Header list of 1lsi.pdb file
Complete list - b 23 2 Bytes
HEADER NEUROTOXIN 26-NOV-95 1LSI
TITLE LSIII (NMR, 23 STRUCTURES)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LSIII;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LONG NEUROTOXIN 1 (COMPONENT LSIII)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LATICAUDA SEMIFASCIATA;
SOURCE 3 ORGANISM_COMMON: BROAD-BANDED BLUE SEA KRAIT;
SOURCE 4 ORGANISM_TAXID: 8631
KEYWDS VENOM, MULTIGENE FAMILY, NEUROTOXIN
EXPDTA SOLUTION NMR
NUMMDL 23
AUTHOR P.J.CONNOLLY,A.S.STERN,J.C.HOCH
REVDAT 3 23-FEB-22 1LSI 1 REMARK
REVDAT 2 24-FEB-09 1LSI 1 VERSN
REVDAT 1 15-MAR-96 1LSI 0
JRNL AUTH P.J.CONNOLLY,A.S.STERN,J.C.HOCH
JRNL TITL SOLUTION STRUCTURE OF LSIII, A LONG NEUROTOXIN FROM THE
JRNL TITL 2 VENOM OF LATICAUDA SEMIFASCIATA.
JRNL REF BIOCHEMISTRY V. 35 418 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8555211
JRNL DOI 10.1021/BI9520287
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.J.CONNOLLY,A.S.STERN,J.C.HOCH
REMARK 1 TITL ESTIMATING PROTEIN FOLD FROM INCOMPLETE AND APPROXIMATE NMR
REMARK 1 TITL 2 DATA
REMARK 1 REF J.AM.CHEM.SOC. V. 116 2675 1994
REMARK 1 REFN ISSN 0002-7863
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: NULL
REMARK 4
REMARK 4 1LSI 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_1000174815.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 23
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: 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: 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 CYS A 3 -46.28 83.89
REMARK 500 1 TYR A 4 -88.59 42.98
REMARK 500 1 ASN A 6 -165.82 -64.29
REMARK 500 1 PRO A 7 32.80 -79.44
REMARK 500 1 THR A 10 -174.74 66.23
REMARK 500 1 GLN A 11 -33.98 -170.46
REMARK 500 1 THR A 12 148.52 69.73
REMARK 500 1 SER A 31 94.68 -39.89
REMARK 500 1 SER A 32 73.63 43.88
REMARK 500 1 ARG A 33 -94.41 -133.42
REMARK 500 1 VAL A 36 73.04 -104.28
REMARK 500 1 CYS A 45 110.33 -34.18
REMARK 500 1 SER A 47 -152.22 -106.49
REMARK 500 1 ASN A 49 -97.59 -49.37
REMARK 500 1 THR A 50 -142.90 -71.64
REMARK 500 1 SER A 58 -4.30 -141.52
REMARK 500 1 ALA A 59 -115.75 -163.11
REMARK 500 1 ASP A 60 31.26 -97.70
REMARK 500 1 TYR A 65 77.20 37.46
REMARK 500 2 CYS A 3 -68.35 82.72
REMARK 500 2 TYR A 4 -163.59 36.84
REMARK 500 2 LEU A 5 83.79 60.00
REMARK 500 2 HIS A 8 28.87 -158.07
REMARK 500 2 ASP A 9 -166.26 169.27
REMARK 500 2 THR A 10 178.29 73.86
REMARK 500 2 GLN A 11 105.33 176.54
REMARK 500 2 THR A 12 166.66 -40.66
REMARK 500 2 GLN A 17 -157.74 -70.59
REMARK 500 2 ASN A 27 -160.26 -107.66
REMARK 500 2 SER A 31 93.01 -39.69
REMARK 500 2 SER A 32 67.08 39.63
REMARK 500 2 ARG A 33 -93.67 -139.19
REMARK 500 2 LYS A 35 165.11 -44.45
REMARK 500 2 ALA A 42 -178.00 170.15
REMARK 500 2 CYS A 45 126.87 -38.05
REMARK 500 2 ASN A 49 40.82 -84.04
REMARK 500 2 THR A 50 85.77 -68.65
REMARK 500 2 ALA A 59 -113.79 -163.20
REMARK 500 2 ASP A 60 32.85 -96.22
