Header list of 2nbt.pdb file
Complete list - r 16 2 Bytes
HEADER TOXIN 29-OCT-97 2NBT
TITLE NEURONAL BUNGAROTOXIN, NMR, 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEURONAL BUNGAROTOXIN;
COMPND 3 CHAIN: A, B
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
KEYWDS TOXIN, VENOM, NEUROTOXIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR R.E.OSWALD,M.J.SUTCLIFFE,M.BAMBERGER,R.H.LORING,E.BRASWELL,C.M.DOBSON
REVDAT 3 16-MAR-22 2NBT 1 REMARK
REVDAT 2 24-FEB-09 2NBT 1 VERSN
REVDAT 1 11-MAR-98 2NBT 0
SPRSDE 11-MAR-98 2NBT 1NBT
JRNL AUTH M.J.SUTCLIFFE,C.M.DOBSON,R.E.OSWALD
JRNL TITL SOLUTION STRUCTURE OF NEURONAL BUNGAROTOXIN DETERMINED BY
JRNL TITL 2 TWO-DIMENSIONAL NMR SPECTROSCOPY: CALCULATION OF TERTIARY
JRNL TITL 3 STRUCTURE USING SYSTEMATIC HOMOLOGOUS MODEL BUILDING,
JRNL TITL 4 DYNAMICAL SIMULATED ANNEALING, AND RESTRAINED MOLECULAR
JRNL TITL 5 DYNAMICS.
JRNL REF BIOCHEMISTRY V. 31 2962 1992
JRNL REFN ISSN 0006-2960
JRNL PMID 1550821
JRNL DOI 10.1021/BI00126A017
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.E.OSWALD,M.J.SUTCLIFFE,M.BAMBERGER,R.H.LORING,E.BRASWELL,
REMARK 1 AUTH 2 C.M.DOBSON
REMARK 1 TITL SOLUTION STRUCTURE OF NEURONAL BUNGAROTOXIN DETERMINED BY
REMARK 1 TITL 2 TWO-DIMENSIONAL NMR SPECTROSCOPY: SEQUENCE-SPECIFIC
REMARK 1 TITL 3 ASSIGNMENTS, SECONDARY STRUCTURE, AND DIMER FORMATION
REMARK 1 REF BIOCHEMISTRY V. 30 4901 1991
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 2NBT 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_1000178397.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 4.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; HOHAHA; COSY; RELAY;
REMARK 210 DOUBLE RELAY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AM-500; AM-600; HOME-BUILT 500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; NICOLET
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR, COMPOSER
REMARK 210 METHOD USED : HOMOLOGY MODELLING FOLLOWED BY
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 14
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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: 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 H LYS A 24 O GLU A 39 1.48
REMARK 500 H LYS B 24 O GLU B 39 1.48
REMARK 500 O PRO A 47 H PHE A 49 1.49
REMARK 500 O PRO B 47 H PHE B 49 1.49
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 THR A 2 -155.65 -155.05
REMARK 500 1 SER A 6 -60.06 175.26
REMARK 500 1 PRO A 7 -93.96 -67.92
REMARK 500 1 GLN A 12 7.60 -160.75
REMARK 500 1 THR A 13 -152.90 -90.22
REMARK 500 1 CYS A 14 57.60 168.64
REMARK 500 1 LYS A 29 121.51 63.20
