Header list of 1idi.pdb file
Complete list - 23 20 Bytes
HEADER TOXIN 04-APR-01 1IDI TITLE THE NMR SOLUTION STRUCTURE OF ALPHA-BUNGAROTOXIN CAVEAT 1IDI THERE ARE SEVERAL CHIRALITY ERRORS IN CHAIN A. COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-BUNGAROTOXIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: LONG NEUROTOXIN 1 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BUNGARUS MULTICINCTUS; SOURCE 3 ORGANISM_COMMON: MANY-BANDED KRAIT; SOURCE 4 ORGANISM_TAXID: 8616; SOURCE 5 OTHER_DETAILS: PURCHASED FROM SIGMA KEYWDS ALPHA-BUNGAROTOXIN, ALPHA-NEUROTOXIN, NMR SOLUTION STRUCTURE, TOXIN EXPDTA SOLUTION NMR AUTHOR H.ZENG,L.MOISE,M.A.GRANT,E.HAWROT REVDAT 5 23-FEB-22 1IDI 1 REMARK REVDAT 4 24-FEB-09 1IDI 1 VERSN REVDAT 3 01-APR-03 1IDI 1 JRNL REVDAT 2 27-JUN-01 1IDI 1 JRNL REVDAT 1 25-APR-01 1IDI 0 JRNL AUTH H.ZENG,L.MOISE,M.A.GRANT,E.HAWROT JRNL TITL THE SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN JRNL TITL 2 ALPHA-BUNGAROTOXIN AND AN 18-MER COGNATE PEPTIDE DERIVED JRNL TITL 3 FROM THE ALPHA 1 SUBUNIT OF THE NICOTINIC ACETYLCHOLINE JRNL TITL 4 RECEPTOR FROM TORPEDO CALIFORNICA. JRNL REF J.BIOL.CHEM. V. 276 22930 2001 JRNL REFN ISSN 0021-9258 JRNL PMID 11312275 JRNL DOI 10.1074/JBC.M102300200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.1, CNSSOLVE 1.0 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, A.T. ET AL. (CNSSOLVE) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1IDI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-01. REMARK 100 THE DEPOSITION ID IS D_1000013182. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 4.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2.0 MM FREE ALPHA-BUNGAROTOXIN, REMARK 210 50 MM PERDEUTERATED POTASSIUM REMARK 210 ACETATE BUFFER (PH 4.0) WITH 5% REMARK 210 D2O AND 0.05% SODIUM AZIDE 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 : NMRPIPE 1.8, SPARKY 3.95 REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 1 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE CHIRALITY ERROR IS IN THR 8 CB, OG1; LYS 38 CA, CB; REMARK 210 GLU 55 CA, HA. THERE IS NO CHIRALITY ERROR IF MOLMOL IS USED TO REMARK 210 VIEW THE STRUCTURE. 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: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 HIS A 4 CG HIS A 4 CD2 0.055 REMARK 500 HIS A 68 CG HIS A 68 CD2 0.059 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 HIS A 4 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 DEGREES REMARK 500 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 TYR A 54 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 PRO A 67 CA - C - N ANGL. DEV. = 17.6 DEGREES REMARK 500 PRO A 67 O - C - N ANGL. DEV. = -11.5 DEGREES REMARK 500 HIS A 68 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 DEGREES REMARK 500 ARG A 72 NE - CZ - NH1 ANGL. DEV. = 4.1 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 -142.31 -136.65 REMARK 500 CYS A 3 -103.82 -77.55 REMARK 500 THR A 5 -99.23 -89.47 REMARK 500 THR A 6 71.85 97.45 REMARK 500 ALA A 7 -57.26 63.78 REMARK 500 THR A 8 -105.00 -106.99 REMARK 500 SER A 9 -60.40 -129.97 REMARK 500 ILE A 11 -176.46 -63.48 REMARK 500 ALA A 13 -102.49 -144.44 REMARK 500 THR A 15 -69.26 -142.20 REMARK 500 PRO A 17 -167.99 -63.74 REMARK 500 ASN A 21 -78.05 33.90 REMARK 500 LEU A 22 -101.37 74.54 REMARK 500 MET A 27 -134.26 -62.88 REMARK 500 TRP A 28 -157.85 77.87 REMARK 500 CYS A 29 -47.63 -167.56 REMARK 500 ASP A 30 -100.28 72.62 REMARK 500 CYS A 33 -84.24 -127.00 REMARK 500 LYS A 38 49.48 142.34 REMARK 500 VAL A 39 141.18 123.07 REMARK 500 VAL A 40 117.11 51.20 REMARK 500 GLU A 41 -117.72 -97.07 REMARK 500 LEU A 42 161.16 172.21 REMARK 500 ALA A 45 -66.69 -145.95 REMARK 500 THR A 47 -43.78 -140.05 REMARK 500 CYS A 48 88.61 62.40 REMARK 500 SER A 50 -110.61 -104.58 REMARK 500 LYS A 51 94.10 59.87 REMARK 500 LYS A 52 -78.73 -146.91 REMARK 500 GLU A 55 -170.33 159.93 REMARK 500 CYS A 59 114.82 -27.33 REMARK 500 ASP A 63 107.71 -44.39 REMARK 500 LYS A 64 -65.40 76.17 REMARK 500 CYS A 65 -75.30 67.50 REMARK 500 ASN A 66 153.73 91.38 REMARK 500 PRO A 67 -86.88 -80.20 REMARK 500 HIS A 68 37.93 73.69 REMARK 500 LYS A 70 117.08 57.29 REMARK 500 GLN A 71 -94.81 -127.04 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 MET A 27 TRP A 28 148.86 REMARK 500 TRP A 28 CYS A 29 -146.09 REMARK 500 LYS A 38 VAL A 39 -102.60 REMARK 500 VAL A 40 GLU A 41 146.72 REMARK 500 SER A 50 LYS A 51 144.49 REMARK 500 TYR A 54 GLU A 55 30.61 REMARK 500 VAL A 57 THR A 58 -137.23 REMARK 500 THR A 58 CYS A 59 137.22 REMARK 500 CYS A 65 ASN A 66 144.50 REMARK 500 HIS A 68 PRO A 69 120.17 REMARK 500 PRO A 69 LYS A 70 148.88 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1IDG RELATED DB: PDB REMARK 900 1IDG IS THE AVERAGE STRUCTURE OF THE COMPLEX BETWEEN ALPHA- REMARK 900 BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDE REMARK 900 RELATED ID: 1IDH RELATED DB: PDB REMARK 900 1IDH IS THE 20 ENSEMBLE STRUCTURES OF THE COMPLEX BETWEEN ALPHA- REMARK 900 BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDE REMARK 900 RELATED ID: 1IDL RELATED DB: PDB REMARK 900 1IDL IS THE 20 ENSEMBLE STRUCTURES OF ALPHA-BUNGAROTOXIN DBREF 1IDI 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 SSBOND 1 CYS A 3 CYS A 23 1555 1555 1.99 SSBOND 2 CYS A 16 CYS A 44 1555 1555 2.01 SSBOND 3 CYS A 29 CYS A 33 1555 1555 2.00 SSBOND 4 CYS A 48 CYS A 59 1555 1555 2.00 SSBOND 5 CYS A 60 CYS A 65 1555 1555 2.00 CISPEP 1 GLY A 37 LYS A 38 0 1.78 CISPEP 2 PRO A 67 HIS A 68 0 -5.93 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 20 Bytes