HEADER HYDROLASE 25-APR-05 2BPU
TITLE THE KEDGE HOLMIUM DERIVATIVE OF HEN EGG-WHITE LYSOZYME AT
TITLE 2 HIGH RESOLUTION FROM SINGLE WAVELENGTH ANOMALOUS
TITLE 3 DIFFRACTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LYSOZYME HEWL, 1,4-BETA-N-ACETYLMURAMIDASE C,
COMPND 5 ALLERGEN GAL D 4, GAL D IV;
COMPND 6 EC: 3.2.1.17
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031
KEYWDS HYDROLASE, HOLMIUM, KEDGE, ULTRA HIGH ENERGY, HIGH
KEYWDS 2 RESOLUTION, COMPTON, EXPERIMENTAL PHASES, ALLERGEN,
KEYWDS 3 HYDROLASE BACTERIOLYTIC ENZYME, GLYCOSIDASE, SAD
EXPDTA X-RAY DIFFRACTION
AUTHOR J.JAKONCIC,M.DI MICHIEL,Z.ZHONG,V.HONKIMAKI,Y.JOUANNEAU,
AUTHOR 2 V.STOJANOFF
REVDAT 2 24-FEB-09 2BPU 1 VERSN
REVDAT 1 24-AUG-06 2BPU 0
JRNL AUTH J.JAKONCIC,M.DI MICHIEL,Z.ZHONG,V.HONKIMAKI,
JRNL AUTH 2 Y.JOUANNEAU,V.STOJANOFF
JRNL TITL ANOMALOUS DIFFRACTION AT ULTRA-HIGH ENERGY FOR
JRNL TITL 2 PROTEIN CRYSTALLOGRAPHY.
JRNL REF J.APPL.CRYSTALLOGR. V. 39 831 2006
JRNL REFN ISSN 0021-8898
JRNL DOI 10.1107/S0021889806036387
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOODWITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 25072
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 + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1338
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.38
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1723
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE SET COUNT : 93
REMARK 3 BIN FREE R VALUE : 0.2770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1012
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 111
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.069
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.060
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.036
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.927
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1038 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 898 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1409 ; 1.275 ; 1.904
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2082 ; 0.866 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 132 ; 5.639 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 51 ;34.350 ;23.137
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 171 ;10.826 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;17.433 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 146 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1190 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 231 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 239 ; 0.238 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 914 ; 0.184 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 532 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 572 ; 0.082 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 69 ; 0.206 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 6 ; 0.309 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 43 ; 0.287 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.135 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 641 ; 1.060 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1020 ; 1.641 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 426 ; 2.359 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 387 ; 3.600 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. DISORDERED LOOPS WERE MANUALLY CONSTRUCTED.
REMARK 3 124 (TOTAL RESIDUES 129) WERE AUTOMATICALLY CONSTRUCTED WITH
REMARK 3 ARP.
REMARK 4
REMARK 4 2BPU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-APR-05.
REMARK 100 THE PDBE ID CODE IS EBI-23765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 105.0
REMARK 200 PH : 4.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X17B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.2229
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49334
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.4
