Header list of 1ljz.pdb file
Complete list - l 24 2 Bytes
HEADER RECEPTOR, TOXIN 23-APR-02 1LJZ
TITLE NMR STRUCTURE OF AN ACHR-PEPTIDE (TORPEDO CALIFORNICA, ALPHA-SUBUNIT
TITLE 2 RESIDUES 182-202) IN COMPLEX WITH ALPHA-BUNGAROTOXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-BUNGAROTOXIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LONG NEUROTOXIN 1, ALPHA-BTX, BGTX;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ACETYLCHOLINE RECEPTOR PROTEIN;
COMPND 7 CHAIN: B;
COMPND 8 FRAGMENT: ACETYLCHOLINE RECEPTOR PEPTIDE (RESIDUES 182-202);
COMPND 9 SYNONYM: ACHR;
COMPND 10 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 STRAIN: BANDED KRAIT;
SOURCE 6 SECRETION: VENOM;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 OTHER_DETAILS: SYNTHESIZED PEPTIDE
KEYWDS BUNGAROTOXIN, ACETYLCHOLINE RECEPTOR, BETA-HAIRPIN, INTERMOLECULAR
KEYWDS 2 BETA-SHEET, RECEPTOR, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 19
AUTHOR A.O.SAMSON,T.SCHERF,M.EISENSTEIN,J.H.CHILL,J.ANGLISTER
REVDAT 4 24-JUL-13 1LJZ 1 ATOM VERSN
REVDAT 3 24-FEB-09 1LJZ 1 VERSN
REVDAT 2 29-JUL-03 1LJZ 1 JRNL
REVDAT 1 17-JUL-02 1LJZ 0
JRNL AUTH A.SAMSON,T.SCHERF,M.EISENSTEIN,J.CHILL,J.ANGLISTER
JRNL TITL THE MECHANISM FOR ACETYLCHOLINE RECEPTOR INHIBITION BY
JRNL TITL 2 ALPHA-NEUROTOXINS AND SPECIES-SPECIFIC RESISTANCE TO
JRNL TITL 3 ALPHA-BUNGAROTOXIN REVEALED BY NMR.
JRNL REF NEURON V. 35 319 2002
JRNL REFN ISSN 0896-6273
JRNL PMID 12160749
JRNL DOI 10.1016/S0896-6273(02)00773-0
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LJZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-02.
REMARK 100 THE RCSB ID CODE IS RCSB016012.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 4; 4
REMARK 210 IONIC STRENGTH : 50 MM NH4AC; 50 MM NH4AC
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : ACETYLCHOLINE RECEPTOR PEPTIDE/
REMARK 210 ALPHA-BUNGAROTOXIN; ACETYLCHOLINE
REMARK 210 RECEPTOR PEPTIDE/ALPHA-
REMARK 210 BUNGAROTOXIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1, XWINNMR 3, AURELIA 2.8.11
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 19
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES
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 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 ALA A 31 H SER A 35 1.59
REMARK 500 O ALA A 31 N SER A 35 2.03
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 ALA A 7 -48.25 -130.69
REMARK 500 1 THR A 8 -136.52 -90.35
REMARK 500 1 PRO A 18 -167.58 -51.95
REMARK 500 1 TRP A 28 -149.26 -145.25
REMARK 500 1 ALA A 31 -11.91 96.57
REMARK 500 1 SER A 34 -80.00 -91.80
REMARK 500 1 SER A 35 -52.54 -141.06
REMARK 500 1 ARG A 36 -91.47 -79.31
REMARK 500 1 TYR A 54 -32.32 177.92
