Header list of 1haj.pdb file
Complete list - p 30 2 Bytes
HEADER TOXIN/PEPTIDE 05-APR-01 1HAJ
TITLE A BETA-HAIRPIN STRUCTURE IN A 13-MER PEPTIDE THAT BINDS
TITLE 2 A-BUNGAROTOXIN WITH HIGH AFFINITY AND NEUTRALIZES ITS
TITLE 3 TOXICITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-BUNGAROTOXIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LONG NEUROTOXIN 1, BGTX, ALPHA-BTX, A-BTX;
COMPND 5 OTHER_DETAILS: ALPHA-NEUROTOXIN;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PEPTIDE;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: HIGH AFFINITY PEPTIDE;
COMPND 10 OTHER_DETAILS: A CHEMICALLY SYNTHESIZED PEPTIDE THAT
COMPND 11 INHIBITS A-BTX BINDING TO ACHR WITH AN IC50 OF 2 NM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BUNGARUS MULTICINCTUS;
SOURCE 3 ORGANISM_COMMON: MANY-BANDED KRAIT;
SOURCE 4 ORGANISM_TAXID: 8616;
SOURCE 5 SECRETION: VENOM;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 9 ORGANISM_TAXID: 32630;
SOURCE 10 OTHER_DETAILS: MIMOTOPE OF THE NICOTINIC ACETYLCHOLINE
SOURCE 11 RECEPTOR
KEYWDS TOXIN/PEPTIDE, COMPLEX (TOXIN/PEPTIDE), ACETYLCHOLINE
KEYWDS 2 RECEPTOR MIMITOPE, ALPHA-BUNGAROTOXIN, PROTEIN-PEPTIDE
KEYWDS 3 COMPLEX, TOXIN, BETA-HAIRPIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR T.SCHERF,R.KASHER,M.BALASS,M.FRIDKIN,S.FUCHS,
AUTHOR 2 E.KATCHALSKI-KATZIR
REVDAT 4 30-SEP-15 1HAJ 1 SOURCE REMARK VERSN
REVDAT 3 24-FEB-09 1HAJ 1 VERSN
REVDAT 2 16-AUG-01 1HAJ 1 SHEET
REVDAT 1 25-MAY-01 1HAJ 0
JRNL AUTH T.SCHERF,R.KASHER,M.BALASS,M.FRIDKIN,S.FUCHS,
JRNL AUTH 2 E.KATCHALSKI-KATZIR
JRNL TITL A BETA-HAIRPIN STRUCTURE IN A 13-MER PEPTIDE THAT
JRNL TITL 2 BINDS ALPHA-BUNGAROTOXIN WITH HIGH AFFINITY AND
JRNL TITL 3 NEUTRALIZES ITS TOXICITY
JRNL REF PROC.NATL.ACAD.SCI.USA V. 98 6629 2001
JRNL REFN ISSN 0027-8424
JRNL PMID 11381118
JRNL DOI 10.1073/PNAS.111164298
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.KASHER,M.BALASS,T.SCHERF,M.FRIDKIN,S.FUCHS,
REMARK 1 AUTH 2 E.KATCHALSKI-KATZIR
REMARK 1 TITL DESIGN AND SYNTHESIS OF PEPTIDES THAT BIND
REMARK 1 TITL 2 A-BUNGAROTOXIN WITH HIGH AFFINITY
REMARK 1 REF CHEM.BIOL. V. 8 147 2001
REMARK 1 REFN ISSN 1074-5521
REMARK 1 PMID 11251289
REMARK 1 DOI 10.1016/S1074-5521(00)90063-2
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, DELANO, GROS ET AL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RMS DEVIATIONS FROM IDEAL VALUES:
REMARK 3 BOND LENGTH (A) 0.0033,ANGLES (DEG) 0.52 IMPROPERS (DEG) 0.45
REMARK 4
REMARK 4 1HAJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-APR-01.