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 : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):NULL
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 18.66250
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.35350
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.35350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.99375
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.35350
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.35350
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 9.33125
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.35350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.35350
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.99375
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.35350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.35350
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 9.33125
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 18.66250
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 GENERATING THE BIOMOLECULE
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 HO HO A1134 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2041 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2061 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HO HO A 1136 - O HOH A 2109 1.83
REMARK 500 HO HO A 1136 - O HOH A 2111 2.09
REMARK 500 HO HO A 1136 - O HOH A 2108 2.01
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 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1133 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 64 O
REMARK 620 2 HOH A2059 O 87.8
REMARK 620 3 SER A 72 OG 170.8 83.7
REMARK 620 4 ARG A 73 O 92.0 166.6 97.0
REMARK 620 5 HOH A2057 O 97.0 77.4 84.7 89.3
REMARK 620 6 SER A 60 O 88.9 101.8 89.3 91.6 174.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1130
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1131
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1132
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1133
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HO A1134
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HO A1135
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HO A1136
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
REMARK 900 EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 194L RELATED DB: PDB
REMARK 900 THE 1.40 A STRUCTURE OF SPACEHAB-01 HEN
REMARK 900 EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1A2Y RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME, D18A MUTANT, IN
REMARK 900 COMPLEX WITH MOUSE MONOCLONAL ANTIBODY D1.3
REMARK 900 RELATED ID: 1AKI RELATED DB: PDB
REMARK 900 THE STRUCTURE OF THE ORTHORHOMBIC FORM OF
REMARK 900 HEN EGG-WHITE LYSOZYME AT 1.5 ANGSTROMS
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1AT5 RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME WITH A SUCCINIMIDE
REMARK 900 RESIDUE
REMARK 900 RELATED ID: 1AT6 RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME WITH A ISOASPARTATE
REMARK 900 RESIDUE
REMARK 900 RELATED ID: 1AZF RELATED DB: PDB
REMARK 900 CHICKEN EGG WHITE LYSOZYME CRYSTAL GROWN IN
REMARK 900 BROMIDE SOLUTION
REMARK 900 RELATED ID: 1B0D RELATED DB: PDB
REMARK 900 STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON
REMARK 900 POLYMORPHIC LYSOZYME CRYSTALS
REMARK 900 RELATED ID: 1B2K RELATED DB: PDB
REMARK 900 STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON
REMARK 900 POLYMORPHIC LYSOZYME CRYSTALS
REMARK 900 RELATED ID: 1BGI RELATED DB: PDB
REMARK 900 ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH
REMARK 900 TEMPERATURE (310K)
REMARK 900 RELATED ID: 1BHZ RELATED DB: PDB
REMARK 900 LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF
REMARK 900 HEN EGG WHITE LYSOZYME FROM MASC DATA
REMARK 900 RELATED ID: 1BVK RELATED DB: PDB
REMARK 900 HUMANIZED ANTI-LYSOZYME FV COMPLEXED WITH
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 1BVX RELATED DB: PDB
REMARK 900 THE 1.8 A STRUCTURE OF GEL GROWN
