Header list of 1hoy.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 12-DEC-00 1HOY TITLE NMR STRUCTURE OF THE COMPLEX BETWEEN A-BUNGAROTOXIN AND A MIMOTOPE OF TITLE 2 THE NICOTINIC ACETYLCHOLINE RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: LONG NEUROTOXIN 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ALPHA-BUNGAROTOXIN; 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: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. KEYWDS ALPHA-BUNGAROTOXIN, PROTEIN-PEPTIDE COMPLEX, ACCHOR MIMOTOPE, TOXIN, KEYWDS 2 BETA-STRANDS EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.SCARSELLI,O.SPIGA,A.CIUTTI,L.BRACCI,B.LELLI,L.LOZZI,D.CALAMANDREI, AUTHOR 2 A.BERNINI,D.DI MARO,N.NICCOLAI,P.NERI REVDAT 5 23-FEB-22 1HOY 1 REMARK REVDAT 4 24-FEB-09 1HOY 1 VERSN REVDAT 3 30-SEP-03 1HOY 1 DBREF REVDAT 2 27-FEB-02 1HOY 1 JRNL REMARK REVDAT 1 27-DEC-00 1HOY 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,D.A. ET AL (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 1607 NOE-DERIVED DISTANCE CONSTRAINTS REMARK 4 REMARK 4 1HOY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-00. REMARK 100 THE DEPOSITION ID IS D_1000012489. 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 : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5MM A-BUNGAROTOXIN;0.5MM REMARK 210 PEPTIDE; 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 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 : XWINNMR 2.1, NMRVIEW 4.1.1, REMARK 210 DYANA 1.5 REMARK 210 METHOD USED : MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20 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 HG1 THR A 6 H LEU A 42 1.14 REMARK 500 HB2 CYS A 16 HG CYS A 44 1.17 REMARK 500 HZ3 LYS A 70 HE21 GLN A 71 1.22 REMARK 500 HG2 PRO A 49 HG11 VAL A 57 1.27 REMARK 500 O GLU B 9 CD PRO B 13 1.35 REMARK 500 O HIS A 68 HD3 LYS A 70 1.41 REMARK 500 O GLU B 9 HD2 PRO B 13 1.45 REMARK 500 O GLU B 9 HD3 PRO B 13 1.52 REMARK 500 O GLU B 9 CG PRO B 13 1.56 REMARK 500 O TRP A 28 HB3 LYS A 38 1.58 REMARK 500 OD1 ASP A 30 HE ARG B 2 1.59 REMARK 500 O HIS A 68 CD LYS A 70 1.99 REMARK 500 O TYR A 54 N GLU A 56 2.05 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 8 -104.24 -74.89 REMARK 500 1 SER A 9 -161.64 -62.81 REMARK 500 1 ILE A 11 103.31 166.23 REMARK 500 1 LEU A 22 -170.83 -174.66 REMARK 500 1 TRP A 28 -101.67 -166.16 REMARK 500 1 CYS A 29 119.28 -175.69 REMARK 500 1 ASP A 30 178.04 -48.21 REMARK 500 1 CYS A 33 59.14 37.50 REMARK 500 1 SER A 34 176.53 -59.51 REMARK 500 1 VAL A 39 -162.20 -104.68 REMARK 500 1 VAL A 40 75.95 -153.50 REMARK 500 1 LEU A 42 -179.34 -66.68 REMARK 500 1 CYS A 48 97.66 -34.84 REMARK 500 1 SER A 50 139.36 -25.11 REMARK 500 1 LYS A 51 -114.93 -93.85 REMARK 500 1 LYS A 52 -52.59 -155.93 REMARK 500 1 PRO A 53 -107.21 -75.00 REMARK 500 1 GLU A 55 72.91 -36.63 REMARK 500 1 THR A 58 -145.61 -127.57 REMARK 500 1 CYS A 60 114.91 -179.95 REMARK 500 1 THR A 62 165.13 -49.30 REMARK 500 1 HIS A 68 158.04 -37.83 REMARK 500 1 LYS A 70 -40.03 -160.99 REMARK 500 1 GLN A 71 78.21 -57.05 REMARK 500 1 TYR B 4 -165.47 -58.80 REMARK 500 1 SER B 6 -4.61 -148.68 REMARK 500 1 PRO B 10 24.88 -74.92 REMARK 500 2 THR A 8 -103.83 -74.97 REMARK 500 2 SER A 9 -161.26 -63.55 REMARK 500 2 ILE A 11 103.33 165.98 REMARK 500 2 LEU A 22 -171.37 -173.65 REMARK 500 2 TRP A 28 -101.40 -167.27 REMARK 500 2 CYS A 29 118.11 -176.41 REMARK 500 2 ASP A 30 177.73 -47.07 REMARK 500 2 CYS A 33 62.43 37.10 REMARK 500 2 VAL A 39 -161.73 -103.42 REMARK 500 2 VAL A 40 76.35 -153.93 REMARK 500 2 LEU A 42 -178.34 -66.54 REMARK 500 2 CYS A 48 97.68 -33.03 REMARK 500 2 SER A 50 139.44 -24.86 REMARK 500 2 LYS A 51 -114.62 -93.91 REMARK 500 2 LYS A 52 -52.35 -156.29 REMARK 500 2 PRO A 53 -106.38 -74.94 REMARK 500 2 GLU A 55 72.49 -36.14 REMARK 500 2 THR A 58 -144.28 -127.40 REMARK 500 2 CYS A 60 114.85 179.76 REMARK 500 2 THR A 62 166.20 -49.64 REMARK 500 2 HIS A 68 158.11 -38.32 REMARK 500 2 LYS A 70 -41.05 -160.87 REMARK 500 2 GLN A 71 79.94 -54.56 REMARK 500 REMARK 500 THIS ENTRY HAS 554 RAMACHANDRAN OUTLIERS. 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 MINIMIZED AVERAGE STRUCTURE DBREF 1HOY A 1 74 UNP P60615 NXL1A_BUNMU 1 74 DBREF 1HOY B 1 14 PDB 1HOY 1HOY 1 14 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 14 HIS ARG TYR TYR GLU SER SER LEU GLU PRO TRP TYR PRO SEQRES 2 B 14 ASP SHEET 1 A 2 CYS A 3 HIS A 4 0 SHEET 2 A 2 ALA A 13 VAL A 14 -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 GLU A 41 O LYS A 26 SSBOND 1 CYS A 3 CYS A 23 1555 1555 2.59 SSBOND 2 CYS A 48 CYS A 59 1555 1555 2.98 SSBOND 3 CYS A 60 CYS A 65 1555 1555 2.41 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 23 2 Bytes