HEADER HYDROLASE 03-NOV-13 4NGZ
TITLE PREVIOUSLY DE-IONIZED HEW LYSOZYME CRYSTALLIZED IN 0.5 M YBCL3/30%
TITLE 2 (V/V) GLYCEROL AND COLLECTED AT 125K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C, ALLERGEN GAL D IV;
COMPND 5 EC: 3.2.1.17
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: BANTAM,CHICKENS;
SOURCE 4 ORGANISM_TAXID: 9031
KEYWDS HOFMEISTER SERIES, PROTEIN CATION INTERACTIONS, HEW LYSOZYME, ESI-
KEYWDS 2 MASS SPECTROMETRY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.BENAS,L.LEGRAND,M.RIES-KAUTT
REVDAT 5 20-SEP-23 4NGZ 1 REMARK SSBOND LINK
REVDAT 4 17-JUL-19 4NGZ 1 REMARK
REVDAT 3 15-NOV-17 4NGZ 1 REMARK
REVDAT 2 13-AUG-14 4NGZ 1 JRNL
REVDAT 1 28-MAY-14 4NGZ 0
JRNL AUTH P.BENAS,N.AUZEIL,L.LEGRAND,F.BRACHET,A.REGAZZETTI,
JRNL AUTH 2 M.RIES-KAUTT
JRNL TITL WEAK PROTEIN-CATIONIC CO-ION INTERACTIONS ADDRESSED BY X-RAY
JRNL TITL 2 CRYSTALLOGRAPHY AND MASS SPECTROMETRY.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 2217 2014
JRNL REFN ISSN 0907-4449
JRNL PMID 25084340
JRNL DOI 10.1107/S1399004714011304
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.BENAS,L.LEGRAND,M.RIES-KAUTT
REMARK 1 TITL STRONG AND SPECIFIC EFFECTS OF CATIONS ON LYSOZYME CHLORIDE
REMARK 1 TITL 2 SOLUBILITY.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 58 1582 2002
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 12351866
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 11957
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.400
REMARK 3 FREE R VALUE TEST SET COUNT : 1241
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 849
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.18
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE SET COUNT : 82
REMARK 3 BIN FREE R VALUE : 0.3210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1001
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 129
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.51000
REMARK 3 B22 (A**2) : 0.51000
REMARK 3 B33 (A**2) : -1.01000
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): 0.125
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.113
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.067
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.669
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1075 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 970 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1430 ; 1.296 ; 1.907
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2207 ; 0.861 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 132 ; 5.379 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 52 ;36.818 ;22.885
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 172 ;13.763 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;17.710 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 148 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1249 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 281 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 528 ; 1.374 ; 1.302
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 526 ; 1.318 ; 1.292
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 660 ; 1.907 ; 1.940
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 546 ; 3.380 ; 1.637
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 129
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9690 58.3630 0.6620
REMARK 3 T TENSOR
REMARK 3 T11: 0.0238 T22: 0.0308
REMARK 3 T33: 0.0188 T12: 0.0032
REMARK 3 T13: 0.0068 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 1.3921 L22: 1.6645
REMARK 3 L33: 0.9653 L12: -0.8730
REMARK 3 L13: 0.1722 L23: 0.2733
REMARK 3 S TENSOR
REMARK 3 S11: -0.0270 S12: 0.0133 S13: 0.0697
REMARK 3 S21: 0.0503 S22: 0.0566 S23: -0.1463
REMARK 3 S31: -0.0201 S32: 0.0706 S33: -0.0296
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.50
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4NGZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-13.
