HEADER HYDROLASE(ACID PROTEASE) 21-SEP-94 2HPE 2HPE 2 COMPND HIV-2 PROTEASE MUTANT WITH LYS 57 REPLACED BY LEU (K57L) 2HPE 3 COMPND 2 COMPLEXED WITH UNIDENTIFIED PEPTIDE FRAGMENT IN ACTIVE SITE 2HPE 4 COMPND 3 (COMPLEX 1) 2HPE 5 SOURCE HIV-2 EXPRESSED IN (ESCHERICHIA COLI) 2HPE 6 AUTHOR A.M.MULICHAK,K.D.WATENPAUGH 2HPE 7 REVDAT 1 15-OCT-94 2HPE 0 2HPE 8 REMARK 1 2HPE 9 REMARK 1 REFERENCE 1 2HPE 10 REMARK 1 AUTH A.M.MULICHAK,K.D.WATENPAUGH 2HPE 11 REMARK 1 TITL COMPARISON OF THE STRUCTURES OF HIV-2 PROTEASE 2HPE 12 REMARK 1 TITL 2 COMPLEXES IN THREE CRYSTAL SPACE GROUPS WITH AN 2HPE 13 REMARK 1 TITL 3 HIV-1 PROTEASE COMPLEX STRUCTURE 2HPE 14 REMARK 1 REF TO BE PUBLISHED 2HPE 15 REMARK 1 REFN 0353 2HPE 16 REMARK 1 REFERENCE 2 2HPE 17 REMARK 1 AUTH A.M.MULICHAK,J.O.HUI,A.G.TOMASSELLI,R.L.HEINRIKSON, 2HPE 18 REMARK 1 AUTH 2 K.A.CURRY,C.-S.TOMICH,S.THAISRIVONGS,T.K.SAWYER, 2HPE 19 REMARK 1 AUTH 3 K.D.WATENPAUGH 2HPE 20 REMARK 1 TITL THE CRYSTALLOGRAPHIC STRUCTURE OF THE PROTEASE FROM 2HPE 21 REMARK 1 TITL 2 HUMAN IMMUNODEFICIENCY VIRUS TYPE 2 WITH TWO 2HPE 22 REMARK 1 TITL 3 SYNTHETIC PEPTIDIC TRANSITION STATE ANALOG 2HPE 23 REMARK 1 TITL 4 INHIBITORS 2HPE 24 REMARK 1 REF J.BIOL.CHEM. V. 168 13103 1993 2HPE 25 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 2HPE 26 REMARK 2 2HPE 27 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. 2HPE 28 REMARK 3 2HPE 29 REMARK 3 REFINEMENT. 2HPE 30 REMARK 3 PROGRAM 1 CEDAR 2HPE 31 REMARK 3 AUTHORS 1 WATENPAUGH,HERMANS 2HPE 32 REMARK 3 PROGRAM 2 PROLSQ 2HPE 33 REMARK 3 AUTHORS 2 KONNERT,HENDRICKSON 2HPE 34 REMARK 3 R VALUE 0.150 2HPE 35 REMARK 3 NUMBER OF REFLECTIONS 9218 2HPE 36 REMARK 3 RESOLUTION RANGE 10.0 - 2.0 ANGSTROMS 2HPE 37 REMARK 3 DATA CUTOFF 2.0 SIGMA(F) 2HPE 38 REMARK 3 RMSD BOND DISTANCES 0.02 ANGSTROMS 2HPE 39 REMARK 3 RMSD BOND ANGLES 2. DEGREES 2HPE 40 REMARK 3 2HPE 41 REMARK 3 DATA COLLECTION. 