Header list of 1dqc.pdb file
Complete list - b 16 2 Bytes
HEADER ANTIMICROBIAL PROTEIN 04-JAN-00 1DQC
TITLE SOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMICROBIAL PROTEIN WITH
TITLE 2 CHITIN-BINDING FUNCTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TACHYCITIN;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TACHYPLEUS TRIDENTATUS;
SOURCE 3 ORGANISM_TAXID: 6853;
SOURCE 4 CELL: HEMOCYTE
KEYWDS DISULFIDE-RICH, ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR T.SUETAKE,S.TSUDA,S.KAWABATA,K.MIURA,K.KAWANO
REVDAT 4 16-FEB-22 1DQC 1 REMARK LINK
REVDAT 3 24-FEB-09 1DQC 1 VERSN
REVDAT 2 01-APR-03 1DQC 1 JRNL
REVDAT 1 13-SEP-00 1DQC 0
JRNL AUTH T.SUETAKE,S.TSUDA,S.KAWABATA,K.MIURA,S.IWANAGA,K.HIKICHI,
JRNL AUTH 2 K.NITTA,K.KAWANO
JRNL TITL CHITIN-BINDING PROTEINS IN INVERTEBRATES AND PLANTS COMPRISE
JRNL TITL 2 A COMMON CHITIN-BINDING STRUCTURAL MOTIF.
JRNL REF J.BIOL.CHEM. V. 275 17929 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 10770921
JRNL DOI 10.1074/JBC.C000184200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.7, X-PLOR 3.851
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1070 RESTRAINTS, 1009 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 35
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 26 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1DQC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-00.
REMARK 100 THE DEPOSITION ID IS D_1000010289.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 4.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM TACHYCITIN; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : ALPHA
REMARK 210 SPECTROMETER MANUFACTURER : JEOL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PIPP 4.0.4, 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 : 25
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 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 CYS A 68 H LEU A 70 1.57
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 83.93 44.02
REMARK 500 1 PHE A 4 -79.79 -126.46
REMARK 500 1 ARG A 5 15.43 57.60
REMARK 500 1 SER A 10 48.11 -156.02
REMARK 500 1 ASP A 14 -136.96 -134.75
REMARK 500 1 TYR A 22 -73.44 -130.05
REMARK 500 1 PHE A 27 -166.42 -79.77
REMARK 500 1 LYS A 32 -138.76 49.67
REMARK 500 1 CYS A 33 46.98 -84.22
REMARK 500 1 VAL A 52 -158.12 -122.59
REMARK 500 1 ASP A 54 151.61 177.17
REMARK 500 1 TRP A 55 160.48 -42.86
REMARK 500 1 HIS A 69 59.85 -67.34
REMARK 500 2 LEU A 2 73.76 -115.91
REMARK 500 2 ALA A 3 -156.60 -91.19
REMARK 500 2 PHE A 4 -158.85 36.36
REMARK 500 2 ARG A 5 20.16 -163.89
REMARK 500 2 ASP A 14 50.51 -160.03
REMARK 500 2 ASP A 15 -160.22 60.53
REMARK 500 2 CYS A 24 53.29 -142.66
REMARK 500 2 CYS A 25 -37.26 -160.15
REMARK 500 2 HIS A 31 84.61 -159.92
REMARK 500 2 LYS A 32 85.94 50.60
REMARK 500 2 CYS A 33 25.40 43.99
REMARK 500 2 PRO A 41 56.84 -67.73
REMARK 500 2 LYS A 42 88.03 39.37
REMARK 500 2 LYS A 51 35.09 38.96
REMARK 500 2 TRP A 55 162.28 -42.93
REMARK 500 2 THR A 62 36.27 -143.58
REMARK 500 2 LYS A 66 44.01 -88.76
REMARK 500 2 GLU A 67 -54.08 -141.59
REMARK 500 2 CYS A 68 -52.06 72.48
REMARK 500 3 LEU A 2 110.26 55.41
REMARK 500 3 ALA A 3 -137.86 -90.44
REMARK 500 3 PHE A 4 -144.44 54.64
REMARK 500 3 ARG A 5 -29.88 -168.37
REMARK 500 3 SER A 10 51.63 -147.29
REMARK 500 3 ASP A 14 -71.52 -153.54
REMARK 500 3 ASP A 15 59.13 171.38
REMARK 500 3 CYS A 24 -33.58 -164.33
REMARK 500 3 LYS A 32 -84.59 59.27
REMARK 500 3 LYS A 42 66.54 172.46
REMARK 500 3 LYS A 51 27.44 40.82
REMARK 500 3 TRP A 55 164.20 -42.84
REMARK 500 3 ALA A 59 -87.25 -99.83
REMARK 500 3 CYS A 61 21.48 -155.29
REMARK 500 3 CYS A 68 61.10 -67.32
REMARK 500 3 TRP A 71 175.37 175.79
REMARK 500 4 LEU A 2 115.74 65.75
REMARK 500 4 ARG A 5 14.63 -151.25
REMARK 500
REMARK 500 THIS ENTRY HAS 439 RAMACHANDRAN OUTLIERS.
