HEADER HYDROLASE/INHIBITOR 08-NOV-01 1GPQ
TITLE STRUCTURE OF IVY COMPLEXED WITH ITS TARGET, HEWL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INHIBITOR OF VERTEBRATE LYSOZYME;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: IVY;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: COMPLEXED WITH HEWL IN CRYSTAL;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: LYSOZYME C;
COMPND 9 CHAIN: C, D;
COMPND 10 EC: 3.2.1.17;
COMPND 11 OTHER_DETAILS: COMPLEXED WITH IVY IN CRYSTAL
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 9 ORGANISM_COMMON: CHICKEN;
SOURCE 10 ORGANISM_TAXID: 9031
KEYWDS HYDROLASE-INHIBITOR COMPLEX, LYSOZYME-INHIBITOR COMPLEX, TYPE-C
KEYWDS 2 LYSOZYME INHIBITOR, HYDROLASE, GLYCOSIDASE, BACTERIAL TARGETS AT
KEYWDS 3 IGS-CNRS, FRANCE, BIGS, STRUCTURAL GENOMICS
EXPDTA X-RAY DIFFRACTION
AUTHOR C.ABERGEL,V.MONCHOIS,J.-M.CLAVERIE
REVDAT 4 13-DEC-23 1GPQ 1 REMARK
REVDAT 3 29-JUN-11 1GPQ 1 VERSN
REVDAT 2 24-FEB-09 1GPQ 1 VERSN
REVDAT 1 11-MAR-03 1GPQ 0
JRNL AUTH C.ABERGEL,V.MONCHOIS,D.BYRNE,S.CHENIVESSE,F.LEMBO,
JRNL AUTH 2 J.LAZZARONI,J.CLAVERIE
JRNL TITL STRUCTURE AND EVOLUTION OF THE IVY PROTEIN FAMILY,
JRNL TITL 2 UNEXPECTED LYSOZYME INHIBITORS IN GRAM-NEGATIVE BACTERIA.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 104 6394 2007
JRNL REFN ISSN 0027-8424
JRNL PMID 17405861
JRNL DOI 10.1073/PNAS.0611019104
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH V.MONCHOIS,C.ABERGEL,J.STURGIS,S.JEUDY,J.-M.CLAVERIE
REMARK 1 TITL ESCHERICHIA COLI YKFE "ORFAN" GENE ENCODES A POTENT
REMARK 1 TITL 2 INHIBITOR OF C-TYPE LYSOZYME
REMARK 1 REF J.BIOL.CHEM. V. 276 18437 2001
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 11278658
REMARK 1 DOI 10.1074/JBC.M010297200
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.ABERGEL,V.MONCHOIS,S.CHENIVESSE,S.JEUDY,J.-M.CLAVERIE
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC STUDY OF
REMARK 1 TITL 2 B0220, AN "ORFAN" PROTEIN OF UNKNOWN FUNCTION FROM
REMARK 1 TITL 3 ESCHERICHIA COLI
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 56 1694 2000
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 11092949
REMARK 1 DOI 10.1107/S0907444900015316
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 688920.930
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 58780
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5962
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8832
REMARK 3 BIN R VALUE (WORKING SET) : 0.1860
REMARK 3 BIN FREE R VALUE : 0.2130
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 991
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.007
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3923
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 635
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.66000
REMARK 3 B22 (A**2) : 2.36000
REMARK 3 B33 (A**2) : -0.69000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.93000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.16
REMARK 3 ESD FROM SIGMAA (A) : 0.05
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.06
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.970
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.340 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.110 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.050 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.040 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 48.18
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GPQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1290008683.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 9.00
