Header list of 1idh.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 04-APR-01 1IDH TITLE THE NMR SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN ALPHA- TITLE 2 BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-BUNGAROTOXIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: LONG NEUROTOXIN 1; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA CHAIN; COMPND 7 CHAIN: B; COMPND 8 SYNONYM: NACHR-ALPHA1-SUBUNIT; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BUNGARUS MULTICINCTUS; SOURCE 3 ORGANISM_COMMON: MANY-BANDED KRAIT; SOURCE 4 ORGANISM_TAXID: 8616; SOURCE 5 OTHER_DETAILS: PURCHASED FROM SIGMA; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA; SOURCE 8 ORGANISM_COMMON: PACIFIC ELECTRIC RAY; SOURCE 9 ORGANISM_TAXID: 7787; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 11 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 12 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PET-31B(+) KEYWDS ALPHA-BUNGAROTOXIN, NICOTINIC ACETYLCHOLINE RECEPTOR, ALPHA 1 KEYWDS 2 SUBUNIT, PROTEIN-PROTEIN INTERACTION, CATION-PI INTERACTION, TOXIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR H.ZENG,L.MOISE,M.A.GRANT,E.HAWROT REVDAT 7 23-FEB-22 1IDH 1 REMARK REVDAT 6 24-FEB-09 1IDH 1 VERSN REVDAT 5 30-SEP-03 1IDH 1 JRNL DBREF REVDAT 4 21-NOV-01 1IDH 1 ATOM REVDAT 3 14-NOV-01 1IDH 1 REMARK SEQRES SEQADV REVDAT 2 27-JUN-01 1IDH 1 JRNL REVDAT 1 25-APR-01 1IDH 0 JRNL AUTH H.ZENG,L.MOISE,M.A.GRANT,E.HAWROT JRNL TITL THE SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN JRNL TITL 2 ALPHA-BUNGAROTOXIN AND AN 18-MER COGNATE PEPTIDE DERIVED JRNL TITL 3 FROM THE ALPHA 1 SUBUNIT OF THE NICOTINIC ACETYLCHOLINE JRNL TITL 4 RECEPTOR FROM TORPEDO CALIFORNICA. JRNL REF J.BIOL.CHEM. V. 276 22930 2001 JRNL REFN ISSN 0021-9258 JRNL PMID 11312275 JRNL DOI 10.1074/JBC.M102300200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.1, CNSSOLVE 1.0 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, A.T. ET AL. (CNSSOLVE) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1IDH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-APR-01. REMARK 100 THE DEPOSITION ID IS D_1000013181. 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 : 2.1 MM ALPHA REMARK 210 -BUNGAROTOXIN/ALPHA18MER COMPLEX, REMARK 210 ALPHA18MER IS 15N LABELED, 50 REMARK 210 MM PERDEUTERATED POTASSIUM REMARK 210 ACETATE BUFFER (PH 4.0) WITH 5% REMARK 210 D2O AND 0.05% SODIUM AZIDE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_TOCSY; 3D HNHA; REMARK 210 3D_15N-SEPARATED_NOESY; 2D_TOCSY; REMARK 210 2D_NOESY; 2D 1H-15N HSQC 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 : 300 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS REMARK 210 ARE THE 20 STRUCTURES WITH THE REMARK 210 LOWEST ENERGY FROM 120 REMARK 210 ACCEPTABLE STRUCTURES WHICH WERE REMARK 210 FROM 300 TOTAL CALCULATED REMARK 210 STRUCTURES AND HAD NO RESTRAINT REMARK 210 VIOLATIONS. THE BEST REMARK 210 REPRESENTATIVE CONFORMER IS THE REMARK 210 LOWEST POTENTIAL ENERGY REMARK 210 STRUCTURE OF THE ENSEMBLE. REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8 REMARK 210 REMARK 210 REMARK: THE AUTHORS RECOMMEND USING THE GRAPHICS PROGRAM, MOLMOL, REMARK 210 TO VIEW THIS ENSEMBLE OF 20 