Header list of 2dd6.pdb file
Complete list - 10 20 Bytes
HEADER ANTIMICROBIAL PROTEIN 19-JAN-06 2DD6
TITLE SOLUTION STRUCTURE OF DERMASEPTIN ANTIMICROBIAL PEPTIDE TRUNCATED,
TITLE 2 MUTATED ANALOG, K4-S4(1-13)A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DERMASEPTIN-4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-13;
COMPND 5 SYNONYM: DS IV;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS IS A TRUNCATED, MUTATED, AMIDATED SEQUENCE THAT
SOURCE 4 OCCURS NATURALLY IN FROG SKIN SECRETIONS.
KEYWDS ALPHA HELIX, ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR D.E.SHALEV,S.ROTEM,A.FISH,A.MOR
REVDAT 4 10-NOV-21 2DD6 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 2DD6 1 VERSN
REVDAT 2 25-APR-06 2DD6 1 JRNL
REVDAT 1 28-FEB-06 2DD6 0
JRNL AUTH D.E.SHALEV,S.ROTEM,A.FISH,A.MOR
JRNL TITL CONSEQUENCES OF N-ACYLATION ON STRUCTURE AND MEMBRANE
JRNL TITL 2 BINDING PROPERTIES OF DERMASEPTIN DERIVATIVE K4-S4-(1-13)
JRNL REF J.BIOL.CHEM. V. 281 9432 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16407175
JRNL DOI 10.1074/JBC.M513051200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, X-PLOR 3.856
REMARK 3 AUTHORS : BRUKER (XWINNMR), NILGES, KUSZEWSKI, BRNGER (X
REMARK 3 -PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 250
REMARK 3 RESTRAINTS COMPRISING: 83 INTRARESIDUAL; 78 I,I+1; 34 I,I+2; 37
REMARK 3 I,I+3; 18 LONG RANGE
REMARK 4
REMARK 4 2DD6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000025275.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 78 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : PEPTIDE CONCENTRATION 2.2MM
REMARK 210 NATURAL ABUNDANCE; 20:1 MOLAR
REMARK 210 RATIO OF DPC-D38 TO PEPTIDE; 10%
REMARK 210 PHOSPHATE BUFFER; 10% D2O; 0.02%
REMARK 210 NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.1, SPARKY 3, X-PLOR
REMARK 210 3.856, PROCHECK
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY, STRUCTURES WITH THE
REMARK 210 LEAST RESTRAINT VIOLATIONS
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 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 VAL A 10 H ALA A 13 1.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 ALA A 13 C ALA A 13 O -0.147
REMARK 500 1 ALA A 13 C NH2 A 14 N -0.207
REMARK 500 4 ALA A 13 C ALA A 13 O 0.129
REMARK 500 13 ALA A 13 C ALA A 13 O -0.255
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 1 ALA A 13 O - C - N ANGL. DEV. = -12.4 DEGREES
REMARK 500 4 ALA A 13 N - CA - C ANGL. DEV. = 16.2 DEGREES
REMARK 500 4 ALA A 13 CA - C - N ANGL. DEV. = -18.5 DEGREES
REMARK 500 7 ALA A 13 CB - CA - C ANGL. DEV. = 12.2 DEGREES
REMARK 500 13 ALA A 13 O - C - N ANGL. DEV. = -56.9 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 1.37 -157.43
REMARK 500 1 TRP A 3 -24.71 177.26
REMARK 500 1 THR A 5 -35.52 -144.83
REMARK 500 2 LEU A 2 1.44 -154.72
REMARK 500 2 TRP A 3 -23.81 173.12
REMARK 500 2 THR A 5 -35.04 -153.66
REMARK 500 3 LEU A 2 4.28 -154.71
REMARK 500 3 TRP A 3 -24.88 170.09
REMARK 500 3 THR A 5 -40.57 -149.52
REMARK 500 4 LEU A 2 3.69 -154.76
REMARK 500 4 TRP A 3 -24.56 171.07
REMARK 500 4 THR A 5 -38.31 -146.45
REMARK 500 5 LEU A 2 0.01 -154.45
REMARK 500 5 TRP A 3 -23.80 173.80
REMARK 500 5 THR A 5 -35.70 -150.93
REMARK 500 6 LEU A 2 5.35 -156.21
REMARK 500 6 TRP A 3 -23.82 166.53
REMARK 500 6 THR A 5 -35.98 -166.21
REMARK 500 7 LEU A 2 1.60 -157.81
REMARK 500 7 TRP A 3 -25.40 176.09
REMARK 500 7 THR A 5 -37.01 -147.71
REMARK 500 8 LEU A 2 -3.01 -154.49
REMARK 500 8 TRP A 3 -23.41 172.50
REMARK 500 8 THR A 5 -35.93 -156.54
REMARK 500 9 LEU A 2 4.79 -155.37
REMARK 500 9 TRP A 3 -23.64 166.81
REMARK 500 9 THR A 5 -35.84 -167.24
REMARK 500 10 LEU A 2 -4.32 -154.72
REMARK 500 10 TRP A 3 -23.11 173.51
REMARK 500 10 THR A 5 -36.43 -156.94
REMARK 500 11 LEU A 2 -0.52 -156.25
REMARK 500 11 TRP A 3 -24.09 176.47
REMARK 500 11 THR A 5 -35.14 -153.78
REMARK 500 12 LEU A 2 5.35 -156.34
REMARK 500 12 TRP A 3 -23.72 166.53
REMARK 500 12 THR A 5 -36.26 -165.90
REMARK 500 13 LEU A 2 8.32 -156.44
REMARK 500 13 TRP A 3 -25.76 164.36
REMARK 500 13 THR A 5 -40.28 -158.70
REMARK 500 14 LEU A 2 5.23 -155.63
REMARK 500 14 TRP A 3 -23.71 166.22
REMARK 500 14 THR A 5 -35.59 -166.90
REMARK 500 15 LEU A 2 0.48 -154.75
REMARK 500 15 TRP A 3 -24.09 173.42
REMARK 500 15 THR A 5 -35.93 -154.09
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: 2DCX RELATED DB: PDB
REMARK 900 ACYLATED DERIVATIVE OF THE DERMASEPTIN ANALOG, NC12-K4-S4(1-13)A.
DBREF 2DD6 A 1 13 UNP P80280 DMS4_PHYSA 1 13
SEQADV 2DD6 LYS A 4 UNP P80280 MET 4 ENGINEERED MUTATION
SEQRES 1 A 14 ALA LEU TRP LYS THR LEU LEU LYS LYS VAL LEU LYS ALA
SEQRES 2 A 14 NH2
HET NH2 A 14 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 THR A 5 LEU A 11 1 7
LINK C ALA A 13 N NH2 A 14 1555 1555 1.13
LINK O ALA A 13 N NH2 A 14 1555 1555 1.82
SITE 1 AC1 1 ALA 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