HEADER TOXIN/PEPTIDE 02-MAY-01 1HC9
TITLE ALPHA-BUNGAROTOXIN COMPLEXED WITH HIGH AFFINITY PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-BUNGAROTOXIN ISOFORM V31;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA-BTX V31, ALPHA-BGT(V31), BGTX V31, LONG NEUROTOXIN 1;
COMPND 5 OTHER_DETAILS: ALPHA-NEUROTOXIN;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ALPHA-BUNGAROTOXIN ISOFORM A31;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: ALPHA-BTX A31, ALPHA-BGT(A31), BGTX A31, LONG NEUROTOXIN 1;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: PEPTIDE INHIBITOR;
COMPND 12 CHAIN: C, D;
COMPND 13 SYNONYM: HIGH AFFINITY PEPTIDE;
COMPND 14 ENGINEERED: YES;
COMPND 15 OTHER_DETAILS: A SYNTHESIZED PEPTIDE MIMICKING ACHR LOOP THAT
COMPND 16 INHIBITS A-BTX BINDING TO ACHR
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 ORGANISM_SCIENTIFIC: BUNGARUS MULTICINCTUS;
SOURCE 8 ORGANISM_COMMON: MANY-BANDED KRAIT;
SOURCE 9 ORGANISM_TAXID: 8616;
SOURCE 10 SECRETION: VENOM;
SOURCE 11 MOL_ID: 3;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 14 ORGANISM_TAXID: 32630;
SOURCE 15 OTHER_DETAILS: MIMOTOPE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR
KEYWDS TOXIN/PEPTIDE, COMPLEX (TOXIN-PEPTIDE), ACETYLCHOLINE RECEPTOR
KEYWDS 2 MIMITOPE, ALPHA-BUNGAROTOXIN, 3- FINGER, PROTEIN-PEPTIDE COMPLEX,
KEYWDS 3 TOXIN, TOXIN-PEPTIDE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HAREL,R.KASHER,J.L.SUSSMAN
REVDAT 7 13-DEC-23 1HC9 1 REMARK SHEET
REVDAT 6 22-MAR-17 1HC9 1 SOURCE
REVDAT 5 19-DEC-12 1HC9 1 JRNL
REVDAT 4 20-JUN-12 1HC9 1 COMPND SOURCE JRNL REMARK
REVDAT 4 2 1 VERSN DBREF SEQADV FORMUL
REVDAT 3 24-FEB-09 1HC9 1 VERSN
REVDAT 2 05-FEB-04 1HC9 1 ATOM
REVDAT 1 10-NOV-01 1HC9 0
JRNL AUTH M.HAREL,R.KASHER,A.NICOLAS,J.M.GUSS,M.BALASS,M.FRIDKIN,
JRNL AUTH 2 A.B.SMIT,K.BREJC,T.K.SIXMA,E.KATCHALSKI-KATZIR,J.L.SUSSMAN,
JRNL AUTH 3 S.FUCHS
JRNL TITL THE BINDING SITE OF ACETYLCHOLINE RECEPTOR AS VISUALIZED IN
JRNL TITL 2 THE X-RAY STRUCTURE OF A COMPLEX BETWEEN ALPHA-BUNGAROTOXIN
JRNL TITL 3 AND A MIMOTOPE PEPTIDE.
JRNL REF NEURON V. 32 265 2001
JRNL REFN ISSN 0896-6273
JRNL PMID 11683996
JRNL DOI 10.1016/S0896-6273(01)00461-5
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.47
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 22236
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2203
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3256
REMARK 3 BIN R VALUE (WORKING SET) : 0.2930
REMARK 3 BIN FREE R VALUE : 0.3210
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 376
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1337
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 217
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.13000
REMARK 3 B22 (A**2) : 2.34000
REMARK 3 B33 (A**2) : -4.46000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.22
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.790
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.300 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.110 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.870 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.740 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 70.30
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES WITH ALTERNATE CONFORMATIONS:
REMARK 3 A12, A48, A50, A52, A56, A59, B34, B56, B71 THE 2 IODIDE IONS I1
REMARK 3 A AND I1 B HAVE OCCUPANCY OF 0.4
REMARK 4
REMARK 4 1HC9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-MAY-01.
