Header list of 1sx0.pdb file
Complete list - 2 20 Bytes
HEADER PROTEIN TRANSPORT 30-MAR-04 1SX0 TITLE SOLUTION NMR STRUCTURE AND X-RAY ABSORPTION ANALYSIS OF THE C-TERMINAL TITLE 2 ZINC-BINDING DOMAIN OF THE SECA ATPASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: SECA; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL ZINC BINDING DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: SOLID PHASE PEPTIDE SYNTHESIS, N-TERMINALLY SOURCE 4 ACETYLATED. THE SEQUENCE OF THIS PEPTIDE NATURALLY EXISTS IN SOURCE 5 ESCHERICHIA COLI KEYWDS ZINC, METAL ION, TETRAHEDRAL COORDINATION, NO SECONDARY STRUCTURE, KEYWDS 2 STRUCTURAL ZINC COORDINATION, PROTEIN TRANSPORT EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR B.R.DEMPSEY,M.WRONA,J.M.MOULIN,G.B.GLOOR,F.JALILEHVAND,G.LAJOIE, AUTHOR 2 G.S.SHAW,B.H.SHILTON REVDAT 4 02-MAR-22 1SX0 1 REMARK REVDAT 3 24-FEB-09 1SX0 1 VERSN REVDAT 2 10-AUG-04 1SX0 1 JRNL REVDAT 1 06-JUL-04 1SX0 0 JRNL AUTH B.R.DEMPSEY,M.WRONA,J.M.MOULIN,G.B.GLOOR,F.JALILEHVAND, JRNL AUTH 2 G.LAJOIE,G.S.SHAW,B.H.SHILTON JRNL TITL SOLUTION NMR STRUCTURE AND X-RAY ABSORPTION ANALYSIS OF THE JRNL TITL 2 C-TERMINAL ZINC-BINDING DOMAIN OF THE SECA ATPASE. JRNL REF BIOCHEMISTRY V. 43 9361 2004 JRNL REFN ISSN 0006-2960 JRNL PMID 15260479 JRNL DOI 10.1021/BI0493057 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1, CNS 1.1 REMARK 3 AUTHORS : BRUNGER ET AL. (CNS), BRUNGER ET AL. (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES BASED ON 307 RESTRAINTS, 274 REMARK 3 ARE NOE-DERIVED DISTANCE RESTRAINTS, 33 ARE DIHEDRAL ANGLE REMARK 3 RESTRAINTS. REMARK 4 REMARK 4 1SX0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-04. REMARK 100 THE DEPOSITION ID IS D_1000022055. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298; 298 REMARK 210 PH : 7.0; 7.0 REMARK 210 IONIC STRENGTH : 50MM NACL, 5MM NAN3, 3.4MM REMARK 210 ZNCL2; 50MM NACL, 5MM NAN3, 7MM REMARK 210 ZNCL2 REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 1.7MM SECA ZINC BINDING DOMAIN REMARK 210 NA; 20MM DEUTERATED PIPES BUFFER, REMARK 210 50MM NACL, 5MM NAN3, 0.5MM TCEP, REMARK 210 3.4MM ZNCL2; 3.5MM SECA ZINC REMARK 210 BINDING DOMAIN NA; 20MM REMARK 210 DEUTERATED PIPES BUFFER, 50MM REMARK 210 NACL, 5MM NAN3, 0.5MM TCEP, 7MM REMARK 210 ZNCL2; 1.7MM SECA ZINC BINDING REMARK 210 DOMAIN NA; 20MM DEUTERATED PIPES REMARK 210 BUFFER, 50MM NACL, 5MM NAN3, REMARK 210 0.5MM TCEP, 3.4MM ZNCL2; 3.5MM REMARK 210 SECA ZINC BINDING DOMAIN NA; REMARK 210 20MM DEUTERATED PIPES BUFFER, REMARK 210 50MM NACL, 5MM NAN3, 0.5MM TCEP, REMARK 210 7MM ZNCL2 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : UNITY; INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.1, VNMR 6.1C, REMARK 210 PIPP/STAPP 4.3.3 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 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 