Header list of 1kc4.pdb file
Complete list - t 27 2 Bytes
HEADER TOXIN 07-NOV-01 1KC4
TITLE NMR STRUCTURAL ANALYSIS OF THE COMPLEX FORMED BETWEEN ALPHA-
TITLE 2 BUNGAROTOXIN AND THE PRINCIPAL ALPHA-NEUROTOXIN BINDING SEQUENCE ON
TITLE 3 THE ALPHA7 SUBUNIT OF A NEURONAL NICOTINIC ACETYLCHOLINE RECEPTOR
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: NEURONAL ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA-7 CHAIN;
COMPND 7 CHAIN: B;
COMPND 8 FRAGMENT: ALPHA-NEUROTOXIN BINDING SITE;
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 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 7 ORGANISM_COMMON: CHICKEN;
SOURCE 8 ORGANISM_TAXID: 9031;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BLR(DE3)PLYSS;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PET31B(+)
KEYWDS ALPHA-BUNGAROTOXIN, NICOTINIC ACETYLCHOLINE RECEPTOR ALPHA 7 SUBUNIT,
KEYWDS 2 ALPHA-NEUROTOXIN, LIGAND-GATED ION CHANNELS, PROTEIN-PROTEIN
KEYWDS 3 INTERACTIONS, PROTEIN-PEPTIDE COMPLEX, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR L.MOISE,A.PISERCHIO,V.J.BASUS,E.HAWROT
REVDAT 4 27-OCT-21 1KC4 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1KC4 1 VERSN
REVDAT 2 17-APR-02 1KC4 1 JRNL
REVDAT 1 13-MAR-02 1KC4 0
JRNL AUTH L.MOISE,A.PISERCHIO,V.J.BASUS,E.HAWROT
JRNL TITL NMR STRUCTURAL ANALYSIS OF ALPHA-BUNGAROTOXIN AND ITS
JRNL TITL 2 COMPLEX WITH THE PRINCIPAL ALPHA-NEUROTOXIN-BINDING SEQUENCE
JRNL TITL 3 ON THE ALPHA 7 SUBUNIT OF A NEURONAL NICOTINIC ACETYLCHOLINE
JRNL TITL 4 RECEPTOR.
JRNL REF J.BIOL.CHEM. V. 277 12406 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11790782
JRNL DOI 10.1074/JBC.M110320200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.M.LEVANDOSKI,Y.LIN,L.MOISE,J.T.MCLAUGHLIN,E.COOPER,
REMARK 1 AUTH 2 E.HAWROT
REMARK 1 TITL CHIMERIC ANALYSIS OF A NEURONAL NICOTINIC ACETYLCHOLINE
REMARK 1 TITL 2 RECEPTOR REVEALS AMINO ACIDS CONFERRING SENSITIVITY TO
REMARK 1 TITL 3 ALPHA-BUNGAROTOXIN.
REMARK 1 REF J.BIOL.CHEM. V. 274 26113 1999
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.274.37.26113
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.E.MCLANE,X.D.WU,R.SCHOEPFER,J.M.LINDSTROM,
REMARK 1 AUTH 2 B.M.CONTI-TRONCONI
REMARK 1 TITL IDENTIFICATION OF SEQUENCE SEGMENTS FORMING THE
REMARK 1 TITL 2 ALPHA-BUNGAROTOXIN BINDING SITES ON TWO NICOTINIC
REMARK 1 TITL 3 ACETYLCHOLINE RECEPTOR ALPHA SUBUNITS FROM THE AVIAN BRAIN.
REMARK 1 REF J.BIOL.CHEM. V. 266 15230 1991
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
REMARK 1 AUTH V.J.BASUS,M.BILLETER,R.A.LOVE,R.M.STROUD,I.D.KUNTZ
REMARK 1 TITL STRUCTURAL STUDIES OF ALPHA-BUNGAROTOXIN. 1.
REMARK 1 TITL 2 SEQUENCE-SPECIFIC 1H NMR RESONANCE ASSIGNMENTS.