REMARK 500 2 TYR A 65 143.31 -38.44
REMARK 500 3 GLU A 2 38.55 -140.04
REMARK 500 3 CYS A 3 -56.64 -154.90
REMARK 500 3 TYR A 4 -163.03 39.82
REMARK 500 3 LEU A 5 89.39 64.27
REMARK 500 3 HIS A 8 23.42 -155.21
REMARK 500 3 ASP A 9 -174.11 -173.29
REMARK 500 3 THR A 10 163.72 66.11
REMARK 500 3 GLN A 11 19.49 -161.66
REMARK 500 3 THR A 12 145.94 58.09
REMARK 500 3 GLN A 17 -155.96 -69.88
REMARK 500
REMARK 500 THIS ENTRY HAS 505 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 0.31 SIDE CHAIN
REMARK 500 1 ARG A 33 0.22 SIDE CHAIN
REMARK 500 2 ARG A 1 0.22 SIDE CHAIN
REMARK 500 2 ARG A 33 0.14 SIDE CHAIN
REMARK 500 3 ARG A 1 0.28 SIDE CHAIN
REMARK 500 3 ARG A 33 0.14 SIDE CHAIN
REMARK 500 4 ARG A 1 0.30 SIDE CHAIN
REMARK 500 4 ARG A 33 0.20 SIDE CHAIN
REMARK 500 5 ARG A 1 0.30 SIDE CHAIN
REMARK 500 5 ARG A 33 0.19 SIDE CHAIN
REMARK 500 6 ARG A 1 0.26 SIDE CHAIN
REMARK 500 6 ARG A 33 0.32 SIDE CHAIN
REMARK 500 7 ARG A 1 0.20 SIDE CHAIN
REMARK 500 8 ARG A 1 0.31 SIDE CHAIN
REMARK 500 8 ARG A 33 0.32 SIDE CHAIN
REMARK 500 9 ARG A 1 0.29 SIDE CHAIN
REMARK 500 10 ARG A 1 0.21 SIDE CHAIN
REMARK 500 10 ARG A 33 0.28 SIDE CHAIN
REMARK 500 11 ARG A 33 0.24 SIDE CHAIN
REMARK 500 12 ARG A 1 0.13 SIDE CHAIN
REMARK 500 12 ARG A 33 0.23 SIDE CHAIN
REMARK 500 13 ARG A 1 0.28 SIDE CHAIN
REMARK 500 13 ARG A 33 0.29 SIDE CHAIN
REMARK 500 14 ARG A 1 0.30 SIDE CHAIN
REMARK 500 14 ARG A 33 0.31 SIDE CHAIN
REMARK 500 15 ARG A 1 0.27 SIDE CHAIN
REMARK 500 15 ARG A 33 0.20 SIDE CHAIN
REMARK 500 16 ARG A 1 0.13 SIDE CHAIN
REMARK 500 16 ARG A 33 0.19 SIDE CHAIN
REMARK 500 17 ARG A 1 0.28 SIDE CHAIN
REMARK 500 17 ARG A 33 0.31 SIDE CHAIN
REMARK 500 18 ARG A 1 0.31 SIDE CHAIN
REMARK 500 18 ARG A 33 0.26 SIDE CHAIN
REMARK 500 19 ARG A 1 0.31 SIDE CHAIN
REMARK 500 19 ARG A 33 0.31 SIDE CHAIN
REMARK 500 20 ARG A 1 0.08 SIDE CHAIN
REMARK 500 20 ARG A 33 0.26 SIDE CHAIN
REMARK 500 21 ARG A 1 0.28 SIDE CHAIN
REMARK 500 21 ARG A 33 0.26 SIDE CHAIN
REMARK 500 22 ARG A 1 0.23 SIDE CHAIN
REMARK 500 22 ARG A 33 0.29 SIDE CHAIN
REMARK 500 23 ARG A 1 0.13 SIDE CHAIN
REMARK 500 23 ARG A 33 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1LSI A 1 66 UNP P01379 NXL1_LATSE 1 66
SEQRES 1 A 66 ARG GLU CYS TYR LEU ASN PRO HIS ASP THR GLN THR CYS
SEQRES 2 A 66 PRO SER GLY GLN GLU ILE CYS TYR VAL LYS SER TRP CYS
SEQRES 3 A 66 ASN ALA TRP CYS SER SER ARG GLY LYS VAL LEU GLU PHE
SEQRES 4 A 66 GLY CYS ALA ALA THR CYS PRO SER VAL ASN THR GLY THR
SEQRES 5 A 66 GLU ILE LYS CYS CYS SER ALA ASP LYS CYS ASN THR TYR
SEQRES 6 A 66 PRO
SHEET 1 A 3 VAL A 36 ALA A 42 0
SHEET 2 A 3 ILE A 19 TRP A 25 -1
SHEET 3 A 3 GLU A 53 CYS A 57 -1
SSBOND 1 CYS A 3 CYS A 20 1555 1555 2.02
SSBOND 2 CYS A 13 CYS A 41 1555 1555 2.02
SSBOND 3 CYS A 26 CYS A 30 1555 1555 2.02
SSBOND 4 CYS A 45 CYS A 56 1555 1555 2.02
SSBOND 5 CYS A 57 CYS A 62 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 - b 23 2 Bytes