TYR ASP ASP LYS 4BLM 122 SEQRES 20 B 265 LEU ILE ALA GLU ALA THR LYS VAL VAL MET LYS ALA LEU 4BLM 123 SEQRES 21 B 265 ASN MET ASN GLY LYS 4BLM 124 FTNOTE 1 4BLM 125 FTNOTE 1 RESIDUES PRO A 167 AND PRO B 167 ARE CIS PROLINES. 4BLM 126 HELIX 1 A1 ASP A 31 ASP A 41 1 4BLM 127 HELIX 2 A2 SER A 70 LYS A 86 1 4BLM 128 HELIX 3 A2S SER A 87 ASN A 92 1 SINGLE TURN ONLY 4BLM 129 HELIX 4 A3 ASN A 106 HIS A 112 1 4BLM 130 HELIX 5 A4 LYS A 120 TYR A 129 1 4BLM 131 HELIX 6 A5 ASP A 131 ILE A 142 1 4BLM 132 HELIX 7 A6 GLY A 144 LYS A 154 1 4BLM 133 HELIX 8 A7 GLU A 166 VAL A 172 1 4BLM 134 HELIX 9 A8 ARG A 184 GLU A 196 1 4BLM 135 HELIX 10 A9 SER A 201 LYS A 212 1 4BLM 136 HELIX 11 A10 ASP A 218 VAL A 225 1 4BLM 137 HELIX 12 A11 ASP A 276 ASN A 291 1 4BLM 138 HELIX 13 B1 ASP B 31 ASP B 41 1 4BLM 139 HELIX 14 B2 SER B 70 LYS B 86 1 4BLM 140 HELIX 15 B2S SER B 87 ASN B 92 1 SINGLE TURN ONLY 4BLM 141 HELIX 16 B3 ASN B 106 HIS B 112 1 4BLM 142 HELIX 17 B4 LYS B 120 TYR B 129 1 4BLM 143 HELIX 18 B5 ASP B 131 ILE B 142 1 4BLM 144 HELIX 19 B6 GLY B 144 LYS B 154 1 4BLM 145 HELIX 20 B7 GLU B 166 VAL B 172 1 4BLM 146 HELIX 21 B8 ARG B 184 GLU B 196 1 4BLM 147 HELIX 22 B9 SER B 201 LYS B 212 1 4BLM 148 HELIX 23 B10 ASP B 218 VAL B 225 1 4BLM 149 HELIX 24 B11 ASP B 276 ASN B 291 1 4BLM 150 SHEET 1 S1A 5 ASN A 54 TYR A 60 0 4BLM 151 SHEET 2 S1A 5 LYS A 43 THR A 51 -1 N ALA A 48 O VAL A 57 4BLM 152 SHEET 3 S1A 5 ASP A 257 ASP A 268 1 N ALA A 262 O PHE A 47 4BLM 153 SHEET 4 S1A 5 GLY A 242 PRO A 252 -1 N ALA A 248 O LEU A 261 4BLM 154 SHEET 5 S1A 5 TRP A 229 SER A 240 1 N LYS A 234 O ILE A 247 4BLM 155 SHEET 1 S2A 3 ASP A 63 PHE A 66 0 4BLM 156 SHEET 2 S2A 3 GLN A 178 ALA A 183 -1 N SER A 181 O PHE A 66 4BLM 157 SHEET 3 S2A 3 VAL A 159 GLU A 163 1 N ASN A 161 O THR A 180 4BLM 158 SHEET 1 S1B 5 ASN B 54 TYR B 60 0 4BLM 159 SHEET 2 S1B 5 LYS B 43 THR B 51 -1 N ALA B 48 O VAL B 57 4BLM 160 SHEET 3 S1B 5 ASP B 257 ASP B 268 1 N ALA B 262 O PHE B 47 4BLM 161 SHEET 4 S1B 5 GLY B 242 PRO B 252 -1 N ALA B 248 O LEU B 261 4BLM 162 SHEET 5 S1B 5 TRP B 229 SER B 240 1 N LYS B 234 O ILE B 247 4BLM 163 SHEET 1 S2B 3 ASP B 63 PHE B 66 0 4BLM 164 SHEET 2 S2B 3 GLN B 178 ALA B 183 -1 N SER B 181 O PHE B 66 4BLM 165 SHEET 3 S2B 3 VAL B 159 GLU B 163 1 N ASN B 161 O THR B 180 4BLM 166 SITE 1 CTA 6 SER A 70 LYS A 73 SER A 130 GLU A 166 4BLM 167 SITE 2 CTA 6 LYS A 234 THR A 235 4BLM 168 SITE 1 CTB 6 SER B 70 LYS B 73 SER B 130 GLU B 166 4BLM 169 SITE 2 CTB 6 LYS B 234 THR B 235 4BLM 170 CRYST1 66.800 90.700 43.600 90.00 104.50 90.00 P 21 4 4BLM 171 ORIGX1 1.000000 0.000000 0.000000 0.00000 4BLM 172 ORIGX2 0.000000 1.000000 0.000000 0.00000 4BLM 173 ORIGX3 0.000000 0.000000 1.000000 0.00000 4BLM 174 SCALE1 0.014970 0.000000 0.003872 0.00000 4BLM 175 SCALE2 0.000000 0.011025 0.000000 0.00000 4BLM 176 SCALE3 0.000000 0.000000 0.023690 0.00000 4BLM 177 MTRIX1 1 0.870800 0.001040 0.491640 17.66990 1 4BLM 178 MTRIX2 1 0.001100 -1.000000 0.000180 91.02260 1 4BLM 179 MTRIX3 1 0.491640 0.000390 -0.870800 26.83430 1 4BLM 180