REMARK 100 THE PDBE ID CODE IS EBI-6053.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM COMPLEX IN 90% WATER,10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY, HOHAHA, DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; DRX800
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR, AURELIA, CNS
REMARK 210 METHOD USED : DISTANCE GEOMETRY,
REMARK 210 DYNAMICAL SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURES WERE DETERMINED USING STANDARD 2D
REMARK 210 1H-NMR SPECTROSCOPY.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1220 ANGSTROM**2
REMARK 350 SURFACE AREA FOR THE COMPLEX: 5530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8 KCAL/MOL
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 400
REMARK 400 COMPOUND
REMARK 400 THE PEPTIDE BINDS ALPHA-BUNGAROTOXIN AND THUS INHIBITS THE
REMARK 400 BINDING OF THE TOXIN TO THE NICOTINIC RECEPTORS.
REMARK 400 THE OBSERVED QUATERNARY STATE IS MONOMERIC IN SOLUTION WHILE
REMARK 400 IN THE CRYSTAL STRUCTURES IT IS OBSERVED TO BE DIMERIC
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 ASP A 30 N PHE A 32 1.97
REMARK 500 O ASP A 30 H PHE A 32 1.39
REMARK 500 H ASP A 30 O GLY A 37 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 ALA A 7 43.40 -90.16
REMARK 500 1 PRO A 18 79.00 -49.73
REMARK 500 1 TRP A 28 122.78 -170.45
REMARK 500 1 CYS A 29 109.98 -58.40
REMARK 500 1 ALA A 31 58.19 -35.64
REMARK 500 1 PHE A 32 23.81 -172.50
REMARK 500 1 CYS A 33 -26.69 -39.40
REMARK 500 1 SER A 35 -80.41 -90.03
REMARK 500 1 ARG A 36 -81.60 -69.37
REMARK 500 1 LYS A 38 105.33 -45.21
REMARK 500 1 LYS A 64 34.56 38.85
REMARK 500 1 ASN A 66 52.72 -114.87
REMARK 500 2 PRO A 18 67.05 -61.06
REMARK 500 2 TRP A 28 121.27 -170.27
REMARK 500 2 ALA A 31 55.53 -36.59
REMARK 500 2 PHE A 32 28.14 -172.95
REMARK 500 2 CYS A 33 -28.12 -37.89
REMARK 500 2 SER A 35 -80.47 -91.32
REMARK 500 2 ARG A 36 -80.79 -69.01
REMARK 500 2 LYS A 38 106.15 -39.85
REMARK 500 2 TYR A 54 -51.36 -178.17
REMARK 500 2 GLU A 55 52.55 -119.30
REMARK 500 2 GLU A 56 -168.81 -160.28
REMARK 500 2 SER A 61 55.79 -111.28
REMARK 500 2 SER B 80 -78.25 -52.76
REMARK 500 3 TRP A 28 124.98 -170.61
REMARK 500 3 CYS A 29 108.93 -42.58
REMARK 500 3 ALA A 31 54.84 -36.05
REMARK 500 3 PHE A 32 26.55 -173.19
REMARK 500 3 CYS A 33 -28.60 -37.66
REMARK 500 3 SER A 35 -74.12 -94.85
REMARK 500 3 ARG A 36 -81.69 -69.16
REMARK 500 3 LYS A 38 104.41 -39.59
REMARK 500 3 PRO A 49 -177.99 -66.78
REMARK 500 3 THR A 62 61.02 -109.18
REMARK 500 3 ASP A 63 -158.10 53.04
REMARK 500 3 LYS A 64 65.41 -61.53
REMARK 500 3 ASN A 66 57.20 -109.89
REMARK 500 3 HIS A 68 137.44 -39.81