REMARK 900 TETRAGONAL HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1BWH RELATED DB: PDB
REMARK 900 THE 1.8 A STRUCTURE OF GROUND CONTROL
REMARK 900 GROWN TETRAGONAL HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1BWI RELATED DB: PDB
REMARK 900 THE 1.8 A STRUCTURE OF MICROBATCH OIL
REMARK 900 DROP GROWN TETRAGONAL HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1BWJ RELATED DB: PDB
REMARK 900 THE 1.8 A STRUCTURE OF MICROGRAVITY GROWN
REMARK 900 TETRAGONAL HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1C08 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV-HEN
REMARK 900 LYSOZYME COMPLEX
REMARK 900 RELATED ID: 1C10 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEW LYSOZYME UNDER
REMARK 900 PRESSURE OF XENON (8 BAR)
REMARK 900 RELATED ID: 1DPW RELATED DB: PDB
REMARK 900 STRUCTURE OF HEN EGG-WHITE LYSOZYME IN
REMARK 900 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
REMARK 900 ANTIBODY HYHEL-63 COMPLEXED WITH HEN EGG
REMARK 900 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
REMARK 900 GROWN AT PH 6.5
REMARK 900 RELATED ID: 1F10 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME
REMARK 900 GROWN AT PH 6.5 AT 88% 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
REMARK 900 .3, KAPPA) - LYSOZYME COMPLEX
REMARK 900 RELATED ID: 1FLQ RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE
REMARK 900 SUBSTITUTED FORGLYCINE
REMARK 900 RELATED ID: 1FLU RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE
REMARK 900 SUBSTITUTED FORGLYCINE
REMARK 900 RELATED ID: 1FLW RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE
REMARK 900 SUBSTITUTED FORGLYCINE
REMARK 900 RELATED ID: 1FLY RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE
REMARK 900 SUBSTITUTED FORGLYCINE
REMARK 900 RELATED ID: 1FN5 RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE
REMARK 900 SUBSTITUTED FORGLYCINE
REMARK 900 RELATED ID: 1G7H RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME
REMARK 900 (HEL) COMPLEXEDWITH THE MUTANT ANTI-HEL
REMARK 900 MONOCLONAL ANTIBODY D1.3(VLW92A)
REMARK 900 RELATED ID: 1G7I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME
REMARK 900 (HEL) COMPLEXEDWITH THE MUTANT ANTI-HEL
REMARK 900 MONOCLONAL ANTIBODY D1.3 (VLW92F)
REMARK 900 RELATED ID: 1G7J RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME
REMARK 900 (HEL) COMPLEXEDWITH THE MUTANT ANTI-HEL
REMARK 900 MONOCLONAL ANTIBODY D1.3 (VLW92H)
REMARK 900 RELATED ID: 1G7L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME
REMARK 900 (HEL) COMPLEXEDWITH THE MUTANT ANTI-HEL
REMARK 900 MONOCLONAL ANTIBODY D1.3 (VLW92S)
REMARK 900 RELATED ID: 1G7M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME
REMARK 900 (HEL) COMPLEXEDWITH THE MUTANT ANTI-HEL
REMARK 900 MONOCLONAL ANTIBODY D1.3 (VLW92V)
REMARK 900 RELATED ID: 1GPQ RELATED DB: PDB
REMARK 900 STRUCTURE OF IVY COMPLEXED WITH ITS TARGET
REMARK 900 , HEWL
REMARK 900 RELATED ID: 1GWD RELATED DB: PDB
REMARK 900 TRI-IODIDE DERIVATIVE OF HEN EGG-WHITE
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 1GXV RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF LYSOZYME AT LOW AND
REMARK 900 HIGH PRESSURE
REMARK 900 RELATED ID: 1GXX RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF LYSOZYME AT LOW AND
REMARK 900 HIGH PRESSURE
REMARK 900 RELATED ID: 1H6M RELATED DB: PDB
REMARK 900 COVALENT GLYCOSYL-ENZYME INTERMEDIATE OF HEN
REMARK 900 EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1H87 RELATED DB: PDB
REMARK 900 GADOLINIUM DERIVATIVE OF TETRAGONAL HEN EGG-
REMARK 900 WHITE LYSOZYME AT 1.7 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
REMARK 900 THR (S91T)
REMARK 900 RELATED ID: 1HEN RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH ILE 55 REPLACED BY
REMARK 900 VAL AND SER 91 REPLACED BY THR (I55V,
REMARK 900 S91T)
REMARK 900 RELATED ID: 1HEO RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH ILE 55 REPLACED BY
REMARK 900 VAL (I55V)
