Header list of 1scy.pdb file
Complete list - 29 20 Bytes
HEADER NEUROTOXIN 02-JUN-94 1SCY
TITLE DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF SCYLLATOXIN BY 1H
TITLE 2 NUCLEAR MAGNETIC RESONANCE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SCYLLATOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEIURUS QUINQUESTRIATUS HEBRAEUS;
SOURCE 3 ORGANISM_TAXID: 6884;
SOURCE 4 STRAIN: HEBRAEUS
KEYWDS NEUROTOXIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR J.C.MARTINS,F.J.M.VAN DE VEN,F.A.M.BORREMANS
REVDAT 3 29-NOV-17 1SCY 1 REMARK HELIX
REVDAT 2 24-FEB-09 1SCY 1 VERSN
REVDAT 1 26-JAN-95 1SCY 0
JRNL AUTH J.C.MARTINS,F.J.VAN DE VEN,F.A.BORREMANS
JRNL TITL DETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF
JRNL TITL 2 SCYLLATOXIN BY 1H NUCLEAR MAGNETIC RESONANCE.
JRNL REF J.MOL.BIOL. V. 253 590 1995
JRNL REFN ISSN 0022-2836
JRNL PMID 7473736
JRNL DOI 10.1006/JMBI.1995.0575
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.C.MARTINS,W.ZHANG,A.TARTAR,M.LAZDUNSKI,F.A.M.BORREMANS
REMARK 1 TITL SOLUTION CONFORMATION OF LEIUROTOXIN I (SCYLLATOXIN) BY 1H
REMARK 1 TITL 2 NUCLEAR MAGNETIC RESONANCE. RESONANCE ASSIGNMENT AND
REMARK 1 TITL 3 SECONDARY STRUCTURE
REMARK 1 REF FEBS LETT. V. 260 249 1990
REMARK 1 REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA, AMBER
REMARK 3 AUTHORS : GUNTERT,BRAUN,WUTHRICH (DIANA),
REMARK 3 PEARLMAN,CASE,CALDWELL,SIEBEL,SINGH,WEINER,KOLLMAN
REMARK 3 (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SCY 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_1000176327.
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 : 25
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: 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 3 CYS A 28 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 4 CYS A 28 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 7 CYS A 28 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 9 CYS A 28 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 12 CYS A 28 CA - CB - SG ANGL. DEV. = 8.5 DEGREES
REMARK 500 13 CYS A 28 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 14 CYS A 28 CA - CB - SG ANGL. DEV. = 8.1 DEGREES
REMARK 500 15 CYS A 28 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 16 CYS A 28 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 17 CYS A 28 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 18 CYS A 28 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 19 CYS A 28 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 20 CYS A 28 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 21 CYS A 28 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 22 CYS A 28 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 25 CYS A 28 CA - CB - SG ANGL. DEV. = 7.2 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 PHE A 2 84.77 -69.00
REMARK 500 1 LYS A 30 -76.68 -84.74
REMARK 500 2 PHE A 2 -56.89 67.86
REMARK 500 2 LYS A 20 94.39 -165.38
REMARK 500 7 PHE A 2 -39.24 -145.05
REMARK 500 9 PHE A 2 -49.99 -176.31
REMARK 500 10 PHE A 2 -59.99 -150.77
REMARK 500 11 PHE A 2 -53.26 70.67
REMARK 500 12 PHE A 2 -48.52 -143.93
REMARK 500 13 LEU A 18 94.61 -68.01
REMARK 500 15 PHE A 2 -178.43 44.87
REMARK 500 15 ILE A 22 66.42 -111.73
REMARK 500 18 PHE A 2 -71.78 61.78
REMARK 500 20 PHE A 2 85.77 -68.61
REMARK 500 22 PHE A 2 -80.17 59.68
REMARK 500 23 PHE A 2 32.87 -168.73
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 GLY A 19 LYS A 20 2 -140.41
REMARK 500 ASP A 24 LYS A 25 4 -145.00
REMARK 500 LYS A 20 CYS A 21 8 -146.10
REMARK 500 CYS A 21 ILE A 22 12 149.75
REMARK 500 LYS A 20 CYS A 21 13 -145.12
REMARK 500 ASP A 24 LYS A 25 14 -146.47
REMARK 500 ALA A 1 PHE A 2 15 -131.47
REMARK 500 CYS A 3 ASN A 4 18 145.88
REMARK 500 ALA A 1 PHE A 2 22 -148.70
REMARK 500 ASP A 24 LYS A 25 22 -130.72
REMARK 500 CYS A 21 ILE A 22 23 146.01
REMARK 500 ASP A 24 LYS A 25 24 -129.36
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 13 0.15 SIDE CHAIN
REMARK 500 2 ARG A 13 0.08 SIDE CHAIN
REMARK 500 3 ARG A 13 0.12 SIDE CHAIN
REMARK 500 5 PHE A 2 0.07 SIDE CHAIN
REMARK 500 6 GLU A 27 0.09 SIDE CHAIN
REMARK 500 11 ARG A 13 0.08 SIDE CHAIN
REMARK 500 16 ARG A 13 0.11 SIDE CHAIN
REMARK 500 18 ARG A 13 0.07 SIDE CHAIN
REMARK 500 19 ARG A 13 0.12 SIDE CHAIN
REMARK 500 20 ARG A 13 0.08 SIDE CHAIN
REMARK 500 21 ARG A 13 0.08 SIDE CHAIN
REMARK 500 22 ARG A 6 0.09 SIDE CHAIN
REMARK 500 23 GLU A 27 0.10 SIDE CHAIN
REMARK 500 25 ARG A 13 0.08 SIDE CHAIN
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 32
DBREF 1SCY A 1 31 UNP P16341 SCKL_LEIQH 1 31
SEQRES 1 A 32 ALA PHE CYS ASN LEU ARG MET CYS GLN LEU SER CYS ARG
SEQRES 2 A 32 SER LEU GLY LEU LEU GLY LYS CYS ILE GLY ASP LYS CYS
SEQRES 3 A 32 GLU CYS VAL LYS HIS NH2
HET NH2 A 32 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 H1 LEU A 5 SER A 14 1 10
SHEET 1 S1 2 LEU A 18 ILE A 22 0
SHEET 2 S1 2 LYS A 25 VAL A 29 -1
SSBOND 1 CYS A 3 CYS A 21 1555 1555 2.07
SSBOND 2 CYS A 8 CYS A 26 1555 1555 2.09
SSBOND 3 CYS A 12 CYS A 28 1555 1555 2.08
LINK C HIS A 31 N NH2 A 32 1555 1555 1.36
SITE 1 AC1 1 HIS A 31
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 - 29 20 Bytes