HEADER SUGAR BINDING PROTEIN 23-JUL-17 5Y22
TITLE NMR-BASED MODEL OF THE 22 AMINO ACID PEPTIDE IN POLYSIALYLTRANSFERASE
TITLE 2 DOMAIN (PSTD) OF THE POLYSIALYLTRANSFERASE ST8SIA IV
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 22AA-PSTD PEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 258-279;
COMPND 5 EC: 2.4.99.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606
KEYWDS POLYSIALYLTRANSFERASE DOMAIN (PSTD) POLYSIALYLTRANSFERASE ST8SIA IV
KEYWDS 2 POLYSIALIC ACID (POLYSIA), SUGAR BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.LU,S.M.LIAO,J.M.HUANG,Z.L.LU,D.CHEN,X.H.LIU,G.P.ZHOU,R.B.HUANG
REVDAT 2 14-JUN-23 5Y22 1 REMARK
REVDAT 1 29-NOV-17 5Y22 0
JRNL AUTH B.LU,S.M.LIAO,D.CHEN,X.H.LIU,G.P.ZHOU,R.B.HUANG
JRNL TITL NMR-BASED MODEL OF THE 22 AMINO ACID PEPTIDE IN
JRNL TITL 2 POLYSIALYLTRANSFERASE DOMAIN (PSTD) OF THE
JRNL TITL 3 POLYSIALYLTRANSFERASE ST8SIA IV
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 8.9, CNS 1.2.1
REMARK 3 AUTHORS : DELAGLIO, GRZESIEK, VUISTER, ZHU, PFEIFER AND BAX
REMARK 3 (NMRPIPE), BRUNGER, ADAMS, CLORE, GROS, NILGES AND
REMARK 3 READ (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5Y22 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1300003524.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.0 MM 22AA-PSTD PEPTIDE, 40 %
REMARK 210 TRIFLUOROETHANOL-D3,
REMARK 210 TRIFLUOROETHANOL/WATER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 2D 1H-1H NOESY; 2D 1H-1H TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : DD2
REMARK 210 SPECTROMETER MANUFACTURER : AGILENT
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANALYSIS 2.4, ARIA 2.3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: 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 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 2 PRO A 21 27.63 -78.79
REMARK 500 4 PRO A 21 105.48 -43.11
REMARK 500 5 ARG A 2 121.37 73.39
REMARK 500 5 PRO A 21 88.99 -61.47
REMARK 500 8 PRO A 21 84.53 -63.80
REMARK 500 10 ILE A 18 91.97 52.56
REMARK 500 11 ILE A 18 77.89 47.27
REMARK 500 11 PRO A 21 44.10 -76.55
REMARK 500 12 ILE A 18 71.92 -105.62
REMARK 500 12 PRO A 21 102.56 -47.97
REMARK 500 13 ILE A 18 84.62 60.13
REMARK 500 17 ARG A 2 123.53 70.07
REMARK 500 17 PRO A 21 105.96 -55.95
REMARK 500 18 ASN A 14 -63.16 -93.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 36109 RELATED DB: BMRB
REMARK 900 NMR-BASED MODEL OF THE 22 AMINO ACID PEPTIDE IN
REMARK 900 POLYSIALYLTRANSFERASE DOMAIN (PSTD) OF THE POLYSIALYLTRANSFERASE
REMARK 900 ST8SIA IV
DBREF 5Y22 A 1 22 UNP Q92187 SIA8D_HUMAN 258 279
SEQRES 1 A 22 LEU ARG LEU ILE HIS ALA VAL ARG GLY TYR TRP LEU THR
SEQRES 2 A 22 ASN LYS VAL PRO ILE LYS ARG PRO SER
HELIX 1 AA1 ARG A 2 THR A 13 1 12
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
(ATOM LINES ARE NOT SHOWN.)
END