REMARK 500 1 PHE A 30 -44.33 70.88
REMARK 500 1 CYS A 31 24.68 49.09
REMARK 500 1 SER A 32 17.55 -159.98
REMARK 500 1 ALA A 44 -91.31 -53.41
REMARK 500 1 GLN A 48 51.85 -65.22
REMARK 500 1 PHE A 49 -162.12 36.07
REMARK 500 1 ARG A 50 138.36 -172.66
REMARK 500 1 TYR A 53 -168.37 -106.24
REMARK 500 1 SER A 55 109.60 168.97
REMARK 500 1 THR A 60 19.13 50.73
REMARK 500 1 THR B 2 -155.74 -155.44
REMARK 500 1 SER B 6 -59.60 175.14
REMARK 500 1 PRO B 7 -93.17 -68.62
REMARK 500 1 GLN B 12 7.44 -160.88
REMARK 500 1 THR B 13 -153.14 -90.26
REMARK 500 1 CYS B 14 57.85 168.86
REMARK 500 1 LYS B 29 121.92 62.68
REMARK 500 1 PHE B 30 -43.98 70.33
REMARK 500 1 CYS B 31 24.42 49.03
REMARK 500 1 SER B 32 17.13 -159.51
REMARK 500 1 ALA B 44 -92.13 -53.79
REMARK 500 1 GLN B 48 52.05 -64.98
REMARK 500 1 PHE B 49 -162.22 35.77
REMARK 500 1 ARG B 50 138.51 -172.26
REMARK 500 1 TYR B 53 -168.88 -106.03
REMARK 500 1 SER B 55 109.26 168.84
REMARK 500 1 THR B 60 19.35 50.56
REMARK 500 2 THR A 2 -93.82 -142.61
REMARK 500 2 CYS A 3 -74.43 -115.43
REMARK 500 2 PRO A 11 -140.04 -67.92
REMARK 500 2 GLN A 12 98.76 -162.00
REMARK 500 2 ASN A 16 -143.97 -136.37
REMARK 500 2 GLN A 18 103.71 49.04
REMARK 500 2 ASP A 19 53.91 -97.20
REMARK 500 2 ASP A 28 -138.17 -152.29
REMARK 500 2 LYS A 29 121.31 -39.77
REMARK 500 2 PHE A 30 -36.83 72.30
REMARK 500 2 CYS A 31 16.16 54.29
REMARK 500 2 SER A 32 -3.91 -141.57
REMARK 500 2 ILE A 33 -51.16 -129.83
REMARK 500 2 ARG A 34 50.50 -159.11
REMARK 500 2 VAL A 43 -95.80 -131.11
REMARK 500 2 ALA A 44 -39.29 178.28
REMARK 500
REMARK 500 THIS ENTRY HAS 366 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 1 0.28 SIDE CHAIN
REMARK 500 1 ARG A 34 0.29 SIDE CHAIN
REMARK 500 1 ARG A 50 0.28 SIDE CHAIN
REMARK 500 1 ARG A 54 0.30 SIDE CHAIN
REMARK 500 1 ARG B 1 0.28 SIDE CHAIN
REMARK 500 1 ARG B 34 0.29 SIDE CHAIN
REMARK 500 1 ARG B 50 0.27 SIDE CHAIN
REMARK 500 1 ARG B 54 0.30 SIDE CHAIN
REMARK 500 2 ARG A 1 0.25 SIDE CHAIN
REMARK 500 2 ARG A 34 0.20 SIDE CHAIN
REMARK 500 2 ARG A 50 0.14 SIDE CHAIN
REMARK 500 2 ARG A 54 0.32 SIDE CHAIN
REMARK 500 2 ARG B 1 0.25 SIDE CHAIN
REMARK 500 2 ARG B 34 0.20 SIDE CHAIN
REMARK 500 2 ARG B 50 0.14 SIDE CHAIN
REMARK 500 2 ARG B 54 0.32 SIDE CHAIN
REMARK 500 3 ARG A 1 0.26 SIDE CHAIN
REMARK 500 3 ARG A 34 0.32 SIDE CHAIN
REMARK 500 3 ARG A 50 0.31 SIDE CHAIN
REMARK 500 3 ARG A 54 0.16 SIDE CHAIN
REMARK 500 3 ARG B 1 0.26 SIDE CHAIN
REMARK 500 3 ARG B 34 0.32 SIDE CHAIN
REMARK 500 3 ARG B 50 0.31 SIDE CHAIN
REMARK 500 3 ARG B 54 0.16 SIDE CHAIN
REMARK 500 4 ARG A 1 0.31 SIDE CHAIN
REMARK 500 4 ARG A 34 0.32 SIDE CHAIN