REMARK 500 4 PRO A 18 72.79 -58.74
REMARK 500 4 TRP A 28 123.15 -170.60
REMARK 500 4 ALA A 31 66.18 -36.49
REMARK 500 4 PHE A 32 -23.07 -171.22
REMARK 500 4 CYS A 33 -61.14 14.78
REMARK 500 4 SER A 35 -83.27 -85.56
REMARK 500 4 ARG A 36 -80.95 -69.53
REMARK 500 4 LYS A 38 103.84 -45.73
REMARK 500 4 THR A 47 8.65 -162.62
REMARK 500 4 CYS A 48 97.50 -39.62
REMARK 500 4 LYS A 51 35.12 -162.69
REMARK 500
REMARK 500 THIS ENTRY HAS 140 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: KABSCH AND SANDER ALGORITHM
REMARK 700 STRAND: S1A 1; STRANDS S2D & S2E FORM B-HAIRPIN WITHIN THE
REMARK 700 BOUND PEPTIDE, THAT COMBINES TO S2A-S2C TO FORM 5-STRANDED
REMARK 700 INTERMOLECULAR BETA-SHEET.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ABT RELATED DB: PDB
REMARK 900 ALPHA-BUNGAROTOXIN COMPLEXED WITH THE 185 -
REMARK 900 196 FRAGMENT OF THE ALPHA-SUBUNIT OF THE
REMARK 900 TORPEDO NICOTINIC ACETYLCHOLINE RECEPTOR (NMR,
REMARK 900 4 STRUCTURES)
REMARK 900 RELATED ID: 1BXP RELATED DB: PDB
REMARK 900 SOLUTION NMR STRUCTURE OF THE COMPLEX OF
REMARK 900 ALPHA-BUNGAROTOXIN WITH A LIBRARY DERIVED
REMARK 900 PEPTIDE, 20 STRUCTURES
REMARK 900 RELATED ID: 1HAA RELATED DB: PDB
REMARK 900 A BETA-HAIRPIN STRUCTURE IN A 13-MER
REMARK 900 PEPTIDE THAT BINDS A-BUNGAROTOXIN WITH HIGH
REMARK 900 AFFINITY AND NEUTRALIZES ITS TOXICITY
REMARK 900 RELATED ID: 1HN7 RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE COMPLEX BETWEEN A-
REMARK 900 BUNGAROTOXIN AND AMIMOTOPE OF THE NICOTINIC
REMARK 900 ACETILCHOLINE RECEPTOR
REMARK 900 RELATED ID: 1HOY RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE COMPLEX BETWEEN A-
REMARK 900 BUNGAROTOXIN AND AMIMOTOPE OF THE NICOTINIC
REMARK 900 ACETILCHOLINE RECEPTOR
REMARK 900 RELATED ID: 2BTX RELATED DB: PDB
REMARK 900 SOLUTION NMR STRUCTURE OF THE COMPLEX OF
REMARK 900 ALPHA-BUNGAROTOXIN WITH A LIBRARY DERIVED
REMARK 900 PEPTIDE, NMR, MINIMIZED AVERAGE STRUCTURE
DBREF 1HAJ A 1 74 UNP P01378 NXL1_BUNMU 1 74
DBREF 1HAJ B 75 87 PDB 1HAJ 1HAJ 75 87
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 13 TRP ARG TYR TYR GLU SER SER LEU GLU PRO TYR PRO ASP
SHEET 1 S1A 2 VAL A 2 THR A 5 0
SHEET 2 S1A 2 SER A 12 THR A 15 -1 O SER A 12 N THR A 5
SHEET 1 S2B 4 GLU A 56 CYS A 60 0
SHEET 2 S2B 4 LEU A 22 ASP A 30 -1 O CYS A 23 N CYS A 60
SHEET 3 S2B 4 GLY A 37 ALA A 45 -1 O GLY A 37 N ASP A 30
SHEET 4 S2B 4 ARG B 76 TYR B 78 -1 O TYR B 77 N VAL A 40
SHEET 1 S3C 1 PRO B 84 TYR B 85 0
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 2.04
SSBOND 4 CYS A 48 CYS A 59 1555 1555 2.03
SSBOND 5 CYS A 60 CYS A 65 1555 1555 2.03
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 - p 30 2 Bytes