Header list of 1rgj.pdb file
Complete list - 2 20 Bytes
HEADER TOXIN 12-NOV-03 1RGJ
TITLE NMR STRUCTURE OF THE COMPLEX BETWEEN ALPHA-BUNGAROTOXIN AND MIMOTOPE
TITLE 2 OF THE NICOTINIC ACETYLCHOLINE RECEPTOR WITH ENHANCED ACTIVITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LONG NEUROTOXIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA-BUNGAROTOXIN, ALPHA-BTX, BGTX;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: MIMOTOPE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR;
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;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED
KEYWDS NEUROTOXIN, PROTEIN-PEPTIDE COMPLEX, ALPHA-BUNGAROTOXIN, BETA-
KEYWDS 2 STRANDS, TOXIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR A.BERNINI,O.SPIGA,A.CIUTTI,M.SCARSELLI,L.BRACCI,L.LOZZI,B.LELLI,
AUTHOR 2 P.NERI,N.NICCOLAI
REVDAT 4 02-MAR-22 1RGJ 1 REMARK
REVDAT 3 24-FEB-09 1RGJ 1 VERSN
REVDAT 2 11-JAN-05 1RGJ 1 JRNL
REVDAT 1 25-NOV-03 1RGJ 0
SPRSDE 25-NOV-03 1RGJ 1P67
JRNL AUTH A.BERNINI,A.CIUTTI,O.SPIGA,M.SCARSELLI,S.KLEIN,S.VANNETTI,
JRNL AUTH 2 L.BRACCI,L.LOZZI,B.LELLI,C.FALCIANI,P.NERI,N.NICCOLAI
JRNL TITL NMR AND MD STUDIES ON THE INTERACTION BETWEEN LIGAND
JRNL TITL 2 PEPTIDES AND ALPHA-BUNGAROTOXIN.
JRNL REF J.MOL.BIOL. V. 339 1169 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15178256
JRNL DOI 10.1016/J.JMB.2004.04.041
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, AMBER 4.1
REMARK 3 AUTHORS : KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RGJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020727.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM ALPHA-BUNGAROTOXIN, 2MM
REMARK 210 PEPTIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY
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: 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 SG CYS A 23 HB2 ASN A 66 1.25
REMARK 500 HB THR A 58 HD22 ASN A 66 1.30
REMARK 500 SG CYS A 60 HG CYS A 65 1.30
REMARK 500 H LEU A 22 O ALA A 45 1.58
REMARK 500 O ASP A 30 H PHE A 32 1.59
REMARK 500 O VAL A 2 OD2 ASP A 63 2.16
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 PRO A 10 -159.18 -74.99
REMARK 500 SER A 12 -179.40 -179.63
REMARK 500 CYS A 16 172.37 -47.61
REMARK 500 PRO A 18 29.08 -74.90
REMARK 500 ARG A 25 89.07 -168.14
REMARK 500 LYS A 26 174.90 -45.88
REMARK 500 MET A 27 137.44 177.03
REMARK 500 TRP A 28 143.49 -175.35
REMARK 500 CYS A 29 83.11 -61.67
REMARK 500 ASP A 30 177.35 -43.45
REMARK 500 ALA A 31 44.80 -70.40
REMARK 500 PHE A 32 32.41 -176.77
REMARK 500 CYS A 33 -14.74 -49.85
REMARK 500 ARG A 36 -92.32 -91.24
REMARK 500 LYS A 38 83.81 59.52
REMARK 500 GLU A 41 52.56 -95.44
REMARK 500 LEU A 42 141.28 -27.00
REMARK 500 THR A 47 -165.41 179.33
REMARK 500 PRO A 49 -158.48 -74.96
REMARK 500 SER A 50 -72.28 -57.68
REMARK 500 LYS A 51 165.06 99.79
REMARK 500 THR A 58 -171.73 -65.19
REMARK 500 LYS A 70 12.30 -151.17
REMARK 500 GLN A 71 131.79 -19.40
REMARK 500 ARG A 72 141.43 168.26
REMARK 500 TYR B 4 128.66 4.66
REMARK 500 GLU B 5 -18.12 -40.58
REMARK 500 SER B 7 -119.56 -158.47
REMARK 500 LEU B 8 22.45 -155.40
REMARK 500 TRP B 11 66.15 174.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JBD RELATED DB: PDB
REMARK 900 ALPHA-BUNGAROTOXIN COMPLEXED WITH ANOTHER PEPTIDE
REMARK 900 RELATED ID: 1HOY RELATED DB: PDB
REMARK 900 ALPHA-BUNGAROTOXIN COMPLEXED WITH ANOTHER PEPTIDE. 20 NMR STRUCTURES
REMARK 900 RELATED ID: 1IK8 RELATED DB: PDB
REMARK 900 ALPHA-BUNGAROTOXIN. MINIMIZED AVERAGE STRUCTURE
REMARK 900 RELATED ID: 1IKC RELATED DB: PDB
REMARK 900 ALPHA-BUNGAROTOXIN. 30 NMR STRUCTURES
DBREF 1RGJ A 1 74 UNP P60615 NXL1A_BUNMU 1 74
DBREF 1RGJ B 1 13 PDB 1RGJ 1RGJ 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 PHE ARG TYR TYR GLU SER SER LEU GLU PRO TRP ASP ASP
SHEET 1 A 2 VAL A 2 HIS A 4 0
SHEET 2 A 2 ALA A 13 THR A 15 -1 O VAL A 14 N CYS A 3
SHEET 1 B 2 LEU A 22 TYR A 24 0
SHEET 2 B 2 GLY A 43 ALA A 45 -1 O ALA A 45 N LEU A 22
SHEET 1 C 2 LYS A 26 MET A 27 0
SHEET 2 C 2 GLU A 56 VAL A 57 -1 O GLU A 56 N MET A 27
SSBOND 1 CYS A 3 CYS A 23 1555 1555 1.46
SSBOND 2 CYS A 16 CYS A 44 1555 1555 0.89
SSBOND 3 CYS A 29 CYS A 33 1555 1555 1.64
SSBOND 4 CYS A 48 CYS A 59 1555 1555 2.15
SSBOND 5 CYS A 60 CYS A 65 1555 1555 1.43
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 - 2 20 Bytes