REMARK 900 RELATED ID: 1HEP RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH THR 40 REPLACED BY
REMARK 900 SER, ILE 55 REPLACED BY VAL, AND SER 91
REMARK 900 REPLACED BY THR (T40S,I55V,S91T)
REMARK 900 RELATED ID: 1HEQ RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH THR 40 REPLACED BY
REMARK 900 SER AND SER 91 REPLACED BY THR (T40S,
REMARK 900 S91T)
REMARK 900 RELATED ID: 1HER RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH THR 40 REPLACED BY
REMARK 900 SER (T40S)
REMARK 900 RELATED ID: 1HEW RELATED DB: PDB
REMARK 900 LYSOZYME COMPLEXED WITH THE INHIBITOR TRI-N
REMARK 900 -ACETYLCHITOTRIOSE
REMARK 900 RELATED ID: 1HF4 RELATED DB: PDB
REMARK 900 STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON
REMARK 900 POLYMORPHIC LYSOZYME CRYSTALS
REMARK 900 RELATED ID: 1HSW RELATED DB: PDB
REMARK 900 LYSOZYME (MUCOPEPTIDE N-ACETYLMURAMYL HYDROLASE
REMARK 900 )
REMARK 900 RELATED ID: 1HSX RELATED DB: PDB
REMARK 900 LYSOZYME GROWN AT BASIC PH AND ITS LOW
REMARK 900 HUMIDITY VARIANT
REMARK 900 RELATED ID: 1IC4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT(
REMARK 900 HD32A)-HEN LYSOZYMECOMPLEX
REMARK 900 RELATED ID: 1IC5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT(
REMARK 900 HD99A)-HEN LYSOZYMECOMPLEX
REMARK 900 RELATED ID: 1IC7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT(
REMARK 900 HD32A99A)-HENLYSOZYME COMPLEX
REMARK 900 RELATED ID: 1IEE RELATED DB: PDB
REMARK 900 STRUCTURE OF TETRAGONAL HEN EGG WHITE
REMARK 900 LYSOZYME AT 0.94 AFROM CRYSTALS GROWN BY
REMARK 900 THE COUNTER-DIFFUSION METHOD
REMARK 900 RELATED ID: 1IO5 RELATED DB: PDB
REMARK 900 HYDROGEN AND HYDRATION OF HEN EGG-WHITE
REMARK 900 LYSOZYME DETERMINEDBY NEUTRON DIFFRACTION
REMARK 900 RELATED ID: 1IOQ RELATED DB: PDB
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY
REMARK 900 A CAVITY-FILLINGMUTATION
REMARK 900 RELATED ID: 1IOR RELATED DB: PDB
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY
REMARK 900 A CAVITY-FILLINGMUTATION
REMARK 900 RELATED ID: 1IOS RELATED DB: PDB
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY
REMARK 900 A CAVITY-FILLINGMUTATION
REMARK 900 RELATED ID: 1IOT RELATED DB: PDB
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY
REMARK 900 A CAVITY-FILLINGMUTATION
REMARK 900 RELATED ID: 1IR7 RELATED DB: PDB
REMARK 900 IM MUTANT OF LYSOZYME
REMARK 900 RELATED ID: 1IR8 RELATED DB: PDB
REMARK 900 IM MUTANT OF LYSOZYME
REMARK 900 RELATED ID: 1IR9 RELATED DB: PDB
REMARK 900 IM MUTANT OF LYSOZYME
REMARK 900 RELATED ID: 1J1O RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT
REMARK 900 LY50F COMPLEXEDWITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1J1P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT
REMARK 900 LS91A COMPLEXEDWITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1J1X RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT
REMARK 900 LS93A COMPLEXEDWITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1JA2 RELATED DB: PDB
REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN
REMARK 900 EGG LYSOZYME: APOWDER DIFFRACTION STUDY
REMARK 900 RELATED ID: 1JA4 RELATED DB: PDB
REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN
REMARK 900 EGG LYSOZYME: APOWDER DIFFRACTION STUDY
REMARK 900 RELATED ID: 1JA6 RELATED DB: PDB
REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN
REMARK 900 EGG LYSOZYME: APOWDER DIFFRACTION STUDY
REMARK 900 RELATED ID: 1JA7 RELATED DB: PDB
REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN
REMARK 900 EGG LYSOZYME: APOWDER DIFFRACTION STUDY
REMARK 900 RELATED ID: 1JIS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN
REMARK 900 AT PH 4.6
REMARK 900 RELATED ID: 1JIT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN
REMARK 900 IN PRESENCE30% TREHALOSE
REMARK 900 RELATED ID: 1JIY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN
REMARK 900 IN PRESENCE20% SORBITOL
REMARK 900 RELATED ID: 1JJ0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN
REMARK 900 IN PRESENCEOF 30% SUCROSE
