HEADER ELECTRON TRANSPORT PROTEIN(CUPROPROTEIN)14-OCT-86 2AZA 2AZA 3 COMPND AZURIN (OXIDIZED) 2AZA 4 SOURCE (ALCALIGENES $DENITRIFICANS, STRAIN /NCTC$ 8582) 2AZA 5 AUTHOR E.N.BAKER,G.E.NORRIS 2AZA 6 REVDAT 4 15-JAN-90 2AZAC 1 SHEET 2AZAC 1 REVDAT 3 09-JAN-89 2AZAB 1 JRNL 2AZAB 1 REVDAT 2 06-MAR-87 2AZAA 3 ATOM HETATM TER 2AZAA 1 REVDAT 1 15-JAN-87 2AZA 0 2AZA 7 SPRSDE 15-JAN-87 2AZA 1AZA 2AZA 8 JRNL AUTH E.N.BAKER 2AZAB 2 JRNL TITL STRUCTURE OF AZURIN FROM ALCALIGENES 2AZAB 3 JRNL TITL 2 $DENITRIFICANS. REFINEMENT AT 1.8 ANGSTROMS 2AZAB 4 JRNL TITL 3 RESOLUTION AND COMPARISON OF THE TWO 2AZAB 5 JRNL TITL 4 CRYSTALLOGRAPHICALLY INDEPENDENT MOLECULES 2AZAB 6 JRNL REF J.MOL.BIOL. V. 203 1071 1988 2AZAB 7 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 2AZAB 8 REMARK 1 2AZA 9 REMARK 1 REFERENCE 1 2AZA 10 REMARK 1 AUTH G.E.NORRIS,B.F.ANDERSON,E.N.BAKER 2AZA 11 REMARK 1 TITL BLUE COPPER PROTEINS. THE COPPER SITE IN AZURIN 2AZA 12 REMARK 1 TITL 2 FROM ALCALIGENES $DENITRIFICANS 2AZA 13 REMARK 1 REF J.AM.CHEM.SOC. V. 108 2784 1986 2AZA 14 REMARK 1 REFN ASTM JACSAT US ISSN 0002-7863 004 2AZA 15 REMARK 1 REFERENCE 2 2AZA 16 REMARK 1 AUTH G.E.NORRIS,B.F.ANDERSON,E.N.BAKER 2AZA 17 REMARK 1 TITL STRUCTURE OF AZURIN FROM ALCALIGENES 2AZA 18 REMARK 1 TITL 2 $DENITRIFICANS AT 2.5 ANGSTROMS RESOLUTION 2AZA 19 REMARK 1 REF J.MOL.BIOL. V. 165 501 1983 2AZA 20 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 2AZA 21 REMARK 1 REFERENCE 3 2AZA 22 REMARK 1 AUTH G.E.NORRIS,B.F.ANDERSON,E.N.BAKER,S.V.RUMBALL 2AZA 23 REMARK 1 TITL PURIFICATION AND PRELIMINARY CRYSTALLOGRAPHIC 2AZA 24 REMARK 1 TITL 2 STUDIES ON AZURIN AND CYTOCHROME $C(PRIME) FROM 2AZA 25 REMARK 1 TITL 3 ALCALIGENES $DENITRIFICANS AND ALCALIGENES $SP. 2AZA 26 REMARK 1 TITL 4 /NCIB$ 11015 2AZA 27 REMARK 1 REF J.MOL.BIOL. V. 135 309 1979 2AZA 28 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 2AZA 29 REMARK 1 REFERENCE 4 2AZA 30 REMARK 1 AUTH R.P.AMBLER 2AZA 31 REMARK 1 EDIT A.PREVIERO,J.-*F.PECHERE,C.PREVIERO 2AZA 32 REMARK 1 REF RECENT DEVELOPMENTS IN THE 289 1971 2AZA 33 REMARK 1 REF 2 CHEMICAL STUDY OF PROTEIN 2AZA 34 REMARK 1 REF 3 STRUCTURES 2AZA 35 REMARK 1 PUBL INSERM, PARIS 2AZA 36 REMARK 1 REFN 985 2AZA 37 REMARK 2 2AZA 38 REMARK 2 RESOLUTION. 1.8 ANGSTROMS. 