HEADER HYDROLASE (O-GLYCOSYL) 16-SEP-77 8LYZ
TITLE AN X-RAY STUDY OF THE STRUCTURE AND BINDING PROPERTIES OF IODINE-
TITLE 2 INACTIVATED LYSOZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEN EGG WHITE LYSOZYME;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.17;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031
KEYWDS HYDROLASE (O-GLYCOSYL)
EXPDTA X-RAY DIFFRACTION
AUTHOR C.R.BEDDELL,C.C.F.BLAKE,S.J.OATLEY
REVDAT 12 29-NOV-17 8LYZ 1 HELIX
REVDAT 11 24-FEB-09 8LYZ 1 VERSN
REVDAT 10 01-APR-03 8LYZ 1 JRNL
REVDAT 9 14-JUL-86 8LYZ 3 SEQRES TURN ATOM
REVDAT 8 22-OCT-84 8LYZ 1 SHEET
REVDAT 7 27-JAN-84 8LYZ 1 REMARK
REVDAT 6 30-SEP-83 8LYZ 1 REVDAT
REVDAT 5 01-MAR-82 8LYZ 1 REMARK
REVDAT 4 21-MAY-81 8LYZ 3 ATOM
REVDAT 3 25-MAY-78 8LYZ 1 SEQRES
REVDAT 2 01-NOV-77 8LYZ 1 SSBOND
REVDAT 1 24-OCT-77 8LYZ 0
JRNL AUTH C.R.BEDDELL,C.C.BLAKE,S.J.OATLEY
JRNL TITL AN X-RAY STUDY OF THE STRUCTURE AND BINDING PROPERTIES OF
JRNL TITL 2 IODINE-INACTIVATED LYSOZYME.
JRNL REF J.MOL.BIOL. V. 97 643 1975
JRNL REFN ISSN 0022-2836
JRNL PMID 1185784
JRNL DOI 10.1016/S0022-2836(75)80064-7
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.DIAMOND
REMARK 1 TITL REAL-SPACE REFINEMENT OF THE STRUCTURE OF HEN EGG-WHITE
REMARK 1 TITL 2 LYSOZYME
REMARK 1 REF J.MOL.BIOL. V. 82 371 1974
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.C.PHILLIPS
REMARK 1 TITL CRYSTALLOGRAPHIC STUDIES OF LYSOZYME AND ITS INTERACTIONS
REMARK 1 TITL 2 WITH INHIBITORS AND SUBSTRATES
REMARK 1 EDIT E.F.OSSERMAN, R.F.CANFIELD, S.BEYCHOK
REMARK 1 REF LYSOZYME 9 1974
REMARK 1 PUBL ACADEMIC PRESS,NEW YORK
REMARK 1 REFN
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.IMOTO,L.N.JOHNSON,A.C.T.NORTH,D.C.PHILLIPS,J.A.RUPLEY
REMARK 1 TITL VERTEBRATE LYSOZYMES
REMARK 1 EDIT P.BOYER
REMARK 1 REF THE ENZYMES,THIRD EDITION V. 7 665 1972
REMARK 1 PUBL ACADEMIC PRESS,NEW YORK
REMARK 1 REFN
REMARK 1 REFERENCE 4
REMARK 1 AUTH M.LEVITT
REMARK 1 TITL ENERGY REFINEMENT OF HEN EGG-WHITE LYSOZYME
REMARK 1 REF J.MOL.BIOL. V. 82 393 1974
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 5
REMARK 1 AUTH L.O.FORD,L.N.JOHNSON,P.A.MACHIN,D.C.PHILLIPS,R.TJIAN
REMARK 1 TITL CRYSTAL STRUCTURE OF A LYSOZYME-TETRASACCHARIDE LACTONE
REMARK 1 TITL 2 COMPLEX
REMARK 1 REF J.MOL.BIOL. V. 88 349 1974
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 6
REMARK 1 AUTH C.C.F.BLAKE,G.A.MAIR,A.C.T.NORTH,D.C.PHILLIPS,V.R.SARMA
REMARK 1 TITL ON THE CONFORMATION OF THE HEN EGG-WHITE LYSOZYME MOLECULE
REMARK 1 REF PROC.R.SOC.LONDON,SER.B V. 167 365 1967
REMARK 1 REFN ISSN 0080-4649
REMARK 1 REFERENCE 7
REMARK 1 AUTH C.C.F.BLAKE,L.N.JOHNSON,G.A.MAIR,A.C.T.NORTH,D.C.PHILLIPS,
REMARK 1 AUTH 2 V.R.SARMA
REMARK 1 TITL CRYSTALLOGRAPHIC STUDIES OF THE ACTIVITY OF HEN EGG-WHITE
REMARK 1 TITL 2 LYSOZYME
REMARK 1 REF PROC.R.SOC.LONDON,SER.B V. 167 378 1967
REMARK 1 REFN ISSN 0080-4649
REMARK 1 REFERENCE 8
REMARK 1 AUTH D.C.PHILLIPS
REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF AN ENZYME MOLECULE
REMARK 1 REF SCI.AM. V. 215 78 1966
REMARK 1 REFN ISSN 0036-8733
REMARK 1 REFERENCE 9
REMARK 1 AUTH C.C.F.BLAKE,D.F.KOENIG,G.A.MAIR,A.C.T.NORTH,D.C.PHILLIPS,
REMARK 1 AUTH 2 V.R.SARMA
REMARK 1 TITL STRUCTURE OF HEN EGG-WHITE LYSOZYME, A THREE-DIMENSIONAL
REMARK 1 TITL 2 FOURIER SYNTHESIS AT 2 ANGSTROMS RESOLUTION
REMARK 1 REF NATURE V. 206 757 1965
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 10
REMARK 1 AUTH L.N.JOHNSON,D.C.PHILLIPS
REMARK 1 TITL STRUCTURE OF SOME CRYSTALLINE LYSOZYME-INHIBITOR COMPLEXES
REMARK 1 TITL 2 DETERMINED BY X-RAY ANALYSIS AT 6 ANGSTROMS RESOLUTION
REMARK 1 REF NATURE V. 206 761 1965
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 11
REMARK 1 EDIT R.J.FELDMANN
REMARK 1 REF ATLAS OF MACROMOLECULAR 492 1976
REMARK 1 REF 2 STRUCTURE ON MICROFICHE
REMARK 1 PUBL TRACOR JITCO INC.,ROCKVILLE,MD.