REMARK 900 RELATED ID: 1JJ1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME
REMARK 900 GROWN AT PH 4.6IN PRESENCE OF 5%
REMARK 900 SORBITOL
REMARK 900 RELATED ID: 1JJ3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN
REMARK 900 AT PH 4.6
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
REMARK 900 COMPLEXES
REMARK 900 RELATED ID: 1JTT RELATED DB: PDB
REMARK 900 DEGENERATE INTERFACES IN ANTIGEN-ANTIBODY
REMARK 900 COMPLEXES
REMARK 900 RELATED ID: 1KIP RELATED DB: PDB
REMARK 900 FV MUTANT Y(B 32)A (VH DOMAIN) OF
REMARK 900 MOUSE MONOCLONAL ANTIBODY D1.3 COMPLEXED
REMARK 900 WITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1KIQ RELATED DB: PDB
REMARK 900 FV MUTANT Y(B 101)F (VH DOMAIN) OF
REMARK 900 MOUSE MONOCLONAL ANTIBODY D1.3 COMPLEXED
REMARK 900 WITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1KIR RELATED DB: PDB
REMARK 900 FV MUTANT Y(A 50)S (VL DOMAIN) OF
REMARK 900 MOUSE MONOCLONAL ANTIBODY D1.3 COMPLEXED
REMARK 900 WITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1KXW RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN
REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED
REMARK 900 SIDE CHAINS
REMARK 900 RELATED ID: 1KXX RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN
REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED
REMARK 900 SIDE CHAINS
REMARK 900 RELATED ID: 1KXY RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN
REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED
REMARK 900 SIDE CHAINS
REMARK 900 RELATED ID: 1LCN RELATED DB: PDB
REMARK 900 MONOCLINIC HEN EGG WHITE LYSOZYME, THIOCYANATE
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 1LJ3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN
REMARK 900 AT PH 4.6
REMARK 900 RELATED ID: 1LJ4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN
REMARK 900 AT PH 4.6
REMARK 900 RELATED ID: 1LJE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN
REMARK 900 IN PRESENCEOF 10% SUCROSE
REMARK 900 RELATED ID: 1LJF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN
REMARK 900 IN PRESENCEOF 10% SUCROSE
REMARK 900 RELATED ID: 1LJG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN
REMARK 900 IN PRESENCEOF 5% GLYCEROL
REMARK 900 RELATED ID: 1LJH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN
REMARK 900 IN PRESENCEOF 5% GLYCEROL
REMARK 900 RELATED ID: 1LJI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN
REMARK 900 IN PRESENCE10% SORBITOL
REMARK 900 RELATED ID: 1LJJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN
REMARK 900 IN PRESENCEOF 10% TREHALOSE
REMARK 900 RELATED ID: 1LJK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN
REMARK 900 IN PRESENCEOF 15% TREHALOSE
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
REMARK 900 HUMAN FIBRINOGEN GAMMA; CHAIN: NULL;
REMARK 900 ENGINEERED; THE 14-RESIDUE C-TERMINUS (
REMARK 900 RESIDUES 398 - 411) OF THE HUMAN FIBRINOGEN
REMARK 900 GAMMA CHAIN FUSED TO THE C-TERMINUS OF
REMARK 900 CHICKEN EGG WHITE LYSOZYME; MUTATION: N-TERM
REMARK 900 MET
REMARK 900 RELATED ID: 1LSM RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH ILE 55 REPLACED BY
REMARK 900 LEU, SER 91 REPLACED BY THR, AND ASP 101
REMARK 900 REPLACED BY SER (I55L,S91T,D101S)
REMARK 900 RELATED ID: 1LSN RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH SER 91 REPLACED BY
REMARK 900 ALA (S91A)
REMARK 900 RELATED ID: 1LSY RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH ASP 52 REPLACED BY
REMARK 900 SER (D52S)
REMARK 900 RELATED ID: 1LSZ RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH ASP 52 REPLACED BY
REMARK 900 SER (D52S) COMPLEXED WITH GLCNAC4 (TETRA-N-
REMARK 900 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
REMARK 900 SULFURS AND CHLORINES
REMARK 900 RELATED ID: 1LZ9 RELATED DB: PDB
REMARK 900 ANOMALOUS SIGNAL OF SOLVENT BROMINES USED
REMARK 900 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-
REMARK 900 CHITOTRIOSE (PH 4.7)
REMARK 900 RELATED ID: 1LZC RELATED DB: PDB