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9798
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58982
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.13100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SOLVE, AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1HEL
REMARK 200
REMARK 200 REMARK: UNCOMPLEXED, AND UNREFINED MAD IVY STRUCTURE WAS ALSO USED
REMARK 200 FOR MOLECULAR REPLACEMENT
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4000, 5% GLYCEROL, CHES BUFFER
REMARK 280 0.1M PH 9.0, PROTEIN CONCENTRATION: 5MG.ML-1, PH 9.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
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 29.78000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLN A 1
REMARK 465 ARG A 129
REMARK 465 HIS A 130
REMARK 465 HIS A 131
REMARK 465 HIS A 132
REMARK 465 HIS A 133
REMARK 465 HIS A 134
REMARK 465 HIS A 135
REMARK 465 GLN B 1
REMARK 465 HIS B 130
REMARK 465 HIS B 131
REMARK 465 HIS B 132
REMARK 465 HIS B 133
REMARK 465 HIS B 134
REMARK 465 HIS B 135
REMARK 465 ARG C 128
REMARK 465 LEU C 129
REMARK 465 LEU D 129
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 CYS B 57 CB - CA - C ANGL. DEV. = -12.7 DEGREES
REMARK 500 CYS B 57 CA - CB - SG ANGL. DEV. = 25.1 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 ASP A 61 47.24 -150.87
REMARK 500 ASN A 76 -22.51 78.22
REMARK 500 ILE A 105 -76.18 -114.51
REMARK 500 ASP B 3 -57.14 173.51
REMARK 500 ASP B 61 43.73 -149.17
REMARK 500 LYS B 88 -33.35 -144.54
REMARK 500 ILE B 105 -71.68 -117.10
REMARK 500 ARG D 68 17.23 -140.79
REMARK 500 SER D 100 46.73 -76.62
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 A2009 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH A2014 DISTANCE = 7.03 ANGSTROMS
REMARK 525 HOH C2018 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH C2025 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH C2069 DISTANCE = 7.06 ANGSTROMS
REMARK 525 HOH C2076 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH C2079 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH D2004 DISTANCE = 7.36 ANGSTROMS
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 132L RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 193L RELATED DB: PDB
REMARK 900 THE 1.33 A STRUCTURE OF TETRAGONAL HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 194L RELATED DB: PDB
REMARK 900 THE 1.40 A STRUCTURE OF SPACEHAB-01 HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1A2Y RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME, D18A MUTANT, IN COMPLEX WITH MOUSE
REMARK 900 MONOCLONAL ANTIBODY D1.3
REMARK 900 RELATED ID: 1AKI RELATED DB: PDB
REMARK 900 THE STRUCTURE OF THE ORTHORHOMBIC FORM OF HEN EGG-WHITE LYSOZYME AT
REMARK 900 1.5 ANGSTROMS RESOLUTION
REMARK 900 RELATED ID: 1AT5 RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME WITH A SUCCINIMIDE RESIDUE
REMARK 900 RELATED ID: 1AT6 RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME WITH A ISOASPARTATE RESIDUE
REMARK 900 RELATED ID: 1AZF RELATED DB: PDB
REMARK 900 CHICKEN EGG WHITE LYSOZYME CRYSTAL GROWN IN BROMIDE SOLUTION
REMARK 900 RELATED ID: 1B0D RELATED DB: PDB
REMARK 900 STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON POLYMORPHIC LYSOZYME
REMARK 900 CRYSTALS
REMARK 900 RELATED ID: 1B2K RELATED DB: PDB
REMARK 900 STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON POLYMORPHIC LYSOZYME
REMARK 900 CRYSTALS
REMARK 900 RELATED ID: 1BGI RELATED DB: PDB
REMARK 900 ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH TEMPERATURE (310K)