REMARK 100 THE DEPOSITION ID IS D_1000083190.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAY-00
REMARK 200 TEMPERATURE (KELVIN) : 125
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, TRUNCATE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13242
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 19.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 9.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.20200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 193L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PREVIOUSLY DE-IONIZED LYSOZYME, NO
REMARK 280 BUFFER ADDED, 0.5 M YBCL3, 30% (V/V) GLYCEROL , PH 4.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 18.50850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.29450
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.29450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.76275
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.29450
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.29450
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 9.25425
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.29450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.29450
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.76275
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.29450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.29450
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 9.25425
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 18.50850
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 YB YB A 202 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 379 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 380 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 O HOH A 312 O HOH A 381 1.45
REMARK 500
REMARK 500 REMARK: NULL
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 YB A 201 YB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 46 OD1
REMARK 620 2 ASP A 52 OD2 74.0
REMARK 620 3 HOH A 301 O 59.6 100.4
REMARK 620 4 HOH A 302 O 122.2 81.3 75.3
REMARK 620 5 HOH A 303 O 40.0 90.0 91.2 162.2
REMARK 620 6 HOH A 304 O 118.7 160.2 76.4 79.0 109.5
REMARK 620 7 HOH A 305 O 65.9 137.7 71.0 131.7 50.2 60.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 YB A 203 YB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 101 OD2
REMARK 620 2 ASP A 101 OD1 51.0
REMARK 620 3 HOH A 308 O 102.1 54.5
REMARK 620 4 HOH A 309 O 149.6 149.4 95.5
REMARK 620 5 HOH A 310 O 75.1 124.7 147.6 76.7
REMARK 620 6 HOH A 311 O 78.3 81.5 72.0 83.9 75.9
REMARK 620 7 HOH A 312 O 100.1 67.4 68.3 109.4 144.1 138.9
REMARK 620 8 HOH A 381 O 112.3 102.0 101.2 88.0 109.8 168.7 38.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 YB A 202 YB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 129 OXT
REMARK 620 2 LEU A 129 O 45.8
REMARK 620 3 LEU A 129 OXT 36.6 9.9
REMARK 620 4 LEU A 129 O 37.1 46.2 44.1
REMARK 620 5 HOH A 306 O 86.7 94.0 89.2 123.3
REMARK 620 6 HOH A 307 O 88.7 133.0 123.0 107.4 67.6
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 YB A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 205
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NEB RELATED DB: PDB
REMARK 900 HEW LYSOZYME IN 0.5 M MNCL2 COLLECTED AT ROOM TEMPERATURE
REMARK 900 RELATED ID: 4NFV RELATED DB: PDB
REMARK 900 HEW LYSOZYME IN 1.1 M MNCL2 COLLECTED AT ROOM TEMPERATURE
