HEADER HYDROLASE (O-GLYCOSYL) 01-FEB-75 6LYZ TITLE REAL-SPACE REFINEMENT OF THE STRUCTURE OF HEN EGG-WHITE TITLE 2 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 KEYWDS HYDROLASE (O-GLYCOSYL) EXPDTA X-RAY DIFFRACTION AUTHOR R.DIAMOND,D.C.PHILLIPS,C.C.F.BLAKE,A.C.T.NORTH REVDAT 9 16-OCT-87 6LYZ 1 FTNOTE TURN REVDAT 8 25-APR-86 6LYZ 3 SOURCE SEQRES ATOM REVDAT 7 07-FEB-84 6LYZ 1 FTNOTE REVDAT 6 30-SEP-83 6LYZ 1 REVDAT REVDAT 5 01-MAR-82 6LYZ 1 REMARK REVDAT 4 20-APR-81 6LYZ 1 SHEET REVDAT 3 01-NOV-77 6LYZ 1 COMPND SOURCE AUTHOR JRNL REVDAT 3 2 1 REMARK FORMUL SSBOND REVDAT 2 16-MAY-77 6LYZ 3 SEQRES ATOM REVDAT 1 12-APR-77 6LYZ 0 JRNL AUTH R.DIAMOND JRNL TITL REAL-SPACE REFINEMENT OF THE STRUCTURE OF HEN JRNL TITL 2 EGG-WHITE LYSOZYME. JRNL REF J.MOL.BIOL. V. 82 371 1974 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.C.PHILLIPS REMARK 1 TITL CRYSTALLOGRAPHIC STUDIES OF LYSOZYME AND ITS REMARK 1 TITL 2 INTERACTIONS 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 ISBN 0-12-528950-2 REMARK 1 REFERENCE 2 REMARK 1 AUTH T.IMOTO,L.N.JOHNSON,A.C.T.NORTH,D.C.PHILLIPS, REMARK 1 AUTH 2 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 ISBN 0-12-122711-1 REMARK 1 REFERENCE 3 REMARK 1 AUTH C.R.BEDDELL,C.C.F.BLAKE,S.J.OATLEY REMARK 1 TITL AN X-RAY STUDY OF THE STRUCTURE AND BINDING REMARK 1 TITL 2 PROPERTIES OF IODINE-INACTIVATED LYSOZYME REMARK 1 REF J.MOL.BIOL. V. 97 643 1975 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 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 ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REFERENCE 5 REMARK 1 AUTH C.C.F.BLAKE,G.A.MAIR,A.C.T.NORTH,D.C.PHILLIPS, REMARK 1 AUTH 2 V.R.SARMA REMARK 1 TITL ON THE CONFORMATION OF THE HEN EGG-WHITE LYSOZYME REMARK 1 TITL 2 MOLECULE REMARK 1 REF PROC.R.SOC.LONDON,SER.B V. 167 365 1967 REMARK 1 REFN ASTM PRLBA4 UK ISSN 0080-4649 REMARK 1 REFERENCE 6 REMARK 1 AUTH C.C.F.BLAKE,L.N.JOHNSON,G.A.MAIR,A.C.T.NORTH, REMARK 1 AUTH 2 D.C.PHILLIPS,V.R.SARMA REMARK 1 TITL CRYSTALLOGRAPHIC STUDIES OF THE ACTIVITY OF HEN REMARK 1 TITL 2 EGG-WHITE LYSOZYME REMARK 1 REF PROC.R.SOC.LONDON,SER.B V. 167 378 1967 REMARK 1 REFN ASTM PRLBA4 UK ISSN 0080-4649 REMARK 1 REFERENCE 7 REMARK 1 AUTH D.C.PHILLIPS REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF AN ENZYME REMARK 1 TITL 2 MOLECULE REMARK 