REMARK 1 REF BIOCHEMISTRY V. 27 2763 1988
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, CNS 1.0
REMARK 3 AUTHORS : BRUNGER, A.T., ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RMS DEVIATIONS FROM IDEAL VALUES: BOND
REMARK 3 LENGTH(A) 0.0039, ANGLES(DEG) 0.61, IMPROPERS(DEG) 0.53
REMARK 4
REMARK 4 1KC4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014797.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.6 MM ALPHA-BUNGAROTOXIN/[U
REMARK 210 -15N]-ALPHA 7 19MER COMPLEX 30
REMARK 210 MM SODIUM PHOSPHATE, PH 5.5 50
REMARK 210 MICROMOLAR SODIUM AZIDE 50
REMARK 210 MICROMOLAR TMSP; 1.6 MM ALPHA-
REMARK 210 BUNGAROTOXIN/[U-15N]-ALPHA 7
REMARK 210 19MER COMPLEX 30 MM SODIUM
REMARK 210 PHOSPHATE, PH 5.5 50 MICROMOLAR
REMARK 210 SODIUM AZIDE 50 MICROMOLAR TMSP
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_TOCSY; 2D 1H-15N HSQC;
REMARK 210 HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 400 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 3.87
REMARK 210 METHOD USED : DISTANCE GEOMETRY DYNAMICAL
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE THE 10 WITH THE LOWEST
REMARK 210 ENERGY FROM A POOL OF OVER 100
REMARK 210 ACCEPTED STRUCTURES THAT HAD NO
REMARK 210 RESTRAINT VIOLATIONS.
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE WELL-DEFINED REGIONS IN THE COMPLEX, EXHIBITING
REMARK 210 EXTENSIVE LONG RANGE NOES, ARE: BGTX: 1-16, 22-28, 39-48, AND 54-
REMARK 210 68 ALPHA 7 19MER: 185-194
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 197
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 LYS B 191 H TYR B 194 1.52
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 HIS A 4 166.57 -45.45
REMARK 500 1 ALA A 7 45.14 76.08
REMARK 500 1 SER A 9 -61.05 -177.47
REMARK 500 1 ILE A 11 106.98 -53.71
REMARK 500 1 ALA A 13 125.54 82.82
REMARK 500 1 CYS A 16 65.23 -160.23
REMARK 500 1 PRO A 17 49.10 -105.14
REMARK 500 1 ASN A 21 67.02 -159.81
REMARK 500 1 LEU A 22 -174.40 -66.90
REMARK 500 1 CYS A 29 -55.64 -144.38
REMARK 500 1 ASP A 30 149.95 62.43
REMARK 500 1 ALA A 31 68.80 75.78
REMARK 500 1 PHE A 32 88.87 53.04
REMARK 500 1 CYS A 33 21.42 -143.98
REMARK 500 1 SER A 34 -99.33 179.47
REMARK 500 1 SER A 35 -56.44 -141.45
REMARK 500 1 ARG A 36 51.85 -92.11
REMARK 500 1 VAL A 40 50.86 -161.56
REMARK 500 1 GLU A 41 85.67 -62.74
REMARK 500 1 LEU A 42 178.69 -58.04
REMARK 500 1 CYS A 48 60.46 -112.98
REMARK 500 1 PRO A 49 -170.64 -49.36
REMARK 500 1 SER A 50 131.98 -176.60
REMARK 500 1 LYS A 51 -159.80 -176.14
REMARK 500 1 LYS A 52 75.37 -105.24
REMARK 500 1 TYR A 54 -0.06 66.85
REMARK 500 1 GLU A 55 86.82 154.90
REMARK 500 1 GLU A 56 -150.80 -161.16
REMARK 500 1 CYS A 60 102.36 175.32
REMARK 500 1 SER A 61 -143.13 -78.87
REMARK 500 1 THR A 62 -88.85 81.82
REMARK 500 1 ASP A 63 136.93 175.09
REMARK 500 1 HIS A 68 -57.62 104.71
REMARK 500 1 LYS B 181 85.52 -157.66
REMARK 500 1 THR B 183 71.19 -160.13
REMARK 500 1 GLU B 184 -72.24 -107.93
REMARK 500 1 TYR B 187 -147.20 -126.34
REMARK 500 1 CYS B 189 -25.86 170.62
