Header list of 1sxm.pdb file
Complete list - r 2 2 Bytes
HEADER TOXIN 07-SEP-95 1SXM
TITLE SCORPION TOXIN (NOXIUSTOXIN) WITH HIGH AFFINITY FOR VOLTAGE DEPENDENT
TITLE 2 POTASSIUM CHANNEL AND LOW AFFINITY FOR CALCIUM DEPENDENT POTASSIUM
TITLE 3 CHANNEL (NMR AT 20 DEGREES, PH3.5, 39 STRUCTURES)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NOXIUSTOXIN;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CENTRUROIDES NOXIUS;
SOURCE 3 ORGANISM_COMMON: MEXICAN SCORPION;
SOURCE 4 ORGANISM_TAXID: 6878
KEYWDS TOXIN
EXPDTA SOLUTION NMR
NUMMDL 39
AUTHOR M.DAUPLAIS,B.GILQUIN,L.D.POSSANI,G.GURROLA-BRIONES,C.ROUMESTAND,
AUTHOR 2 A.MENEZ
REVDAT 3 02-MAR-22 1SXM 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1SXM 1 VERSN
REVDAT 1 29-JAN-96 1SXM 0
JRNL AUTH M.DAUPLAIS,B.GILQUIN,L.D.POSSANI,G.GURROLA-BRIONES,
JRNL AUTH 2 C.ROUMESTAND,A.MENEZ
JRNL TITL DETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF
JRNL TITL 2 NOXIUSTOXIN: ANALYSIS OF STRUCTURAL DIFFERENCES WITH RELATED
JRNL TITL 3 SHORT-CHAIN SCORPION TOXINS.
JRNL REF BIOCHEMISTRY V. 34 16563 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 8527429
JRNL DOI 10.1021/BI00051A004
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 1SXM 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_1000176560.
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 : 39
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: 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 H SER A 23 H SER A 24 1.35
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 25 CYS A 34 CA - CB - SG ANGL. DEV. = 6.7 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 1 THR A 8 22.88 -153.39
REMARK 500 1 SER A 9 149.72 -171.96
REMARK 500 1 LEU A 20 -67.39 -93.90
REMARK 500 1 SER A 23 -8.52 -152.99
REMARK 500 1 SER A 24 71.12 -105.42
REMARK 500 1 ASN A 31 -84.61 77.72
REMARK 500 1 TYR A 37 -148.23 -111.61
REMARK 500 2 THR A 8 22.37 -151.03
REMARK 500 2 LEU A 20 -67.11 -93.38
REMARK 500 2 SER A 23 -15.10 -146.42
REMARK 500 2 SER A 24 72.80 -103.43
REMARK 500 2 ASN A 31 -84.60 77.33
REMARK 500 2 TYR A 37 -147.05 -114.34
REMARK 500 3 ASN A 4 71.40 -113.38
REMARK 500 3 THR A 8 22.99 -155.02
REMARK 500 3 SER A 9 148.01 -174.79
REMARK 500 3 LEU A 20 -66.80 -94.04
REMARK 500 3 SER A 23 -14.20 -147.42
REMARK 500 3 SER A 24 72.46 -103.51
REMARK 500 3 ASN A 31 -84.58 77.58
REMARK 500 3 TYR A 37 -147.43 -121.50
REMARK 500 4 THR A 8 26.91 -154.00
REMARK 500 4 SER A 9 148.29 -170.40
REMARK 500 4 LEU A 20 -66.70 -92.74
REMARK 500 4 SER A 23 -11.38 -147.63
REMARK 500 4 SER A 24 69.17 -105.13
REMARK 500 4 ASN A 31 -85.54 78.75
REMARK 500 4 TYR A 37 -160.98 -118.55
REMARK 500 5 ILE A 3 -169.93 -113.56
REMARK 500 5 THR A 8 26.37 -151.92
REMARK 500 5 CYS A 13 -19.01 -144.93
REMARK 500 5 LEU A 20 -67.38 -93.77
REMARK 500 5 SER A 23 -15.39 -146.37
REMARK 500 5 SER A 24 74.74 -102.85
REMARK 500 5 ASN A 31 -84.13 78.43
REMARK 500 5 TYR A 37 -146.23 -113.63
REMARK 500 6 THR A 8 27.85 -154.83
REMARK 500 6 SER A 9 149.14 -171.23
REMARK 500 6 LEU A 20 -66.46 -92.16
REMARK 500 6 SER A 23 -36.59 -141.72
REMARK 500 6 ASN A 31 -84.78 78.58
REMARK 500 6 TYR A 37 -159.72 -122.52
REMARK 500 7 THR A 8 27.27 -154.96
REMARK 500 7 SER A 9 147.32 -172.06
REMARK 500 7 LEU A 20 -66.66 -92.02
REMARK 500 7 SER A 23 -6.96 -148.47
REMARK 500 7 SER A 24 64.46 -107.39
REMARK 500 7 ASN A 31 -84.24 79.05
REMARK 500 7 TYR A 37 -168.05 -114.55
REMARK 500 8 THR A 8 18.86 -148.80
REMARK 500
REMARK 500 THIS ENTRY HAS 244 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 40
DBREF 1SXM A 1 39 UNP P08815 SCKN1_CENNO 1 39
SEQADV 1SXM TYR A 21 UNP P08815 THR 21 CONFLICT
SEQRES 1 A 40 THR ILE ILE ASN VAL LYS CYS THR SER PRO LYS GLN CYS
SEQRES 2 A 40 SER LYS PRO CYS LYS GLU LEU TYR GLY SER SER ALA GLY
SEQRES 3 A 40 ALA LYS CYS MET ASN GLY LYS CYS LYS CYS TYR ASN ASN
SEQRES 4 A 40 NH2
HET NH2 A 40 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 PRO A 16 LEU A 20 1 5
SHEET 1 A 2 ALA A 27 MET A 30 0
SHEET 2 A 2 LYS A 33 CYS A 36 -1 N LYS A 35 O LYS A 28
SSBOND 1 CYS A 7 CYS A 29 1555 1555 2.03
SSBOND 2 CYS A 13 CYS A 34 1555 1555 2.02
SSBOND 3 CYS A 17 CYS A 36 1555 1555 2.01
LINK C ASN A 39 N NH2 A 40 1555 1555 1.37
SITE 1 AC1 1 ASN A 39
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 - r 2 2 Bytes