1 REF SCI.AM. V. 215 78 1966 REMARK 1 REFN ASTM SCAMAC US ISSN 0036-8733 REMARK 1 REFERENCE 8 REMARK 1 AUTH C.C.F.BLAKE,D.F.KOENIG,G.A.MAIR,A.C.T.NORTH, REMARK 1 AUTH 2 D.C.PHILLIPS,V.R.SARMA REMARK 1 TITL STRUCTURE OF HEN EGG-WHITE LYSOZYME, A REMARK 1 TITL 2 THREE-DIMENSIONAL FOURIER SYNTHESIS AT 2 ANGSTROMS REMARK 1 TITL 3 RESOLUTION REMARK 1 REF NATURE V. 206 757 1965 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 REMARK 1 REFERENCE 9 REMARK 1 AUTH L.N.JOHNSON,D.C.PHILLIPS REMARK 1 TITL STRUCTURE OF SOME CRYSTALLINE LYSOZYME-INHIBITOR REMARK 1 TITL 2 COMPLEXES DETERMINED BY X-RAY ANALYSIS AT 6 REMARK 1 TITL 3 ANGSTROMS RESOLUTION REMARK 1 REF NATURE V. 206 761 1965 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 REMARK 1 REFERENCE 10 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 ISBN 0-917934-01-6 REMARK 1 REFERENCE 11 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 REMARK 1 PUBL 2 SPRING,MD. REMARK 1 REFN ISBN 0-912466-02-2 REMARK 2 REMARK 2 RESOLUTION. 2.00 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) : 2.00 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 : 1001 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 101 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 6LYZ COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-18) 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 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 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,1/2+Z REMARK 290 3555 1/2-Y,1/2+X,3/4+Z REMARK 290 4555 1/2+Y,1/2-X,1/4+Z REMARK 290 5555 1/2-X,1/2+Y,3/4-Z REMARK 290 6555 1/2+X,1/2-Y,1/4-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,1/2-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). 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 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 91 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 REMARK 500 O LYS A 97 OD1 ASP A 101 1.01 REMARK 500 O LYS A 97 CG ASP A 101 1.47 REMARK 500 NE2 GLN A 121 O HOH 14 1.57 REMARK 500 OE1 GLN A 121 O HOH 13 1.60 REMARK 500 CD GLN A 121 O HOH 13 1.64 REMARK 500 NH1 ARG A 5 O TRP A 123 1.70 REMARK 500 O LYS A 97 OD2 ASP A 101 1.70 REMARK 500 NH1 ARG A 45 NH1 ARG A 68 1.74 REMARK 500 NH2 ARG A 5 O ARG A 125 1.77 REMARK 500 OD1 ASP A 87 OG1 THR A 89 2.08 REMARK 500 O HOH 57 O