STRUCTURE WAS DETERMINED USING STANDARD TWO-DIMENSIONAL 1H REMARK 210 NMR TECHNIQUES. REMARK 210 THIS SET OF STRUCTURES IS THE CALCULATION OF THE INITIAL FOLD OF REMARK 210 THE DOMAIN WITHOUT USING RESTRAINTS FOR ZINC COORDINATION. REMARK 210 A SECOND SET OF STRUCTURES HAS BEEN DEPOSITED THAT IS A REFINEMENT REMARK 210 OF THIS FOLD USING ZINC COORDINATION RESTRAINTS BASED ON EXAFS REMARK 210 DATA FOR THIS DOMAIN. 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 O GLY A 3 H ASP A 6 1.59 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 CYS A 19 -71.40 -150.19 REMARK 500 2 ARG A 4 -29.99 -36.97 REMARK 500 2 SER A 12 -62.44 -90.21 REMARK 500 2 TYR A 16 -70.44 -47.14 REMARK 500 2 CYS A 19 -75.16 -150.32 REMARK 500 3 ARG A 4 -35.46 -32.02 REMARK 500 3 CYS A 8 134.85 -35.35 REMARK 500 3 CYS A 19 -70.35 -119.96 REMARK 500 3 HIS A 20 -74.85 -87.79 REMARK 500 4 ARG A 4 -30.14 -36.38 REMARK 500 4 CYS A 19 -71.47 -150.32 REMARK 500 5 CYS A 8 134.41 -39.19 REMARK 500 5 TYR A 16 -70.09 -48.19 REMARK 500 5 CYS A 19 -74.66 -150.37 REMARK 500 6 LYS A 15 172.86 -58.82 REMARK 500 6 CYS A 19 -71.85 -150.07 REMARK 500 7 CYS A 8 135.27 -39.60 REMARK 500 7 CYS A 19 -120.21 -150.29 REMARK 500 8 CYS A 8 134.48 -39.59 REMARK 500 8 TYR A 16 -71.95 -50.15 REMARK 500 8 CYS A 19 -72.80 -150.33 REMARK 500 9 CYS A 19 -70.10 -150.22 REMARK 500 9 HIS A 20 -86.17 -94.08 REMARK 500 10 SER A 12 -61.46 -90.20 REMARK 500 10 CYS A 19 -70.05 -150.78 REMARK 500 10 HIS A 20 -85.20 -99.65 REMARK 500 11 ARG A 4 -30.61 -36.38 REMARK 500 11 CYS A 19 -69.95 -150.39 REMARK 500 11 HIS A 20 -83.99 -91.08 REMARK 500 12 CYS A 8 134.40 -39.23 REMARK 500 12 CYS A 19 -71.74 -150.05 REMARK 500 13 CYS A 19 -79.20 -123.06 REMARK 500 14 ARG A 4 -34.27 -33.17 REMARK 500 14 CYS A 8 134.55 -34.09 REMARK 500 14 CYS A 19 -69.15 -150.17 REMARK 500 15 ARG A 4 -29.66 -37.68 REMARK 500 15 SER A 12 -73.94 -90.07 REMARK 500 15 LYS A 14 -168.57 -79.99 REMARK 500 15 CYS A 19 -71.25 -150.41 REMARK 500 15 HIS A 20 -84.05 -95.93 REMARK 500 16 ARG A 4 -35.03 -32.53 REMARK 500 16 CYS A 8 134.69 -35.25 REMARK 500 16 CYS A 19 -69.14 -150.33 REMARK 500 17 ARG A 4 -29.99 -37.23 REMARK 500 17 CYS A 19 -70.31 -150.69 REMARK 500 17 HIS A 20 -86.86 -100.24 REMARK 500 18 ARG A 4 -29.46 -37.42 REMARK 500 18 CYS A 19 -70.02 -150.37 REMARK 500 19 CYS A 19 -120.57 -150.20 REMARK 500 20 ARG A 4 -31.01 -35.57 REMARK 500 REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1SX1 RELATED DB: PDB REMARK 900 SOLUTION NMR STRUCTURE AND X-RAY ABSORPTION ANALYSIS OF THE C- REMARK 900 TERMINAL ZINC-BINDING DOMAIN OF THE SECA ATPASE DBREF 1SX0 A 1 22 PDB 1SX0 1SX0 1 22 SEQRES 1 A 22 LYS VAL GLY ARG ASN ASP PRO CYS PRO CYS GLY SER GLY SEQRES 2 A 22 LYS LYS TYR LYS GLN CYS HIS GLY ARG 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 - 2 20 Bytes