HEADER HYDROLASE 28-OCT-15 5B07
TITLE LYSOZYME (DENATURED BY DCL AND REFOLDED)
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: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031
KEYWDS REFOLDED, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.KITA,Y.MORIMOTO
REVDAT 3 08-NOV-23 5B07 1 REMARK LINK
REVDAT 2 10-FEB-16 5B07 1 JRNL
REVDAT 1 13-JAN-16 5B07 0
JRNL AUTH A.KITA,Y.MORIMOTO
JRNL TITL AN EFFECTIVE DEUTERIUM EXCHANGE METHOD FOR NEUTRON CRYSTAL
JRNL TITL 2 STRUCTURE ANALYSIS WITH UNFOLDING-REFOLDING PROCESSES
JRNL REF MOL BIOTECHNOL. V. 58 130 2016
JRNL REFN ESSN 1559-0305
JRNL PMID 26718545
JRNL DOI 10.1007/S12033-015-9908-8
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 10639
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 584
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 763
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.75
REMARK 3 BIN R VALUE (WORKING SET) : 0.1340
REMARK 3 BIN FREE R VALUE SET COUNT : 43
REMARK 3 BIN FREE R VALUE : 0.2460
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 : 28
REMARK 3 SOLVENT ATOMS : 137
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.75
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): 0.121
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.114
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.065
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.009
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1037 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 960 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1397 ; 1.759 ; 1.909
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2184 ; 1.206 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 128 ; 5.882 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 50 ;34.698 ;23.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 166 ;11.081 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;20.150 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 144 ; 0.134 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1206 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 271 ; 0.002 ; 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): 515 ; 1.545 ; 1.681
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 514 ; 1.515 ; 1.678
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 642 ; 2.079 ; 2.512
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 643 ; 2.083 ; 2.516
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 522 ; 3.155 ; 2.043
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 522 ; 3.151 ; 2.044
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 756 ; 4.368 ; 2.928
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1394 ; 6.372 ;15.422
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1395 ; 6.370 ;15.431
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5B07 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1300000300.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS VII
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11225
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.40
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 82.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2YVB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NACL, ETHYLENE GLYCOL, PH 4.6, 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 18.40000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.40800
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.40800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.60000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.40800
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.40800
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 9.20000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.40800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.40800
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.60000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.40800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.40800
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 9.20000
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 18.40000
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 TOTAL BURIED SURFACE AREA: 260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
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 HOH A2163 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2234 LIES ON A SPECIAL POSITION.
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 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 5 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP A 18 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ASP A 66 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
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 NA A2009 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 21 O
REMARK 620 2 HOH A2122 O 88.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A2012 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 41 O
REMARK 620 2 THR A 43 OG1 112.5
REMARK 620 3 TYR A 53 OH 87.4 31.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A2008 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 49 O