REMARK 900 LYSOZYME CO-CRYSTALLIZED WITH TETRA-N-ACETYL
REMARK 900 -CHITOTETRAOSE (PH 4.7)
REMARK 900 RELATED ID: 1LZD RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH TRP 62 REPLACED BY
REMARK 900 TYR (W62Y)
REMARK 900 RELATED ID: 1LZE RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH TRP 62 REPLACED BY
REMARK 900 TYR (W62Y) CO-CRYSTALLIZED WITH TRI-N-
REMARK 900 ACETYL-CHITOTRIOSE (PH 4.7)
REMARK 900 RELATED ID: 1LZG RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH TRP 62 REPLACED BY
REMARK 900 PHE (W62F) CO-CRYSTALLIZED WITH TRI-N-
REMARK 900 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
REMARK 900 VH ANTIBODY FRAGMENT IN COMPLEX WITH
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 1MLC RELATED DB: PDB
REMARK 900 MONOCLONAL ANTIBODY FAB D44.1 RAISED AGAINST
REMARK 900 CHICKEN EGG-WHITE LYSOZYME COMPLEXED WITH
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 1N4F RELATED DB: PDB
REMARK 900 PARA-ARSANILATE DERIVATIVE OF HEN EGG-WHITE
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 1NBY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-63 COMPLEXED WITH
REMARK 900 HEL MUTANT K96A
REMARK 900 RELATED ID: 1NBZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-63 COMPLEXED WITH
REMARK 900 HEL MUTANT K96A
REMARK 900 RELATED ID: 1NDG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FAB FRAGMENT OF
REMARK 900 ANTIBODY HYHEL-8COMPLEXED WITH ITS ANTIGEN
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 1NDM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FAB FRAGMENT OF
REMARK 900 ANTIBODY HYHEL-26COMPLEXED WITH LYSOZYME
REMARK 900 RELATED ID: 1P2C RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF AN ANTI-
REMARK 900 LYSOZYME ANTIBODY
REMARK 900 RELATED ID: 1PS5 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE MONOCLINIC C2 FORM OF HEN
REMARK 900 EGG-WHITELYSOZYME AT 2.0 ANGSTROMS
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1QIO RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE CAUSED
REMARK 900 BY INTENSE SYNCHROTRON RADIATION TO HEN
REMARK 900 EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1QTK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEW LYSOZYME UNDER
REMARK 900 PRESSURE OF KRYPTON (55 BAR)
REMARK 900 RELATED ID: 1RCM RELATED DB: PDB
REMARK 900 LYSOZYME (PARTIALLY REDUCED, CARBOXYMETHYLATED (
REMARK 900 6,127-RCM))
REMARK 900 RELATED ID: 1RFP RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN
REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED
REMARK 900 SIDE CHAINS
REMARK 900 RELATED ID: 1RI8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CAMELID SINGLE
REMARK 900 DOMAIN ANTIBODY1D2L19 IN COMPLEX WITH HEN
REMARK 900 EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1RJC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CAMELID SINGLE
REMARK 900 DOMAIN ANTIBODY CAB-LYS2 IN COMPLEX WITH
REMARK 900 HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1SF4 RELATED DB: PDB
REMARK 900 BINDING OF N,N'-DIACETYLCHITOBIOSE TO HEW
REMARK 900 LYSOZYME: APOWDER DIFFRACTION STUDY
REMARK 900 RELATED ID: 1SF6 RELATED DB: PDB
REMARK 900 BINDING OF N,N',N"-TRIACETYLCHITOTRIOSE TO
REMARK 900 HEW LYSOZYME: APOWDER DIFFRACTION STUDY
REMARK 900 RELATED ID: 1SF7 RELATED DB: PDB
REMARK 900 BINDING OF TETRA-N-ACETYLCHITOTETRAOSE TO
REMARK 900 HEW LYSOZYME: APOWDER DIFFRACTION STUDY
REMARK 900 RELATED ID: 1SFB RELATED DB: PDB
REMARK 900 BINDING OF PENTA-N-ACETYLCHITOPENTAOSE TO
REMARK 900 HEW LYSOZYME: APOWDER DIFFRACTION STUDY
REMARK 900 RELATED ID: 1SFG RELATED DB: PDB
REMARK 900 BINDING OF HEXA-N-ACETYLCHITOHEXAOSE: A
REMARK 900 POWDER DIFFRACTIONSTUDY
REMARK 900 RELATED ID: 1SQ2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE NURSE
REMARK 900 SHARK NEW ANTIGENRECEPTOR (NAR) VARIABLE
REMARK 900 DOMAIN IN COMPLEX WITH LYXOZYME
REMARK 900 RELATED ID: 1T6V RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE NURSE
REMARK 900 SHARK NEW ANTIGENRECEPTOR (NAR) VARIABLE
