Header list of 1z64.pdb file
Complete list - 2 20 Bytes
HEADER ANTIMICROBIAL PROTEIN 21-MAR-05 1Z64
TITLE NMR SOLUTION STRUCTURE OF PLEUROCIDIN IN DPC MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLERUOCIDIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 23-47;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOPLEURONECTES AMERICANUS;
SOURCE 3 ORGANISM_COMMON: WINTER FLOUNDER;
SOURCE 4 ORGANISM_TAXID: 8265;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS HELIX; MICELLE, ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 11
AUTHOR R.T.SYVITSKI,I.BURTON,N.R.MATTATALL,S.E.DOUGLAS,D.L.JAKEMAN
REVDAT 4 02-MAR-22 1Z64 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1Z64 1 VERSN
REVDAT 2 24-MAY-05 1Z64 1 JRNL
REVDAT 1 12-APR-05 1Z64 0
JRNL AUTH R.T.SYVITSKI,I.BURTON,N.R.MATTATALL,S.E.DOUGLAS,D.L.JAKEMAN
JRNL TITL STRUCTURAL CHARACTERIZATION OF THE ANTIMICROBIAL PEPTIDE
JRNL TITL 2 PLEUROCIDIN FROM WINTER FLOUNDER.
JRNL REF BIOCHEMISTRY V. 44 7282 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15882067
JRNL DOI 10.1021/BI0504005
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Z64 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032345.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 0MM NACL
REMARK 210 PRESSURE : ATMOSPHERIC ATM
REMARK 210 SAMPLE CONTENTS : 2MM PEPTIDE U-15; 50MM PHOSPHATE
REMARK 210 BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; DOSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.105, X-PLOR 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY; SIMULATED
REMARK 210 ANNEALING; MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: STRUCTURE WAS DETERMINED USING 2D AND 3D HETRONUCLEAR
REMARK 210 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 LYS A 7 H HIS A 11 1.49
REMARK 500 O ALA A 9 H GLY A 13 1.53
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 SER A 4 -86.62 -47.78
REMARK 500 1 PHE A 6 -75.07 -43.75
REMARK 500 1 HIS A 23 -59.47 -125.95
REMARK 500 2 TRP A 2 -48.62 -151.65
REMARK 500 2 SER A 4 -79.51 -47.42
REMARK 500 2 ALA A 19 -70.61 -79.14
REMARK 500 3 TRP A 2 17.46 56.93
REMARK 500 3 SER A 4 -81.30 -40.54
REMARK 500 3 HIS A 23 29.28 172.63
REMARK 500 3 TYR A 24 18.57 57.76
REMARK 500 4 SER A 4 -90.26 -43.05
REMARK 500 4 LYS A 18 -72.16 -72.49
REMARK 500 4 HIS A 23 23.18 176.39
REMARK 500 4 TYR A 24 19.08 57.05
REMARK 500 5 SER A 4 -86.21 -45.45
REMARK 500 5 PHE A 6 -75.43 -44.01
REMARK 500 5 HIS A 23 -62.12 -127.53
REMARK 500 6 TRP A 2 -62.71 -101.83
REMARK 500 6 SER A 4 -86.15 -47.38
REMARK 500 6 PHE A 6 -74.92 -43.40
REMARK 500 6 LEU A 21 -54.34 -120.11
REMARK 500 7 SER A 4 -76.03 -47.29
REMARK 500 7 LYS A 18 -72.50 -74.14
REMARK 500 7 HIS A 23 23.43 176.42
REMARK 500 7 TYR A 24 19.53 55.46
REMARK 500 8 SER A 4 -85.28 -45.74
REMARK 500 8 PHE A 6 -74.93 -43.22
REMARK 500 9 SER A 4 -86.70 -50.42
REMARK 500 9 PHE A 6 -74.48 -43.43
REMARK 500 9 HIS A 23 -44.56 -136.39
REMARK 500 10 TRP A 2 31.10 -172.83
REMARK 500 10 SER A 4 -85.89 -43.71
REMARK 500 10 PHE A 6 -73.06 -42.30
REMARK 500 10 HIS A 23 -47.17 -138.52
REMARK 500 11 SER A 4 -90.39 -53.14
REMARK 500 11 PHE A 5 -16.94 -47.93
REMARK 500 11 ALA A 19 -72.87 -79.92
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 26
DBREF 1Z64 A 1 25 UNP P81941 PLE1_PSEAM 23 47
SEQADV 1Z64 NH2 A 26 UNP P81941 AMIDATION
SEQRES 1 A 26 GLY TRP GLY SER PHE PHE LYS LYS ALA ALA HIS VAL GLY
SEQRES 2 A 26 LYS HIS VAL GLY LYS ALA ALA LEU THR HIS TYR LEU NH2
HET NH2 A 26 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 TRP A 2 LEU A 21 1 20
LINK C LEU A 25 N NH2 A 26 1555 1555 1.31
SITE 1 AC1 1 LEU A 25
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 - 2 20 Bytes