Header list of 1bxp.pdb file
Complete list - b 16 2 Bytes
HEADER COMPLEX (TOXIN/PEPTIDE) 23-AUG-98 1BXP
TITLE SOLUTION NMR STRUCTURE OF THE COMPLEX OF ALPHA-BUNGAROTOXIN WITH A
TITLE 2 LIBRARY DERIVED PEPTIDE, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-BUNGAROTOXIN;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: PEPTIDE MET-ARG-TYR-TYR-GLU-SER-SER-LEU-LYS-SER-TYR-PRO-
COMPND 6 ASP;
COMPND 7 CHAIN: B;
COMPND 8 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 SECRETION: VENOM;
SOURCE 6 MOL_ID: 2
KEYWDS COMPLEX (TOXIN-PEPTIDE), ALPHA-BUNGAROTOXIN, LIBRARY PEPTIDE, COMPLEX
KEYWDS 2 (TOXIN-PEPTIDE) COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.SCHERF,M.BALASS,S.FUCHS,E.KATCHALSKI-KATZIR,J.ANGLISTER
REVDAT 5 16-FEB-22 1BXP 1 REMARK
REVDAT 4 24-FEB-09 1BXP 1 VERSN
REVDAT 3 30-SEP-03 1BXP 1 DBREF
REVDAT 2 16-FEB-99 1BXP 1 SOURCE COMPND REMARK TITLE
REVDAT 2 2 1 KEYWDS HEADER
REVDAT 1 27-JAN-99 1BXP 0
JRNL AUTH T.SCHERF,M.BALASS,S.FUCHS,E.KATCHALSKI-KATZIR,J.ANGLISTER
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE COMPLEX OF
JRNL TITL 2 ALPHA-BUNGAROTOXIN WITH A LIBRARY-DERIVED PEPTIDE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 94 6059 1997
JRNL REFN ISSN 0027-8424
JRNL PMID 9177168
JRNL DOI 10.1073/PNAS.94.12.6059
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.BALASS,E.KATCHALSKI-KATZIR,S.FUCHS
REMARK 1 TITL THE ALPHA-BUNGAROTOXIN BINDING SITE ON THE NICOTINIC
REMARK 1 TITL 2 ACETYLCHOLINE RECEPTOR: ANALYSIS USING A PHAGE-EPITOPE
REMARK 1 TITL 3 LIBRARY
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 94 6054 1997
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DETAILS OF THE STRUCTURE DETERMINATION
REMARK 3 AND ALL STRUCTURAL STATISTICS ARE GIVEN IN THE PAPER CITED ON *
REMARK 3 JRNL* RECORDS ABOVE. THE STRUCTURES ARE BASED ON 941
REMARK 3 INTRAMOLECULAR CONSTRAINTS WITHIN THE BOUND TOXIN (INCLUDING 291
REMARK 3 LONG-RANGE INTERACTIONS), 98 INTRAPEPTIDE INTERACTIONS
REMARK 3 (INCLUDING 7 LONG-RANGE INTERACTIONS), AND 62 INTERMOLECULAR
REMARK 3 CONSTRAINTS BETWEEN THE BUNGAROTOXIN AND THE 13-RESIDUE PEPTIDE
REMARK 3 USED IN THIS STUDY (LISTED HERE AS RESIDUES 75 B - 87 B).
REMARK 4
REMARK 4 1BXP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172137.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; DQF-COSY; TOCSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AM500; DMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY/ DYNAMICAL
REMARK 210 SIMMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO NOE VIOLATIONS,OVERALL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 2D 1H-NMR
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: 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 SER A 9 -59.50 -171.19
REMARK 500 1 PRO A 10 -96.15 -100.15
REMARK 500 1 ILE A 11 121.25 166.18
REMARK 500 1 LEU A 22 -154.62 -162.32
REMARK 500 1 TRP A 28 -96.13 -168.88
REMARK 500 1 CYS A 29 143.82 -172.90
REMARK 500 1 ASP A 30 -158.45 -90.67
REMARK 500 1 CYS A 33 94.87 -42.99
REMARK 500 1 LYS A 38 -146.88 -91.39
REMARK 500 1 VAL A 39 -149.36 -114.15
REMARK 500 1 VAL A 40 84.28 -156.85
REMARK 500 1 THR A 47 138.83 -170.27
REMARK 500 1 CYS A 48 97.03 -39.69
REMARK 500 1 SER A 50 119.36 53.98
REMARK 500 1 LYS A 51 47.97 -172.32
REMARK 500 1 PRO A 53 -90.85 -86.30
REMARK 500 1 CYS A 60 119.83 -172.40
REMARK 500 1 ASP A 63 95.19 -45.09
REMARK 500 1 LYS A 70 -81.76 -99.40
REMARK 500 1 ARG A 72 101.12 -41.22
REMARK 500 1 TYR B 3 58.41 -97.34
REMARK 500 1 TYR B 4 -173.35 -65.63
REMARK 500 1 GLU B 5 36.76 -84.92
REMARK 500 1 SER B 6 35.92 176.79
REMARK 500 1 SER B 7 145.11 173.79
REMARK 500 1 LEU B 8 37.96 -140.36