REMARK 900 RELATED ID: 1BHZ RELATED DB: PDB
REMARK 900 LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF HEN EGG WHITE
REMARK 900 LYSOZYME FROM MASC DATA
REMARK 900 RELATED ID: 1BVK RELATED DB: PDB
REMARK 900 HUMANIZED ANTI-LYSOZYME FV COMPLEXED WITH LYSOZYME
REMARK 900 RELATED ID: 1BVX RELATED DB: PDB
REMARK 900 THE 1.8 A STRUCTURE OF GEL GROWN TETRAGONAL HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1BWH RELATED DB: PDB
REMARK 900 THE 1.8 A STRUCTURE OF GROUND CONTROL GROWN TETRAGONAL HEN EGG
REMARK 900 WHITE LYSOZYME
REMARK 900 RELATED ID: 1BWI RELATED DB: PDB
REMARK 900 THE 1.8 A STRUCTURE OF MICROBATCH OIL DROP GROWN TETRAGONAL HEN EGG
REMARK 900 WHITE LYSOZYME
REMARK 900 RELATED ID: 1BWJ RELATED DB: PDB
REMARK 900 THE 1.8 A STRUCTURE OF MICROGRAVITY GROWN TETRAGONAL HEN EGG WHITE
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 1C08 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV-HEN LYSOZYME COMPLEX
REMARK 900 RELATED ID: 1C10 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEW LYSOZYME UNDER PRESSURE OF XENON (8 BAR)
REMARK 900 RELATED ID: 1DPW RELATED DB: PDB
REMARK 900 STRUCTURE OF HEN EGG-WHITE LYSOZYME IN COMPLEX WITH MPD
REMARK 900 RELATED ID: 1DPX RELATED DB: PDB
REMARK 900 STRUCTURE OF HEN EGG-WHITE LYSOZYME
REMARK 900 RELATED ID: 1DQJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ANTI-LYSOZYME ANTIBODY HYHEL-63 COMPLEXED
REMARK 900 WITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1E8L RELATED DB: PDB
REMARK 900 NMR SOLUTION STRUCTURE OF HEN LYSOZYME
REMARK 900 RELATED ID: 1F0W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME GROWN AT PH 6.5
REMARK 900 RELATED ID: 1F10 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME GROWN AT PH 6.5 AT 88%
REMARK 900 RELATIVE HUMIDITY
REMARK 900 RELATED ID: 1F3J RELATED DB: PDB
REMARK 900 HISTOCOMPATIBILITY ANTIGEN I-AG7
REMARK 900 RELATED ID: 1FDL RELATED DB: PDB
REMARK 900 IGG1 FAB FRAGMENT (ANTI-LYSOZYME ANTIBODY D1 .3, KAPPA) - LYSOZYME
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 1FLQ RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE SUBSTITUTED FORGLYCINE
REMARK 900 RELATED ID: 1FLU RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE SUBSTITUTED FORGLYCINE
REMARK 900 RELATED ID: 1FLW RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE SUBSTITUTED FORGLYCINE
REMARK 900 RELATED ID: 1FLY RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE SUBSTITUTED FORGLYCINE
REMARK 900 RELATED ID: 1FN5 RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE SUBSTITUTED FORGLYCINE
REMARK 900 RELATED ID: 1G7H RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME (HEL) COMPLEXEDWITH THE
REMARK 900 MUTANT ANTI-HEL MONOCLONAL ANTIBODY D1.3(VLW92A)
REMARK 900 RELATED ID: 1G7I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME (HEL) COMPLEXEDWITH THE
REMARK 900 MUTANT ANTI-HEL MONOCLONAL ANTIBODY D1.3 (VLW92F)
REMARK 900 RELATED ID: 1G7J RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME (HEL) COMPLEXEDWITH THE
REMARK 900 MUTANT ANTI-HEL MONOCLONAL ANTIBODY D1.3 (VLW92H)
REMARK 900 RELATED ID: 1G7L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME (HEL) COMPLEXEDWITH THE
REMARK 900 MUTANT ANTI-HEL MONOCLONAL ANTIBODY D1.3 (VLW92S)
REMARK 900 RELATED ID: 1G7M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME (HEL) COMPLEXEDWITH THE
REMARK 900 MUTANT ANTI-HEL MONOCLONAL ANTIBODY D1.3 (VLW92V)
REMARK 900 RELATED ID: 1H6M RELATED DB: PDB
REMARK 900 COVALENT GLYCOSYL-ENZYME INTERMEDIATE OF HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1H87 RELATED DB: PDB