REMARK 500 1 CYS B 190 20.67 -146.63
REMARK 500 1 TYR B 194 -77.56 15.15
REMARK 500 1 PRO B 195 99.16 -55.40
REMARK 500 2 HIS A 4 166.74 -49.98
REMARK 500 2 THR A 5 -55.24 -164.94
REMARK 500 2 THR A 6 75.24 -35.08
REMARK 500 2 SER A 9 -63.72 -173.11
REMARK 500 2 SER A 12 -152.37 -123.61
REMARK 500 2 PRO A 17 164.08 -42.92
REMARK 500 2 CYS A 29 -58.95 138.41
REMARK 500 2 ASP A 30 -169.85 46.23
REMARK 500 2 ALA A 31 -72.10 68.37
REMARK 500
REMARK 500 THIS ENTRY HAS 413 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ABT RELATED DB: PDB
REMARK 900 1ABT IS ALPHA-BUNGAROTOXIN COMPLEXED WITH THE 185 - 196 FRAGMENT OF
REMARK 900 THE -SUBUNIT OF THE TORPEDO NICOTINIC ACETYLCHOLINE RECEPTOR (NMR,
REMARK 900 4 STRUCTURES)
REMARK 900 RELATED ID: 1IDH RELATED DB: PDB
REMARK 900 1IDH IS THE NMR SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN
REMARK 900 ALPHA-BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDE
REMARK 900 RELATED ID: 2ABX RELATED DB: PDB
REMARK 900 1ABX IS THE CRYSTAL STRUCTURE OF ALPHA-BUNGAROTOXIN AT 2.5 A
REMARK 900 RESOLUTION: RELATION TO SOLUTION STRUCTURE AND BINDING TO
REMARK 900 ACETYLCHOLINE RECEPTOR.
REMARK 900 RELATED ID: 1I9B RELATED DB: PDB
REMARK 900 1I9B IS THE X-RAY STRUCTURE OF ACETYLCHOLINE BINDING PROTEIN (ACHBP)
REMARK 900 RELATED ID: 1HAJ RELATED DB: PDB
REMARK 900 1HAJ IS 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: 1HC9 RELATED DB: PDB
REMARK 900 1HC9 IS A-BUNGAROTOXIN COMPLEXED WITH HIGH AFFINITY PEPTIDE.
REMARK 900 RELATED ID: 1BXP RELATED DB: PDB
REMARK 900 1BXP IS THE SOLUTION NMR STRUCTURE OF THE COMPLEX OF ALPHA-
REMARK 900 BUNGAROTOXIN WITH A LIBRARY DERIVED PEPTIDE, 20 STRUCTURES.
REMARK 900 RELATED ID: 1JBD RELATED DB: PDB
REMARK 900 1JBD IS THE NMR STRUCTURE OF THE COMPLEX BETWEEN ALPHA-BUNGAROTOXIN
REMARK 900 AND A MIMOTOPE OF THE NICOTINIC ACETILCHOLINE RECEPTOR.
REMARK 900 RELATED ID: 1IKC RELATED DB: PDB
REMARK 900 1IKC IS THE NMR STRUCTURE OF ALPHA-BUNGAROTOXIN.
REMARK 900 RELATED ID: 1KFH RELATED DB: PDB
REMARK 900 1KFH IS THE SOLUTION STRUCTURE OF ALPHA-BUNGAROTOXIN BY NMR
REMARK 900 SPECTROSCOPY.
REMARK 900 RELATED ID: 1KL8 RELATED DB: PDB
REMARK 900 1KL8 IS THE NMR STRUCTURAL ANALYSIS OF THE COMPLEX FORMED BETWEEN
REMARK 900 ALPHA-BUNGAROTOXIN AND THE PRINCIPAL ALPHA-NEUROTOXIN BINDING
REMARK 900 SEQUENCE ON THE ALPHA7 SUBUNIT OF A NEURONAL NICOTINIC
REMARK 900 ACETYLCHOLINE RECEPTOR
DBREF 1KC4 A 1 74 UNP P60615 NXL1A_BUNMU 1 74
DBREF 1KC4 B 178 196 UNP P22770 ACHA7_CHICK 201 219
SEQADV 1KC4 HSL B 197 UNP P22770 ENGINEERED MUTATION
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 20 ILE PRO GLY LYS ARG THR GLU SER PHE TYR GLU CYS CYS
SEQRES 2 B 20 LYS GLU PRO TYR PRO ASP HSL
SHEET 1 A 3 GLU A 41 ALA A 45 0
SHEET 2 A 3 LEU A 22 LYS A 26 -1 N LEU A 22 O ALA A 45
SHEET 3 A 3 VAL A 57 THR A 58 -1 O THR A 58 N ARG A 25
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 189 CYS B 190 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
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