Header list of 1lxg.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 05-JUN-02 1LXG TITLE SOLUTION STRUCTURE OF ALPHA-COBRATOXIN COMPLEXED WITH A COGNATE TITLE 2 PEPTIDE (STRUCTURE ENSEMBLE) COMPND MOL_ID: 1; COMPND 2 MOLECULE: LONG NEUROTOXIN 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: NEUROTOXIN 3, ALPHA-COBRATOXIN; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: NAJA KAOUTHIA; SOURCE 3 ORGANISM_COMMON: MONOCLED COBRA; SOURCE 4 ORGANISM_TAXID: 8649; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA; SOURCE 7 ORGANISM_COMMON: PACIFIC ELECTRIC RAY; SOURCE 8 ORGANISM_TAXID: 7787; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PET-31B(+) KEYWDS TOXIN, ALPHA-COBRATOXIN, NICOTINIC ACETYLCHOLINE RECEPTOR, PROTEIN- KEYWDS 2 PROTEIN INTERACTION EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR H.ZENG,E.HAWROT REVDAT 3 23-FEB-22 1LXG 1 REMARK SEQADV REVDAT 2 24-FEB-09 1LXG 1 VERSN REVDAT 1 20-NOV-02 1LXG 0 JRNL AUTH H.ZENG,E.HAWROT JRNL TITL NMR-BASED BINDING SCREEN AND STRUCTURAL ANALYSIS OF THE JRNL TITL 2 COMPLEX FORMED BETWEEN ALPHA-COBRATOXIN AND AN 18-MER JRNL TITL 3 COGNATE PEPTIDE DERIVED FROM THE ALPHA1 SUBUNIT OF THE JRNL TITL 4 NICOTINIC ACETYLCHOLINE RECEPTOR FROM TORPEDO CALIFORNICA JRNL REF J.BIOL.CHEM. V. 277 37439 2002 JRNL REFN ISSN 0021-9258 JRNL PMID 12133834 JRNL DOI 10.1074/JBC.M205483200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.0, CNS 1.1 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, A.T. ET AL. (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1LXG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-02. REMARK 100 THE DEPOSITION ID IS D_1000016378. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 4.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.6 MM ALPHA-COBRATOXIN/ALPHA18 REMARK 210 -MER COMPLEX, ALPHA18-MER IS U- REMARK 210 15N, 50 MM PERDEUTERATED REMARK 210 POTASSIUM ACETATE BUFFER (PH 4.0) REMARK 210 WITH 5% D2O AND 0.05% SODIUM REMARK 210 AZIDE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : HSQC; 3D TOCSY-HSQC; 3D NOESY REMARK 210 -HSQC; HNHA; 2D TOCSY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 1.8, SPARKY 3.95 REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 5 REMARK 210 REMARK 210 REMARK: NULL 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 1-10 REMARK 465 RES C SSSEQI REMARK 465 HSL B 199 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 ARG A 2 39.08 72.68 REMARK 500 1 CYS A 3 -81.13 -60.68 REMARK 500 1 PHE A 4 -85.19 -153.57 REMARK 500 1 ILE A 5 -167.18 -68.38 REMARK 500 1 PRO A 7 -77.69 -55.25 REMARK 500 1 SER A 11 -58.94 78.90 REMARK 500 1 LYS A 12 -164.00 -76.99 REMARK 500 1 ASP A 13 52.56 -158.53 REMARK 