REMARK 900 GADOLINIUM DERIVATIVE OF TETRAGONAL HEN EGG- WHITE LYSOZYME AT 1.7
REMARK 900 A RESOLUTION
REMARK 900 RELATED ID: 1HC0 RELATED DB: PDB
REMARK 900 STRUCTURE OF LYSOZYME WITH PERIODATE
REMARK 900 RELATED ID: 1HEL RELATED DB: PDB
REMARK 900 HEN EGG-WHITE LYSOZYME WILD TYPE
REMARK 900 RELATED ID: 1HEM RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH SER 91 REPLACED BY THR (S91T)
REMARK 900 RELATED ID: 1HEN RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH ILE 55 REPLACED BY VAL AND SER 91 REPLACED BY
REMARK 900 THR (I55V,S91T)
REMARK 900 RELATED ID: 1HEO RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH ILE 55 REPLACED BY VAL (I55V)
REMARK 900 RELATED ID: 1HEP RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH THR 40 REPLACED BY SER, ILE 55 REPLACED BY VAL,
REMARK 900 AND SER 91 REPLACED BY THR (T40S,I55V,S91T)
REMARK 900 RELATED ID: 1HEQ RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH THR 40 REPLACED BY SER AND SER 91 REPLACED BY
REMARK 900 THR (T40S,S91T)
REMARK 900 RELATED ID: 1HER RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH THR 40 REPLACED BY SER (T40S)
REMARK 900 RELATED ID: 1HEW RELATED DB: PDB
REMARK 900 LYSOZYME COMPLEXED WITH THE INHIBITOR TRI-N -ACETYLCHITOTRIOSE
REMARK 900 RELATED ID: 1HF4 RELATED DB: PDB
REMARK 900 STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON POLYMORPHIC LYSOZYME
REMARK 900 CRYSTALS
REMARK 900 RELATED ID: 1HSW RELATED DB: PDB
REMARK 900 LYSOZYME (MUCOPEPTIDE N-ACETYLMURAMYL HYDROLASE)
REMARK 900 RELATED ID: 1HSX RELATED DB: PDB
REMARK 900 LYSOZYME GROWN AT BASIC PH AND ITS LOW HUMIDITY VARIANT
REMARK 900 RELATED ID: 1IC4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT( HD32A)-HEN LYSOZYMECOMPLEX
REMARK 900 RELATED ID: 1IC5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT( HD99A)-HEN LYSOZYMECOMPLEX
REMARK 900 RELATED ID: 1IC7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT( HD32A99A)-HENLYSOZYME
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 1IEE RELATED DB: PDB
REMARK 900 STRUCTURE OF TETRAGONAL HEN EGG WHITE LYSOZYME AT 0.94 AFROM
REMARK 900 CRYSTALS GROWN BY THE COUNTER-DIFFUSION METHOD
REMARK 900 RELATED ID: 1IO5 RELATED DB: PDB
REMARK 900 HYDROGEN AND HYDRATION OF HEN EGG-WHITE LYSOZYME DETERMINEDBY
REMARK 900 NEUTRON DIFFRACTION
REMARK 900 RELATED ID: 1IOQ RELATED DB: PDB
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLINGMUTATION
REMARK 900 RELATED ID: 1IOR RELATED DB: PDB
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLINGMUTATION
REMARK 900 RELATED ID: 1IOS RELATED DB: PDB
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLINGMUTATION
REMARK 900 RELATED ID: 1IOT RELATED DB: PDB
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLINGMUTATION
REMARK 900 RELATED ID: 1JA2 RELATED DB: PDB
REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME: APOWDER
REMARK 900 DIFFRACTION STUDY
REMARK 900 RELATED ID: 1JA4 RELATED DB: PDB
REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME: APOWDER
REMARK 900 DIFFRACTION STUDY
REMARK 900 RELATED ID: 1JA6 RELATED DB: PDB
REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME: APOWDER
REMARK 900 DIFFRACTION STUDY
REMARK 900 RELATED ID: 1JA7 RELATED DB: PDB
REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME: APOWDER
REMARK 900 DIFFRACTION STUDY
REMARK 900 RELATED ID: 1JPO RELATED DB: PDB
REMARK 900 LOW TEMPERATURE ORTHORHOMBIC LYSOZYME
REMARK 900 RELATED ID: 1JTO RELATED DB: PDB
REMARK 900 DEGENERATE INTERFACES IN ANTIGEN-ANTIBODY COMPLEXES
REMARK 900 RELATED ID: 1KIP RELATED DB: PDB
