Header list of 1x22.pdb file
Complete list - b 12 2 Bytes
HEADER ANTIBIOTIC 18-APR-05 1X22
TITLE SOLUTION STRUCTURE OF A NOVEL MORICIN ANALOGUE, AN ANTIBACTERIAL
TITLE 2 PEPTIDE FROM A LEPIDOPTERAN INSECT, SPODOPTERA LITURA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MORICIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SL MORICIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: SPODOPTERA LITURA;
SOURCE 4 ORGANISM_TAXID: 69820;
SOURCE 5 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN A LEPIDOPTERAN
SOURCE 6 INSECT
KEYWDS INSECT IMMUNITY, ANTIBACTERIAL PEPTIDE, MORICIN, PURIFICATION, GENE
KEYWDS 2 EXPRESSION, SOLUTION STRUCTURE, ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.OIZUMI,H.HEMMI,M.MINAMI,A.ASAOKA,M.YAMAKAWA
REVDAT 3 13-NOV-13 1X22 1 DBREF SOURCE VERSN
REVDAT 2 24-FEB-09 1X22 1 VERSN
REVDAT 1 06-SEP-05 1X22 0
JRNL AUTH Y.OIZUMI,H.HEMMI,M.MINAMI,A.ASAOKA,M.YAMAKAWA
JRNL TITL ISOLATION, GENE EXPRESSION AND SOLUTION STRUCTURE OF A NOVEL
JRNL TITL 2 MORICIN ANALOGUE, ANTIBACTERIAL PEPTIDE FROM A LEPIDOPTERAN
JRNL TITL 3 INSECT, SPODOPTERA LITURA
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1752 83 2005
JRNL REFN ISSN 0006-3002
JRNL PMID 16115804
JRNL DOI 10.1016/J.BBAPAP.2005.07.013
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X22 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-APR-05.
REMARK 100 THE RCSB ID CODE IS RCSB024280.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 2.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM SL MORICIN; CD3OH; 99.5%D;
REMARK 210 1.5MM SL MORICIN; CD3OD; 99.8%D
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, SPARKY 3.105, X-
REMARK 210 PLOR 3.851
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 5
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 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 O PHE A 35 H LYS A 38 1.44
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 LYS A 2 66.65 -111.65
REMARK 500 1 PRO A 4 90.55 -42.23
REMARK 500 1 PHE A 35 -87.54 -53.73
REMARK 500 1 LYS A 36 -75.41 10.15
REMARK 500 1 LYS A 38 -74.13 -97.75
REMARK 500 1 HIS A 39 -170.88 44.60
REMARK 500 2 LYS A 2 152.06 178.47
REMARK 500 2 ALA A 13 -70.67 -80.60
REMARK 500 2 ALA A 28 -71.78 -34.93
REMARK 500 2 VAL A 31 -76.49 -57.42
REMARK 500 2 TYR A 32 -31.10 -38.48
REMARK 500 2 LYS A 38 -58.50 -149.44
REMARK 500 2 HIS A 39 -91.21 36.45
REMARK 500 3 PRO A 4 101.23 -46.33
REMARK 500 3 PHE A 35 -84.10 -39.60
REMARK 500 3 LYS A 36 -76.97 16.98
REMARK 500 3 LYS A 41 145.96 68.30
REMARK 500 4 LYS A 2 171.62 62.98
REMARK 500 4 PHE A 35 -85.21 -41.53
REMARK 500 4 LYS A 36 -77.45 17.80
REMARK 500 4 LYS A 38 -66.62 72.57
REMARK 500 4 HIS A 39 -30.46 -36.54
REMARK 500 4 LYS A 40 123.75 -31.07
REMARK 500 5 LYS A 2 -158.24 -117.40
REMARK 500 5 VAL A 31 -73.40 -66.26
REMARK 500 5 TYR A 32 -31.73 -39.39
REMARK 500 5 PHE A 35 -64.18 -90.17
REMARK 500 5 LYS A 38 -66.33 -127.95
REMARK 500 5 HIS A 39 -172.76 44.60
REMARK 500 5 LYS A 41 154.14 63.86
REMARK 500 6 VAL A 31 -81.91 -66.25
REMARK 500 6 TYR A 32 -36.12 -30.29
REMARK 500 6 LYS A 38 -62.04 77.96
REMARK 500 6 HIS A 39 159.47 -35.94
REMARK 500 6 LYS A 40 95.66 156.61
REMARK 500 6 LYS A 41 -58.12 179.97
REMARK 500 7 PRO A 4 110.76 -32.34
REMARK 500 7 LYS A 36 -57.77 -26.81
REMARK 500 7 LYS A 38 -58.57 -126.54
REMARK 500 7 HIS A 39 -94.39 53.26
REMARK 500 8 LYS A 2 127.48 -171.32
REMARK 500 8 ALA A 28 -75.11 -34.49
REMARK 500 8 PHE A 35 -77.55 -44.68
REMARK 500 8 LYS A 36 -72.82 0.86
REMARK 500 8 HIS A 39 -89.14 43.76
REMARK 500 8 LYS A 41 46.07 -177.32
REMARK 500 9 ILE A 3 57.89 31.93
REMARK 500 9 PHE A 35 -84.08 -36.00
REMARK 500 9 LYS A 36 -80.68 20.84
REMARK 500 9 HIS A 39 -113.68 -127.23
REMARK 500
REMARK 500 THIS ENTRY HAS 121 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5749 RELATED DB: BMRB
DBREF 1X22 A 1 42 UNP Q7YZB4 Q7YZB4_SPOLT 25 66
SEQRES 1 A 42 GLY LYS ILE PRO VAL LYS ALA ILE LYS LYS ALA GLY ALA
SEQRES 2 A 42 ALA ILE GLY LYS GLY LEU ARG ALA ILE ASN ILE ALA SER
SEQRES 3 A 42 THR ALA HIS ASP VAL TYR SER PHE PHE LYS PRO LYS HIS
SEQRES 4 A 42 LYS LYS LYS
HELIX 1 1 PRO A 4 LYS A 36 1 33
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 12 2 Bytes