2AZA 39 REMARK 3 2AZA 40 REMARK 3 REFINEMENT. BY THE RESTRAINED LEAST SQUARES PROCEDURE OF 2AZA 41 REMARK 3 J. KONNERT AND W. HENDRICKSON (PROGRAM *PROLSQ*) AND BY 2AZA 42 REMARK 3 USE OF PROGRAM *TNT* OF D. TRONRUD AND L. TEN EYCK. 2AZA 43 REMARK 3 THE R-VALUE IS 0.157 FOR ALL DATA (21980 REFLECTIONS 2AZA 44 REMARK 3 WITH NO SIGMA CUTOFF). THE RMS DEVIATION FROM IDEALITY OF 2AZA 45 REMARK 3 THE BOND LENGTHS IS 0.016 ANGSTROMS. THE RMS DEVIATION 2AZA 46 REMARK 3 FROM IDEALITY OF THE BOND ANGLES IS 2.9 DEGREES. 2AZA 47 REMARK 4 2AZA 48 REMARK 4 THE CRYSTAL CONTAINS TWO MOLECULES PER ASYMMETRIC UNIT. 2AZA 49 REMARK 4 MOLECULE 1 (CHAIN INDICATOR *A*) CONSISTS OF 129 RESIDUES, 2AZA 50 REMARK 4 ONE COPPER ATOM, TWO SULFATE IONS, AND 141 WATER 2AZA 51 REMARK 4 MOLECULES. MOLECULE 2 (CHAIN INDICATOR *B*) CONSISTS OF 2AZA 52 REMARK 4 129 RESIDUES, ONE COPPER ATOM, ONE SULFATE ION, AND 140 2AZA 53 REMARK 4 WATER MOLECULES. 2AZA 54 REMARK 5 2AZA 55 REMARK 5 RESIDUE 42 IS INCLUDED HERE AS SER BOTH IN THE *ATOM* AND 2AZA 56 REMARK 5 *SEQRES* RECORDS. RESIDUE 42 IS ALA IN THE CHEMICALLY 2AZA 57 REMARK 5 DETERMINED SEQUENCE. RESIDUE 43 IS INCLUDED HERE AS ALA 2AZA 58 REMARK 5 IN BOTH THE *ATOM* AND *SEQRES* RECORDS. RESIDUE 43 IS 2AZA 59 REMARK 5 VAL IN THE CHEMICALLY DETERMINED SEQUENCE. 2AZA 60 REMARK 6 2AZA 61 REMARK 6 DISORDERED SIDE CHAIN CONFIGURATIONS HAVE BEEN IDENTIFIED 2AZA 62 REMARK 6 FOR RESIDUES GLN A 28, SER A 42, LYS A 85, LYS A 122, 2AZA 63 REMARK 6 GLN B 28, LYS B 85. 2AZA 64 REMARK 7 2AZA 65 REMARK 7 THE SOLVENT MOLECULES (ALL TAKEN AS WATER) ARE DIVIDED 2AZA 66 REMARK 7 INTO TWO GROUPS. THOSE PRINCIPALLY ASSOCIATED WITH 2AZA 67 REMARK 7 MOLECULE 1 FOLLOW THE COORDINATES FOR MOLECULE 1 (CHAIN 2AZA 68 REMARK 7 *A*) AND ARE NUMBERED FROM 137 TO 277. THOSE ASSOCIATED 2AZA 69 REMARK 7 WITH MOLECULE 2 FOLLOW THE COORDINATES FOR MOLECULE 2 2AZA 70 REMARK 7 (CHAIN *B*) AND ARE NUMBERED FROM 137 TO 275. WATER 2AZA 71 REMARK 7 HOH B 136 CORRESPONDS TO SUL A 136. SUL A 136 WAS TAKEN 2AZA 72 REMARK 7 AS THE S ATOM OF A DISORDERED SULFATE ION BECAUSE THE 2AZA 73 REMARK 7 OCCUPANCY IS TOO HIGH FOR IT TO BE A WATER. THE FIRST 91 2AZA 74 REMARK 7 WATER MOLECULES IN EACH GROUP OCCUPY EQUIVALENT SITES IN 2AZA 75 REMARK 7 THE TWO MOLECULES. THEY ARE ARRANGED IN INCREASING ORDER 2AZA 76 REMARK 7 OF THEIR MEAN (BETWEEN THE TWO MOLECULES) B VALUES. THE 2AZA 77 REMARK 7 REMAINING WATER MOLECULES (228-277 FOR MOLECULE 1 AND 2AZA 78 REMARK 7 228-275 FOR MOLECULE 2) DO NOT CORRESPOND AND ARE ORDERED 2AZA 79 REMARK 7 BY THEIR INDIVIDUAL B VALUES. 