REMARK 900 DOMAIN IN COMPLEX WITH LYSOZYME
REMARK 900 RELATED ID: 1UA6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT
REMARK 900 SFSF COMPLEXED WITHHEN EGG WHITE LYSOZYME
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 1UC0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE HEN-EGG
REMARK 900 WHITE LYSOZYMESINGLY LABELED WITH 2',3'-
REMARK 900 EPOXYPROPYL BETA-GLYCOSIDE OF N-
REMARK 900 ACETYLLACTOSAMINE
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
REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED
REMARK 900 SIDE CHAINS
REMARK 900 RELATED ID: 1UIB RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN
REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED
REMARK 900 SIDE CHAINS
REMARK 900 RELATED ID: 1UIC RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN
REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED
REMARK 900 SIDE CHAINS
REMARK 900 RELATED ID: 1UID RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN
REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED
REMARK 900 SIDE CHAINS
REMARK 900 RELATED ID: 1UIE RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN
REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED
REMARK 900 SIDE CHAINS
REMARK 900 RELATED ID: 1UIF RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN
REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED
REMARK 900 SIDE CHAINS
REMARK 900 RELATED ID: 1UIG RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN
REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED
REMARK 900 SIDE CHAINS
REMARK 900 RELATED ID: 1UIH RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN
REMARK 900 LYSOZYME WITH THE HELIX DIPOLE AND CHARGED
REMARK 900 SIDE CHAINS
REMARK 900 RELATED ID: 1UUZ RELATED DB: PDB
REMARK 900 IVY:A NEW FAMILY OF PROTEIN
REMARK 900 RELATED ID: 1V7S RELATED DB: PDB
REMARK 900 TRICLINIC HEN LYSOZYME CRYSTALLIZED AT 313K
REMARK 900 FROM A D2OSOLUTION
REMARK 900 RELATED ID: 1V7T RELATED DB: PDB
REMARK 900 TRICLINIC LYSOZYME WITH LOW SOLVENT CONTENT
REMARK 900 OBTAINED BYPHASE TRANSITION
REMARK 900 RELATED ID: 1VAT RELATED DB: PDB
REMARK 900 IODINE DERIVATIVE OF HEN EGG-WHITE LYSOZYME
REMARK 900 RELATED ID: 1VAU RELATED DB: PDB
REMARK 900 XENON DERIVATIVE OF HEN EGG-WHITE LYSOZYME
REMARK 900 RELATED ID: 1VDP RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE MONOCLINIC FORM
REMARK 900 OF HEN EGGWHITE LYSOZYME AT 1.7
REMARK 900 ANGSTROMS RESOLUTION IN SPACE
REMARK 900 RELATED ID: 1VDQ RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE ORTHORHOMBIC
REMARK 900 FORM OF HEN EGGWHITE LYSOZYME AT 1.5
REMARK 900 ANGSTROMS RESOLUTION
REMARK 900 RELATED ID: 1VDS RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE TETRAGONAL FORM
REMARK 900 OF HEN EGGWHITE LYSOZYME AT 1.6
REMARK 900 ANGSTROMS RESOLUTION IN SPACE
REMARK 900 RELATED ID: 1VDT RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE TETRAGONAL FORM
REMARK 900 OF HEN EGGWHITE LYSOZYME AT 1.7
REMARK 900 ANGSTROMS RESOLUTION UNDER BASICCONDITIONS IN
REMARK 900 SPACE
REMARK 900 RELATED ID: 1VED RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE ORTHORHOMBIC
REMARK 900 FORM OF HEN EGGWHITE LYSOZYME AT 1.9
REMARK 900 ANGSTROMS RESOLUTION IN SPACE
REMARK 900 RELATED ID: 1VFB RELATED DB: PDB
REMARK 900 FV FRAGMENT OF MOUSE MONOCLONAL ANTIBODY D1
REMARK 900 .3 COMPLEXED WITH HEN EGG LYSOZYME
REMARK 900 RELATED ID: 1W6Z RELATED DB: PDB
REMARK 900 HIGH ENERGY TATRAGONAL LYSOZYME X-RAY
REMARK 900 STRUCTURE
REMARK 900 RELATED ID: 1WTM RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HEW LYSOZYME ORTHORHOMBIC
REMARK 900 CRYSTAL FORMEDIN THE EARTH'S MAGNETIC
REMARK 900 FIELD
REMARK 900 RELATED ID: 1WTN RELATED DB: PDB
REMARK 900 THE STRUCTURE OF HEW LYSOZYME ORTHORHOMBIC
REMARK 900 CRYSTAL GROWTHUNDER A HIGH MAGNETIC FIELD
REMARK 900 RELATED ID: 1XEI RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY
REMARK 900 LOW LEVELS OF HYDRATION