HOH 57A 2.08 REMARK 500 NE ARG A 21 O HOH 89 2.10 REMARK 500 O ILE A 98 OD2 ASP A 101 2.11 REMARK 500 O HOH 30 O HOH 32 2.12 REMARK 500 O HOH 100 O HOH 101 2.12 REMARK 500 O THR A 69 O HOH 96 2.13 REMARK 500 CG1 VAL A 109 O HOH 69 2.13 REMARK 500 O HOH 25 O HOH 26 2.13 REMARK 500 OG SER A 24 O HOH 23 2.15 REMARK 500 C LYS A 97 OD1 ASP A 101 2.16 REMARK 500 O HOH 28 O HOH 29 2.18 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH 63 O HOH 83 6456 0.06 REMARK 500 O HOH 11 O HOH 56 8555 0.13 REMARK 500 O HOH 8A O HOH 94 4454 0.16 REMARK 500 CD ARG A 128 O HOH 57 8555 0.74 REMARK 500 NE ARG A 128 O HOH 57 8555 1.58 REMARK 500 CG ARG A 128 O HOH 57 8555 1.85 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PRO A 70 N - CA - C ANGL. DEV. = 25.2 DEGREES REMARK 500 THR A 118 N - CA - C ANGL. DEV. =-29.2 DEGREES REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 SER A 100 ASP A 101 -144.45 REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 19 DISTANCE = 5.70 ANGSTROMS REMARK 525 HOH 77 DISTANCE = 5.17 ANGSTROMS REMARK 525 HOH 91 DISTANCE = 5.70 ANGSTROMS REMARK 525 HOH 95 DISTANCE = 5.89 ANGSTROMS DBREF 6LYZ 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 FTNOTE 1 POSSIBLE HYDROGEN BONDS TO CARBONYL OF TYR 53, N OF LEU 56, FTNOTE 1 OG OF SER 91 FTNOTE 2 POSSIBLE HYDROGEN BONDS TO HOH 44, HOH 61, CARBONYL OF ASP FTNOTE 2 87, N AND OG OF SER 91 FTNOTE 3 POSSIBLE HYDROGEN BONDS TO HOH 4, NZ OF LYS 1, CARBONYL OF FTNOTE 3 VAL 2, OE1 OF GLU 7 FTNOTE 4 POSSIBLE HYDROGEN BONDS TO HOH 3, HOH 40, OE OF GLU 7 FTNOTE 4 POSSIBLE HYDROGEN BOND TO NE OF ARG 5 FTNOTE 5 POSSIBLE HYDROGEN BONDS TO NE OF ARG 14, CARBONYL OF ARG FTNOTE 5 128, HOH 40 FTNOTE 6 POSSIBLE HYDROGEN BONDS TO NZ OF LYS 33, NE OF ARG 73, HOH FTNOTE 6 40 FTNOTE 7 POSSIBLE HYDROGEN BONDS TO CARBONYLS OF ILE 124, CYS 127, FTNOTE 7 HOH 39 FTNOTE 8 POSSIBLE HYDROGEN BONDS TO OD1 OF ASP 48, N OF GLY 126 FTNOTE 9 POSSIBLE HYDROGEN BOND TO NE OF ARG 61 FTNOTE 10 POSSIBLE HYDROGEN BOND TO NE OF ARG 5 FTNOTE 11 POSSIBLE HYDROGEN BOND TO N OF CYS 6 FTNOTE 12 POSSIBLE HYDROGEN BOND TO NE OF ARG 14 FTNOTE 13 POSSIBLE HYDROGEN BOND TO OG OF SER 24 FTNOTE 14 POSSIBLE HYDROGEN BOND TO AMIDE OF GLN 121 FTNOTE 15 POSSIBLE HYDROGEN BONDS TO HOH 24A, AMIDE OF GLN 121 FTNOTE 16 POSSIBLE HYDROGEN BOND TO OD OF ASP 119 FTNOTE 