500 1 CYS A 14 167.36 53.59 REMARK 500 1 TRP A 25 67.46 -100.24 REMARK 500 1 ASP A 27 -89.82 47.54 REMARK 500 1 CYS A 30 -174.52 49.44 REMARK 500 1 SER A 31 -90.41 -110.71 REMARK 500 1 ILE A 32 -154.52 -81.55 REMARK 500 1 ARG A 33 33.59 -73.32 REMARK 500 1 ASP A 38 58.30 22.56 REMARK 500 1 LEU A 39 -37.98 -30.91 REMARK 500 1 CYS A 41 63.11 93.99 REMARK 500 1 ALA A 42 -154.85 -166.04 REMARK 500 1 CYS A 45 97.42 -43.04 REMARK 500 1 THR A 47 -54.02 156.46 REMARK 500 1 VAL A 48 -148.77 27.35 REMARK 500 1 LYS A 49 -154.77 67.44 REMARK 500 1 THR A 50 91.64 42.75 REMARK 500 1 CYS A 57 139.99 -170.02 REMARK 500 1 THR A 59 -153.56 65.11 REMARK 500 1 ASP A 60 67.79 66.50 REMARK 500 1 ASN A 61 30.09 88.21 REMARK 500 1 PRO A 64 94.96 -43.88 REMARK 500 1 PRO A 66 -73.18 -54.79 REMARK 500 1 ARG A 70 88.79 -164.79 REMARK 500 1 ARG B 182 -89.94 -154.99 REMARK 500 1 VAL B 188 -97.94 -76.65 REMARK 500 1 TYR B 189 158.08 60.39 REMARK 500 1 TYR B 190 -69.94 74.27 REMARK 500 1 THR B 191 118.41 171.44 REMARK 500 1 CYS B 192 -40.86 169.53 REMARK 500 1 PRO B 194 -150.40 -83.81 REMARK 500 1 ASP B 195 132.79 -29.76 REMARK 500 1 THR B 196 -74.50 -81.95 REMARK 500 2 ILE A 5 78.81 46.07 REMARK 500 2 THR A 6 139.37 62.52 REMARK 500 2 PRO A 7 -88.56 -68.72 REMARK 500 2 ILE A 9 -73.42 179.79 REMARK 500 2 THR A 10 -74.81 177.42 REMARK 500 2 ASP A 13 154.47 64.01 REMARK 500 2 ASN A 16 102.82 -55.72 REMARK 500 2 HIS A 18 -66.93 -156.44 REMARK 500 2 TRP A 25 -72.96 -130.02 REMARK 500 2 CYS A 26 38.55 33.18 REMARK 500 REMARK 500 THIS ENTRY HAS 408 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1LXH RELATED DB: PDB REMARK 900 1LXH IS THE MINIMIZED AVERAGE STRUCTURE. DBREF 1LXG A 1 71 UNP P01391 NXL1_NAJKA 1 71 DBREF 1LXG B 181 198 UNP P02710 ACHA_TORCA 205 222 SEQADV 1LXG HSL B 199 UNP P02710 CLONING ARTIFACT SEQRES 1 A 71 ILE ARG CYS PHE ILE THR PRO ASP ILE THR SER LYS ASP SEQRES 2 A 71 CYS PRO ASN GLY HIS VAL CYS TYR THR LYS THR TRP CYS SEQRES 3 A 71 ASP ALA PHE CYS SER ILE ARG GLY LYS ARG VAL ASP LEU SEQRES 4 A 71 GLY CYS ALA ALA THR CYS PRO THR VAL LYS THR GLY VAL SEQRES 5 A 71 ASP ILE GLN CYS CYS SER THR ASP ASN CYS ASN PRO PHE SEQRES 6 A 71 PRO THR ARG LYS ARG PRO SEQRES 1 B 19 TYR ARG GLY TRP LYS HIS TRP VAL TYR TYR THR CYS CYS SEQRES 2 B 19 PRO ASP THR PRO TYR HSL SHEET 1 A 2 CYS A 20 TYR A 21 0 SHEET 2 A 2 CYS A 56 CYS A 57 -1 O CYS A 57 N CYS A 20 SSBOND 1 CYS A 3 CYS A 20 1555 1555 2.03 SSBOND 2 CYS A 14 CYS A 41 1555 1555 2.03 SSBOND 3 CYS A 26 CYS A 30 1555 1555 2.03 SSBOND 4 CYS A 45 CYS A 56 1555 1555 2.03 SSBOND 5 CYS A 57 CYS A 62 1555 1555 2.03 SSBOND 6 CYS B 192 CYS B 193 1555 1555 2.06 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 - b 23 2 Bytes