REMARK 100 THE DEPOSITION ID IS D_1290006056.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19144
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 23.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : 0.08100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.55500
REMARK 200 R SYM FOR SHELL (I) : 0.59400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1NTN 1-66 RESIDUES
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% PEG 3350, 0.1M PIPES BUFFER PH
REMARK 280 7.5, PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.63150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.63150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 21.02100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 76.67800
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 21.02100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 76.67800
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 36.63150
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 21.02100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 76.67800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 36.63150
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 21.02100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 76.67800
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: COMPLEX OF THE ALPHA-BUNGAROTOXIN AND THE
REMARK 300 PEPTIDE INHIBITOR
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: 1510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 350
REMARK 350 BIOMOLECULE: 2
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: 1480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 MIMICKS BINDING
REMARK 400 OF THE TOXIN TO THE NICOTINIC ACETYLCHOLINE RECEPTOR.
REMARK 400 RESIDUES A31 IS SEEN AS VAL WITH OCCUPANCY 0.3 AND ALA
REMARK 400 WITH OCCUPANCY 0.7, ACCORDING TO A WELL KNOWN MUTATION OF
REMARK 400 ALPHA-BUNGAROTOXIN
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP D 13
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 VAL A 31 CG1 CG2
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 ASP A 30 -164.36 -120.12
REMARK 500 ASP A 30 -164.62 -120.12
REMARK 500 TYR A 54 42.79 -105.79
REMARK 500 ASN A 66 56.49 -114.65
REMARK 500 ASN B 66 57.22 -118.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2002 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH A2015 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH A2021 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH B2005 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH B2006 DISTANCE = 7.65 ANGSTROMS
REMARK 525 HOH B2008 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH B2009 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH D2002 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH D2003 DISTANCE = 6.94 ANGSTROMS
REMARK 525 HOH D2012 DISTANCE = 6.21 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 1075
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 1075
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ABT RELATED DB: PDB
REMARK 900 ALPHA-BUNGAROTOXIN COMPLEXED WITH THE 185 - 196 FRAGMENT OF THE
REMARK 900 ALPHA-SUBUNIT OF THE 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 ALPHA-BUNGAROTOXIN WITH A
REMARK 900 LIBRARY DERIVED PEPTIDE, 20 STRUCTURES
REMARK 900 RELATED ID: 1HAA RELATED DB: PDB
REMARK 900 A BETA-HAIRPIN STRUCTURE IN A 13-MER PEPTIDE THAT BINDS A-
REMARK 900 BUNGAROTOXIN WITH HIGH AFFINITY AND NEUTRALIZES ITS TOXICITY
REMARK 900 RELATED ID: 1HAJ RELATED DB: PDB
REMARK 900 A BETA-HAIRPIN STRUCTURE IN A 13-MER PEPTIDE THAT BINDS A-
