Header list of 1ik8.pdb file
Complete list - 23 202 Bytes
HEADER TOXIN 03-MAY-01 1IK8
TITLE NMR STRUCTURE OF ALPHA-BUNGAROTOXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LONG NEUROTOXIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA-BUNGAROTOXIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BUNGARUS MULTICINCTUS;
SOURCE 3 ORGANISM_COMMON: MANY-BANDED KRAIT;
SOURCE 4 ORGANISM_TAXID: 8616
KEYWDS ALPHA-BUNGAROTOXIN, TOXIN, NICOTINIC-ACETILCHOLINE RECEPTOR
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR N.NICCOLAI,A.CIUTTI,O.SPIGA
REVDAT 4 23-FEB-22 1IK8 1 REMARK
REVDAT 3 24-FEB-09 1IK8 1 VERSN
REVDAT 2 27-FEB-02 1IK8 1 JRNL REMARK
REVDAT 1 16-MAY-01 1IK8 0
JRNL AUTH M.SCARSELLI,O.SPIGA,A.CIUTTI,A.BERNINI,L.BRACCI,B.LELLI,
JRNL AUTH 2 L.LOZZI,D.CALAMANDREI,D.DI MARO,S.KLEIN,N.NICCOLAI
JRNL TITL NMR STRUCTURE OF ALPHA-BUNGAROTOXIN FREE AND BOUND TO A
JRNL TITL 2 MIMOTOPE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR.
JRNL REF BIOCHEMISTRY V. 41 1457 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11814338
JRNL DOI 10.1021/BI011012F
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH O.SPIGA,A.BERNINI,M.SCARSELLI,A.CIUTTI,L.BRACCI,L.LOZZI,
REMARK 1 AUTH 2 B.LELLI,D.DI MARO,D.CALAMANDREI,N.NICCOLAI
REMARK 1 TITL PEPTIDE-PROTEIN INTERACTIONS STUDIED BY SURFACE PLASMON AND
REMARK 1 TITL 2 NUCLEAR MAGNETIC RESONANCES
REMARK 1 REF FEBS LETT. V. 511 33 2002
REMARK 1 REFN ISSN 0014-5793
REMARK 1 DOI 10.1016/S0014-5793(01)03274-4
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, AMBER 4.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), PEARLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1096 RESTRAINTS
REMARK 4
REMARK 4 1IK8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-01.
REMARK 100 THE DEPOSITION ID IS D_1000013359.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.67
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 0.5MM ALPHA-BUNGAROTOXIN; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY
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 : XWINNMR 2.1, NMRVIEW 4.1, DYANA
REMARK 210 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED AVERAGE STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 VAL A 14 OG1 THR A 15 1.42
REMARK 500 SG CYS A 16 CB CYS A 44 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 VAL A 2 CG1 - CB - CG2 ANGL. DEV. = 10.2 DEGREES
REMARK 500 THR A 5 CA - CB - CG2 ANGL. DEV. = -14.9 DEGREES
REMARK 500 ALA A 13 N - CA - CB ANGL. DEV. = 13.3 DEGREES
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 VAL A 2 -103.32 -176.97
REMARK 500 THR A 5 -112.53 -144.42
REMARK 500 THR A 6 -147.99 -72.12
REMARK 500 ALA A 7 76.11 104.20
REMARK 500 THR A 8 58.64 81.81
REMARK 500 SER A 9 -150.62 102.03
REMARK 500 ILE A 11 -152.70 52.86
REMARK 500 SER A 12 39.83 -177.64
REMARK 500 ALA A 13 -35.19 99.74
REMARK 500 VAL A 14 -78.28 3.76
REMARK 500 THR A 15 21.34 107.04
REMARK 500 CYS A 16 -146.78 65.82
REMARK 500 PRO A 17 -144.72 -79.88
REMARK 500 PRO A 18 -113.79 -75.11
REMARK 500 GLU A 20 62.81 65.91
REMARK 500 ASN A 21 146.18 98.82
REMARK 500 LEU A 22 155.23 93.87
REMARK 500 CYS A 23 106.49 -160.46
REMARK 500 MET A 27 166.87 84.30
REMARK 500 TRP A 28 -42.09 161.79
REMARK 500 CYS A 29 62.48 -113.04
REMARK 500 ASP A 30 -79.54 12.04
REMARK 500 ALA A 31 -0.85 174.25
REMARK 500 CYS A 33 46.45 25.53
REMARK 500 SER A 35 -175.41 98.63
REMARK 500 ARG A 36 -135.01 59.74
REMARK 500 LYS A 38 16.83 -146.33
REMARK 500 VAL A 39 77.94 -119.38
REMARK 500 VAL A 40 -167.66 -104.50
REMARK 500 LEU A 42 87.57 -14.18
REMARK 500 CYS A 44 149.14 44.14
REMARK 500 ALA A 45 39.47 -151.84
REMARK 500 ALA A 46 -98.37 131.63
REMARK 500 CYS A 48 88.22 38.38
REMARK 500 SER A 50 -53.54 81.30
REMARK 500 LYS A 51 -133.61 79.08
REMARK 500 PRO A 53 -72.41 -74.97
REMARK 500 TYR A 54 -166.97 33.35
REMARK 500 GLU A 55 -112.33 -19.09
REMARK 500 THR A 58 -158.91 170.66
REMARK 500 CYS A 59 111.70 178.76
REMARK 500 CYS A 60 -159.67 -118.19
REMARK 500 SER A 61 47.63 153.01
REMARK 500 ASP A 63 -33.79 112.86
REMARK 500 LYS A 64 173.19 177.76
REMARK 500 CYS A 65 48.52 158.26
REMARK 500 ASN A 66 52.60 -164.53
REMARK 500 PRO A 67 -142.01 -76.83
REMARK 500 HIS A 68 122.63 163.78
REMARK 500 PRO A 69 -163.35 -75.03
REMARK 500
REMARK 500 THIS ENTRY HAS 53 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 VAL A 2 -11.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HN7 RELATED DB: PDB
REMARK 900 1HN7 CONTAINS THE SAME PROTEIN COMPLEXED WITH A PEPTIDE
REMARK 900 RELATED ID: 1HOY RELATED DB: PDB
REMARK 900 1HOY IS THE NMR STRUCTURE OF THE COMPLEX BETWEEN A-BUNGAROTOXIN AND
REMARK 900 A MIMOTOPE OF THE NICOTINIC ACETILCHOLINE RECEPTOR
DBREF 1IK8 A 1 74 UNP P60615 NXL1A_BUNMU 1 74
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
SHEET 1 A 2 MET A 27 TRP A 28 0
SHEET 2 A 2 VAL A 39 VAL A 40 -1 O VAL A 39 N TRP A 28
SSBOND 1 CYS A 3 CYS A 23 1555 1555 2.09
SSBOND 2 CYS A 16 CYS A 44 1555 1555 2.57
SSBOND 3 CYS A 29 CYS A 33 1555 1555 1.64
SSBOND 4 CYS A 48 CYS A 59 1555 1555 1.55
SSBOND 5 CYS A 60 CYS A 65 1555 1555 2.16
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
Complete list - 23 202 Bytes