Header list of 1nh5.pdb file
Complete list - n 24 2 Bytes
HEADER TOXIN 18-DEC-02 1NH5
TITLE AUTOMATIC ASSIGNMENT OF NMR DATA AND DETERMINATION OF THE PROTEIN
TITLE 2 STRUCTURE OF A NEW WORLD SCORPION NEUROTOXIN USING NOAH/DIAMOD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROTOXIN 5;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CSEV5, CSE V5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CENTRUROIDES EXILICAUDA;
SOURCE 3 ORGANISM_TAXID: 6879
KEYWDS SCORPION NEUROTOXIN, NEW WORLD TOXIN, NOAH, DIAMOD, FANTOM, AUTOMATED
KEYWDS 2 PEAK ASSIGNMENT, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.XU,M.J.JABLONSKY,P.L.JACKSON,N.R.KRISHNA,W.BRAUN
REVDAT 4 24-JAN-18 1NH5 1 JRNL
REVDAT 3 01-MAY-13 1NH5 1 MODEL VERSN
REVDAT 2 24-FEB-09 1NH5 1 VERSN
REVDAT 1 07-JAN-03 1NH5 0
JRNL AUTH Y.XU,M.J.JABLONSKY,P.L.JACKSON,W.BRAUN,N.R.KRISHNA
JRNL TITL AUTOMATIC ASSIGNMENT OF NOESY CROSS PEAKS AND DETERMINATION
JRNL TITL 2 OF THE PROTEIN STRUCTURE OF A NEW WORLD SCORPION NEUROTOXIN
JRNL TITL 3 USING NOAH/DIAMOD
JRNL REF J.MAGN.RESON. V. 148 35 2001
JRNL REFN ISSN 0022-2364
JRNL PMID 11133274
JRNL DOI 10.1006/JMRE.2000.2220
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NOAH/DIAMOD/FANTOM
REMARK 3 AUTHORS : W. BRAUN ETC.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NH5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-02.
REMARK 100 THE DEPOSITION ID IS D_1000017866.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313.00
REMARK 210 PH : 4.00
REMARK 210 IONIC STRENGTH : 1 MM
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AM600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SELF-CORRECTING DG/ VTF
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : VTF VALUES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: HOMONUCLEAR 1H NMR SPECTROSCOPY
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 ASP A 7 -70.84 -174.61
REMARK 500 1 LYS A 12 -178.22 69.66
REMARK 500 1 LYS A 28 -55.08 -160.35
REMARK 500 2 ASP A 7 -75.21 -170.94
REMARK 500 2 CYS A 11 76.73 -114.99
REMARK 500 2 LYS A 12 145.87 78.81
REMARK 500 2 LYS A 28 -60.24 -160.00
REMARK 500 2 THR A 56 -64.77 72.05
REMARK 500 2 ASN A 57 -0.44 71.18
REMARK 500 3 ASP A 7 -70.60 -170.40
REMARK 500 3 LYS A 28 -58.45 -158.79
REMARK 500 3 THR A 56 70.76 55.64
REMARK 500 3 CYS A 59 -83.70 50.00
REMARK 500 4 ASP A 7 -71.98 -176.00
REMARK 500 4 LYS A 12 154.68 72.01
REMARK 500 4 SER A 14 76.39 55.22
REMARK 500 4 LYS A 28 -53.15 -164.81
REMARK 500 4 SER A 39 -179.43 177.38
REMARK 500 4 CYS A 40 107.27 -58.96
REMARK 500 4 THR A 56 82.60 62.34
REMARK 500 5 ASP A 7 -74.00 -166.12
REMARK 500 5 CYS A 11 71.81 -110.00
REMARK 500 5 LYS A 12 177.66 70.00
REMARK 500 5 LYS A 28 -64.04 -146.01
REMARK 500 5 MET A 38 48.65 31.46
REMARK 500 5 ASP A 53 48.56 -141.32
REMARK 500 5 THR A 56 70.72 59.72
REMARK 500 6 ASP A 7 -71.53 -179.90
REMARK 500 6 LYS A 12 110.45 75.82
REMARK 500 6 LYS A 28 -57.39 -156.43
REMARK 500 6 ASP A 53 33.34 -145.23
REMARK 500 6 THR A 56 -74.24 74.89
REMARK 500 6 ASN A 57 42.34 33.70
REMARK 500 7 ASP A 7 -73.82 -170.30
REMARK 500 7 LYS A 12 165.26 70.65
REMARK 500 7 SER A 14 -54.70 72.46
REMARK 500 7 CYS A 15 134.64 74.12
REMARK 500 7 LYS A 28 -44.24 -172.14
REMARK 500 7 ASP A 53 34.71 -147.25
REMARK 500 7 SER A 54 71.12 -161.45
REMARK 500 7 THR A 56 -69.94 76.82
REMARK 500 7 ASN A 57 50.12 33.01
REMARK 500 8 ASP A 7 -73.53 -165.64
REMARK 500 8 SER A 14 84.54 56.15
REMARK 500 8 LYS A 28 -56.51 -159.63
REMARK 500 8 ASP A 53 38.35 -152.85
REMARK 500 8 SER A 54 62.83 -153.01
REMARK 500 8 THR A 56 -69.08 78.54
REMARK 500 8 ASN A 57 42.17 36.25
REMARK 500 9 ASP A 7 -71.14 -159.62
REMARK 500
REMARK 500 THIS ENTRY HAS 115 RAMACHANDRAN OUTLIERS.
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 ASP A 7 SER A 8 6 -149.21
REMARK 500 VAL A 51 SER A 52 6 144.79
REMARK 500 ILE A 58 CYS A 59 9 -146.95
REMARK 500 ILE A 58 CYS A 59 11 -51.65
REMARK 500 LYS A 28 LYS A 29 19 -147.27
REMARK 500 ILE A 58 CYS A 59 20 -52.83
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1NH5 A 1 59 UNP P58779 SCX5_CENSC 1 59
SEQADV 1NH5 GLY A 60 UNP P58779 INSERTION
SEQRES 1 A 60 LYS ASP GLY TYR PRO VAL ASP SER LYS GLY CYS LYS LEU
SEQRES 2 A 60 SER CYS VAL ALA ASN ASN TYR CYS ASP ASN GLN CYS LYS
SEQRES 3 A 60 MET LYS LYS ALA SER GLY GLY HIS CYS TYR ALA MET SER
SEQRES 4 A 60 CYS TYR CYS GLU GLY LEU PRO GLU ASN ALA LYS VAL SER
SEQRES 5 A 60 ASP SER ALA THR ASN ILE CYS GLY
HELIX 1 1 ALA A 17 LYS A 26 1 10
SHEET 1 A 4 GLY A 32 TYR A 36 0
SHEET 2 A 4 SER A 39 GLU A 43 -1 O GLU A 43 N GLY A 32
SHEET 3 A 4 ASP A 2 PRO A 5 -1 N GLY A 3 O CYS A 42
SHEET 4 A 4 VAL A 51 SER A 52 -1 O SER A 52 N TYR A 4
SSBOND 1 CYS A 11 CYS A 59 1555 1555 1.94
SSBOND 2 CYS A 15 CYS A 35 1555 1555 2.02
SSBOND 3 CYS A 21 CYS A 40 1555 1555 2.01
SSBOND 4 CYS A 21 CYS A 25 1555 1555 2.89
SSBOND 5 CYS A 25 CYS A 42 1555 1555 1.97
SSBOND 6 CYS A 25 CYS A 40 1555 1555 2.60
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 - n 24 2 Bytes