REMARK 900 FV MUTANT Y(B 32)A (VH DOMAIN) OF MOUSE MONOCLONAL ANTIBODY D1.3
REMARK 900 COMPLEXED WITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1KIQ RELATED DB: PDB
REMARK 900 FV MUTANT Y(B 101)F (VH DOMAIN) OF MOUSE MONOCLONAL ANTIBODY D1.3
REMARK 900 COMPLEXED WITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1KIR RELATED DB: PDB
REMARK 900 FV MUTANT Y(A 50)S (VL DOMAIN) OF MOUSE MONOCLONAL ANTIBODY D1.3
REMARK 900 COMPLEXED WITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1KXW RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1KXX RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1KXY RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1LCN RELATED DB: PDB
REMARK 900 MONOCLINIC HEN EGG WHITE LYSOZYME, THIOCYANATE COMPLEX
REMARK 900 RELATED ID: 1LKR RELATED DB: PDB
REMARK 900 MONOCLINIC HEN EGG WHITE LYSOZYME IODIDE
REMARK 900 RELATED ID: 1LKS RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME NITRATE
REMARK 900 RELATED ID: 1LMA RELATED DB: PDB
REMARK 900 LYSOZYME (88 PERCENT HUMIDITY)
REMARK 900 RELATED ID: 1LPI RELATED DB: PDB
REMARK 900 HEW LYSOZYME: TRP...NA CATION-PI INTERACTION
REMARK 900 RELATED ID: 1LSA RELATED DB: PDB
REMARK 900 LYSOZYME (120 K)
REMARK 900 RELATED ID: 1LSB RELATED DB: PDB
REMARK 900 LYSOZYME (180 K)
REMARK 900 RELATED ID: 1LSC RELATED DB: PDB
REMARK 900 LYSOZYME (250 K)
REMARK 900 RELATED ID: 1LSD RELATED DB: PDB
REMARK 900 LYSOZYME (280 K)
REMARK 900 RELATED ID: 1LSE RELATED DB: PDB
REMARK 900 LYSOZYME (295 K)
REMARK 900 RELATED ID: 1LSF RELATED DB: PDB
REMARK 900 LYSOZYME (95 K)
REMARK 900 RELATED ID: 1LSG RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: LYSOZYME MODIFIED WITH HUMAN FIBRINOGEN GAMMA;
REMARK 900 CHAIN: NULL; ENGINEERED; THE 14-RESIDUE C-TERMINUS ( RESIDUES 398 -
REMARK 900 411) OF THE HUMAN FIBRINOGEN GAMMA CHAIN FUSED TO THE C-TERMINUS OF
REMARK 900 CHICKEN EGG WHITE LYSOZYME; MUTATION: N-TERM MET
REMARK 900 RELATED ID: 1LSM RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH ILE 55 REPLACED BY LEU, SER 91 REPLACED BY THR,
REMARK 900 AND ASP 101 REPLACED BY SER (I55L,S91T,D101S)
REMARK 900 RELATED ID: 1LSN RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH SER 91 REPLACED BY ALA (S91A)
REMARK 900 RELATED ID: 1LSY RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH ASP 52 REPLACED BY SER (D52S)
REMARK 900 RELATED ID: 1LSZ RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH ASP 52 REPLACED BY SER (D52S) COMPLEXED WITH
REMARK 900 GLCNAC4 (TETRA-N- ACETYL CHITOTETRAOSE)
REMARK 900 RELATED ID: 1LYO RELATED DB: PDB
REMARK 900 CROSS-LINKED LYSOZYME CRYSTAL IN NEAT WATER
REMARK 900 RELATED ID: 1LYS RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 1LYZ RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 1LZ8 RELATED DB: PDB
REMARK 900 LYSOZYME PHASED ON ANOMALOUS SIGNAL OF SULFURS AND CHLORINES
REMARK 900 RELATED ID: 1LZ9 RELATED DB: PDB
REMARK 900 ANOMALOUS SIGNAL OF SOLVENT BROMINES USED FOR PHASING OF LYSOZYME
REMARK 900 RELATED ID: 1LZA RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 1LZB RELATED DB: PDB
REMARK 900 LYSOZYME CO-CRYSTALLIZED WITH TRI-N-ACETYL- CHITOTRIOSE (PH 4.7)
REMARK 900 RELATED ID: 1LZC RELATED DB: PDB
REMARK 900 LYSOZYME CO-CRYSTALLIZED WITH TETRA-N-ACETYL -CHITOTETRAOSE (PH 4.7)
REMARK 900 RELATED ID: 1LZD RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH TRP 62 REPLACED BY TYR (W62Y)
REMARK 900 RELATED ID: 1LZE RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH TRP 62 REPLACED BY TYR (W62Y) CO-CRYSTALLIZED
REMARK 900 WITH TRI-N- ACETYL-CHITOTRIOSE (PH 4.7)
