Header list of 1t55.pdb file
Complete list - 10 20 Bytes
HEADER ANTIBIOTIC 02-MAY-04 1T55
TITLE ANTIBIOTIC ACTIVITY AND STRUCTURAL ANALYSIS OF A SCORPION-DERIVED
TITLE 2 ANTIMICROBIAL PEPTIDE ISCT AND ITS ANALOGS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOTOXIC LINEAR PEPTIDE ISCT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ISCT;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OPISTHACANTHUS MADAGASCARIENSIS;
SOURCE 3 ORGANISM_TAXID: 167108;
SOURCE 4 TISSUE: VENOM;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COIL-HELIX, ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.LEE,S.Y.SHIN,K.KIM,S.S.LIM,K.S.HAHM,Y.KIM
REVDAT 3 10-NOV-21 1T55 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1T55 1 VERSN
REVDAT 1 19-OCT-04 1T55 0
JRNL AUTH K.LEE,S.Y.SHIN,K.KIM,S.S.LIM,K.S.HAHM,Y.KIM
JRNL TITL ANTIBIOTIC ACTIVITY AND STRUCTURAL ANALYSIS OF THE
JRNL TITL 2 SCORPION-DERIVED ANTIMICROBIAL PEPTIDE ISCT AND ITS ANALOGS
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 323 712 2004
JRNL REFN ISSN 0006-291X
JRNL PMID 15369808
JRNL DOI 10.1016/J.BBRC.2004.08.144
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 2000.1, DGII 2000.1
REMARK 3 AUTHORS : HAVEL (DGII)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T55 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000022324.
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 : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.0MM PEPTIDE; 200MM SDS-D25
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 ILE A 1 CA
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
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 12 PRO A 8 C - N - CD ANGL. DEV. = -13.2 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 LEU A 2 -89.51 -112.68
REMARK 500 2 LEU A 2 -172.72 -65.47
REMARK 500 2 TRP A 6 -45.60 -143.27
REMARK 500 3 LEU A 2 148.45 58.50
REMARK 500 3 TRP A 6 -37.94 -143.27
REMARK 500 4 LEU A 12 64.29 -167.37
REMARK 500 5 LEU A 2 -144.83 -83.07
REMARK 500 7 LEU A 12 40.16 -170.87
REMARK 500 8 LEU A 2 -89.10 -42.68
REMARK 500 9 LEU A 2 164.10 56.58
REMARK 500 9 ILE A 5 13.16 -144.41
REMARK 500 10 LEU A 2 -37.27 -144.97
REMARK 500 10 ILE A 5 13.83 -142.62
REMARK 500 11 LEU A 2 -84.81 60.54
REMARK 500 12 LEU A 2 -90.29 -42.40
REMARK 500 12 LYS A 4 47.69 -79.96
REMARK 500 12 ILE A 5 -36.69 -152.65
REMARK 500 12 TRP A 6 -36.57 -145.10
REMARK 500 13 LEU A 2 -85.55 58.80
REMARK 500 14 LEU A 2 -89.83 50.42
REMARK 500 14 ILE A 5 40.09 -143.96
REMARK 500 14 TRP A 6 -37.83 -148.12
REMARK 500 16 LEU A 2 -164.45 51.90
REMARK 500 17 LEU A 2 -163.79 -55.83
REMARK 500 18 TRP A 6 -35.99 -145.75
REMARK 500 19 LEU A 2 -169.86 -108.82
REMARK 500 19 ILE A 5 20.67 -145.81
REMARK 500 20 ILE A 5 24.88 -142.84
REMARK 500 20 TRP A 6 -36.78 -137.98
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 14
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1T51 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN OF WILD TYPE
REMARK 900 RELATED ID: 1T52 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH E7K MUTANT
REMARK 900 RELATED ID: 1T54 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH W6A MUTANT
DBREF 1T55 A 1 13 UNP Q8MMJ7 TXT1_OPIMA 24 36
SEQADV 1T55 LYS A 7 UNP Q8MMJ7 GLU 30 ENGINEERED MUTATION
SEQADV 1T55 PRO A 8 UNP Q8MMJ7 GLY 31 ENGINEERED MUTATION
SEQADV 1T55 LYS A 11 UNP Q8MMJ7 SER 34 ENGINEERED MUTATION
SEQRES 1 A 14 ILE LEU GLY LYS ILE TRP LYS PRO ILE LYS LYS LEU PHE
SEQRES 2 A 14 NH2
HET NH2 A 14 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 PRO A 8 PHE A 13 1 6
LINK C PHE A 13 N NH2 A 14 1555 1555 1.31
SITE 1 AC1 1 PHE A 13
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 - 10 20 Bytes