REMARK 500 4 ARG A 50 0.20 SIDE CHAIN
REMARK 500 4 ARG A 54 0.32 SIDE CHAIN
REMARK 500 4 ARG B 1 0.31 SIDE CHAIN
REMARK 500 4 ARG B 34 0.32 SIDE CHAIN
REMARK 500 4 ARG B 50 0.20 SIDE CHAIN
REMARK 500 4 ARG B 54 0.32 SIDE CHAIN
REMARK 500 5 ARG A 1 0.19 SIDE CHAIN
REMARK 500 5 ARG A 34 0.23 SIDE CHAIN
REMARK 500 5 ARG A 50 0.32 SIDE CHAIN
REMARK 500 5 ARG A 54 0.31 SIDE CHAIN
REMARK 500 5 ARG B 1 0.18 SIDE CHAIN
REMARK 500 5 ARG B 34 0.23 SIDE CHAIN
REMARK 500 5 ARG B 50 0.32 SIDE CHAIN
REMARK 500 5 ARG B 54 0.31 SIDE CHAIN
REMARK 500 6 ARG A 1 0.22 SIDE CHAIN
REMARK 500 6 ARG A 34 0.21 SIDE CHAIN
REMARK 500 6 ARG A 50 0.24 SIDE CHAIN
REMARK 500 6 ARG A 54 0.28 SIDE CHAIN
REMARK 500 6 ARG B 1 0.22 SIDE CHAIN
REMARK 500 6 ARG B 34 0.21 SIDE CHAIN
REMARK 500 6 ARG B 50 0.24 SIDE CHAIN
REMARK 500 6 ARG B 54 0.28 SIDE CHAIN
REMARK 500 7 ARG A 1 0.30 SIDE CHAIN
REMARK 500 7 ARG A 34 0.26 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 78 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2NBT A 1 66 UNP P01398 NXL1_BUNMU 22 87
DBREF 2NBT B 1 66 UNP P01398 NXL1_BUNMU 22 87
SEQRES 1 A 66 ARG THR CYS LEU ILE SER PRO SER SER THR PRO GLN THR
SEQRES 2 A 66 CYS PRO ASN GLY GLN ASP ILE CYS PHE LEU LYS ALA GLN
SEQRES 3 A 66 CYS ASP LYS PHE CYS SER ILE ARG GLY PRO VAL ILE GLU
SEQRES 4 A 66 GLN GLY CYS VAL ALA THR CYS PRO GLN PHE ARG SER ASN
SEQRES 5 A 66 TYR ARG SER LEU LEU CYS CYS THR THR ASP ASN CYS ASN
SEQRES 6 A 66 HIS
SEQRES 1 B 66 ARG THR CYS LEU ILE SER PRO SER SER THR PRO GLN THR
SEQRES 2 B 66 CYS PRO ASN GLY GLN ASP ILE CYS PHE LEU LYS ALA GLN
SEQRES 3 B 66 CYS ASP LYS PHE CYS SER ILE ARG GLY PRO VAL ILE GLU
SEQRES 4 B 66 GLN GLY CYS VAL ALA THR CYS PRO GLN PHE ARG SER ASN
SEQRES 5 B 66 TYR ARG SER LEU LEU CYS CYS THR THR ASP ASN CYS ASN
SEQRES 6 B 66 HIS
SHEET 1 S1 6 VAL A 37 GLY A 41 0
SHEET 2 S1 6 CYS A 21 GLN A 26 -1 N PHE A 22 O GLY A 41
SHEET 3 S1 6 SER A 55 CYS A 59 -1 N CYS A 59 O CYS A 21
SHEET 4 S1 6 SER B 55 CYS B 59 -1 N CYS B 58 O LEU A 56
SHEET 5 S1 6 CYS B 21 GLN B 26 -1 N ALA B 25 O SER B 55
SHEET 6 S1 6 VAL B 37 GLY B 41 -1 N VAL B 37 O GLN B 26
SSBOND 1 CYS A 3 CYS A 21 1555 1555 2.02
SSBOND 2 CYS A 14 CYS A 42 1555 1555 2.02
SSBOND 3 CYS A 27 CYS A 31 1555 1555 2.02
SSBOND 4 CYS A 46 CYS A 58 1555 1555 2.03
SSBOND 5 CYS A 59 CYS A 64 1555 1555 2.02
SSBOND 6 CYS B 3 CYS B 21 1555 1555 2.02
SSBOND 7 CYS B 14 CYS B 42 1555 1555 2.02
SSBOND 8 CYS B 27 CYS B 31 1555 1555 2.02
SSBOND 9 CYS B 46 CYS B 58 1555 1555 2.03
SSBOND 10 CYS B 59 CYS B 64 1555 1555 2.02
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 - r 16 2 Bytes