PDB Short entry for 1PAR
HEADER GENE-REGULATING PROTEIN 22-MAR-94 1PAR 1PAR 2
COMPND ARC REPRESSOR AND A SYNTHETIC 22-MER DNA (21 BASE-PAIRS AND 1PAR 3
COMPND 2 ONE BASE 5' OVERHANG) CONTAINING THE SEQUENCE OF THE ARC 1PAR 4
COMPND 3 OPERATOR 1PAR 5
SOURCE BACTERIOPHAGE P22 1PAR 6
AUTHOR B.E.RAUMANN,M.A.ROULD,C.O.PABO,R.T.SAUER 1PAR 7
REVDAT 1 31-JUL-94 1PAR 0 1PAR 8
REMARK 1 1PAR 9
REMARK 1 REFERENCE 1 1PAR 10
REMARK 1 AUTH B.E.RAUMANN,M.A.ROULD,C.O.PABO,R.T.SAUER 1PAR 11
REMARK 1 TITL DNA RECOGNITION BY BETA-SHEETS IN THE ARC 1PAR 12
REMARK 1 TITL 2 REPRESSOR-OPERATOR CRYSTAL STRUCTURE 1PAR 13
REMARK 1 REF PLANT MOL.BIOL. V. 367 754 1994 1PAR 14
REMARK 1 REFN ASTM PMBIDB NE ISSN 0167-4412 2006 1PAR 15
REMARK 2 1PAR 16
REMARK 2 RESOLUTION. 2.6 ANGSTROMS. 1PAR 17
REMARK 3 1PAR 18
REMARK 3 REFINEMENT. 1PAR 19
REMARK 3 PROGRAM 1 X-PLOR 1PAR 20
REMARK 3 AUTHORS 1 BRUNGER 1PAR 21
REMARK 3 PROGRAM 2 TNT 1PAR 22
REMARK 3 AUTHORS 2 TRONRUD,TEN EYCK,MATTHEWS 1PAR 23
REMARK 3 R VALUE 0.225 1PAR 24
REMARK 3 RMSD BOND DISTANCES 0.010 ANGSTROMS 1PAR 25
REMARK 3 RMSD BOND ANGLES 1.51 DEGREES 1PAR 26
REMARK 3 1PAR 27
REMARK 3 NUMBER OF REFLECTIONS 11253 1PAR 28
REMARK 3 RESOLUTION RANGE 21.0 - 2.6 ANGSTROMS 1PAR 29
REMARK 3 DATA CUTOFF 0.0 SIGMA(F) 1PAR 30
REMARK 3 PERCENT COMPLETION 95.0 1PAR 31
REMARK 3 1PAR 32
REMARK 3 NUMBER OF PROTEIN ATOMS 1712 1PAR 33
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 896 1PAR 34
REMARK 3 NUMBER OF SOLVENT ATOMS 45 1PAR 35
REMARK 3 1PAR 36
REMARK 3 HEAVY ATOM DERIVATIVE DATA WERE COLLECTED FROM A CRYSTAL 1PAR 37
REMARK 3 CONTAINING 5-IODO-URIDINE AT OPERATOR POSITIONS 3 AND 103. 1PAR 38
REMARK 3 SINGLE ISOMORPHOUS REPLACEMENT/ANOMALOUS SCATTERING PHASES 1PAR 39
REMARK 3 WERE CALCULATED WITH PHARE OF THE CCP4 SUITE OF PROGRAMS 1PAR 40
REMARK 3 (1). FRODO (2) WAS USE D FOR MODEL BUILDING AN D RIGID 1PAR 41
REMARK 3 BODY MINIMIZATION, POWELL POSITIONAL MINIMIZATION, AND 1PAR 42
REMARK 3 SIMULATED ANNEALING REFINEMENT WERE DONE WITH X-PLOR (3). 1PAR 43
REMARK 3 THE MODEL WAS CHECKED AND REBUILT USING SIMULATED 1PAR 44
REMARK 3 ANNEALING OMIT MAP. AT THE LAST STAGE OF REFINEMENT, 1PAR 45
REMARK 3 TIGHTLY RESTRAINED INDIVIDUAL B-FACTORS AND 45 WATER 1PAR 46
REMARK 3 MOLECULES WERE INCLUDED, AND CONVENTIONAL LEAST SQUARES 1PAR 47
REMARK 3 REFINEMENT WITH TNT (4) WAS USED. (1) S.E.R.C. (U.K.) 1PAR 48
REMARK 3 COLLABORATIVE COMPUTING PROJECT NO. 4 (DARESBURY 1PAR 49
REMARK 3 LABORATORY, WARRINGTON, U.K., 1979). (2) JONES, T. A 1PAR 50
REMARK 3 J.APPL.CRYSTALLOGR. 11, 268-272 (1978). (3) BRUNGER, A.T. 1PAR 51
REMARK 3 X-PLOR V3.1 MANUAL (YALE UNIVERSITY PRESS, NEW HAVEN, 1PAR 52
