HEADER HYDROLASE 12-JUN-02 1H09
TITLE MULTIMODULAR PNEUMOCOCCAL CELL WALL ENDOLYSIN FROM PHAGE
TITLE 2 CP-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MUREIN HYDROLASE, ENDOLYSIN, MURAMIDASE, CP-1
COMPND 5 LYSIN;
COMPND 6 EC: 3.2.1.17;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTERIOPHAGE CP-1;
SOURCE 3 ORGANISM_TAXID: 10747;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: DH1;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PCIP100
KEYWDS MUREIN HYDROLASE, LYSOZYME, MULTIMODULAR, HYDROLASE,
KEYWDS 2 GLYCOSIDASE, BACTERIOLYTIC ENZYME, PNEUMOCOCCAL CELL WALL
KEYWDS 3 DEGRADATION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.HERMOSO,B.MONTERROSO,A.ALBERT,P.GARCIA,M.MENENDEZ,
AUTHOR 2 M.MARTINEZ-RIPOLL,J.L.GARCIA
REVDAT 3 24-FEB-09 1H09 1 VERSN
REVDAT 2 17-OCT-03 1H09 1 JRNL
REVDAT 1 26-JUN-03 1H09 0
JRNL AUTH J.A.HERMOSO,B.MONTERROSO,A.ALBERT,B.GALAN,
JRNL AUTH 2 O.AHRAZEM,P.GARCIA,M.MARTINEZ-RIPOLL,J.L.GARCIA,
JRNL AUTH 3 M.MENENDEZ
JRNL TITL STRUCTURAL BASIS FOR SELECTIVE RECOGNITION OF
JRNL TITL 2 PNEUMOCOCCAL CELL WALL BY MODULAR ENDOLYSIN FROM
JRNL TITL 3 PHAGE CP-1
JRNL REF STRUCTURE V. 11 1239 2003
JRNL REFN ISSN 0969-2126
JRNL PMID 14527392
JRNL DOI 10.1016/J.STR.2003.09.005
REMARK 2
REMARK 2 RESOLUTION. 2.1 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.1
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1701629.16
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 28272
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 SET) : 0.206
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1429
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.2
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4276
REMARK 3 BIN R VALUE (WORKING SET) : 0.258
REMARK 3 BIN FREE R VALUE : 0.304
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.4
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 246
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2763
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 326
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.3
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.6
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.22
REMARK 3 B22 (A**2) : 2.13
REMARK 3 B33 (A**2) : -3.35
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.18
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.3
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.7
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.69
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 50.8
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1H09 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUN-02.
REMARK 100 THE PDBE ID CODE IS EBI-9958.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-01
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.004
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28359
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 39.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.34900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: SOLVE, SHARP, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: SAD WITH A NON-ISOMORPHOUS HG DERIVATIVE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.7M NA FORMATE, 0.1M NA
REMARK 280 CIT.(PH6),1.8MM N-DECYL-MALTOSIDE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+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 64.64000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.64000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 38.97500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.89000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 38.97500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.89000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.64000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.97500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 47.89000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.64000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 38.97500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 47.89000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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 400
REMARK 400 COMPOUND
REMARK 400 THIS PROTEIN IS A MODULAR ENZYME, THE FIRST RESIDUES (2-188)
REMARK 400 FORM THE CATALYTIC MODULE, WITH RESIDUES 189-199 FORMING
REMARK 400 THE LINKER AND FINALLY, THE CELL WALL ANCHORING MODULE IS