REMARK 620 2 THR A 51 OG1 99.4
REMARK 620 3 ASP A 66 OD2 153.9 95.2
REMARK 620 4 THR A 69 OG1 86.7 140.8 68.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A2005 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 53 O
REMARK 620 2 SER A 91 OG 117.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A2011 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 65 OD1
REMARK 620 2 HOH A2101 O 120.1
REMARK 620 3 HOH A2146 O 73.1 50.7
REMARK 620 4 HOH A2209 O 107.2 131.3 149.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A2006 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 83 O
REMARK 620 2 SER A 91 OG 76.5
REMARK 620 3 HOH A2115 O 97.2 88.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A2007 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2129 O
REMARK 620 2 HOH A2230 O 138.9
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 2007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 2008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 2009
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 2010
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 2011
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 2012
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 2013
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 2014
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 2015
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 2016
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5B05 RELATED DB: PDB
REMARK 900 HEN EGG LYSOZYME (CONTROL EXPERIMENT)
REMARK 900 RELATED ID: 5B06 RELATED DB: PDB
REMARK 900 HEN EGG LYSOZYME (DENATURED BY NAOD AND REFOLDED)
DBREF 5B07 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 EDO A2001 4
HET EDO A2002 4
HET EDO A2003 4
HET EDO A2004 4
HET NA A2005 1
HET NA A2006 1
HET NA A2007 1
HET NA A2008 1
HET NA A2009 1
HET NA A2010 1
HET NA A2011 1
HET NA A2012 1
HET CL A2013 1
HET CL A2014 1
HET CL A2015 1
HET CL A2016 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO 4(C2 H6 O2)
FORMUL 6 NA 8(NA 1+)
FORMUL 14 CL 4(CL 1-)
FORMUL 18 HOH *137(H2 O)
HELIX 1 AA1 GLY A 4 HIS A 15 1 12
HELIX 2 AA2 ASN A 19 TYR A 23 5 5
HELIX 3 AA3 SER A 24 ASN A 37 1 14
HELIX 4 AA4 PRO A 79 SER A 85 5 7
HELIX 5 AA5 ILE A 88 SER A 100 1 13
HELIX 6 AA6 ASN A 103 ALA A 107 5 5
HELIX 7 AA7 TRP A 108 CYS A 115 1 8
HELIX 8 AA8 ASP A 119 ARG A 125 5 7
SHEET 1 AA1 3 THR A 43 ARG A 45 0
SHEET 2 AA1 3 THR A 51 TYR A 53 -1 O ASP A 52 N ASN A 44
SHEET 3 AA1 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 2.04
SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.05
SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.06
SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.06
LINK O ARG A 21 NA NA A2009 1555 1555 2.79
LINK O GLN A 41 NA NA A2012 1555 1555 2.73
LINK OG1 THR A 43 NA NA A2012 1555 1555 2.76
LINK O GLY A 49 NA NA A2008 1555 1555 2.91
LINK OG1 THR A 51 NA NA A2008 1555 1555 2.72
LINK O TYR A 53 NA NA A2005 1555 1555 2.85
LINK OH TYR A 53 NA NA A2012 1555 8555 2.79
LINK OD1 ASN A 65 NA NA A2011 1555 1555 2.90
LINK OD2 ASP A 66 NA NA A2008 1555 1555 2.78
LINK OG1 THR A 69 NA NA A2008 1555 1555 3.10
LINK O LEU A 83 NA NA A2006 1555 1555 2.60
LINK OG SER A 91 NA NA A2005 1555 1555 2.97
LINK OG SER A 91 NA NA A2006 1555 1555 3.00
LINK NA NA A2006 O HOH A2115 1555 1555 2.54
LINK NA NA A2007 O HOH A2129 1555 1555 2.98
LINK NA NA A2007 O HOH A2230 1555 8555 2.80
LINK NA NA A2009 O HOH A2122 1555 4555 2.83
LINK NA NA A2010 O HOH A2152 1555 1555 2.83
LINK NA NA A2011 O HOH A2101 1555 1555 2.46
LINK NA NA A2011 O HOH A2146 1555 1555 3.13
LINK NA NA A2011 O HOH A2209 1555 1555 2.62
SITE 1 AC1 9 GLN A 57 ILE A 58 ASN A 59 TRP A 63
SITE 2 AC1 9 ALA A 107 TRP A 108 HOH A2114 HOH A2158
SITE 3 AC1 9 HOH A2174
SITE 1 AC2 7 ARG A 21 VAL A 99 SER A 100 ASP A 101
SITE 2 AC2 7 GLY A 102 ASN A 103 GLY A 104
SITE 1 AC3 4 GLY A 4 ARG A 5 CYS A 6 GLU A 7
SITE 1 AC4 5 ASN A 65 ASN A 74 ASN A 77 ILE A 78
SITE 2 AC4 5 PRO A 79
SITE 1 AC5 6 TYR A 53 GLY A 54 ILE A 55 LEU A 56
SITE 2 AC5 6 GLN A 57 SER A 91
SITE 1 AC6 5 GLY A 54 ILE A 55 LEU A 83 SER A 91
SITE 2 AC6 5 HOH A2115
SITE 1 AC7 5 VAL A 2 ASN A 65 GLY A 67 HOH A2129
SITE 2 AC7 5 HOH A2230
SITE 1 AC8 7 ARG A 45 GLY A 49 SER A 50 THR A 51
SITE 2 AC8 7 ASP A 66 ARG A 68 THR A 69
SITE 1 AC9 5 ARG A 21 TYR A 23 ARG A 114 CL A2013
SITE 2 AC9 5 HOH A2122
SITE 1 AD1 4 ALA A 42 ASN A 44 ARG A 68 HOH A2152
SITE 1 AD2 6 CYS A 64 ASN A 65 SER A 72 ARG A 73
SITE 2 AD2 6 HOH A2101 HOH A2209
SITE 1 AD3 4 GLN A 41 THR A 43 TYR A 53 ARG A 68
SITE 1 AD4 3 TYR A 23 ASN A 113 NA A2009
SITE 1 AD5 6 GLY A 67 ARG A 68 THR A 69 SER A 72
SITE 2 AD5 6 HOH A2146 HOH A2208
SITE 1 AD6 4 SER A 24 GLY A 26 GLN A 121 HOH A2200
SITE 1 AD7 1 LYS A 33
CRYST1 78.816 78.816 36.800 90.00 90.00 90.00 P 43 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012703 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012703 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027187 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