REMARK 3 1992). (4) TRONRUD, D.E., TEN EYCK, L.F. AND MATTHEWS, 1PAR 53
REMARK 3 B.W. ACTA CRYSTALLOGR. 43, 489-501 (1987). 1PAR 54
REMARK 4 1PAR 55
REMARK 4 THE SITE PRESENTED IN *SITE* RECORDS BELOW IS THE WILD-TYPE 1PAR 56
REMARK 4 SEQUENCE OF THE ARC OPERATOR SITE. 1PAR 57
REMARK 5 1PAR 58
REMARK 5 THE TRANSFORMATION PRESENTED ON *MTRIX 1* RECORDS BELOW 1PAR 59
REMARK 5 WILL YIELD APPROXIMATE COORDINATES FOR CHAIN A WHEN APPLIED 1PAR 60
REMARK 5 TO CHAIN B (DIMER SYMMETRY AXIS). THE TRANSFORMATION 1PAR 61
REMARK 5 PRESENTED ON *MTRIX 2* RECORDS BELOW WILL YIELD APPROXIMATE 1PAR 62
REMARK 5 COORDINATES FOR CHAIN C WHEN APPLIED TO CHAIN D (DIMER 1PAR 63
REMARK 5 SYMMETRY AXIS). THE TRANSFORMATION PRESENTED ON *MTRIX 3* 1PAR 64
REMARK 5 RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAINS 1PAR 65
REMARK 5 A AND B WHEN APPLIED TO CHAINS C AND D, RESPECTIVELY. THIS 1PAR 66
REMARK 5 THIRD TRANSFORMATION RELATES DIMER CD AND THE RIGHT 1PAR 67
REMARK 5 OPERATOR HALF-SITE TO DIMER AB AND THE LEFT OPERATOR 1PAR 68
REMARK 5 HALF-SITE. (TETRAMER SYMMETRY AXIS). 1PAR 69
REMARK 6 1PAR 70
REMARK 6 RESIDUES ALA A 53 AND ILE C 51 - ALA C 53 ARE NOT INCLUDED 1PAR 71
REMARK 6 IN THE MODEL DUE TO POOR ELECTRON DENSITY. 1PAR 72
REMARK 7 1PAR 73
REMARK 7 THE SIDE CHAIN IS INCOMPLETE FOR RESIDUE GLU C 48. 1PAR 74
REMARK 8 1PAR 75
REMARK 8 BY REQUEST OF THE DEPOSITOR, THE PROTEIN DATA BANK HAS NOT 1PAR 76
REMARK 8 APPLIED THE IUPAC-IUB RECOMMENDATIONS REGARDING THE 1PAR 77
REMARK 8 DESIGNATION OF BRANCHES 1 AND 2 OF SIDE-CHAIN ATOMS IN 1PAR 78
REMARK 8 RESIDUES ARG, ASP, GLU, LEU, PHE, TYR, AND VAL TO THIS 1PAR 79
REMARK 8 ENTRY. 1PAR 80
REMARK 9 1PAR 81
REMARK 9 PDB ADVISORY NOTICE: 1PAR 82
REMARK 9 WATER MOLECULE 636 MAKES A CLOSE CONTACT OF 2.O8 ANGSTROMS 1PAR 83
REMARK 9 WITH ATOM N7 OF RESIDUE A 2 OF CHAIN *E*. 1PAR 84
SEQRES 1 A 53 MET LYS GLY MET SER LYS MET PRO GLN PHE ASN LEU ARG 1PAR 85
SEQRES 2 A 53 TRP PRO ARG GLU VAL LEU ASP LEU VAL ARG LYS VAL ALA 1PAR 86
SEQRES 3 A 53 GLU GLU ASN GLY ARG SER VAL ASN SER GLU ILE TYR GLN 1PAR 87
SEQRES 4 A 53 ARG VAL MET GLU SER PHE LYS LYS GLU GLY ARG ILE GLY 1PAR 88
SEQRES 5 A 53 ALA 1PAR 89
SEQRES 1 B 53 MET LYS GLY MET SER LYS MET PRO GLN PHE ASN LEU ARG 1PAR 90
SEQRES 2 B 53 TRP PRO ARG GLU VAL LEU ASP LEU VAL ARG LYS VAL ALA 1PAR 91
SEQRES 3 B 53 GLU GLU ASN GLY ARG SER VAL ASN SER GLU ILE TYR GLN 1PAR 92
SEQRES 4 B 53 ARG VAL MET GLU SER PHE LYS LYS GLU GLY ARG ILE GLY 1PAR 93
SEQRES 5 B 53 ALA 1PAR 94
SEQRES 1 C 53 MET LYS GLY MET SER LYS MET PRO GLN PHE ASN LEU ARG 1PAR 95
SEQRES 2 C 53 TRP PRO ARG GLU VAL LEU ASP LEU VAL ARG LYS VAL ALA 1PAR 96
SEQRES 3 C 53 GLU GLU ASN GLY ARG SER VAL ASN SER GLU ILE TYR GLN 1PAR 97