REMARK 500 1 SER A 61 63.01 -109.33
REMARK 500 1 ASN A 66 59.82 -105.13
REMARK 500 1 PRO A 73 88.43 -54.51
REMARK 500 1 TRP B 184 -162.22 -119.45
REMARK 500 1 CYS B 192 -46.38 157.82
REMARK 500 1 THR B 196 50.43 -140.09
REMARK 500 1 GLU B 203 -76.20 -69.89
REMARK 500 2 ALA A 7 122.06 75.54
REMARK 500 2 THR A 8 -26.17 -38.27
REMARK 500 2 SER A 9 -101.90 -102.09
REMARK 500 2 VAL A 14 -166.70 -108.00
REMARK 500 2 PRO A 18 -161.96 -65.21
REMARK 500 2 ARG A 25 77.41 -116.37
REMARK 500 2 TRP A 28 -135.47 -153.39
REMARK 500 2 ALA A 31 -23.25 93.12
REMARK 500 2 SER A 34 -78.72 -91.29
REMARK 500 2 SER A 35 -49.85 -142.03
REMARK 500 2 ARG A 36 -91.40 -75.62
REMARK 500 2 CYS A 48 133.96 -39.45
REMARK 500 2 LYS A 64 42.90 39.69
REMARK 500 2 ASN A 66 54.61 -110.02
REMARK 500 2 ARG B 182 61.35 -107.26
REMARK 500 2 TRP B 184 -169.58 -106.39
REMARK 500 2 VAL B 188 88.72 -162.54
REMARK 500 2 CYS B 192 -47.05 152.58
REMARK 500 2 ASP B 195 44.85 -96.43
REMARK 500 2 ILE B 201 -164.95 -113.90
REMARK 500 2 GLU B 203 -79.37 -115.49
REMARK 500 3 THR A 5 149.48 -171.23
REMARK 500 3 ALA A 7 -52.45 -148.27
REMARK 500 3 THR A 8 -148.78 -68.88
REMARK 500 3 PRO A 18 -161.99 -61.89
REMARK 500 3 ASN A 21 17.16 -150.38
REMARK 500 3 TRP A 28 -159.11 -142.37
REMARK 500 3 ALA A 31 -28.42 93.73
REMARK 500 3 SER A 34 -77.68 -91.45
REMARK 500 3 SER A 35 -51.63 -141.40
REMARK 500 3 ARG A 36 -91.46 -74.89
REMARK 500 3 THR A 47 59.61 -156.82
REMARK 500 3 CYS A 48 98.36 -39.82
REMARK 500 3 PRO A 49 -163.36 -63.50
REMARK 500
REMARK 500 THIS ENTRY HAS 405 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1L4W RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF AN ACHR-PEPTIDE (TORPEDO CALIFORNICA,
REMARK 900 ALPHA-SUBUNIT RESIDUES 182-202) IN COMPLEX WITH ALPHA-
REMARK 900 BUNGAROTOXIN
DBREF 1LJZ A 1 74 UNP P60615 NXL1A_BUNMU 1 74
DBREF 1LJZ B 182 202 UNP P02711 ACHA_TORMA 206 226
SEQADV 1LJZ GLU B 180 UNP P02711 INSERTION
SEQADV 1LJZ GLU B 181 UNP P02711 INSERTION
SEQADV 1LJZ GLU B 203 UNP P02711 INSERTION
SEQADV 1LJZ GLU B 204 UNP P02711 INSERTION
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 25 GLU GLU ARG GLY TRP LYS HIS TRP VAL TYR TYR THR CYS
SEQRES 2 B 25 CYS PRO ASP THR PRO TYR LEU ASP ILE THR GLU GLU
SHEET 1 A 2 HIS A 4 THR A 5 0
SHEET 2 A 2 SER A 12 ALA A 13 -1 O SER A 12 N THR A 5
SHEET 1 B 3 GLU A 41 ALA A 45 0
SHEET 2 B 3 LEU A 22 MET A 27 -1 N LEU A 22 O ALA A 45
SHEET 3 B 3 GLU A 56 CYS A 60 -1 O CYS A 60 N CYS A 23
SHEET 1 C 2 CYS A 29 ASP A 30 0
SHEET 2 C 2 GLY A 37 LYS A 38 -1 O GLY A 37 N ASP A 30
SHEET 1 D 2 HIS B 186 VAL B 188 0
SHEET 2 D 2 TYR B 198 ASP B 200 -1 O ASP B 200 N HIS B 186
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 - l 24 2 Bytes