Header list of 1x37.pdb file
Complete list - r 2 2 Bytes
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
Complete list - r 2 2 Bytes