REMARK 900 RELATED ID: 1LZG RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH TRP 62 REPLACED BY PHE (W62F) CO-CRYSTALLIZED
REMARK 900 WITH TRI-N- ACETYL-CHITOTRIOSE (PH 4.7)
REMARK 900 RELATED ID: 1LZH RELATED DB: PDB
REMARK 900 LYSOZYME (MONOCLINIC)
REMARK 900 RELATED ID: 1LZN RELATED DB: PDB
REMARK 900 NEUTRON STRUCTURE OF HEN EGG-WHITE LYSOZYME
REMARK 900 RELATED ID: 1LZT RELATED DB: PDB
REMARK 900 LYSOZYME , TRICLINIC CRYSTAL FORM
REMARK 900 RELATED ID: 1MEL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A CAMEL SINGLE-DOMAIN VH ANTIBODY FRAGMENT IN
REMARK 900 COMPLEX WITH LYSOZYME
REMARK 900 RELATED ID: 1MLC RELATED DB: PDB
REMARK 900 MONOCLONAL ANTIBODY FAB D44.1 RAISED AGAINST CHICKEN EGG-WHITE
REMARK 900 LYSOZYME COMPLEXED WITH LYSOZYME
REMARK 900 RELATED ID: 1QIO RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE CAUSED BY INTENSE
REMARK 900 SYNCHROTRON RADIATION TO HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1QTK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEW LYSOZYME UNDER PRESSURE OF KRYPTON (55 BAR)
REMARK 900 RELATED ID: 1RCM RELATED DB: PDB
REMARK 900 LYSOZYME (PARTIALLY REDUCED, CARBOXYMETHYLATED (6,127-RCM))
REMARK 900 RELATED ID: 1RFP RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UCO RELATED DB: PDB
REMARK 900 HEN EGG-WHITE LYSOZYME, LOW HUMIDITY FORM
REMARK 900 RELATED ID: 1UIA RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIB RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIC RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UID RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIE RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIF RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIG RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIH RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1XEI RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION
REMARK 900 RELATED ID: 1XEJ RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION
REMARK 900 RELATED ID: 1XEK RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION
REMARK 900 RELATED ID: 2HFM RELATED DB: PDB
REMARK 900 IGG1 FV FRAGMENT (HYHEL-10) AND LYSOZYME COMPLEX (THEORETICAL MODEL)
REMARK 900 RELATED ID: 2IFF RELATED DB: PDB
REMARK 900 IGG1 FAB FRAGMENT (HYHEL-5) COMPLEXED WITH LYSOZYME MUTANT WITH ARG
REMARK 900 68 REPLACED BY LYS (R68K)
REMARK 900 RELATED ID: 2LYM RELATED DB: PDB
REMARK 900 LYSOZYME (1 ATMOSPHERE, 1.4 M NACL)
REMARK 900 RELATED ID: 2LYO RELATED DB: PDB
REMARK 900 CROSS-LINKED CHICKEN LYSOZYME CRYSTAL IN 90 % ACETONITRILE-WATER
REMARK 900 RELATED ID: 2LYZ RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 2LZH RELATED DB: PDB
REMARK 900 LYSOZYME (ORTHORHOMBIC)
REMARK 900 RELATED ID: 2LZT RELATED DB: PDB
REMARK 900 LYSOZYME , TRICLINIC CRYSTAL FORM
REMARK 900 RELATED ID: 3HFL RELATED DB: PDB
REMARK 900 IGG1 FAB FRAGMENT (HY/HEL-5) COMPLEXED WITH LYSOZYME
REMARK 900 RELATED ID: 3HFM RELATED DB: PDB
REMARK 900 IGG1 FAB FRAGMENT (HYHEL-10) AND LYSOZYME COMPLEX
REMARK 900 RELATED ID: 3LYM RELATED DB: PDB
REMARK 900 LYSOZYME (1000 ATMOSPHERES, 1.4 M NACL)
REMARK 900 RELATED ID: 3LYO RELATED DB: PDB
REMARK 900 CROSS-LINKED CHICKEN LYSOZYME CRYSTAL IN 95 % ACETONITRILE-WATER
REMARK 900 RELATED ID: 3LYT RELATED DB: PDB
REMARK 900 LYSOZYME (100 KELVIN)
REMARK 900 RELATED ID: 3LYZ RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 3LZT RELATED DB: PDB
REMARK 900 REFINEMENT OF TRICLINIC LYSOZYME AT ATOMIC RESOLUTION
REMARK 900 RELATED ID: 4LYM RELATED DB: PDB
REMARK 900 LYSOZYME (MUCOPEPTIDE N-ACETYLMURAMYL HYDROLASE)
