HEADER HYDROLASE 30-APR-05 1X37
TITLE STRUCTURE OF BACILLUS SUBTILIS LON PROTEASE SSD DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP-DEPENDENT PROTEASE LA 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SSD DOMAIN;
COMPND 5 SYNONYM: LON PROTEASE;
COMPND 6 EC: 3.4.21.53;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-21A(+)
KEYWDS AAA+ SUPERFAMILY, PROTEASE, SSD DOMAIN, SOLUTION STRUCTURE, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 16
MDLTYP MINIMIZED AVERAGE
AUTHOR I.WANG,Y.C.LOU,S.C.LO,Y.L.LEE,S.H.WU,C.CHEN
REVDAT 3 02-MAR-22 1X37 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X37 1 VERSN
REVDAT 1 30-OCT-05 1X37 0
JRNL AUTH I.WANG,Y.C.LOU,S.C.LO,Y.L.LEE,S.H.WU,C.CHEN
JRNL TITL STRUCTURAL BASIS AND DNA BINDING PROPERTY OF SSD DOMAIN OF
JRNL TITL 2 BACILLUS SUBTILIS LON PROTEASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, A. T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1157 RESTRAINTS, 968 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 121
REMARK 3 DIHEDRAL ANGLE RESTRAINTS,68 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1X37 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024321.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 5.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.5MM BSLONSSD U-15N, 13C; 50MM
REMARK 210 PHOSPHATE BUFFER WITH 100MM NACL,
REMARK 210 50MM ARG/GLU, 5MM DTT; 1.5MM
REMARK 210 BSLONSSD U-15N, 13C; 50MM
REMARK 210 PHOSPHATE BUFFER WITH 100MM NACL,
REMARK 210 50MM ARG/GLU, 5MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, AURELIA 3.1.6,
REMARK 210 NMRPIPE, NMRVIEW 5.2.2, X-PLOR
REMARK 210 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-16
REMARK 465 RES C SSSEQI
REMARK 465 MET A 0
REMARK 465 GLY A 96
REMARK 465 GLN A 97
REMARK 465 ALA A 98
REMARK 465 GLU A 99
REMARK 465 THR A 100
REMARK 465 GLU A 101
REMARK 465 ASP A 102
REMARK 465 GLN A 103
REMARK 465 VAL A 104
REMARK 465 GLY A 105
REMARK 465 VAL A 106
REMARK 465 VAL A 107
REMARK 465 THR A 108
REMARK 465 GLY A 109
REMARK 465 LEU A 110
REMARK 465 ALA A 111
REMARK 465 TYR A 112
REMARK 465 THR A 113
REMARK 465 THR A 114
REMARK 465 VAL A 115
REMARK 465 LEU A 116
REMARK 465 ARG A 117
REMARK 465 HIS A 118
REMARK 465 HIS A 119
REMARK 465 HIS A 120
REMARK 465 HIS A 121
REMARK 465 HIS A 122
REMARK 465 HIS A 123
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLN A 85 H GLY A 89 1.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 VAL A 12 -37.95 -38.79
REMARK 500 1 LYS A 19 -79.43 -52.15
REMARK 500 1 LYS A 22 -80.45 -71.35
REMARK 500 1 LEU A 26 -39.78 -36.57
REMARK 500 1 LYS A 28 139.31 -39.78
REMARK 500 1 SER A 29 93.74 -33.16
REMARK 500 1 ASN A 30 60.38 -118.61
REMARK 500 1 LEU A 31 119.27 -160.56
REMARK 500 1 ILE A 41 -71.76 -42.96
REMARK 500 1 THR A 46 8.90 46.71
REMARK 500 1 GLU A 48 166.82 175.16
REMARK 500 1 CYS A 62 -71.65 -53.76
REMARK 500 1 LYS A 64 -39.18 -39.92