2AZA 80 REMARK 8 2AZA 81 REMARK 8 THE TRANSFORMATION PROVIDED ON THE *MTRIX* RECORDS BELOW 2AZA 82 REMARK 8 WILL PRODUCE APPROXIMATE COORDINATES FOR MOLECULE 1 (CHAIN 2AZA 83 REMARK 8 INDICATOR *A*) WHEN APPLIED TO THE COORDINATES OF MOLECULE 2AZA 84 REMARK 8 2 (CHAIN INDICATOR *B*). 2AZA 85 REMARK 9 2AZA 86 REMARK 9 ONLY INTERNAL H-BONDS INVOLVING SIDE CHAINS OR 2AZA 87 REMARK 9 CROSSLINKING H BONDS BETWEEN STRANDS ARE PRESENTED ON THE 2AZA 88 REMARK 9 CONECT RECORDS BELOW. 2AZA 89 REMARK 10 2AZA 90 REMARK 10 THE RESIDUES LISTED ON THE *SITE* RECORDS BELOW ARE THOSE 2AZA 91 REMARK 10 INTERACTING WITH THE COPPER ATOM. THE COPPER FORMS FIVE 2AZA 92 REMARK 10 BONDS. 2AZA 93 REMARK 11 2AZA 94 REMARK 11 STRAND 1 OF SHEET B1A (AND B1B) AND STRAND 1 OF SHEET B2A 2AZA 95 REMARK 11 (AND B2B) ARE PARTS OF A PIECE OF EXTENDED CHAIN WHICH IS 2AZA 96 REMARK 11 SPLIT BETWEEN BETWEEN THE TWO SHEETS. RESIDUES 14-16 2AZA 97 REMARK 11 BELONG TO SHEET B1 AND RESIDUES 18-22 BELONG TO SHEET B2 2AZA 98 REMARK 11 WITH A KINK IN BETWEEN. 2AZA 99 REMARK 12 2AZA 100 REMARK 12 TURNS 3A AND 12A (AND 3B AND 12B) ARE MORE LIKE ALPHA-TURNS 2AZA 101 REMARK 12 AS THEY HAVE GOOD 1-5 H-BONDS (O ALA 40 - N MET 44 AND 2AZA 102 REMARK 12 O HIS 117 - N MET 121) WHICH ARE SHORTER THAN THE 1-4 2AZA 103 REMARK 12 H-BONDS (O ALA 40 - MET 43 AND 0 HIS 117 - N MET 120). 2AZA 104 REMARK 13 2AZAA 2 REMARK 13 CORRECTION. MOVE ATOM RECORDS FOR THE B CONFORMATION TO BE 2AZAA 3 REMARK 13 IN THE CORRECT PLACES. THIS REQUIRES RENUMBERING MOST OF 2AZAA 4 REMARK 13 THE ATOMS IN THIS ENTRY. THE CONECT RECORDS ARE NOT 2AZAA 5 REMARK 13 CHANGED BECAUSE THEY WERE BASED ON ATOMS APPEARING IN THE 2AZAA 6 REMARK 13 CORRECT ORDER WITH THE CORRECT NUMBERING. 06-MAR-87. 2AZAA 7 REMARK 14 2AZAB 9 REMARK 14 CORRECTION. INSERT NEW PUBLICATION AS THE JRNL REFERENCE. 2AZAB 10 REMARK 14 09-JAN-89. 2AZAB 11 REMARK 15 2AZAC 2 REMARK 15 CORRECTION. CORRECT STRAND NUMBER IN SHEET B2A. 15-JAN-90. 2AZAC 3 SEQRES 1 A 129 ALA GLN CYS GLU ALA THR ILE GLU SER ASN ASP ALA MET 2AZA 105 SEQRES 2 A 129 GLN TYR ASP LEU LYS GLU MET VAL VAL ASP LYS SER CYS 2AZA 106 SEQRES 3 A 129 LYS GLN PHE THR VAL HIS LEU LYS HIS VAL GLY LYS MET 2AZA 107 SEQRES 4 A 129 ALA LYS SER ALA MET GLY HIS ASN TRP VAL LEU THR LYS 2AZA 108 SEQRES 5 A 129 GLU ALA ASP LYS GLU GLY VAL ALA THR ASP GLY MET ASN 2AZA 109 SEQRES 6 A 129 ALA GLY LEU ALA GLN ASP TYR VAL LYS ALA GLY