HEADER HYDROLASE 29-MAY-01 1JA7
TITLE BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME: A POWDER
TITLE 2 DIFFRACTION STUDY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C; ALLERGEN GAL D 4; GAL D IV;
COMPND 5 EC: 3.2.1.17;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS POWDER DIFFRACTION, RIETVELD REFINEMENT, LYSOZYME, HYDROLASE
EXPDTA POWDER DIFFRACTION
AUTHOR R.B.VON DREELE
REVDAT 5 16-AUG-23 1JA7 1 HETSYN
REVDAT 4 29-JUL-20 1JA7 1 COMPND REMARK HETNAM SITE
REVDAT 4 2 1 ATOM
REVDAT 3 24-FEB-09 1JA7 1 VERSN
REVDAT 2 30-NOV-01 1JA7 1 JRNL
REVDAT 1 15-JUN-01 1JA7 0
JRNL AUTH R.B.VON DREELE
JRNL TITL BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME: A
JRNL TITL 2 POWDER DIFFRACTION STUDY.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 57 1836 2001
JRNL REFN ISSN 0907-4449
JRNL PMID 11717496
JRNL DOI 10.1107/S0907444901015748
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.B.VON DREELE
REMARK 1 TITL COMBINED RIETVELD AND STEREOCHEMICAL RESTRAINT REFINEMENT OF
REMARK 1 TITL 2 A PROTEIN CRYSTAL STRUCTURE
REMARK 1 REF J.APPL.CRYSTALLOGR. V. 32 1084 1999
REMARK 1 REFN ISSN 0021-8898
REMARK 1 DOI 10.1107/S002188989901064X
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.B.VON DREELE,P.W.STEPHENS,R.H.BLESSING,G.D.SMITH
REMARK 1 TITL THE FIRST PROTEIN CRYSTAL STRUCTURE DETERMINED FROM
REMARK 1 TITL 2 RESOLUTION X-RAY POWDER DIFFRACTION DATA: A VARIANT OF THE
REMARK 1 TITL 3 T3R3 HUMAN INSULIN ZINC COMPLEX PRODUCED BY GRINDING
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 56 1549 2000
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444900013901
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 4
REMARK 4 1JA7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1000013553.
REMARK 250
REMARK 250 EXPERIMENTAL DETAILS
REMARK 250 EXPERIMENT TYPE : POWDER DIFFRACTION
REMARK 250 DATE OF DATA COLLECTION : 22-OCT-00
REMARK 250
REMARK 250 REMARK: NULL
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: 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 PRO A 70 C - N - CD ANGL. DEV. = -13.1 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 TRP A 28 -61.07 -105.72
REMARK 500 SER A 36 9.48 -150.42
REMARK 500 MET A 105 -7.64 -56.38
REMARK 500 ASP A 119 64.26 -100.69
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 5 0.27 SIDE CHAIN
REMARK 500 ARG A 14 0.28 SIDE CHAIN
REMARK 500 ARG A 21 0.27 SIDE CHAIN
REMARK 500 ARG A 45 0.22 SIDE CHAIN
REMARK 500 ARG A 61 0.16 SIDE CHAIN
REMARK 500 ARG A 73 0.11 SIDE CHAIN
REMARK 500 ARG A 125 0.24 SIDE CHAIN
REMARK 500 ARG A 128 0.27 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JA2 RELATED DB: PDB
REMARK 900 RELATED ID: 1JA4 RELATED DB: PDB
REMARK 900 RELATED ID: 1JA6 RELATED DB: PDB
DBREF 1JA7 A 1 129 UNP P00698 LYSC_CHICK 19 147
SEQRES 1 A 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 A 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 A 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 A 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 A 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 A 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 A 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 A 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 A 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 A 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
HET NDG A 201 15
HETNAM NDG 2-ACETAMIDO-2-DEOXY-ALPHA-D-GLUCOPYRANOSE
HETSYN NDG N-ACETYL-ALPHA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-
HETSYN 2 NDG ALPHA-D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-
HETSYN 3 NDG ACETAMIDO-2-DEOXY-GLUCOSE; 2-(ACETYLAMINO)-2-DEOXY-A-
HETSYN 4 NDG D-GLUCOPYRANOSE
FORMUL 2 NDG C8 H15 N O6
HELIX 1 1 ALA A 11 HIS A 15 5 5
HELIX 2 2 ASN A 19 TYR A 23 5 5
HELIX 3 3 SER A 24 ASN A 27 5 4
HELIX 4 4 TRP A 28 LYS A 33 1 6
HELIX 5 5 CYS A 80 SER A 85 1 6
HELIX 6 6 SER A 91 VAL A 99 1 9
HELIX 7 7 ASN A 103 TRP A 108 5 6
HELIX 8 8 VAL A 109 CYS A 115 1 7
HELIX 9 9 VAL A 120 ARG A 125 1 6
SHEET 1 A 2 ASP A 52 TYR A 53 0
SHEET 2 A 2 ILE A 58 ASN A 59 -1 N ILE A 58 O TYR A 53
SSBOND 1 CYS A 6 CYS A 127 1555 1555 2.02
SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.04
SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.06
SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.02
CRYST1 78.963 78.963 38.215 90.00 90.00 90.00 P 43 21 2 8
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 0.012664 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012664 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026168 0.00000
(ATOM LINES ARE NOT SHOWN.)
END