REMARK 500 1 SER B 10 50.69 36.13
REMARK 500 2 THR A 8 -91.50 -98.42
REMARK 500 2 SER A 9 -160.75 -68.97
REMARK 500 2 ILE A 11 113.84 178.42
REMARK 500 2 TRP A 28 -98.68 -177.99
REMARK 500 2 CYS A 33 100.14 -42.19
REMARK 500 2 LYS A 38 -144.03 -91.35
REMARK 500 2 VAL A 39 -151.82 -115.07
REMARK 500 2 GLU A 41 77.63 -110.79
REMARK 500 2 ALA A 45 150.00 -170.02
REMARK 500 2 CYS A 48 99.93 -40.16
REMARK 500 2 LYS A 51 51.42 -170.15
REMARK 500 2 LYS A 52 114.99 -170.33
REMARK 500 2 PRO A 53 39.30 -76.25
REMARK 500 2 TYR A 54 -37.74 -140.39
REMARK 500 2 GLU A 55 -169.35 -79.50
REMARK 500 2 GLU A 56 54.59 -162.05
REMARK 500 2 CYS A 60 125.76 -171.19
REMARK 500 2 PRO A 69 87.76 -61.94
REMARK 500 2 LYS A 70 -88.46 -90.73
REMARK 500 2 TYR B 3 53.66 -97.88
REMARK 500 2 TYR B 4 -168.72 -65.63
REMARK 500 2 SER B 6 -18.07 167.28
REMARK 500 2 LEU B 8 58.47 -140.47
REMARK 500
REMARK 500 THIS ENTRY HAS 479 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 25 0.31 SIDE CHAIN
REMARK 500 1 ARG A 36 0.22 SIDE CHAIN
REMARK 500 1 ARG A 72 0.23 SIDE CHAIN
REMARK 500 1 ARG B 2 0.21 SIDE CHAIN
REMARK 500 2 ARG A 25 0.29 SIDE CHAIN
REMARK 500 2 ARG A 36 0.08 SIDE CHAIN
REMARK 500 2 ARG A 72 0.32 SIDE CHAIN
REMARK 500 2 ARG B 2 0.31 SIDE CHAIN
REMARK 500 3 ARG A 25 0.31 SIDE CHAIN
REMARK 500 3 ARG A 36 0.32 SIDE CHAIN
REMARK 500 3 ARG A 72 0.29 SIDE CHAIN
REMARK 500 3 ARG B 2 0.23 SIDE CHAIN
REMARK 500 4 ARG A 25 0.17 SIDE CHAIN
REMARK 500 4 ARG A 36 0.11 SIDE CHAIN
REMARK 500 4 ARG A 72 0.13 SIDE CHAIN
REMARK 500 4 ARG B 2 0.30 SIDE CHAIN
REMARK 500 5 ARG A 25 0.13 SIDE CHAIN
REMARK 500 5 ARG A 36 0.26 SIDE CHAIN
REMARK 500 5 ARG A 72 0.20 SIDE CHAIN
REMARK 500 5 ARG B 2 0.21 SIDE CHAIN
REMARK 500 6 ARG A 25 0.19 SIDE CHAIN
REMARK 500 6 ARG A 36 0.32 SIDE CHAIN
REMARK 500 6 ARG A 72 0.32 SIDE CHAIN
REMARK 500 6 ARG B 2 0.32 SIDE CHAIN
REMARK 500 7 ARG A 25 0.18 SIDE CHAIN
REMARK 500 7 ARG A 36 0.10 SIDE CHAIN
REMARK 500 7 ARG B 2 0.32 SIDE CHAIN
REMARK 500 8 ARG A 25 0.24 SIDE CHAIN
REMARK 500 8 ARG A 36 0.21 SIDE CHAIN
REMARK 500 8 ARG A 72 0.32 SIDE CHAIN
REMARK 500 8 ARG B 2 0.29 SIDE CHAIN
REMARK 500 9 ARG A 25 0.31 SIDE CHAIN
REMARK 500 9 ARG A 36 0.22 SIDE CHAIN
REMARK 500 9 ARG A 72 0.29 SIDE CHAIN
REMARK 500 9 ARG B 2 0.20 SIDE CHAIN
REMARK 500 10 ARG A 25 0.23 SIDE CHAIN
REMARK 500 10 ARG A 36 0.19 SIDE CHAIN
REMARK 500 10 ARG A 72 0.13 SIDE CHAIN
REMARK 500 10 ARG B 2 0.30 SIDE CHAIN
REMARK 500 11 ARG A 25 0.27 SIDE CHAIN
REMARK 500 11 ARG A 36 0.31 SIDE CHAIN
REMARK 500 11 ARG A 72 0.23 SIDE CHAIN
REMARK 500 12 ARG A 25 0.32 SIDE CHAIN
REMARK 500 12 ARG A 36 0.30 SIDE CHAIN
REMARK 500 12 ARG A 72 0.23 SIDE CHAIN
REMARK 500 12 ARG B 2 0.20 SIDE CHAIN
REMARK 500 13 ARG A 25 0.22 SIDE CHAIN
REMARK 500 13 ARG A 36 0.28 SIDE CHAIN
REMARK 500 13 ARG A 72 0.26 SIDE CHAIN
REMARK 500 13 ARG B 2 0.22 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 78 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BXP A 1 74 UNP P60615 NXL1A_BUNMU 1 74
DBREF 1BXP B 1 13 PDB 1BXP 1BXP 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 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 MET ARG TYR TYR GLU SER SER LEU LYS SER TYR PRO ASP
SHEET 1 A 2 VAL A 2 HIS A 4 0
SHEET 2 A 2 ALA A 13 THR A 15 -1 N VAL A 14 O CYS A 3
SHEET 1 B 2 LEU A 22 LYS A 26 0
SHEET 2 B 2 GLU A 41 ALA A 45 -1 N ALA A 45 O LEU A 22
SSBOND 1 CYS A 3 CYS A 23 1555 1555 2.01
SSBOND 2 CYS A 16 CYS A 44 1555 1555 2.02
SSBOND 3 CYS A 29 CYS A 33 1555 1555 2.02
SSBOND 4 CYS A 48 CYS A 59 1555 1555 2.02
SSBOND 5 CYS A 60 CYS A 65 1555 1555 2.01
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 - b 16 2 Bytes