Header list of 1xx8.pdb file
Complete list - 20 20 Bytes
HEADER DNA BINDING PROTEIN 04-NOV-04 1XX8 TITLE NMR STRUCTURE OF THE W24A MUTANT OF THE HYPERTHERMOPHILE SAC7D PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: SAC7D; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS ACIDOCALDARIUS; SOURCE 3 ORGANISM_TAXID: 2285; SOURCE 4 GENE: SAC7D; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: RESETTABLUE(DE3)PLACI (NOVAGEN); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PETBLUE-2 KEYWDS HYPERTHERMOPHILE, DNA-BINDING PROTEIN, DNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 11 MDLTYP MINIMIZED AVERAGE AUTHOR J.L.BEDELL,S.P.EDMONDSON,J.W.SHRIVER REVDAT 3 20-OCT-21 1XX8 1 REMARK SEQADV REVDAT 2 24-FEB-09 1XX8 1 VERSN REVDAT 1 08-FEB-05 1XX8 0 JRNL AUTH J.L.BEDELL,S.P.EDMONDSON,J.W.SHRIVER JRNL TITL ROLE OF A SURFACE TRYPTOPHAN IN DEFINING THE STRUCTURE, JRNL TITL 2 STABILITY, AND DNA BINDING OF THE HYPERTHERMOPHILE PROTEIN JRNL TITL 3 SAC7D JRNL REF BIOCHEMISTRY V. 44 915 2005 JRNL REFN ISSN 0006-2960 JRNL PMID 15654747 JRNL DOI 10.1021/BI047823B REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1C, CNS 1.1 REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER, CLORE (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NOE ASSIGNMENTS, DISTANCE RESTRAINT REMARK 3 CALIBRATION, AND INITIAL STRUCTURES WERE MADE USING ARIA 1.2 REMARK 3 WITH 370 NOE VOLUMES. FINAL STRUCTURE REFINEMENT WAS DONE USING REMARK 3 CNS 1.1 WITH 262 UNAMBIGUOUS DISTANCE RESTRAINTS, 13 H-BONDS, 48 REMARK 3 HNHA COUPLING CONSTANTS, AND 59 NH RESIDUAL DIPOLAR COUPLINGS. REMARK 4 REMARK 4 1XX8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-04. REMARK 100 THE DEPOSITION ID IS D_1000030872. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 4.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 5 MM SAC7D, 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY; REMARK 210 HNHA; 2D_HSQC_IPAP REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 2000, NMRVIEW 5.2.2, ARIA REMARK 210 1.2 REMARK 210 METHOD USED : SIMULATED ANNEALING USING REMARK 210 CARTESION AND TORSION ANGLE REMARK 210 DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: REMARK 210 THIS ENTRY CONSISTS OF 11 MODELS, INCLUDING ONE ENERGY-MINIMIZED REMARK 210 AVERAGE STRUCTURE FOLLOWED BY AN ENSEMBLE OF REMARK 210 THE 10 BEST NMR STRUCTURES. 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 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 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 PHE A 6 176.05 -59.03 REMARK 500 1 LYS A 9 42.53 39.64 REMARK 500 1 GLU A 11 142.42 -171.16 REMARK 500 1 LYS A 19 47.93 -101.49 REMARK 500 1 LYS A 21 -64.32 -93.39 REMARK 500 1 VAL A 26 -101.34 -95.11 REMARK 500 1 ASN A 37 -68.68 73.26 REMARK 500 1 LYS A 65 -65.43 -131.61 REMARK 500 2 LYS A 5 45.66 -100.25 REMARK 500 2 LYS A 9 29.31 49.61 REMARK 500 2 GLU A 14 99.87 28.67 REMARK 500 2 LYS A 22 154.43 76.82 REMARK 500 2 VAL A 26 -86.01 -110.76 REMARK 500 2 ASN A 37 -21.57 170.94 REMARK 500 2 LYS A 52 -75.03 17.68 REMARK 500 2 LEU A 58 -52.09 179.95 REMARK 500 2 ALA A 61 -28.06 -153.27 REMARK 500 2 GLU A 62 27.89 -74.01 REMARK 500 2 ARG A 63 49.81 -151.25 REMARK 500 2 GLU A 64 -49.38 -168.09 REMARK 500 3 LYS A 5 48.18 -102.35 REMARK 500 3 LYS A 9 -3.61 68.47 REMARK 500 3 LYS A 19 61.91 -102.78 REMARK 500 3 VAL A 26 -99.12 -104.26 REMARK 500 3 TYR A 34 -163.00 -122.77 REMARK 500 3 ASP A 36 -81.07 -98.38 REMARK 500 3 LYS A 39 -138.04 -173.89 REMARK 500 3 LYS A 52 -86.50 20.79 REMARK 500 3 GLU A 64 -92.36 -76.36 REMARK 500 3 LYS A 65 -86.76 -78.98 REMARK 500 4 VAL A 4 68.94 63.87 REMARK 500 4 LYS A 9 -13.52 70.52 REMARK 500 4 LYS A 19 54.84 -95.18 REMARK 500 4 LYS A 21 -67.55 -107.45 REMARK 500 4 VAL A 26 -79.63 -134.26 REMARK 500 4 TYR A 34 -167.81 -129.84 REMARK 500 4 ASP A 36 54.18 -151.80 REMARK 500 4 ASN A 37 -178.61 166.85 REMARK 500 4 LYS A 39 -169.11 -169.70 REMARK 500 4 LYS A 52 -91.09 35.67 REMARK 500 4 GLU A 64 33.91 -150.67 REMARK 500 4 LYS A 65 18.95 -159.31 REMARK 500 5 VAL A 2 34.19 -90.17 REMARK 500 5 PHE A 6 173.78 -56.08 REMARK 500 5 THR A 17 -45.34 79.67 REMARK 500 5 ILE A 20 98.15 -65.34 REMARK 500 5 VAL A 26 -80.30 -127.18 REMARK 500 5 MET A 29 -148.65 -111.52 REMARK 500 5 TYR A 34 -52.67 -129.67 REMARK 500 5 ASP A 35 92.47 64.87 REMARK 500 REMARK 500 THIS ENTRY HAS 122 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1SAP RELATED DB: PDB REMARK 900 THE SAME PROTEIN WITH TRP AT RESIDUE 24 INSTEAD OF ALA DBREF 1XX8 A 1 66 UNP P13123 DN71_SULAC 0 65 SEQADV 1XX8 ALA A 24 UNP P13123 TRP 23 ENGINEERED MUTATION SEQRES 1 A 66 MET VAL LYS VAL LYS PHE LYS TYR LYS GLY GLU GLU LYS SEQRES 2 A 66 GLU VAL ASP THR SER LYS ILE LYS LYS VAL ALA ARG VAL SEQRES 3 A 66 GLY LYS MET VAL SER PHE THR TYR ASP ASP ASN GLY LYS SEQRES 4 A 66 THR GLY ARG GLY ALA VAL SER GLU LYS ASP ALA PRO LYS SEQRES 5 A 66 GLU LEU LEU ASP MET LEU ALA ARG ALA GLU ARG GLU LYS SEQRES 6 A 66 LYS HELIX 1 1 ASP A 16 SER A 18 5 3 HELIX 2 2 PRO A 51 ARG A 60 1 10 SHEET 1 A 3 ILE A 20 VAL A 23 0 SHEET 2 A 3 MET A 29 ASP A 35 -1 O THR A 33 N LYS A 22 SHEET 3 A 3 THR A 40 SER A 46 -1 O VAL A 45 N VAL A 30 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 - 20 20 Bytes