17 POSSIBLE HYDROGEN BOND TO HOH 35, NEAR NE1 OF TRP 123 FTNOTE 18 POSSIBLE HYDROGEN BONDS TO N OF TYR 23, ND2 OF ASN 27, NE FTNOTE 18 OF ARG 114 FTNOTE 19 POSSIBLE HYDROGEN BOND TO ND2 OF ASN 37 FTNOTE 20 POSSIBLE HYDROGEN BOND TO CARBONYL OF GLY 67, AND NEAR VAL FTNOTE 20 2 FTNOTE 21 POSSIBLE HYDROGEN BONDS TO N OF LYS 1, OG OF SER 86, HOH FTNOTE 21 34 PRO 79G FTNOTE 22 POSSIBLE HYDROGEN BONDS TO N OF LYS 1, OD1 OF ASN 39, OE1 FTNOTE 22 OF GLN 41, HOH 22 COG 66 FTNOTE 23 POSSIBLE HYDROGEN BOND TO HOH 21 OD 65G FTNOTE 24 POSSIBLE HYDROGEN BONDS TO OG OF SER 24, N OF GLY 26 FTNOTE 25 POSSIBLE HYDROGEN BONDS TO CARBONYL OF THR 118, N OF VAL FTNOTE 25 120, HOH 24A FTNOTE 26 POSSIBLE HYDROGEN BONDS TO HOH 14, HOH 24 FTNOTE 27 POSSIBLE HYDROGEN BONDS TO HOH 26, NE OF ARG 114 FTNOTE 28 POSSIBLE HYDROGEN BONDS TO CARBONYL OF ARG 114, HOH 25, FTNOTE 28 HOH 35 FTNOTE 29 POSSIBLE HYDROGEN BONDS TO HOH 28, CARBONYL OF PHE 34 COE FTNOTE 29 22 FTNOTE 30 POSSIBLE HYDROGEN BONDS TO HOH 27, HOH 29 NODE 19 FTNOTE 31 POSSIBLE HYDROGEN BONDS TO CARBONYL OF GLU 35, HOH 28, HOH FTNOTE 31 30, HOH 31 FTNOTE 32 POSSIBLE HYDROGEN BONDS TO HOH 29, HOH 32 NEH G68 FTNOTE 33 POSSIBLE HYDROGEN BONDS TO ND2 OF ASN 44, OE1 OF GLN 57, FTNOTE 33 HOH 29 FTNOTE 34 POSSIBLE HYDROGEN BONDS TO CARBONYL OF SER 36, ND2 OF ASN FTNOTE 34 39, HOH 30, HOH 33 G68 FTNOTE 35 POSSIBLE HYDROGEN BONDS TO ND2 OF ASN 37, HOH 32 G67 FTNOTE 36 POSSIBLE HYDROGEN BOND TO HOH 20, NEAR OG OF SER 26 FTNOTE 37 POSSIBLE HYDROGEN BONDS TO HOH 16, HOH 26, HOH 55 E116 FTNOTE 38 POSSIBLE HYDROGEN BONDS TO CARBONYL OF PHE 34, NH1 OF ARG FTNOTE 38 114 E22 FTNOTE 39 POSSIBLE HYDROGEN BONDS TO CARBONYL OF GLN 41, NE OF ARG FTNOTE 39 68 OEHG53 FTNOTE 40 POSSIBLE HYDROGEN BONDS TO OG1 OF THR 40, CARBONYL OF LEU FTNOTE 40 84, OG OF SER 86 N86 FTNOTE 41 POSSIBLE HYDROGEN BONDS TO HOH 7, HOH 40, NE OF ARG 14 FTNOTE 42 POSSIBLE HYDROGEN BONDS TO HOH 4, HOH 5, HOH 6, HOH 39, FTNOTE 42 HOH 41, ND1 OF HIS 15 FTNOTE 43 POSSIBLE HYDROGEN BONDS TO HOH 40, NE OF ARG 14, OD2 OF FTNOTE 43 ASP 87 FTNOTE 44 POSSIBLE HYDROGEN BONDS TO CARBONYL OF LYS 13, N OF ASP 18, FTNOTE 44 HOH 63 FTNOTE 45 POSSIBLE HYDROGEN BONDS TO CARBONYLS OF LEU 83, SER 85 FTNOTE 46 POSSIBLE HYDROGEN BONDS TO N OF ALA 110, ND2 OF ASN 113, FTNOTE 46 HOH 47 HOH 32 FTNOTE 47 POSSIBLE