REMARK 900 RELATED ID: 1XEJ RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY
REMARK 900 LOW LEVELS OF HYDRATION
REMARK 900 RELATED ID: 1XEK RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY
REMARK 900 LOW LEVELS OF HYDRATION
REMARK 900 RELATED ID: 1XFP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CDR2 GERMLINE
REMARK 900 REVERSION MUTANT OFCAB-LYS3 IN COMPLEX WITH
REMARK 900 HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1YIK RELATED DB: PDB
REMARK 900 STRUCTURE OF HEN EGG WHITE LYSOZYME SOAKED
REMARK 900 WITH CU-CYCLAM
REMARK 900 RELATED ID: 1YIL RELATED DB: PDB
REMARK 900 STRUCTURE OF HEN EGG WHITE LYSOZYME SOAKED
REMARK 900 WITH CU2-XYLYLBICYCLAM
REMARK 900 RELATED ID: 2BLX RELATED DB: PDB
REMARK 900 HEWL BEFORE A HIGH DOSE X-RAY "BURN"
REMARK 900 RELATED ID: 2BLY RELATED DB: PDB
REMARK 900 HEWL AFTER A HIGH DOSE X-RAY "BURN"
REMARK 900 RELATED ID: 2CDS RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 2HFM RELATED DB: PDB
REMARK 900 IGG1 FV FRAGMENT (HYHEL-10) AND LYSOZYME
REMARK 900 COMPLEX (THEORETICAL MODEL)
REMARK 900 RELATED ID: 2IFF RELATED DB: PDB
REMARK 900 IGG1 FAB FRAGMENT (HYHEL-5) COMPLEXED WITH
REMARK 900 LYSOZYME MUTANT WITH ARG 68 REPLACED BY
REMARK 900 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
REMARK 900 % 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
REMARK 900 WITH LYSOZYME
REMARK 900 RELATED ID: 3HFM RELATED DB: PDB
REMARK 900 IGG1 FAB FRAGMENT (HYHEL-10) AND LYSOZYME
REMARK 900 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
REMARK 900 % 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
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 4LYM RELATED DB: PDB
REMARK 900 LYSOZYME (MUCOPEPTIDE N-ACETYLMURAMYL HYDROLASE
REMARK 900 )
REMARK 900 RELATED ID: 4LYO RELATED DB: PDB
REMARK 900 CROSS-LINKED CHICKEN LYSOZYME CRYSTAL IN
REMARK 900 NEAT ACETONITRILE, THEN 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
REMARK 900 LYSOZYME AT 295K
REMARK 900 RELATED ID: 5LYM RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: LYSOZYME; CHAIN: A, B
REMARK 900 ; EC: 3.2.1.17
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 2BPU 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 CL A1130 1
HET CL A1131 1
HET CL A1132 1
HET NA A1133 1
HET HO A1134 1
HET HO A1135 1
HET HO A1136 1
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM HO HOLMIUM ATOM
FORMUL 2 CL 3(CL 1-)
FORMUL 5 NA NA 1+
FORMUL 6 HO 3(HO)
FORMUL 9 HOH *111(H2 O1)
HELIX 1 1 GLY A 4 HIS A 15 1 12
HELIX 2 2 SER A 24 ASN A 37 1 14
HELIX 3 3 CYS A 80 SER A 85 5 6
HELIX 4 4 ILE A 88 SER A 100 1 13
HELIX 5 5 ASN A 103 ALA A 107 5 5
HELIX 6 6 TRP A 108 CYS A 115 1 8
HELIX 7 7 ASP A 119 ARG A 125 5 7
SHEET 1 AA 3 THR A 43 ARG A 45 0
SHEET 2 AA 3 THR A 51 TYR A 53 -1 O ASP A 52 N ASN A 44
SHEET 3 AA 3 ILE A 58 ASN A 59 -1 O ILE A 58 N TYR A 53
SSBOND 1 CYS A 6 CYS A 127 1555 1555 2.03
SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.03
SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.04
SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.03
LINK NA NA A1133 O CYS A 64 1555 1555 2.48
LINK NA NA A1133 O HOH A2059 1555 1555 2.44
LINK NA NA A1133 OG SER A 72 1555 1555 2.46
LINK NA NA A1133 O ARG A 73 1555 1555 2.50
LINK NA NA A1133 O HOH A2057 1555 1555 2.47
LINK NA NA A1133 O SER A 60 1555 1555 2.25
SITE 1 AC1 3 TYR A 23 ASN A 113 HOH A2016
SITE 1 AC2 3 SER A 24 GLY A 26 GLN A 121
SITE 1 AC3 3 GLY A 67 ARG A 68 THR A 69
SITE 1 AC4 6 SER A 60 CYS A 64 SER A 72 ARG A 73
SITE 2 AC4 6 HOH A2057 HOH A2059
SITE 1 AC5 2 LEU A 129 HOH A2101
SITE 1 AC6 5 ASP A 101 HOH A2102 HOH A2103 HOH A2104
SITE 2 AC6 5 HOH A2105
SITE 1 AC7 6 ASP A 52 HOH A2107 HOH A2108 HOH A2109
SITE 2 AC7 6 HOH A2110 HOH A2111
CRYST1 78.707 78.707 37.325 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 0.012705 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012705 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026792 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