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 5 0.20 SIDE CHAIN
REMARK 500 1 ARG A 36 0.29 SIDE CHAIN
REMARK 500 2 ARG A 5 0.27 SIDE CHAIN
REMARK 500 2 ARG A 8 0.20 SIDE CHAIN
REMARK 500 2 ARG A 36 0.29 SIDE CHAIN
REMARK 500 3 ARG A 5 0.25 SIDE CHAIN
REMARK 500 3 ARG A 8 0.22 SIDE CHAIN
REMARK 500 3 ARG A 36 0.17 SIDE CHAIN
REMARK 500 4 ARG A 5 0.25 SIDE CHAIN
REMARK 500 4 ARG A 8 0.25 SIDE CHAIN
REMARK 500 4 ARG A 36 0.19 SIDE CHAIN
REMARK 500 5 ARG A 5 0.18 SIDE CHAIN
REMARK 500 5 ARG A 8 0.32 SIDE CHAIN
REMARK 500 5 ARG A 36 0.29 SIDE CHAIN
REMARK 500 6 ARG A 5 0.22 SIDE CHAIN
REMARK 500 6 ARG A 8 0.25 SIDE CHAIN
REMARK 500 6 ARG A 36 0.15 SIDE CHAIN
REMARK 500 7 ARG A 5 0.32 SIDE CHAIN
REMARK 500 7 ARG A 8 0.29 SIDE CHAIN
REMARK 500 7 ARG A 36 0.26 SIDE CHAIN
REMARK 500 8 ARG A 5 0.08 SIDE CHAIN
REMARK 500 8 ARG A 8 0.32 SIDE CHAIN
REMARK 500 8 ARG A 36 0.22 SIDE CHAIN
REMARK 500 9 ARG A 5 0.10 SIDE CHAIN
REMARK 500 9 ARG A 8 0.25 SIDE CHAIN
REMARK 500 10 ARG A 5 0.13 SIDE CHAIN
REMARK 500 10 ARG A 8 0.15 SIDE CHAIN
REMARK 500 10 ARG A 36 0.16 SIDE CHAIN
REMARK 500 11 ARG A 5 0.31 SIDE CHAIN
REMARK 500 11 ARG A 36 0.23 SIDE CHAIN
REMARK 500 12 ARG A 5 0.28 SIDE CHAIN
REMARK 500 12 ARG A 8 0.32 SIDE CHAIN
REMARK 500 12 ARG A 36 0.23 SIDE CHAIN
REMARK 500 13 ARG A 5 0.28 SIDE CHAIN
REMARK 500 13 ARG A 8 0.30 SIDE CHAIN
REMARK 500 13 ARG A 36 0.24 SIDE CHAIN
REMARK 500 14 ARG A 5 0.31 SIDE CHAIN
REMARK 500 14 ARG A 8 0.19 SIDE CHAIN
REMARK 500 14 ARG A 36 0.22 SIDE CHAIN
REMARK 500 15 ARG A 5 0.29 SIDE CHAIN
REMARK 500 15 ARG A 8 0.25 SIDE CHAIN
REMARK 500 15 ARG A 36 0.17 SIDE CHAIN
REMARK 500 16 ARG A 5 0.27 SIDE CHAIN
REMARK 500 16 ARG A 8 0.21 SIDE CHAIN
REMARK 500 16 ARG A 36 0.27 SIDE CHAIN
REMARK 500 17 ARG A 5 0.18 SIDE CHAIN
REMARK 500 17 ARG A 36 0.15 SIDE CHAIN
REMARK 500 18 ARG A 5 0.19 SIDE CHAIN
REMARK 500 18 ARG A 8 0.14 SIDE CHAIN
REMARK 500 18 ARG A 36 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 70 PLANE DEVIATIONS.
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 74
DBREF 1DQC A 1 73 UNP P91818 P91818_TACTR 23 95
SEQRES 1 A 74 TYR LEU ALA PHE ARG CYS GLY ARG TYR SER PRO CYS LEU
SEQRES 2 A 74 ASP ASP GLY PRO ASN VAL ASN LEU TYR SER CYS CYS SER
SEQRES 3 A 74 PHE TYR ASN CYS HIS LYS CYS LEU ALA ARG LEU GLU ASN
SEQRES 4 A 74 CYS PRO LYS GLY LEU HIS TYR ASN ALA TYR LEU LYS VAL
SEQRES 5 A 74 CYS ASP TRP PRO SER LYS ALA GLY CYS THR SER VAL ASN
SEQRES 6 A 74 LYS GLU CYS HIS LEU TRP LYS THR NH2
HET NH2 A 74 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 PRO A 56 ALA A 59 1 4
SHEET 1 A 3 PRO A 17 VAL A 19 0
SHEET 2 A 3 SER A 26 HIS A 31 -1 O TYR A 28 N ASN A 18
SHEET 3 A 3 LEU A 34 ASN A 39 -1 O LEU A 34 N HIS A 31
SHEET 1 B 2 HIS A 45 ASN A 47 0
SHEET 2 B 2 VAL A 52 ASP A 54 -1 N ASP A 54 O HIS A 45
SSBOND 1 CYS A 6 CYS A 33 1555 1555 2.02
SSBOND 2 CYS A 12 CYS A 30 1555 1555 2.02
SSBOND 3 CYS A 24 CYS A 61 1555 1555 2.02
SSBOND 4 CYS A 25 CYS A 68 1555 1555 2.02
SSBOND 5 CYS A 40 CYS A 53 1555 1555 2.02
LINK C THR A 73 N NH2 A 74 1555 1555 1.31
SITE 1 AC1 1 THR A 73
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 16 2 Bytes