REMARK 900 RELATED ID: 4NG1 RELATED DB: PDB
REMARK 900 HEW LYSOZYME IN 1.9 M CSCL COLLECTED AT ROOM TEMPERATURE
REMARK 900 RELATED ID: 4NG8 RELATED DB: PDB
REMARK 900 HEW LYSOZYME IN 1.9 M CSCL COLLECTED AT 100K
REMARK 900 RELATED ID: 4NGI RELATED DB: PDB
REMARK 900 HEW LYSOZYME IN 1.0 M RBCL/30% (V/V)GLYCEROL AND COLLECTED AT 125K
REMARK 900 RELATED ID: 4NGJ RELATED DB: PDB
REMARK 900 HEW LYSOZYME IN 1.0 M RBCL COLLECTED AT 100K
REMARK 900 RELATED ID: 4NGK RELATED DB: PDB
REMARK 900 HEW LYSOZYME IN 0.2 M COCL2 COLLECTED AT ROOM TEMPERATURE
REMARK 900 RELATED ID: 4NGL RELATED DB: PDB
REMARK 900 HEW LYSOZYME IN 0.6 M COCL2 COLLECTED AT ROOM TEMPERATURE
REMARK 900 RELATED ID: 4NGO RELATED DB: PDB
REMARK 900 HEW LYSOZYME IN 1.0 M COCL2 COLLECTED AT ROOM TEMPERATURE
REMARK 900 RELATED ID: 4NGV RELATED DB: PDB
REMARK 900 HEW LYSOZYME IN 0.5 M YBCL3 COLLECTED AT ROOM TEMPERATURE
REMARK 900 RELATED ID: 4NGW RELATED DB: PDB
REMARK 900 HEW LYSOZYME IN 0.5 M YBCL3 COLLECTED AT 100K
REMARK 900 RELATED ID: 4NGY RELATED DB: PDB
REMARK 900 HEW LYSOZYME IN 0.75 M YBCL3 COLLECTED AT 100K
DBREF 4NGZ 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 YB A 201 1
HET YB A 202 1
HET YB A 203 1
HET CL A 204 1
HET CL A 205 1
HET CL A 206 1
HETNAM YB YTTERBIUM (III) ION
HETNAM CL CHLORIDE ION
FORMUL 2 YB 3(YB 3+)
FORMUL 5 CL 3(CL 1-)
FORMUL 8 HOH *129(H2 O)
HELIX 1 1 GLY A 4 HIS A 15 1 12
HELIX 2 2 ASN A 19 TYR A 23 5 5
HELIX 3 3 SER A 24 ASN A 37 1 14
HELIX 4 4 PRO A 79 SER A 85 5 7
HELIX 5 5 ILE A 88 SER A 100 1 13
HELIX 6 6 ASN A 103 ALA A 107 5 5
HELIX 7 7 TRP A 108 CYS A 115 1 8
HELIX 8 8 ASP A 119 ARG A 125 5 7
SHEET 1 A 3 THR A 43 ARG A 45 0
SHEET 2 A 3 THR A 51 TYR A 53 -1 O ASP A 52 N ASN A 44
SHEET 3 A 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 2.02
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 OD1 ASN A 46 YB YB A 201 1555 1555 3.27
LINK OD2 ASP A 52 YB YB A 201 1555 1555 2.15
LINK OD2 ASP A 101 YB YB A 203 1555 1555 2.17
LINK OD1 ASP A 101 YB YB A 203 1555 1555 2.74
LINK OXTALEU A 129 YB YB A 202 1555 1555 2.28
LINK O ALEU A 129 YB YB A 202 1555 1555 2.97
LINK OXTBLEU A 129 YB YB A 202 1555 1555 2.30
LINK O BLEU A 129 YB YB A 202 1555 1555 2.99
LINK YB YB A 201 O HOH A 301 1555 1555 2.19
LINK YB YB A 201 O HOH A 302 1555 1555 2.28
LINK YB YB A 201 O HOH A 303 1555 1555 2.07
LINK YB YB A 201 O HOH A 304 1555 1555 2.20
LINK YB YB A 201 O HOH A 305 1555 1555 2.23
LINK YB YB A 202 O HOH A 306 1555 1555 2.21
LINK YB YB A 202 O HOH A 307 1555 1555 2.22
LINK YB YB A 203 O HOH A 308 1555 1555 2.16
LINK YB YB A 203 O HOH A 309 1555 1555 2.20
LINK YB YB A 203 O HOH A 310 1555 1555 2.19
LINK YB YB A 203 O HOH A 311 1555 1555 2.22
LINK YB YB A 203 O HOH A 312 1555 1555 2.21
LINK YB YB A 203 O HOH A 381 1555 1555 2.22
SITE 1 AC1 7 ASN A 46 ASP A 52 HOH A 301 HOH A 302
SITE 2 AC1 7 HOH A 303 HOH A 304 HOH A 305
SITE 1 AC2 3 LEU A 129 HOH A 306 HOH A 307
SITE 1 AC3 7 ASP A 101 HOH A 308 HOH A 309 HOH A 310
SITE 2 AC3 7 HOH A 311 HOH A 312 HOH A 381
SITE 1 AC4 2 TYR A 23 ASN A 113
SITE 1 AC5 3 SER A 24 GLY A 26 GLN A 121
CRYST1 78.589 78.589 37.017 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 0.012724 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012724 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027015 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