REMARK 500 1 ALA A 68 0.86 -57.07
REMARK 500 1 ILE A 69 -9.89 -45.14
REMARK 500 1 VAL A 70 31.37 -89.23
REMARK 500 1 GLU A 73 5.87 -168.86
REMARK 500 1 ARG A 76 105.48 55.67
REMARK 500 1 VAL A 79 65.61 -111.88
REMARK 500 1 THR A 80 -168.94 -66.19
REMARK 500 1 LYS A 90 157.02 80.34
REMARK 500 2 VAL A 12 -38.65 -39.30
REMARK 500 2 LEU A 16 -37.78 -38.71
REMARK 500 2 LYS A 22 -81.10 -67.75
REMARK 500 2 LEU A 26 -39.65 -37.21
REMARK 500 2 LYS A 28 158.28 -46.99
REMARK 500 2 SER A 29 91.64 -45.53
REMARK 500 2 ILE A 41 -77.06 -43.57
REMARK 500 2 ILE A 42 -39.17 -39.88
REMARK 500 2 THR A 46 10.17 51.07
REMARK 500 2 GLU A 48 -98.32 -92.55
REMARK 500 2 CYS A 62 -70.24 -56.77
REMARK 500 2 VAL A 70 4.72 -64.69
REMARK 500 2 ALA A 71 -160.08 -58.40
REMARK 500 2 GLU A 72 -77.54 -54.31
REMARK 500 2 ARG A 74 33.46 -87.65
REMARK 500 2 ARG A 76 81.69 50.04
REMARK 500 2 PHE A 87 -71.15 -79.56
REMARK 500 2 LYS A 90 85.63 -168.95
REMARK 500 2 ILE A 92 -41.01 -135.72
REMARK 500 3 VAL A 12 -38.90 -39.20
REMARK 500 3 LEU A 16 -38.98 -39.95
REMARK 500 3 LYS A 19 -70.49 -48.97
REMARK 500 3 LYS A 22 -81.17 -68.84
REMARK 500 3 LEU A 26 -39.52 -36.95
REMARK 500 3 LYS A 28 154.56 -46.03
REMARK 500 3 SER A 29 92.99 -46.08
REMARK 500 3 ASN A 30 59.03 -113.06
REMARK 500 3 TYR A 45 -70.76 -89.24
REMARK 500 3 THR A 46 12.80 49.54
REMARK 500
REMARK 500 THIS ENTRY HAS 319 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1X37 A 1 115 UNP P37945 LON1_BACSU 490 604
SEQADV 1X37 MET A 0 UNP P37945 INITIATING METHIONINE
SEQADV 1X37 LEU A 116 UNP P37945 EXPRESSION TAG
SEQADV 1X37 ARG A 117 UNP P37945 EXPRESSION TAG
SEQADV 1X37 HIS A 118 UNP P37945 EXPRESSION TAG
SEQADV 1X37 HIS A 119 UNP P37945 EXPRESSION TAG
SEQADV 1X37 HIS A 120 UNP P37945 EXPRESSION TAG
SEQADV 1X37 HIS A 121 UNP P37945 EXPRESSION TAG
SEQADV 1X37 HIS A 122 UNP P37945 EXPRESSION TAG
SEQADV 1X37 HIS A 123 UNP P37945 EXPRESSION TAG
SEQRES 1 A 124 MET ALA GLY TYR THR GLU ILE GLU LYS LEU GLU ILE VAL
SEQRES 2 A 124 LYS ASP HIS LEU LEU PRO LYS GLN ILE LYS GLU HIS GLY
SEQRES 3 A 124 LEU LYS LYS SER ASN LEU GLN LEU ARG ASP GLN ALA ILE
SEQRES 4 A 124 LEU ASP ILE ILE ARG TYR TYR THR ARG GLU ALA GLY VAL
SEQRES 5 A 124 ARG SER LEU GLU ARG GLN LEU ALA ALA ILE CYS ARG LYS
SEQRES 6 A 124 ALA ALA LYS ALA ILE VAL ALA GLU GLU ARG LYS ARG ILE
SEQRES 7 A 124 THR VAL THR GLU LYS ASN LEU GLN ASP PHE ILE GLY LYS
SEQRES 8 A 124 ARG ILE PHE ARG TYR GLY GLN ALA GLU THR GLU ASP GLN
SEQRES 9 A 124 VAL GLY VAL VAL THR GLY LEU ALA TYR THR THR VAL LEU
SEQRES 10 A 124 ARG HIS HIS HIS HIS HIS HIS
HELIX 1 1 THR A 4 LEU A 16 1 13
HELIX 2 2 LEU A 17 LEU A 26 1 10
HELIX 3 3 ARG A 34 THR A 46 1 13
HELIX 4 4 GLY A 50 ALA A 68 1 19
HELIX 5 5 ILE A 69 ALA A 71 5 3
HELIX 6 6 LYS A 82 GLY A 89 1 8
SHEET 1 A 2 GLN A 32 LEU A 33 0
SHEET 2 A 2 THR A 78 VAL A 79 1 O VAL A 79 N GLN A 32
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