REMARK 900 RELATED ID: 4LYO RELATED DB: PDB
REMARK 900 CROSS-LINKED CHICKEN LYSOZYME CRYSTAL IN NEAT ACETONITRILE, THEN
REMARK 900 BACK-SOAKED IN WATER
REMARK 900 RELATED ID: 4LYT RELATED DB: PDB
REMARK 900 LYSOZYME (298 KELVIN)
REMARK 900 RELATED ID: 4LYZ RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 4LZT RELATED DB: PDB
REMARK 900 ATOMIC RESOLUTION REFINEMENT OF TRICLINIC HEW LYSOZYME AT 295K
REMARK 900 RELATED ID: 5LYM RELATED DB: PDB
REMARK 900 STUDIES OF MONOCLINIC HEN EGG WHITE LYSOZYME. IV. X-RAY REFINEMENT
REMARK 900 AT 1.8 ANGSTROM RESOLUTION AND A COMPARISON OF THE VARIABLE REGIONS
REMARK 900 IN THE POLYMORPHIC FORMS
REMARK 900 RELATED ID: 5LYT RELATED DB: PDB
REMARK 900 LYSOZYME (100 KELVIN)
REMARK 900 RELATED ID: 5LYZ RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 6LYT RELATED DB: PDB
REMARK 900 LYSOZYME (298 KELVIN)
REMARK 900 RELATED ID: 6LYZ RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 7LYZ RELATED DB: PDB
REMARK 900 LYSOZYME TRICLINIC CRYSTAL FORM
REMARK 900 RELATED ID: 8LYZ RELATED DB: PDB
REMARK 900 LYSOZYME IODINE-INACTIVATED
DBREF 1GPQ A 1 129 UNP P45502 IVY_ECOLI 29 157
DBREF 1GPQ B 1 129 UNP P45502 IVY_ECOLI 29 157
DBREF 1GPQ C 1 129 UNP P00698 LYC_CHICK 19 147
DBREF 1GPQ D 1 129 UNP P00698 LYC_CHICK 19 147
SEQADV 1GPQ ARG A 129 UNP P45502 LYS 157 CONFLICT
SEQADV 1GPQ HIS A 130 UNP E7H715 EXPRESSION TAG
SEQADV 1GPQ HIS A 131 UNP E7H715 EXPRESSION TAG
SEQADV 1GPQ HIS A 132 UNP E7H715 EXPRESSION TAG
SEQADV 1GPQ HIS A 133 UNP E7H715 EXPRESSION TAG
SEQADV 1GPQ HIS A 134 UNP E7H715 EXPRESSION TAG
SEQADV 1GPQ HIS A 135 UNP E7H715 EXPRESSION TAG
SEQADV 1GPQ ARG B 129 UNP P45502 LYS 157 CONFLICT
SEQADV 1GPQ HIS B 130 UNP E7H715 EXPRESSION TAG
SEQADV 1GPQ HIS B 131 UNP E7H715 EXPRESSION TAG
SEQADV 1GPQ HIS B 132 UNP E7H715 EXPRESSION TAG
SEQADV 1GPQ HIS B 133 UNP E7H715 EXPRESSION TAG
SEQADV 1GPQ HIS B 134 UNP E7H715 EXPRESSION TAG
SEQADV 1GPQ HIS B 135 UNP E7H715 EXPRESSION TAG
SEQRES 1 A 135 GLN ASP ASP LEU THR ILE SER SER LEU ALA LYS GLY GLU
SEQRES 2 A 135 THR THR LYS ALA ALA PHE ASN GLN MET VAL GLN GLY HIS
SEQRES 3 A 135 LYS LEU PRO ALA TRP VAL MET LYS GLY GLY THR TYR THR
SEQRES 4 A 135 PRO ALA GLN THR VAL THR LEU GLY ASP GLU THR TYR GLN
SEQRES 5 A 135 VAL MET SER ALA CYS LYS PRO HIS ASP CYS GLY SER GLN
SEQRES 6 A 135 ARG ILE ALA VAL MET TRP SER GLU LYS SER ASN GLN MET
SEQRES 7 A 135 THR GLY LEU PHE SER THR ILE ASP GLU LYS THR SER GLN
SEQRES 8 A 135 GLU LYS LEU THR TRP LEU ASN VAL ASN ASP ALA LEU SER
SEQRES 9 A 135 ILE ASP GLY LYS THR VAL LEU PHE ALA ALA LEU THR GLY
SEQRES 10 A 135 SER LEU GLU ASN HIS PRO ASP GLY PHE ASN PHE ARG HIS
SEQRES 11 A 135 HIS HIS HIS HIS HIS
SEQRES 1 B 135 GLN ASP ASP LEU THR ILE SER SER LEU ALA LYS GLY GLU
SEQRES 2 B 135 THR THR LYS ALA ALA PHE ASN GLN MET VAL GLN GLY HIS
SEQRES 3 B 135 LYS LEU PRO ALA TRP VAL MET LYS GLY GLY THR TYR THR
SEQRES 4 B 135 PRO ALA GLN THR VAL THR LEU GLY ASP GLU THR TYR GLN
SEQRES 5 B 135 VAL MET SER ALA CYS LYS PRO HIS ASP CYS GLY SER GLN
SEQRES 6 B 135 ARG ILE ALA VAL MET TRP SER GLU LYS SER ASN GLN MET
SEQRES 7 B 135 THR GLY LEU PHE SER THR ILE ASP GLU LYS THR SER GLN
SEQRES 8 B 135 GLU LYS LEU THR TRP LEU ASN VAL ASN ASP ALA LEU SER
SEQRES 9 B 135 ILE ASP GLY LYS THR VAL LEU PHE ALA ALA LEU THR GLY
SEQRES 10 B 135 SER LEU GLU ASN HIS PRO ASP GLY PHE ASN PHE ARG HIS
SEQRES 11 B 135 HIS HIS HIS HIS HIS