HYDROGEN BOND TO OD1 OF ASN 113 FTNOTE 48 POSSIBLE HYDROGEN BONDS TO HOH 45, HOH 48 FTNOTE 49 POSSIBLE HYDROGEN BONDS TO HOH 47, OE1 OF GLU 35, HOH 58, FTNOTE 49 HOH 59 FTNOTE 50 POSSIBLE HYDROGEN BONDS TO N OF GLU 7, N OF THR 118 FTNOTE 51 POSSIBLE HYDROGEN BONDS TO OG OF SER 85, HOH 51, HOH 66 FTNOTE 52 POSSIBLE HYDROGEN BOND TO HOH 50 FTNOTE 53 POSSIBLE HYDROGEN BOND TO HOH 53 FTNOTE 54 POSSIBLE HYDROGEN BOND TO HOH 52 FTNOTE 55 POSSIBLE HYDROGEN BOND TO HOH 35 FTNOTE 56 POSSIBLE HYDROGEN BOND TO NE OF ARG 14 FTNOTE 57 POSSIBLE HYDROGEN BONDS TO HOH 57A, CARBONYLS OF ARG 14, FTNOTE 57 HIS 15 FTNOTE 58 POSSIBLE HYDROGEN BOND TO HOH 57 FTNOTE 59 POSSIBLE HYDROGEN BONDS TO HOH 48, OD2 OF ASP 52 FTNOTE 60 POSSIBLE HYDROGEN BONDS TO HOH 48, HOH 60 FTNOTE 61 POSSIBLE HYDROGEN BOND TO HOH 59 FTNOTE 62 POSSIBLE HYDROGEN BONDS TO HOH 2, OG OF SER 85, CARBONYL FTNOTE 62 OF ASP 87 FTNOTE 63 POSSIBLE HYDROGEN BOND TO OG1 OF THR 89 FTNOTE 64 POSSIBLE HYDROGEN BONDS TO CARBONYL OF GLY 16, HOH 43 FTNOTE 65 POSSIBLE HYDROGEN BONDS TO HOH 65, N OF ARG 45 FTNOTE 66 POSSIBLE HYDROGEN BONDS TO HOH 64, CARBONYL OF ARG 45 FTNOTE 67 POSSIBLE HYDROGEN BOND TO HOH 50 FTNOTE 68 POSSIBLE HYDROGEN BONDS TO HOH 67A, HOH 68, HOH 69, HOH 70 FTNOTE 68 CARBONYL OF GLN 57 FTNOTE 69 POSSIBLE HYDROGEN BONDS TO HOH 67, HOH 68, HOH 70 FTNOTE 70 POSSIBLE HYDROGEN BONDS TO HOH 67, HOH 67A, CARBONYL OF FTNOTE 70 ALA 107 FTNOTE 71 POSSIBLE HYDROGEN BONDS TO HOH 67, N OF VAL 109 FTNOTE 72 POSSIBLE HYDROGEN BONDS TO HOH 67, HOH 67A, OD1 AND OD2 OF FTNOTE 72 ASP 52 FTNOTE 73 POSSIBLE HYDROGEN BOND TO OD1 OF ASN 46 FTNOTE 74 POSSIBLE HYDROGEN BOND TO CARBONYL OF ASN 46 FTNOTE 75 POSSIBLE HYDROGEN BOND TO NZ OF LYS 96, HOH 75 FTNOTE 76 POSSIBLE HYDROGEN BOND TO HOH 73 FTNOTE 77 POSSIBLE HYDROGEN BOND TO N OF ASN 59 FTNOTE 78 EXTENDED DENSITY NEAR CLEFT FTNOTE 79 POSSIBLE HYDROGEN BONDS TO CARBONYL OF GLY 49, OG1 OF THR FTNOTE 79 51, OG OF SER 60, ND2 OF ASP 66, NE OF ARG 68 FTNOTE 81 NO CONTACT FTNOTE 82 POSSIBLE HYDROGEN BONDS TO CARBONYL OF ILE 98, N OF GLY FTNOTE 82 102, N OF ASN 103 FTNOTE 83 POSSIBLE HYDROGEN BOND TO OD2 OF ASN 103, HOH 95 FTNOTE 84 POSSIBLE HYDROGEN BOND TO CARBONYL OF THR 47 FTNOTE 85 POSSIBLE HYDROGEN BONDS TO NE OF ARG 45, CARBONYL OF ASP FTNOTE 85 48, CARBONYL OF ARG 68 FTNOTE 86 POSSIBLE