REMARK 400 FORMED BY RESIDUES 200-339.
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 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 SER A 38 -140.25 53.43
REMARK 500 GLU A 94 10.99 -145.65
REMARK 500 SER A 126 -169.27 179.46
REMARK 500 ASN A 146 52.93 39.01
REMARK 500 ASP A 193 104.60 -26.16
REMARK 500 ASP A 194 -138.03 -149.31
REMARK 500 THR A 198 94.63 63.30
REMARK 500 LYS A 288 -114.46 62.71
REMARK 500 ASN A 296 30.91 -141.15
REMARK 500 THR A 318 -4.68 -49.39
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 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
DBREF 1H09 A 2 339 UNP P15057 LYCA_BPCP1 2 339
SEQRES 1 A 338 VAL LYS LYS ASN ASP LEU PHE VAL ASP VAL SER SER HIS
SEQRES 2 A 338 ASN GLY TYR ASP ILE THR GLY ILE LEU GLU GLN MET GLY
SEQRES 3 A 338 THR THR ASN THR ILE ILE LYS ILE SER GLU SER THR THR
SEQRES 4 A 338 TYR LEU ASN PRO CYS LEU SER ALA GLN VAL GLU GLN SER
SEQRES 5 A 338 ASN PRO ILE GLY PHE TYR HIS PHE ALA ARG PHE GLY GLY
SEQRES 6 A 338 ASP VAL ALA GLU ALA GLU ARG GLU ALA GLN PHE PHE LEU
SEQRES 7 A 338 ASP ASN VAL PRO MET GLN VAL LYS TYR LEU VAL LEU ASP
SEQRES 8 A 338 TYR GLU ASP ASP PRO SER GLY ASP ALA GLN ALA ASN THR
SEQRES 9 A 338 ASN ALA CYS LEU ARG PHE MET GLN MET ILE ALA ASP ALA
SEQRES 10 A 338 GLY TYR LYS PRO ILE TYR TYR SER TYR LYS PRO PHE THR
SEQRES 11 A 338 HIS ASP ASN VAL ASP TYR GLN GLN ILE LEU ALA GLN PHE
SEQRES 12 A 338 PRO ASN SER LEU TRP ILE ALA GLY TYR GLY LEU ASN ASP
SEQRES 13 A 338 GLY THR ALA ASN PHE GLU TYR PHE PRO SER MET ASP GLY
SEQRES 14 A 338 ILE ARG TRP TRP GLN TYR SER SER ASN PRO PHE ASP LYS
SEQRES 15 A 338 ASN ILE VAL LEU LEU ASP ASP GLU GLU ASP ASP LYS PRO
SEQRES 16 A 338 LYS THR ALA GLY THR TRP LYS GLN ASP SER LYS GLY TRP
SEQRES 17 A 338 TRP PHE ARG ARG ASN ASN GLY SER PHE PRO TYR ASN LYS
SEQRES 18 A 338 TRP GLU LYS ILE GLY GLY VAL TRP TYR TYR PHE ASP SER
SEQRES 19 A 338 LYS GLY TYR CYS LEU THR SER GLU TRP LEU LYS ASP ASN
SEQRES 20 A 338 GLU LYS TRP TYR TYR LEU LYS ASP ASN GLY ALA MET ALA
SEQRES 21 A 338 THR GLY TRP VAL LEU VAL GLY SER GLU TRP TYR TYR MET
SEQRES 22 A 338 ASP ASP SER GLY ALA MET VAL THR GLY TRP VAL LYS TYR
SEQRES 23 A 338 LYS ASN ASN TRP TYR TYR MET THR ASN GLU ARG GLY ASN
SEQRES 24 A 338 MET VAL SER ASN GLU PHE ILE LYS SER GLY LYS GLY TRP
SEQRES 25 A 338 TYR PHE MET ASN THR ASN GLY GLU LEU ALA ASP ASN PRO
SEQRES 26 A 338 SER PHE THR LYS GLU PRO ASP GLY LEU ILE THR VAL ALA
FORMUL 2 HOH *326(H2 O1)
HELIX 1 1 SER A 12 GLY A 16 5 5
HELIX 2 2 ILE A 19 GLY A 27 1 9
HELIX 3 3 CYS A 45 GLN A 52 1 8
HELIX 4 4 ASP A 67 ASN A 81 1 15
HELIX 5 5 ASP A 100 ALA A 118 1 19
HELIX 6 6 LYS A 128 VAL A 135 1 8
HELIX 7 7 ASP A 136 PHE A 144 1 9
HELIX 8 8 ASN A 161 PHE A 165 5 5
HELIX 9 9 ASN A 296 ASN A 300 5 5
SHEET 1 AA11 LEU A 7 VAL A 11 0
SHEET 2 AA11 LYS A 183 VAL A 186 -1 O ASN A 184 N PHE A 8
SHEET 3 AA11 ILE A 171 SER A 177 -1 O TRP A 174 N ILE A 185
SHEET 4 AA11 LEU A 148 ALA A 151 1 O LEU A 148 N ARG A 172
SHEET 5 AA11 LYS A 121 TYR A 127 1 O TYR A 124 N TRP A 149
SHEET 6 AA11 TYR A 88 ASP A 92 1 O LEU A 89 N ILE A 123
SHEET 7 AA11 ASN A 54 PHE A 61 1 O ILE A 56 N TYR A 88
SHEET 8 AA11 ASN A 30 GLU A 37 4 O THR A 31 N ILE A 56
SHEET 9 AA11 LEU A 7 VAL A 11 1 O VAL A 9 N ILE A 32
SHEET 10 AA11 LYS A 183 VAL A 186 -1 O ASN A 184 N PHE A 8
SHEET 11 AA11 LEU A 7 VAL A 11 -1 O PHE A 8 N ASN A 184
SHEET 1 AB 2 GLY A 200 ASP A 205 0
SHEET 2 AB 2 GLY A 208 ARG A 213 -1 O GLY A 208 N ASP A 205
SHEET 1 AC 2 LYS A 222 ILE A 226 0
SHEET 2 AC 2 VAL A 229 PHE A 233 -1 O VAL A 229 N ILE A 226
SHEET 1 AD 2 GLU A 243 LYS A 246 0
SHEET 2 AD 2 TRP A 251 LEU A 254 -1 O TYR A 252 N LEU A 245
SHEET 1 AE 2 GLY A 263 VAL A 267 0
SHEET 2 AE 2 GLU A 270 MET A 274 -1 O GLU A 270 N VAL A 267
SHEET 1 AF 6 GLU A 321 LEU A 322 0
SHEET 2 AF 6 GLY A 312 ASN A 317 -1 O ASN A 317 N GLU A 321
SHEET 3 AF 6 VAL A 302 SER A 309 -1 O GLU A 305 N MET A 316
SHEET 4 AF 6 ASN A 290 THR A 295 -1 O TRP A 291 N PHE A 306
SHEET 5 AF 6 GLY A 283 TYR A 287 -1 O GLY A 283 N MET A 294
SHEET 6 AF 6 LEU A 335 THR A 337 1 O LEU A 335 N LYS A 286
CISPEP 1 ASN A 179 PRO A 180 0 0.08
CRYST1 77.950 95.780 129.280 90.00 90.00 90.00 C 2 2 21 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 0.012829 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010440 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007735 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