ASP THR 2AZA 110 SEQRES 7 A 129 ARG VAL ILE ALA HIS THR LYS VAL ILE GLY GLY GLY GLU 2AZA 111 SEQRES 8 A 129 SER ASP SER VAL THR PHE ASP VAL SER LYS LEU THR PRO 2AZA 112 SEQRES 9 A 129 GLY GLU ALA TYR ALA TYR PHE CYS SER PHE PRO GLY HIS 2AZA 113 SEQRES 10 A 129 TRP ALA MET MET LYS GLY THR LEU LYS LEU SER ASN 2AZA 114 SEQRES 1 B 129 ALA GLN CYS GLU ALA THR ILE GLU SER ASN ASP ALA MET 2AZA 115 SEQRES 2 B 129 GLN TYR ASP LEU LYS GLU MET VAL VAL ASP LYS SER CYS 2AZA 116 SEQRES 3 B 129 LYS GLN PHE THR VAL HIS LEU LYS HIS VAL GLY LYS MET 2AZA 117 SEQRES 4 B 129 ALA LYS SER ALA MET GLY HIS ASN TRP VAL LEU THR LYS 2AZA 118 SEQRES 5 B 129 GLU ALA ASP LYS GLU GLY VAL ALA THR ASP GLY MET ASN 2AZA 119 SEQRES 6 B 129 ALA GLY LEU ALA GLN ASP TYR VAL LYS ALA GLY ASP THR 2AZA 120 SEQRES 7 B 129 ARG VAL ILE ALA HIS THR LYS VAL ILE GLY GLY GLY GLU 2AZA 121 SEQRES 8 B 129 SER ASP SER VAL THR PHE ASP VAL SER LYS LEU THR PRO 2AZA 122 SEQRES 9 B 129 GLY GLU ALA TYR ALA TYR PHE CYS SER PHE PRO GLY HIS 2AZA 123 SEQRES 10 B 129 TRP ALA MET MET LYS GLY THR LEU LYS LEU SER ASN 2AZA 124 FTNOTE 1 2AZA 125 FTNOTE 1 SEE REMARK 5. 2AZA 126 FTNOTE 2 2AZA 127 FTNOTE 2 SEE REMARK 6. 2AZA 128 FTNOTE 3 2AZA 129 FTNOTE 3 SEE REMARKS 5 AND 6. 2AZA 130 HET CU A 130 1 COPPER ION 2AZA 131 HET SO4 A 135 5 SULFATE ION 2AZA 132 HET SO4 A 136 5 SULFATE ION 2AZA 133 HET CU B 130 1 COPPER ION 2AZA 134 HET SO4 B 135 5 SULFATE ION 2AZA 135 FORMUL 3 CU 2(CU1) 2AZA 136 FORMUL 4 HOH *281(H2 O1) 2AZA 137 FORMUL 5 SO4 3(O4 S1) 2AZA 138 HELIX 1 AA ASP A 55 GLY A 67 1 3/10 BONDS 63-66, 64-67 2AZA 139 HELIX 2 BA ASP A 98 LEU A 102 5 2AZA 140 HELIX 3 AB ASP B 55 GLY B 67 1 3/10 BONDS 63-66, 64-67 2AZA 141 HELIX 4 BB ASP B 98 LEU B 102 5 2AZA 142 SHEET 1 B1A 4 GLN A 14 ASP A 16 0 2AZA 143 SHEET 2 B1A 4 CYS A 3 ASN A 10 -1 O GLU A 8 N ASP A 16 2AZA 144 SHEET 3 B1A 4 LYS A 27 VAL A 36 1 O THR A 30 N ALA A 5 2AZA 145 SHEET 4 B1A 4 GLU A 91 VAL A 99 -1 O GLU A 91 N HIS A 35 2AZA 146 SHEET 1 B2A 5 LYS A 18 VAL A 22 0 2AZA 147 SHEET 2 B2A 5 MET A 121 SER A 128 1 O THR A 124 N MET A 20 2AZAC 4 SHEET 3 B2A 5 TYR A 108 CYS A 112 -1 O TYR A 108 N LEU A 125 2AZA 149 SHEET 4 B2A 5 HIS A 46 THR A 51 -1 O VAL A 49 N PHE A 111 2AZA 150 SHEET 5 B2A 5 ILE A 81 ILE A 87 -1 O ILE A 87 N HIS A 46 2AZA 151 SHEET 1 B1B 4 GLN B 14 ASP B 16 0 2AZA 152 SHEET 2 B1B 4 CYS B 3 ASN B 10 -1 O GLU B 8 N ASP B 16 2AZA 153 SHEET 3 B1B 4 LYS B 27 VAL B 36 1 O THR