HYDROGEN BONDS TO OH OF TYR 20, OG OF SER 100 FTNOTE 88 POSSIBLE HYDROGEN BONDS TO NE OF ARG 21, OG OF SER 100 FTNOTE 89 ON TWO-FOLD AXIS FTNOTE 90 POSSIBLE HYDROGEN BONDS TO HOH 94, NE1 OF TRP 62, HOH 95 FTNOTE 91 POSSIBLE HYDROGEN BONDS TO HOH 93, NE OF ARG 61 FTNOTE 92 POSSIBLE HYDROGEN BONDS TO HOH 82, HOH 93 FTNOTE 93 POSSIBLE HYDROGEN BONDS TO OD1 OF ASN 65, N AND CARBONYL FTNOTE 93 OF THR 69, OG OF SER 72, NEAR BAD PATCH FTNOTE 94 POSSIBLE HYDROGEN BOND TO CARBONYL OF CYS 76 FTNOTE 95 POSSIBLE HYDROGEN BOND TO NE OF ARG 61 FTNOTE 96 POSSIBLE HYDROGEN BOND TO HOH 100 FTNOTE 97 POSSIBLE HYDROGEN BONDS TO HOH 99, HOH 101, HOH 102 FTNOTE 98 POSSIBLE HYDROGEN BOND TO HOH 100 FTNOTE 99 POSSIBLE HYDROGEN BONDS TO HOH 100, HOH 103 FTNOTE 100 POSSIBLE HYDROGEN BONDS TO HOH 102, HOH 104 FTNOTE 101 POSSIBLE HYDROGEN BOND TO HOH 103 FORMUL 2 HOH *101(H2 O) 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 TURN 1 T1 LYS A 13 GLY A 16 TYPE I. TURN 2 T2 LEU A 17 TYR A 20 NEARLY TYPE II CONFORMATION. TURN 3 T4 TYR A 20 TYR A 23 NEARLY TYPE II CONFORMATION. TURN 4 T5 GLY A 54 GLN A 57 TYPE I,BETW STRNDS 2,3 SHT S2. TURN 5 T6 ASN A 59 TRP A 62 NEARLY TYPE I CONFORMATION. TURN 6 T7 THR A 69 SER A 72 NEARLY TYPE I CONFORMATION. TURN 7 T8 ASN A 74 ASN A 77 TYPE I. TURN 8 T9 ASN A 103 ASN A 106 TYPE I. TURN 9 T10 CYS A 115 THR A 118 TYPE II (IMPERFECT). TURN 10 T11 ILE A 124 CYS A 127 TYPE II (IMPERFECT). SSBOND 1 CYS A 6 CYS A 127 SSBOND 2 CYS A 30 CYS A 115 SSBOND 3 CYS A 64 CYS A 80 SSBOND 4 CYS A 76 CYS A 94 CRYST1 79.100 79.100 37.900 90.00 90.00 90.00 P 43 21 2 8 ORIGX1 1.517067 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.517067 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.583113 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 1 N LYS A 1 3.287 10.092 10.329 5.89 1.50 N ATOM 2 CA LYS A 1 2.445 10.457 9.182 8.16 1.50 C ATOM 3 C LYS A 1 2.500 11.978 9.038 8.04 1.50 C ATOM 4 O LYS A 1 2.588 12.719 10.041 7.07 1.50 O ATOM 5 CB LYS A 1 1.006 9.995 9.385 3.88 1.50 C ATOM 6 CG LYS A 1 0.016 10.546 8.377 3.81 1.50 C ATOM 7 CD LYS A 1 -1.404 10.093 8.699 2.91 1.50 C ATOM 8 CE LYS A 1 -2.269 10.030 7.451 3.97 1.50 C ATOM 9 NZ LYS A 1 -3.559 9.362 7.735 2.08 1.50 N ATOM 10 N VAL A 2 2.441 12.404 7.789 8.75 1.50 N ATOM 11 CA VAL A 2 2.396 13.826 7.425 9.16 1.50 C END