HEADER HYDROLASE(O-GLYCOSYL) 13-SEP-94 1LSM
TITLE THERMAL STABILITY DETERMINANTS OF CHICKEN EGG-WHITE
TITLE 2 LYSOZYME CORE MUTANTS: HYDROPHOBICITY, PACKING VOLUME AND
TITLE 3 CONSERVED BURIED WATER MOLECULES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEN EGG WHITE LYSOZYME;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.17;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 ORGAN: EGG
KEYWDS HYDROLASE(O-GLYCOSYL)
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.HOLLAND,P.SHIH
REVDAT 2 24-FEB-09 1LSM 1 VERSN
REVDAT 1 30-NOV-94 1LSM 0
JRNL AUTH P.SHIH,D.R.HOLLAND,J.F.KIRSCH
JRNL TITL THERMAL STABILITY DETERMINANTS OF CHICKEN
JRNL TITL 2 EGG-WHITE LYSOZYME CORE MUTANTS: HYDROPHOBICITY,
JRNL TITL 3 PACKING VOLUME, AND CONSERVED BURIED WATER
JRNL TITL 4 MOLECULES.
JRNL REF PROTEIN SCI. V. 4 2050 1995
JRNL REFN ISSN 0961-8368
JRNL PMID 8535241
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.P.WILSON,B.A.MALCOLM,B.W.MATTHEWS
REMARK 1 TITL STRUCTURAL AND THERMODYNAMIC ANALYSIS OF
REMARK 1 TITL 2 COMPENSATING MUTATIONS WITHIN THE CORE OF CHICKEN
REMARK 1 TITL 3 EGG WHITE LYSOZYME
REMARK 1 REF J.BIOL.CHEM. V. 267 10842 1992
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.A.MALCOLM,K.P.WILSON,B.W.MATTHEWS,J.F.KIRSCH,
REMARK 1 AUTH 2 A.C.WILSON
REMARK 1 TITL ANCESTRAL LYSOZYMES RECONSTRUCTED, NEUTRALITY
REMARK 1 TITL 2 TESTED, AND THERMOSTABILITY LINKED TO HYDROCARBON
REMARK 1 TITL 3 PACKING
REMARK 1 REF NATURE V. 344 86 1990
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 11062
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1000
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 170
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.015 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 2.300 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LSM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 18.90000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.54000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.54000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 28.35000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.54000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.54000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 9.45000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.54000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.54000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 28.35000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.54000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.54000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 9.45000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 18.90000
REMARK 290
REMARK 290 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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 STRUCTURAL DIFFERENCES BETWEEN WILDTYPE AND THE MUTANT
REMARK 400 MODELS ARE CONFINED TO THE REGION AROUND THE MUTATION
REMARK 400 (RESIDUE 91).
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 203 O HOH A 203 7556 2.09
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 48 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 48 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ASP A 52 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ASP A 66 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 125 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 177 DISTANCE = 5.01 ANGSTROMS
REMARK 525 HOH A 189 DISTANCE = 5.58 ANGSTROMS
REMARK 525 HOH A 190 DISTANCE = 5.36 ANGSTROMS
REMARK 525 HOH A 192 DISTANCE = 5.29 ANGSTROMS
REMARK 525 HOH A 228 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH A 229 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH A 249 DISTANCE = 7.67 ANGSTROMS
REMARK 525 HOH A 258 DISTANCE = 7.82 ANGSTROMS
REMARK 525 HOH A 259 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH A 278 DISTANCE = 8.95 ANGSTROMS
REMARK 525 HOH A 294 DISTANCE = 5.35 ANGSTROMS
REMARK 525 HOH A 304 DISTANCE = 9.92 ANGSTROMS
REMARK 525 HOH A 308 DISTANCE = 20.21 ANGSTROMS
DBREF 1LSM A 1 129 UNP P00698 LYSC_CHICK 19 147
SEQADV 1LSM LEU A 55 UNP P00698 ILE 73 CONFLICT
SEQADV 1LSM THR A 91 UNP P00698 SER 109 CONFLICT
SEQADV 1LSM SER A 101 UNP P00698 ASP 119 CONFLICT
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 LEU 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 THR
SEQRES 8 A 129 VAL ASN CYS ALA LYS LYS ILE VAL SER SER 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
FORMUL 2 HOH *170(H2 O)
HELIX 1 H1 GLY A 4 GLY A 16 1 13
HELIX 2 H2 LEU A 25 PHE A 34 1 10
HELIX 3 H3 PRO A 79 LEU A 84 5 6
HELIX 4 H4 ILE A 88 SER A 100 1 13
HELIX 5 H5 GLY A 104 TRP A 108 5 5
HELIX 6 H6 VAL A 109 ARG A 114 1 6
HELIX 7 H7 VAL A 120 ILE A 124 5 5
SHEET 1 S1 3 ALA A 42 ASN A 46 0
SHEET 2 S1 3 GLY A 49 GLY A 54 -1 O SER A 50 N ASN A 46
SHEET 3 S1 3 LEU A 56 SER A 60 -1 O SER A 60 N THR A 51
SSBOND 1 CYS A 6 CYS A 127 1555 1555 2.01
SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.04
SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.08
SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.03
CRYST1 79.080 79.080 37.800 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 0.012645 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012645 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026455 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