B 30 N ALA B 5 2AZA 154 SHEET 4 B1B 4 GLU B 91 VAL B 99 -1 O GLU B 91 N HIS B 35 2AZA 155 SHEET 1 B2B 5 LYS B 18 VAL B 22 0 2AZA 156 SHEET 2 B2B 5 MET B 121 SER B 128 1 O THR B 124 N MET B 20 2AZA 157 SHEET 3 B2B 5 TYR B 108 CYS B 112 -1 O TYR B 108 N LEU B 125 2AZA 158 SHEET 4 B2B 5 HIS B 46 THR B 51 -1 O VAL B 49 N PHE B 111 2AZA 159 SHEET 5 B2B 5 ILE B 81 ILE B 87 -1 O ILE B 87 N HIS B 46 2AZA 160 TURN 1 1A ASN A 10 MET A 13 TYPE I 2AZA 161 TURN 2 2A ASP A 23 CYS A 26 TYPE I 2AZA 162 TURN 3 3A ALA A 40 ALA A 43 TYPE III 2AZA 163 TURN 4 4A LYS A 52 ASP A 55 TYPE III 2AZA 164 TURN 5 5A GLY A 67 GLN A 70 TYPE III 2AZA 165 TURN 6 6A LEU A 68 ASP A 71 TYPE I 2AZA 166 TURN 7 7A GLN A 70 VAL A 73 TYPE III(PRIME) 2AZA 167 TURN 8 8A LYS A 74 ASP A 77 TYPE II 2AZA 168 TURN 9 9A ASP A 77 VAL A 80 TYPE III 2AZA 169 TURN 10 10A GLY A 88 GLU A 91 TYPE II 2AZA 170 TURN 11 11A THR A 103 GLU A 106 TYPE II 2AZA 171 TURN 12 12A PHE A 114 HIS A 117 TYPE II 2AZA 172 TURN 13 13A HIS A 117 MET A 120 TYPE III 2AZA 173 TURN 14 1B ASN B 10 MET B 13 TYPE I 2AZA 174 TURN 15 2B ASP B 23 CYS B 26 TYPE I 2AZA 175 TURN 16 3B ALA B 40 ALA B 43 TYPE III 2AZA 176 TURN 17 4B LYS B 52 ASP B 55 TYPE III 2AZA 177 TURN 18 5B GLY B 67 GLN B 70 TYPE III 2AZA 178 TURN 19 6B LEU B 68 ASP B 71 TYPE I 2AZA 179 TURN 20 7B GLN B 70 VAL B 73 TYPE III(PRIME) 2AZA 180 TURN 21 8B LYS B 74 ASP B 77 TYPE II 2AZA 181 TURN 22 9B ASP B 77 VAL B 80 TYPE III 2AZA 182 TURN 23 10B GLY B 88 GLU B 91 TYPE II 2AZA 183 TURN 24 11B THR B 103 GLU B 106 TYPE II 2AZA 184 TURN 25 12B PHE B 114 HIS B 117 TYPE II 2AZA 185 TURN 26 13B HIS B 117 MET B 120 TYPE III 2AZA 186 SSBOND 1 CYS A 3 CYS A 26 2AZA 187 SSBOND 2 CYS B 3 CYS B 26 2AZA 188 SITE 1 M1A 5 GLY A 45 HIS A 46 CYS A 112 HIS A 117 2AZA 189 SITE 2 M1A 5 MET A 121 2AZA 190 SITE 1 M1B 5 GLY B 45 HIS B 46 CYS B 112 HIS B 117 2AZA 191 SITE 2 M1B 5 MET B 121 2AZA 192 CRYST1 75.000 74.200 99.500 90.00 90.00 90.00 C 2 2 21 16 2AZA 193 ORIGX1 1.000000 0.000000 0.000000 0.00000 2AZA 194 ORIGX2 0.000000 1.000000 0.000000 0.00000 2AZA 195 ORIGX3 0.000000 0.000000 1.000000 0.00000 2AZA 196 SCALE1 .013333 0.000000 0.000000 0.00000 2AZA 197 SCALE2 0.000000 .013477 0.000000 0.00000 2AZA 198 SCALE3 0.000000 0.000000 .010050 0.00000 2AZA 199 MTRIX1 1 -.101580 .994390 .029520 .79000 1 2AZA 200 MTRIX2 1 .994610 .100900 .023930 -1.08500 1 2AZA 201 MTRIX3 1 .020810 .031790 -.999280 24.50300 1 2AZA 202