SEQRES 4 C 53 ARG VAL MET GLU SER PHE LYS LYS GLU GLY ARG ILE GLY 1PAR 98
SEQRES 5 C 53 ALA 1PAR 99
SEQRES 1 D 53 MET LYS GLY MET SER LYS MET PRO GLN PHE ASN LEU ARG 1PAR 100
SEQRES 2 D 53 TRP PRO ARG GLU VAL LEU ASP LEU VAL ARG LYS VAL ALA 1PAR 101
SEQRES 3 D 53 GLU GLU ASN GLY ARG SER VAL ASN SER GLU ILE TYR GLN 1PAR 102
SEQRES 4 D 53 ARG VAL MET GLU SER PHE LYS LYS GLU GLY ARG ILE GLY 1PAR 103
SEQRES 5 D 53 ALA 1PAR 104
SEQRES 1 E 22 T A T A G T A G A G T G C 1PAR 105
SEQRES 2 E 22 T T C T A T C A T 1PAR 106
SEQRES 1 F 22 A A T G A T A G A A G C A 1PAR 107
SEQRES 2 F 22 C T C T A C T A T 1PAR 108
FORMUL 8 HOH *45(H2 O1) 1PAR 109
HELIX 1 A PRO A 15 GLY A 30 1 HELIX A IN MONOMER A 1PAR 110
HELIX 2 B SER A 32 GLU A 48 1 HELIX B IN MONOMER A 1PAR 111
HELIX 3 A PRO B 15 GLY B 30 1 HELIX A IN MONOMER B 1PAR 112
HELIX 4 B SER B 32 GLU B 48 1 HELIX B IN MONOMER B 1PAR 113
HELIX 5 A PRO C 15 GLY C 30 1 HELIX A IN MONOMER C 1PAR 114
HELIX 6 B SER C 32 GLU C 48 1 HELIX B IN MONOMER C 1PAR 115
HELIX 7 A PRO D 15 GLY D 30 1 HELIX A IN MONOMER D 1PAR 116
HELIX 8 B SER D 32 GLU D 48 1 HELIX B IN MONOMER D 1PAR 117
SHEET 1 AB 2 PRO A 8 TRP A 14 0 1PAR 118
SHEET 2 AB 2 PRO B 8 TRP B 14 -1 O PHE B 10 N LEU A 12 1PAR 119
SHEET 1 CD 2 PRO C 8 TRP C 14 0 1PAR 120
SHEET 2 CD 2 PRO D 8 TRP D 14 -1 O PHE D 10 N LEU C 12 1PAR 121
TURN 1 A1 MET A 1 MET A 4 TYPE II TURN 1PAR 122
TURN 2 A2 MET A 4 MET A 7 TYPE I TURN 1PAR 123
TURN 3 B1 MET B 1 MET B 4 TYPE II TURN 1PAR 124
TURN 4 B2 MET B 4 MET B 7 TYPE I TURN 1PAR 125
TURN 5 C1 MET C 1 MET C 4 TYPE II TURN 1PAR 126
TURN 6 C2 MET C 4 MET C 7 TYPE I TURN 1PAR 127
TURN 7 D1 MET D 1 MET D 4 TYPE II TURN 1PAR 128
TURN 8 D2 MET D 4 MET D 7 TYPE I TURN 1PAR 129
SITE 1 AOP 4 A E 2 T E 22 A F 2 T F 22 1PAR 130
CRYST1 65.670 56.730 53.800 90.00 106.90 90.00 P 21 8 1PAR 131
ORIGX1 1.000000 0.000000 0.000000 0.00000 1PAR 132
ORIGX2 0.000000 1.000000 0.000000 0.00000 1PAR 133
ORIGX3 0.000000 0.000000 1.000000 0.00000 1PAR 134
SCALE1 0.015228 0.000000 0.004627 0.00000 1PAR 135
SCALE2 0.000000 0.017627 0.000000 0.00000 1PAR 136
SCALE3 0.000000 0.000000 0.019426 0.00000 1PAR 137
MTRIX1 1 -0.511800 0.112700 -0.851700 63.45470 1 1PAR 138
MTRIX2 1 0.130700 -0.969600 -0.206800 -8.03550 1 1PAR 139
MTRIX3 1 -0.849100 -0.217200 0.481500 35.21450 1 1PAR 140
MTRIX1 2 0.535600 0.039500 -0.843500 58.08270 1 1PAR 141
MTRIX2 2 0.042600 -0.998900 -0.019800 -4.33970 1 1PAR 142
MTRIX3 2 -0.843400 -0.025300 -0.536700 105.34710 1 1PAR 143
MTRIX1 3 0.014600 0.119900 -0.992700 70.37200 1 1PAR 144
MTRIX2 3 0.100400 -0.987900 -0.117900 -5.90280 1 1PAR 145
MTRIX3 3 -0.994800 -0.098000 -0.026400 71.22350 1 1PAR 146