2HPE 42 REMARK 3 NUMBER OF UNIQUE REFLECTIONS 10638 2HPE 43 REMARK 3 RESOLUTION RANGE 10.0 - 1.0 ANGSTROMS 2HPE 44 REMARK 3 REJECTION CRITERIA 2.0 SIGMA(F) 2HPE 45 REMARK 3 COMPLETENESS OF DATA 85.0 % 2HPE 46 REMARK 3 2HPE 47 REMARK 3 NUMBER OF PROTEIN ATOMS 1551 2HPE 48 REMARK 3 NUMBER OF SOLVENT ATOMS 160 2HPE 49 REMARK 4 2HPE 50 REMARK 4 THE TWO CHAINS OF THE DIMERIC ENZYME HAVE BEEN ASSIGNED 2HPE 51 REMARK 4 CHAIN INDICATORS *A* AND *B*. THE SUBSTRATE HAS BEEN 2HPE 52 REMARK 4 ASSIGNED CHAIN INDICATOR *S*. IN THE PAPERS, CHAIN A 2HPE 53 REMARK 4 RESIDUES ARE NUMBERED 1 - 99 AND CHAIN B RESIDUES ARE 2HPE 54 REMARK 4 NUMBERED 101 - 199, WHILE BOTH CHAINS ARE NUMBERED 1 - 99 2HPE 55 REMARK 4 IN THIS ENTRY. 2HPE 56 REMARK 5 2HPE 57 REMARK 5 THERE IS A PEPTIDE FRAGMENT IN THE SUBSTRATE BINDING 2HPE 58 REMARK 5 POCKET. BECAUSE THE SIDE GROUPS ARE NOT KNOWN FOR CERTAIN, 2HPE 59 REMARK 5 THE RESIDUES HAVE ALL BEEN REPRESENTED AS "UNK". THERE 2HPE 60 REMARK 5 ARE COORDINATES PRESENT FOR FOUR OR FIVE ATOMS OF EACH OF 2HPE 61 REMARK 5 THESE RESIDUES (EACH CORRESPONDING TO THE ATOMS OF A 2HPE 62 REMARK 5 GLYCINE OR ALANINE.) 2HPE 63 REMARK 6 2HPE 64 REMARK 6 ATOMS WITH B-FACTORS GREATER THAN 70.0 A**2 MAY BE 2HPE 65 REMARK 6 CONSIDERED TO BE DISORDERED OR NOT SEEN IN THE ELECTRON 2HPE 66 REMARK 6 DENSITY MAPS. 2HPE 67 REMARK 7 2HPE 68 REMARK 7 CROSS REFERENCE TO SEQUENCE DATABASE 2HPE 69 REMARK 7 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 2HPE 70 REMARK 7 POL_HV2RO A 2HPE 71 REMARK 7 POL_HV2RO B 2HPE 72 SEQRES 1 A 99 PRO GLN PHE SER LEU TRP LYS ARG PRO VAL VAL THR ALA 2HPE 73 SEQRES 2 A 99 TYR ILE GLU GLY GLN PRO VAL GLU VAL LEU LEU ASP THR 2HPE 74 SEQRES 3 A 99 GLY ALA ASP ASP SER ILE VAL ALA GLY ILE GLU LEU GLY 2HPE 75 SEQRES 4 A 99 ASN ASN TYR SER PRO LYS ILE VAL GLY GLY ILE GLY GLY 2HPE 76 SEQRES 5 A 99 PHE ILE ASN THR LEU GLU TYR LYS ASN VAL GLU ILE GLU 2HPE 77 SEQRES 6 A 99 VAL LEU ASN LYS LYS VAL ARG ALA THR ILE MET THR GLY 2HPE 78 SEQRES 7 A 99 ASP THR PRO ILE ASN ILE PHE GLY ARG ASN ILE LEU THR 2HPE 79 SEQRES 8 A 99 ALA LEU GLY MET SER LEU ASN LEU 2HPE 80 SEQRES 1 B 99 PRO GLN PHE SER LEU TRP LYS ARG PRO VAL VAL