HEADER HYDROLASE 04-SEP-02 1IYQ
TITLE TOHO-1 BETA-LACTAMASE IN COMPLEX WITH BENZYLPENICILLIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOHO-1 BETA-LACTAMASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.5.2.6;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PUC119
KEYWDS BETA-LACTAMASE, ACYL-ENZYME, COMPLEX, BENZYLPENICILLIN, PENICILLIN G,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.SHIMAMURA,A.IBUKA,S.FUSHINOBU,T.WAKAGI,M.ISHIGURO,Y.ISHII,
AUTHOR 2 H.MATSUZAWA
REVDAT 4 27-DEC-23 1IYQ 1 REMARK
REVDAT 3 10-NOV-21 1IYQ 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1IYQ 1 VERSN
REVDAT 1 11-DEC-02 1IYQ 0
JRNL AUTH T.SHIMAMURA,A.IBUKA,S.FUSHINOBU,T.WAKAGI,M.ISHIGURO,Y.ISHII,
JRNL AUTH 2 H.MATSUZAWA
JRNL TITL ACYL-INTERMEDIATE STRUCTURES OF THE EXTENDED-SPECTRUM CLASS
JRNL TITL 2 A BETA -LACTAMASE, TOHO-1, IN COMPLEX WITH CEFOTAXIME,
JRNL TITL 3 CEPHALOTHIN, AND BENZYLPENICILLIN.
JRNL REF J.BIOL.CHEM. V. 277 46601 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12221102
JRNL DOI 10.1074/JBC.M207884200
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
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 : 17074
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.227
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 : 1975
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 155
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 1IYQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-SEP-02.
REMARK 100 THE DEPOSITION ID IS D_1000005416.
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 : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26625
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.100
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.12800
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.31133
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.15567
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 33.15567
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 66.31133
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 26
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 PRO A 177 C - N - CA ANGL. DEV. = 9.2 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 CYS A 69 -145.32 56.72
REMARK 500 LEU A 90 -72.20 -35.57
REMARK 500 VAL A 103 -142.87 -121.98
REMARK 500 LYS A 111 -18.81 -49.18
REMARK 500 ASN A 114 -4.58 89.78
REMARK 500 SER A 220 -129.52 -90.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PNM A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IYO RELATED DB: PDB
REMARK 900 1IYO CONTAINS CRYSTAL STRUCTURE OF THE SAME PROTEIN COMPLEXED WITH
REMARK 900 CEF AND SO4
REMARK 900 RELATED ID: 1IYP RELATED DB: PDB
REMARK 900 1IYP CONTAINS CRYSTAL STRUCTURE OF THE SAME PROTEIN COMPLEXED WITH
REMARK 900 CEP AND SO4
DBREF 1IYQ A 26 290 UNP Q47066 BLT1_ECOLI 30 291