SEQRES 1 C 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 C 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 C 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 C 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 C 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 C 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 C 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 C 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 C 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 C 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
SEQRES 1 D 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 D 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 D 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 D 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 D 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 D 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 D 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 D 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 D 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 D 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
FORMUL 5 HOH *635(H2 O)
HELIX 1 1 THR A 5 GLY A 12 1 8
HELIX 2 2 THR A 15 GLN A 24 1 10
HELIX 3 3 ALA A 30 GLY A 35 1 6
HELIX 4 4 GLU A 87 THR A 89 5 3
HELIX 5 5 ASN A 100 SER A 104 5 5
HELIX 6 6 ILE A 105 GLY A 117 1 13
HELIX 7 7 GLY A 117 HIS A 122 1 6
HELIX 8 8 THR B 5 GLY B 12 1 8
HELIX 9 9 THR B 15 GLN B 24 1 10
HELIX 10 10 ALA B 30 GLY B 35 1 6
HELIX 11 11 ASN B 100 SER B 104 5 5
HELIX 12 12 ILE B 105 GLY B 117 1 13
HELIX 13 13 GLY B 117 HIS B 122 1 6
HELIX 14 14 GLY C 4 HIS C 15 1 12
HELIX 15 15 SER C 24 ASN C 37 1 14
HELIX 16 16 CYS C 80 SER C 85 5 6
HELIX 17 17 ILE C 88 SER C 100 1 13
HELIX 18 18 ASN C 103 ALA C 107 5 5
HELIX 19 19 TRP C 108 CYS C 115 1 8
HELIX 20 20 ASP C 119 ARG C 125 5 7
HELIX 21 21 GLY D 4 HIS D 15 1 12
HELIX 22 22 SER D 24 ASN D 37 1 14
HELIX 23 23 CYS D 80 SER D 85 5 6
HELIX 24 24 ILE D 88 SER D 100 1 13
HELIX 25 25 ASN D 103 ALA D 107 5 5
HELIX 26 26 TRP D 108 CYS D 115 1 8
HELIX 27 27 ASP D 119 ARG D 125 5 7
SHEET 1 AA 3 THR A 37 TYR A 38 0
SHEET 2 AA 3 GLU A 49 CYS A 57 -1 O CYS A 57 N THR A 37
SHEET 3 AA 3 GLN A 42 LEU A 46 -1 O GLN A 42 N VAL A 53
SHEET 1 AB 9 THR A 37 TYR A 38 0
SHEET 2 AB 9 GLU A 49 CYS A 57 -1 O CYS A 57 N THR A 37
SHEET 3 AB 9 GLN A 65 TRP A 71 -1 O ILE A 67 N ALA A 56
SHEET 4 AB 9 MET A 78 ASP A 86 -1 O THR A 79 N MET A 70
SHEET 5 AB 9 GLN A 91 LEU A 97 -1 O GLN A 91 N ASP A 86
SHEET 6 AB 9 GLU B 92 LEU B 97 -1 O GLU B 92 N LEU A 94
SHEET 7 AB 9 GLN B 77 ILE B 85 -1 O GLY B 80 N LEU B 97
SHEET 8 AB 9 GLN B 65 SER B 72 -1 O ARG B 66 N SER B 83
SHEET 9 AB 9 GLU B 49 CYS B 57 -1 O GLN B 52 N TRP B 71
SHEET 1 CA 3 THR C 43 ARG C 45 0
SHEET 2 CA 3 THR C 51 TYR C 53 -1 O ASP C 52 N ASN C 44
SHEET 3 CA 3 ILE C 58 ASN C 59 -1 O ILE C 58 N TYR C 53
SHEET 1 DA 3 THR D 43 ARG D 45 0
SHEET 2 DA 3 THR D 51 TYR D 53 -1 O ASP D 52 N ASN D 44
SHEET 3 DA 3 ILE D 58 ASN D 59 -1 O ILE D 58 N TYR D 53
SSBOND 1 CYS A 57 CYS A 62 1555 1555 2.05
SSBOND 2 CYS B 57 CYS B 62 1555 1555 2.06
SSBOND 3 CYS C 6 CYS C 127 1555 1555 2.03
SSBOND 4 CYS C 30 CYS C 115 1555 1555 2.04
SSBOND 5 CYS C 64 CYS C 80 1555 1555 2.03
SSBOND 6 CYS C 76 CYS C 94 1555 1555 2.05
SSBOND 7 CYS D 6 CYS D 127 1555 1555 2.04
SSBOND 8 CYS D 30 CYS D 115 1555 1555 2.04
SSBOND 9 CYS D 64 CYS D 80 1555 1555 2.04
SSBOND 10 CYS D 76 CYS D 94 1555 1555 2.04
CRYST1 55.490 59.560 69.200 90.00 95.39 90.00 P 1 21 1 4
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 0.018021 0.000000 0.001700 0.00000
SCALE2 0.000000 0.016790 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014515 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