REMARK 900 BUNGAROTOXIN WITH HIGH AFFINITY AND NEUTRALIZES ITS TOXICITY
REMARK 900 RELATED ID: 1HN7 RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE COMPLEX BETWEEN A-BUNGAROTOXIN AND AMIMOTOPE
REMARK 900 OF THE NICOTINIC ACETILCHOLINE RECEPTOR
REMARK 900 RELATED ID: 1HOY RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE COMPLEX BETWEEN A-BUNGAROTOXIN AND AMIMOTOPE
REMARK 900 OF THE NICOTINIC ACETILCHOLINE RECEPTOR
REMARK 900 RELATED ID: 1IDG RELATED DB: PDB
REMARK 900 THE NMR SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN ALPHA-
REMARK 900 BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDE
REMARK 900 RELATED ID: 1IDH RELATED DB: PDB
REMARK 900 THE NMR SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN ALPHA-
REMARK 900 BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDE
REMARK 900 RELATED ID: 1IDI RELATED DB: PDB
REMARK 900 THE NMR SOLUTION STRUCTURE OF ALPHA-BUNGAROTOXIN
REMARK 900 RELATED ID: 1IDL RELATED DB: PDB
REMARK 900 THE NMR SOLUTION STRUCTURE OF ALPHA-BUNGAROTOXIN
REMARK 900 RELATED ID: 2BTX RELATED DB: PDB
REMARK 900 SOLUTION NMR STRUCTURE OF THE COMPLEX OF ALPHA-BUNGAROTOXIN WITH A
REMARK 900 LIBRARY DERIVED PEPTIDE, NMR, MINIMIZED AVERAGE STRUCTURE
DBREF 1HC9 A 1 74 UNP P60616 NXL1V_BUNMU 22 95
DBREF 1HC9 B 1 74 UNP P60615 NXL1A_BUNMU 22 95
DBREF 1HC9 C 1 13 PDB 1HC9 1HC9 1 13
DBREF 1HC9 D 1 13 PDB 1HC9 1HC9 1 13
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 VAL 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 74 ILE VAL CYS HIS THR THR ALA THR SER PRO ILE SER ALA
SEQRES 2 B 74 VAL THR CYS PRO PRO GLY GLU ASN LEU CYS TYR ARG LYS
SEQRES 3 B 74 MET TRP CYS ASP ALA PHE CYS SER SER ARG GLY LYS VAL
SEQRES 4 B 74 VAL GLU LEU GLY CYS ALA ALA THR CYS PRO SER LYS LYS
SEQRES 5 B 74 PRO TYR GLU GLU VAL THR CYS CYS SER THR ASP LYS CYS
SEQRES 6 B 74 ASN PRO HIS PRO LYS GLN ARG PRO GLY
SEQRES 1 C 13 TRP ARG TYR TYR GLU SER SER LEU LEU PRO TYR PRO ASP
SEQRES 1 D 13 TRP ARG TYR TYR GLU SER SER LEU LEU PRO TYR PRO ASP
HET IOD A1075 1
HET IOD B1075 1
HETNAM IOD IODIDE ION
FORMUL 5 IOD 2(I 1-)
FORMUL 7 HOH *217(H2 O)
HELIX 1 1 PHE A 32 GLY A 37 1 6
HELIX 2 2 PHE B 32 GLY B 37 1 6
SHEET 1 AA 2 VAL A 2 THR A 5 0
SHEET 2 AA 2 SER A 12 THR A 15 -1 O SER A 12 N THR A 5
SHEET 1 AB 3 GLU A 56 CYS A 60 0
SHEET 2 AB 3 LEU A 22 TRP A 28 -1 O CYS A 23 N CYS A 60
SHEET 3 AB 3 VAL A 39 ALA A 45 -1 O VAL A 39 N TRP A 28
SHEET 1 CB 2 ARG C 2 TYR C 4 0
SHEET 2 CB 2 SER C 7 TYR C 11 -1 O SER C 7 N TYR C 4
SHEET 1 BA 2 VAL B 2 THR B 5 0
SHEET 2 BA 2 SER B 12 THR B 15 -1 O SER B 12 N THR B 5
SHEET 1 BB 3 GLU B 56 CYS B 60 0
SHEET 2 BB 3 LEU B 22 TRP B 28 -1 O CYS B 23 N CYS B 60
SHEET 3 BB 3 VAL B 39 ALA B 45 -1 O VAL B 39 N TRP B 28
SHEET 1 DB 1 TYR D 3 TYR D 4 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 2.03
SSBOND 4 CYS A 48 CYS A 59 1555 1555 2.48
SSBOND 5 CYS A 59 CYS A 59 1555 3655 1.90
SSBOND 6 CYS A 60 CYS A 65 1555 1555 2.03
SSBOND 7 CYS B 3 CYS B 23 1555 1555 2.02
SSBOND 8 CYS B 16 CYS B 44 1555 1555 2.03
SSBOND 9 CYS B 29 CYS B 33 1555 1555 2.04
SSBOND 10 CYS B 48 CYS B 59 1555 1555 2.03
SSBOND 11 CYS B 60 CYS B 65 1555 1555 2.02
CISPEP 1 SER A 9 PRO A 10 0 0.06
CISPEP 2 SER B 9 PRO B 10 0 -0.07
SITE 1 AC1 3 ARG A 25 THR A 58 HOH A2081
SITE 1 AC2 4 ARG B 25 MET B 27 GLU B 56 THR B 58
CRYST1 42.042 153.356 73.263 90.00 90.00 90.00 C 2 2 21 16
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 0.023786 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006521 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013649 0.00000
(ATOM LINES ARE NOT SHOWN.)
END