Header list of 1kdf.pdb file
Complete list - 3 202 Bytes
HEADER ANTIFREEZE PROTEIN 08-JUL-96 1KDF
TITLE NORTH-ATLANTIC OCEAN POUT ANTIFREEZE PROTEIN TYPE III ISOFORM HPLC12
TITLE 2 MUTANT, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIFREEZE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: KDEL;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: TYPE III ISOFORM HPLC 12, QAE-COMPONENT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MACROZOARCES AMERICANUS;
SOURCE 3 ORGANISM_COMMON: OCEAN POUT;
SOURCE 4 ORGANISM_TAXID: 8199;
SOURCE 5 VARIANT: HPLC-12;
SOURCE 6 TISSUE: BLOOD;
SOURCE 7 GENE: K38;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: JM83;
SOURCE 11 EXPRESSION_SYSTEM_GENE: K38
KEYWDS ICE BINDING PROTEIN, THERMAL HYSTERESIS PROTEIN, ANTIFREEZE PROTEIN,
KEYWDS 2 GLYCOPROTEIN
EXPDTA SOLUTION NMR
AUTHOR F.D.SONNICHSEN,C.I.DELUCA,P.L.DAVIES,B.D.SYKES
REVDAT 4 03-NOV-21 1KDF 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1KDF 1 VERSN
REVDAT 2 01-APR-03 1KDF 1 JRNL
REVDAT 1 21-APR-97 1KDF 0
JRNL AUTH F.D.SONNICHSEN,C.I.DELUCA,P.L.DAVIES,B.D.SYKES
JRNL TITL REFINED SOLUTION STRUCTURE OF TYPE III ANTIFREEZE PROTEIN:
JRNL TITL 2 HYDROPHOBIC GROUPS MAY BE INVOLVED IN THE ENERGETICS OF THE
JRNL TITL 3 PROTEIN-ICE INTERACTION.
JRNL REF STRUCTURE V. 4 1325 1996
JRNL REFN ISSN 0969-2126
JRNL PMID 8939756
JRNL DOI 10.1016/S0969-2126(96)00140-2
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.CHAO,F.D.SONNICHSEN,C.I.DELUCA,B.D.SYKES,P.L.DAVIES
REMARK 1 TITL STRUCTURE-FUNCTION RELATIONSHIP IN THE GLOBULAR TYPE III
REMARK 1 TITL 2 ANTIFREEZE PROTEIN: IDENTIFICATION OF A CLUSTER OF SURFACE
REMARK 1 TITL 3 RESIDUES REQUIRED FOR BINDING TO ICE
REMARK 1 REF PROTEIN SCI. V. 3 1760 1994
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH F.D.SONNICHSEN,B.D.SYKES,H.CHAO,P.L.DAVIES
REMARK 1 TITL THE NONHELICAL STRUCTURE OF ANTIFREEZE PROTEIN TYPE III
REMARK 1 REF SCIENCE V. 259 1154 1993
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KDF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174412.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQCOSY; TOCSY; NOESY; 15N_TOCSY
REMARK 210 HMQC; 3D-HCCH-TOCSY HMQC-J; 15N-
REMARK 210 NOESYHMQC; 3D-15N/13C-NOESYHSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : DG_SUB_EMBED, DGSA, REFINE
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : AVERAGE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 MET A 0
REMARK 465 LYS A 66
REMARK 465 ASP A 67
REMARK 465 GLU A 68
REMARK 465 LEU A 69
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 MET A 21 30.82 -98.54
REMARK 500 LEU A 40 35.00 -98.28
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 ARG A 23 0.24 SIDE CHAIN
REMARK 500 ARG A 39 0.29 SIDE CHAIN
REMARK 500 ARG A 47 0.28 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: 1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ICE-BINDING RESIDUES.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KDE RELATED DB: PDB
REMARK 900 ENSEMBLE
DBREF 1KDF A 1 65 UNP P19614 ANPC_MACAM 1 65
SEQADV 1KDF ALA A 64 UNP P19614 PRO 64 ENGINEERED MUTATION
SEQADV 1KDF ALA A 65 UNP P19614 PRO 65 ENGINEERED MUTATION
SEQRES 1 A 70 MET ASN GLN ALA SER VAL VAL ALA ASN GLN LEU ILE PRO
SEQRES 2 A 70 ILE ASN THR ALA LEU THR LEU VAL MET MET ARG SER GLU
SEQRES 3 A 70 VAL VAL THR PRO VAL GLY ILE PRO ALA GLU ASP ILE PRO
SEQRES 4 A 70 ARG LEU VAL SER MET GLN VAL ASN ARG ALA VAL PRO LEU
SEQRES 5 A 70 GLY THR THR LEU MET PRO ASP MET VAL LYS GLY TYR ALA
SEQRES 6 A 70 ALA LYS ASP GLU LEU
HELIX 1 1 LEU A 19 MET A 21 5 3
SHEET 1 A 2 SER A 4 VAL A 6 0
SHEET 2 A 2 ARG A 23 GLU A 25 -1 N GLU A 25 O SER A 4
CISPEP 1 THR A 28 PRO A 29 0 0.18
SITE 1 1 5 GLN A 9 ASN A 14 THR A 15 THR A 18
SITE 2 1 5 GLN A 44
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
Complete list - 3 202 Bytes