Header list of 1dkc.pdb file
Complete list - 16 20 Bytes
HEADER ANTIFUNGAL PROTEIN 07-DEC-99 1DKC
TITLE SOLUTION STRUCTURE OF PAFP-S, AN ANTIFUNGAL PEPTIDE FROM THE SEEDS OF
TITLE 2 PHYTOLACCA AMERICANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIFUNGAL PEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PAFP-S
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PHYTOLACCA AMERICANA;
SOURCE 3 ORGANISM_COMMON: AMERICAN POKEWEED;
SOURCE 4 ORGANISM_TAXID: 3527;
SOURCE 5 OTHER_DETAILS: SEED
KEYWDS THREE-STRANDS BETA SHEET, ANTIFUNGAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR D.C.WANG,G.H.GAO,F.SHAO,J.X.DAI,J.F.WANG
REVDAT 4 16-FEB-22 1DKC 1 REMARK
REVDAT 3 24-FEB-09 1DKC 1 VERSN
REVDAT 2 15-MAR-05 1DKC 1 JRNL
REVDAT 1 13-DEC-00 1DKC 0
JRNL AUTH G.H.GAO,W.LIU,J.X.DAI,J.F.WANG,Z.HU,Y.ZHANG,D.C.WANG
JRNL TITL SOLUTION STRUCTURE OF PAFP-S: A NEW KNOTTIN-TYPE ANTIFUNGAL
JRNL TITL 2 PEPTIDE FROM THE SEEDS OF PHYTOLACCA AMERICANA
JRNL REF BIOCHEMISTRY V. 40 10973 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11551192
JRNL DOI 10.1021/BI010167K
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : UXNMR 1.0, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER (UXNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DKC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-99.
REMARK 100 THE DEPOSITION ID IS D_1000010155.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : NA
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 4MM PROTEIN, 0.2 MM DSS; 4MM
REMARK 210 PROTEIN, 0.2 MM DSS
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 2D COSY; 2D
REMARK 210 TOCSY; E-COSY
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 : FELIX 97
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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 1-10
REMARK 470 RES CSSEQI ATOMS
REMARK 470 ARG A 38 O
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 HZ3 LYS A 5 OG SER A 21 1.31
REMARK 500 HZ2 LYS A 36 OD1 ASN A 37 1.33
REMARK 500 OD1 ASN A 6 HZ1 LYS A 36 1.34
REMARK 500 OG SER A 22 HH22 ARG A 38 1.38
REMARK 500 HG SER A 13 OG SER A 31 1.39
REMARK 500 H PHE A 25 O VAL A 34 1.47
REMARK 500 HZ2 LYS A 5 O CYS A 20 1.53
REMARK 500 O GLY A 8 H CYS A 35 1.54
REMARK 500 HH12 ARG A 9 OD1 ASN A 11 1.55
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 PRO A 17 -78.51 -75.91
REMARK 500 1 SER A 22 -4.14 71.13
REMARK 500 1 ASN A 37 -167.30 -76.66
REMARK 500 2 LYS A 5 -72.94 -76.71
REMARK 500 2 SER A 21 -73.49 -98.93
REMARK 500 2 SER A 22 23.74 -174.33
REMARK 500 3 SER A 21 -75.46 -112.90
REMARK 500 3 SER A 22 14.12 -172.38
REMARK 500 3 GLN A 30 -80.26 -151.79
REMARK 500 3 SER A 31 71.66 174.33
REMARK 500 3 ASN A 37 -76.81 -60.60
REMARK 500 4 ASN A 6 51.37 -97.42
REMARK 500 4 ALA A 14 -71.38 -121.16
REMARK 500 4 SER A 21 -73.36 -101.10
REMARK 500 4 SER A 22 18.65 -168.90
REMARK 500 4 ASN A 37 -83.57 -69.34
REMARK 500 5 PRO A 17 -164.52 -74.16
REMARK 500 5 SER A 21 -75.00 -101.11
REMARK 500 5 SER A 22 18.48 -175.64
REMARK 500 6 SER A 13 44.57 -101.78
REMARK 500 6 SER A 22 -3.17 83.68
REMARK 500 6 ASN A 37 -80.79 -55.23
REMARK 500 7 ASN A 11 -169.91 -166.41
REMARK 500 7 SER A 22 -5.04 84.27
REMARK 500 7 ASN A 37 -89.57 -68.40
REMARK 500 8 ALA A 14 -70.92 -129.79
REMARK 500 8 SER A 21 -75.39 -109.90
REMARK 500 8 SER A 22 25.34 -170.46
REMARK 500 8 SER A 31 60.46 70.61
REMARK 500 9 ASN A 11 -169.91 -160.21
REMARK 500 9 SER A 21 -73.23 -107.46
REMARK 500 9 SER A 22 15.84 -171.17
REMARK 500 9 ASN A 37 -76.01 -75.51
REMARK 500 10 ASN A 11 -141.88 -161.19
REMARK 500 10 SER A 13 -166.52 -126.83
REMARK 500 10 PRO A 17 40.62 -96.49
REMARK 500 10 SER A 21 -72.27 -99.28
REMARK 500 10 SER A 22 13.17 -173.37
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 9 0.31 SIDE CHAIN
REMARK 500 1 ARG A 38 0.31 SIDE CHAIN
REMARK 500 2 ARG A 9 0.32 SIDE CHAIN
REMARK 500 2 ARG A 38 0.29 SIDE CHAIN
REMARK 500 3 ARG A 9 0.32 SIDE CHAIN
REMARK 500 3 ARG A 38 0.28 SIDE CHAIN
REMARK 500 4 ARG A 9 0.31 SIDE CHAIN
REMARK 500 4 ARG A 38 0.29 SIDE CHAIN
REMARK 500 5 ARG A 9 0.31 SIDE CHAIN
REMARK 500 5 ARG A 38 0.29 SIDE CHAIN
REMARK 500 6 ARG A 9 0.29 SIDE CHAIN
REMARK 500 6 ARG A 38 0.29 SIDE CHAIN
REMARK 500 7 ARG A 9 0.31 SIDE CHAIN
REMARK 500 7 ARG A 38 0.31 SIDE CHAIN
REMARK 500 8 ARG A 9 0.29 SIDE CHAIN
REMARK 500 8 ARG A 38 0.26 SIDE CHAIN
REMARK 500 9 ARG A 9 0.30 SIDE CHAIN
REMARK 500 9 ARG A 38 0.27 SIDE CHAIN
REMARK 500 10 ARG A 9 0.26 SIDE CHAIN
REMARK 500 10 ARG A 38 0.26 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1DKC A 1 38 UNP P81418 PAFP_PHYAM 28 65
SEQRES 1 A 38 ALA GLY CYS ILE LYS ASN GLY GLY ARG CYS ASN ALA SER
SEQRES 2 A 38 ALA GLY PRO PRO TYR CYS CYS SER SER TYR CYS PHE GLN
SEQRES 3 A 38 ILE ALA GLY GLN SER TYR GLY VAL CYS LYS ASN ARG
SHEET 1 A 3 GLY A 8 CYS A 10 0
SHEET 2 A 3 TYR A 32 LYS A 36 -1 O GLY A 33 N CYS A 10
SHEET 3 A 3 TYR A 23 ILE A 27 -1 N TYR A 23 O LYS A 36
SSBOND 1 CYS A 3 CYS A 20 1555 1555 2.03
SSBOND 2 CYS A 10 CYS A 24 1555 1555 2.02
SSBOND 3 CYS A 19 CYS A 35 1555 1555 2.02
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 - 16 20 Bytes