THR ALA 2HPE 81 SEQRES 2 B 99 TYR ILE GLU GLY GLN PRO VAL GLU VAL LEU LEU ASP THR 2HPE 82 SEQRES 3 B 99 GLY ALA ASP ASP SER ILE VAL ALA GLY ILE GLU LEU GLY 2HPE 83 SEQRES 4 B 99 ASN ASN TYR SER PRO LYS ILE VAL GLY GLY ILE GLY GLY 2HPE 84 SEQRES 5 B 99 PHE ILE ASN THR LEU GLU TYR LYS ASN VAL GLU ILE GLU 2HPE 85 SEQRES 6 B 99 VAL LEU ASN LYS LYS VAL ARG ALA THR ILE MET THR GLY 2HPE 86 SEQRES 7 B 99 ASP THR PRO ILE ASN ILE PHE GLY ARG ASN ILE LEU THR 2HPE 87 SEQRES 8 B 99 ALA LEU GLY MET SER LEU ASN LEU 2HPE 88 SEQRES 1 S 9 UNK UNK UNK UNK UNK UNK UNK UNK UNK 2HPE 89 FORMUL 4 HOH *160(H2 O1) 2HPE 90 HELIX 1 A1 GLY A 86 LEU A 93 1 2HPE 91 HELIX 2 B1 GLY B 86 LEU B 93 1 2HPE 92 SHEET 1 B1 4 PRO A 1 PHE A 3 0 2HPE 93 SHEET 2 B1 4 SER B 96 LEU B 99 -1 N LEU B 97 O PHE A 3 2HPE 94 SHEET 3 B1 4 SER A 96 LEU A 99 -1 N SER A 96 O ASN B 98 2HPE 95 SHEET 4 B1 4 PRO B 1 PHE B 3 -1 N PHE B 3 O LEU A 97 2HPE 96 SHEET 1 B2 4 GLN A 18 VAL A 20 0 2HPE 97 SHEET 2 B2 4 ALA A 13 ILE A 15 -1 N ALA A 13 O VAL A 20 2HPE 98 SHEET 3 B2 4 GLU A 63 VAL A 66 -1 N GLU A 65 O TYR A 14 2HPE 99 SHEET 4 B2 4 LYS A 69 VAL A 71 -1 N VAL A 71 O ILE A 64 2HPE 100 SHEET 1 B3 4 GLN B 18 VAL B 20 0 2HPE 101 SHEET 2 B3 4 ALA B 13 ILE B 15 -1 N ALA B 13 O VAL B 20 2HPE 102 SHEET 3 B3 4 GLU B 63 VAL B 66 -1 N GLU B 65 O TYR B 14 2HPE 103 SHEET 4 B3 4 LYS B 69 VAL B 71 -1 N VAL B 71 O ILE B 64 2HPE 104 TURN 1 T1A ILE A 15 GLN A 18 TYPE I' 2HPE 105 TURN 2 T2A GLY A 49 GLY A 52 TYPE I 2HPE 106 TURN 3 T3A VAL A 66 LYS A 69 TYPE I' 2HPE 107 TURN 4 T1B ILE B 15 GLN B 18 TYPE I' 2HPE 108 TURN 5 T2B GLY B 49 GLY B 52 TYPE II 2HPE 109 TURN 6 T3B VAL B 66 LYS B 69 TYPE I' 2HPE 110 CRYST1 58.230 43.820 39.180 90.00 106.16 90.00 P 21 2 2HPE 111 ORIGX1 1.000000 0.000000 0.000000 0.00000 2HPE 112 ORIGX2 0.000000 1.000000 0.000000 0.00000 2HPE 113 ORIGX3 0.000000 0.000000 1.000000 0.00000 2HPE 114 SCALE1 0.017173 0.000000 0.004976 0.00000 2HPE 115 SCALE2 0.000000 0.022821 0.000000 0.00000 2HPE 116 SCALE3 0.000000 0.000000 0.026573 0.00000 2HPE 117