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: 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 1-20 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 CYS A 3 100.65 -160.31 REMARK 500 1 HIS A 4 120.36 -36.01 REMARK 500 1 THR A 6 -53.97 81.17 REMARK 500 1 ALA A 7 -96.14 58.98 REMARK 500 1 THR A 8 -68.87 62.01 REMARK 500 1 SER A 9 -67.02 -136.28 REMARK 500 1 PRO A 10 -123.88 -77.52 REMARK 500 1 ILE A 11 158.20 179.77 REMARK 500 1 ALA A 13 91.82 -60.39 REMARK 500 1 VAL A 14 -166.54 -72.93 REMARK 500 1 THR A 15 130.32 75.17 REMARK 500 1 ASN A 21 -74.49 -168.38 REMARK 500 1 TYR A 24 -159.25 34.82 REMARK 500 1 ARG A 25 117.17 97.23 REMARK 500 1 LYS A 26 -93.82 -147.98 REMARK 500 1 MET A 27 -164.12 172.15 REMARK 500 1 TRP A 28 -84.53 -133.18 REMARK 500 1 CYS A 29 175.14 54.53 REMARK 500 1 ASP A 30 -76.23 -86.21 REMARK 500 1 ALA A 31 -130.67 -118.10 REMARK 500 1 CYS A 33 -86.19 34.62 REMARK 500 1 SER A 35 -66.41 -152.95 REMARK 500 1 ARG A 36 -155.36 -86.45 REMARK 500 1 LYS A 38 95.33 -39.38 REMARK 500 1 VAL A 39 -151.53 -145.75 REMARK 500 1 LEU A 42 -88.08 -64.46 REMARK 500 1 CYS A 44 144.66 62.79 REMARK 500 1 ALA A 45 -68.78 -147.06 REMARK 500 1 ALA A 46 -37.01 166.14 REMARK 500 1 CYS A 48 52.81 -142.76 REMARK 500 1 SER A 50 -166.91 -61.46 REMARK 500 1 LYS A 51 39.91 177.86 REMARK 500 1 PRO A 53 -89.58 -71.19 REMARK 500 1 GLU A 55 -78.61 -156.07 REMARK 500 1 GLU A 56 -28.36 166.34 REMARK 500 1 THR A 58 -67.42 -122.84 REMARK 500 1 CYS A 59 146.88 178.73 REMARK 500 1 LYS A 64 43.81 179.54 REMARK 500 1 ASN A 66 105.32 -58.52 REMARK 500 1 PRO A 67 -156.16 -73.51 REMARK 500 1 PRO A 69 177.33 -53.47 REMARK 500 1 LYS B 185 158.43 -47.56 REMARK 500 1 TRP B 187 -89.53 -47.24 REMARK 500 1 TYR B 189 -165.75 -100.63 REMARK 500 1 THR B 191 -76.27 -89.62 REMARK 500 1 CYS B 192 170.27 -42.93 REMARK 500 1 PRO B 194 -70.72 -73.10 REMARK 500 1 ASP B 195 -20.69 166.56 REMARK 500 1 PRO B 197 25.13 -64.26 REMARK 500 2 HIS A 4 143.55 -35.07 REMARK 500 REMARK 500 THIS ENTRY HAS 879 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1IDG RELATED DB: PDB REMARK 900 1IDG IS THE AVERAGE STRUCTURE OF THIS ENSEMBLE REMARK 900 RELATED ID: 1IDI RELATED DB: PDB REMARK 900 1IDI IS THE AVERAGE STRUCTURE OF ALPHA-BUNGAROTOXIN REMARK 900 RELATED ID: 1IDL RELATED DB: PDB REMARK 900 1IDL IS 20 ENSEMBLE STRUCTURES OF ALPHA-BUNGAROTOXIN DBREF 1IDH A 1 74 UNP P60615 NXL1A_BUNMU 1 74 DBREF 1IDH B 181 198 UNP P02710 ACHA_TORCA 205 222 SEQADV 1IDH HSL B 199 UNP P02710 CLONING ARTIFACT SEQRES 1 A 74 ILE VAL CYS HIS THR THR ALA THR SER PRO ILE SER ALA SEQRES 2 A 74 VAL THR CYS PRO PRO GLY GLU ASN LEU CYS TYR ARG LYS SEQRES 3 A 74 MET TRP CYS ASP ALA PHE CYS SER SER ARG GLY LYS VAL SEQRES 4 A 74 VAL GLU LEU GLY CYS ALA ALA THR CYS PRO SER LYS LYS SEQRES 5 A 74 PRO TYR GLU GLU VAL THR CYS CYS SER THR ASP LYS CYS SEQRES 6 A 74 ASN PRO HIS PRO LYS GLN ARG PRO GLY 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 SSBOND 1 CYS A 3 CYS A 23 1555 1555 2.03 SSBOND 2 CYS A 16 CYS A 44 1555 1555 2.03 SSBOND 3 CYS A 29 CYS A 33 1555 1555 2.03 SSBOND 4 CYS A 48 CYS A 59 1555 1555 2.03 SSBOND 5 CYS A 60 CYS A 65 1555 1555 2.03 SSBOND 6 CYS B 192 CYS B 193 1555 1555 2.05 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