REMARK 1 REFN
REMARK 1 REFERENCE 12
REMARK 1 EDIT M.O.DAYHOFF
REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 138 1972
REMARK 1 REF 2 AND STRUCTURE (DATA SECTION)
REMARK 1 PUBL NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER SPRING,MD.
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1000
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8LYZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000180007.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
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 18.95000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.55000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.55000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 28.42500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.55000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.55000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 9.47500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.55000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.55000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 28.42500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.55000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.55000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 9.47500
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 18.95000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 CB ALA A 122 NH2 ARG A 125 1.49
REMARK 500 CB ALA A 122 CZ ARG A 125 1.49
REMARK 500 OE2 GLU A 35 CD1 TRP A 108 1.54
REMARK 500 OD2 ASP A 119 NH1 ARG A 125 1.60
REMARK 500 NH2 ARG A 45 NH2 ARG A 68 1.70
REMARK 500 NH1 ARG A 5 O ARG A 125 1.72
REMARK 500 NH2 ARG A 5 O TRP A 123 1.80
REMARK 500 CA ALA A 122 NE ARG A 125 1.84
REMARK 500 O LYS A 97 OD1 ASP A 101 2.06
REMARK 500 CA ALA A 122 CZ ARG A 125 2.09
REMARK 500 OD1 ASP A 87 OG1 THR A 89 2.12
REMARK 500 O LEU A 56 NE1 TRP A 108 2.12
REMARK 500 CB ALA A 122 NH1 ARG A 125 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 28 NE1 TRP A 28 CE2 -0.094
REMARK 500 ASN A 46 CG ASN A 46 OD1 0.152
REMARK 500 ASN A 59 CG ASN A 59 OD1 0.159
REMARK 500 TRP A 62 NE1 TRP A 62 CE2 -0.097
REMARK 500 TRP A 63 NE1 TRP A 63 CE2 -0.097
REMARK 500 ASP A 66 CG ASP A 66 OD1 0.143
REMARK 500 ASN A 74 CG ASN A 74 OD1 0.155
REMARK 500 TRP A 108 NE1 TRP A 108 CE2 -0.084
REMARK 500 TRP A 111 NE1 TRP A 111 CE2 -0.094
REMARK 500 TRP A 123 NE1 TRP A 123 CE2 -0.097
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLU A 7 OE1 - CD - OE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 LEU A 17 N - CA - C ANGL. DEV. = 17.0 DEGREES
REMARK 500 ASP A 18 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASN A 46 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 ASP A 48 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP A 52 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP A 63 CA - CB - CG ANGL. DEV. = -13.8 DEGREES
REMARK 500 ASP A 66 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 SER A 72 CB - CA - C ANGL. DEV. = -20.6 DEGREES
REMARK 500 SER A 72 N - CA - C ANGL. DEV. = 34.0 DEGREES
REMARK 500 ARG A 73 N - CA - C ANGL. DEV. = -28.0 DEGREES
REMARK 500 CYS A 76 N - CA - CB ANGL. DEV. = 24.8 DEGREES
REMARK 500 ASP A 87 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 101 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 GLY A 102 N - CA - C ANGL. DEV. = 15.7 DEGREES
REMARK 500 CYS A 115 N - CA - CB ANGL. DEV. = 9.3 DEGREES
REMARK 500 THR A 118 N - CA - C ANGL. DEV. = -21.2 DEGREES
REMARK 500 ASP A 119 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG A 128 N - CA - C ANGL. DEV. = -17.9 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 ARG A 21 18.83 52.15
REMARK 500 TRP A 62 -41.61 -133.16
REMARK 500 SER A 72 120.20 -29.08
REMARK 500 CYS A 115 -57.62 -130.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 5 0.16 SIDE CHAIN
REMARK 500 ARG A 14 0.09 SIDE CHAIN
REMARK 500 ARG A 114 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8LYZ 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
HELIX 1 A ARG A 5 HIS A 15 1 11
HELIX 2 B LEU A 25 GLU A 35 1 11
HELIX 3 C CYS A 80 LEU A 84 5 5
HELIX 4 D THR A 89 LYS A 96 1 8
SHEET 1 S1 2 LYS A 1 PHE A 3 0
SHEET 2 S1 2 PHE A 38 THR A 40 -1 N THR A 40 O LYS A 1
SHEET 1 S2 3 ALA A 42 ASN A 46 0
SHEET 2 S2 3 SER A 50 GLY A 54 -1 N ASN A 46 O SER A 50
SHEET 3 S2 3 GLN A 57 SER A 60 -1 N TYR A 53 O ILE A 58
SSBOND 1 CYS A 6 CYS A 127 1555 1555 2.15
SSBOND 2 CYS A 30 CYS A 115 1555 1555 1.99
SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.06
SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.15
CRYST1 79.100 79.100 37.900 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 0.012642 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012642 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026385 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