SEQADV 1IYQ ALA A 166 UNP Q47066 GLU 169 ENGINEERED MUTATION
SEQRES 1 A 262 ALA ASN SER VAL GLN GLN GLN LEU GLU ALA LEU GLU LYS
SEQRES 2 A 262 SER SER GLY GLY ARG LEU GLY VAL ALA LEU ILE ASN THR
SEQRES 3 A 262 ALA ASP ASN SER GLN ILE LEU TYR ARG ALA ASP GLU ARG
SEQRES 4 A 262 PHE ALA MET CYS SER THR SER LYS VAL MET ALA ALA ALA
SEQRES 5 A 262 ALA VAL LEU LYS GLN SER GLU SER ASP LYS HIS LEU LEU
SEQRES 6 A 262 ASN GLN ARG VAL GLU ILE LYS LYS SER ASP LEU VAL ASN
SEQRES 7 A 262 TYR ASN PRO ILE ALA GLU LYS HIS VAL ASN GLY THR MET
SEQRES 8 A 262 THR LEU ALA GLU LEU GLY ALA ALA ALA LEU GLN TYR SER
SEQRES 9 A 262 ASP ASN THR ALA MET ASN LYS LEU ILE ALA HIS LEU GLY
SEQRES 10 A 262 GLY PRO ASP LYS VAL THR ALA PHE ALA ARG SER LEU GLY
SEQRES 11 A 262 ASP GLU THR PHE ARG LEU ASP ARG THR ALA PRO THR LEU
SEQRES 12 A 262 ASN THR ALA ILE PRO GLY ASP PRO ARG ASP THR THR THR
SEQRES 13 A 262 PRO LEU ALA MET ALA GLN THR LEU LYS ASN LEU THR LEU
SEQRES 14 A 262 GLY LYS ALA LEU ALA GLU THR GLN ARG ALA GLN LEU VAL
SEQRES 15 A 262 THR TRP LEU LYS GLY ASN THR THR GLY SER ALA SER ILE
SEQRES 16 A 262 ARG ALA GLY LEU PRO LYS SER TRP VAL VAL GLY ASP LYS
SEQRES 17 A 262 THR GLY SER GLY ASP TYR GLY THR THR ASN ASP ILE ALA
SEQRES 18 A 262 VAL ILE TRP PRO GLU ASN HIS ALA PRO LEU VAL LEU VAL
SEQRES 19 A 262 THR TYR PHE THR GLN PRO GLU GLN LYS ALA GLU ARG ARG
SEQRES 20 A 262 ARG ASP ILE LEU ALA ALA ALA ALA LYS ILE VAL THR HIS
SEQRES 21 A 262 GLY PHE
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 A 403 5
HET PNM A 301 23
HETNAM SO4 SULFATE ION
HETNAM PNM OPEN FORM - PENICILLIN G
FORMUL 2 SO4 3(O4 S 2-)
FORMUL 5 PNM C16 H20 N2 O4 S
FORMUL 6 HOH *155(H2 O)
HELIX 1 1 SER A 28 GLY A 41 1 14
HELIX 2 2 CYS A 69 THR A 71 5 3
HELIX 3 3 SER A 72 GLU A 85 1 14
HELIX 4 4 HIS A 89 ASN A 92 5 4
HELIX 5 5 ALA A 109 VAL A 113 5 5
HELIX 6 6 LEU A 119 TYR A 129 1 11
HELIX 7 7 ASP A 131 GLY A 143 1 13
HELIX 8 8 GLY A 144 LEU A 155 1 12
HELIX 9 9 PRO A 167 THR A 171 5 5
HELIX 10 10 THR A 182 LEU A 195 1 14
HELIX 11 11 ALA A 200 GLY A 213 1 14
HELIX 12 12 SER A 220 LEU A 225 5 6
HELIX 13 13 ARG A 275 HIS A 288 1 14
SHEET 1 A 5 GLN A 56 TYR A 60 0
SHEET 2 A 5 ARG A 43 ASN A 50 -1 N VAL A 46 O TYR A 60
SHEET 3 A 5 LEU A 259 THR A 266 -1 O TYR A 264 N GLY A 45
SHEET 4 A 5 THR A 243 TRP A 251 -1 N ILE A 250 O LEU A 259
SHEET 5 A 5 VAL A 230 GLY A 238 -1 N VAL A 230 O TRP A 251
SHEET 1 B 2 PHE A 66 ALA A 67 0
SHEET 2 B 2 THR A 180 THR A 181 -1 O THR A 181 N PHE A 66
SHEET 1 C 2 ARG A 94 ILE A 97 0
SHEET 2 C 2 GLY A 115 THR A 118 -1 O MET A 117 N VAL A 95
LINK OG SER A 70 C7 PNM A 301 1555 1555 1.37
CISPEP 1 ALA A 166 PRO A 167 0 -0.08
SITE 1 AC1 4 LYS A 197 GLU A 273 ARG A 274 HOH A 596
SITE 1 AC2 10 LYS A 82 ARG A 274 ARG A 275 ARG A 276
SITE 2 AC2 10 ASP A 277 HOH A 543 HOH A 551 HOH A 565
SITE 3 AC2 10 HOH A 611 HOH A 637
SITE 1 AC3 7 TRP A 229 PRO A 252 GLU A 254 ASN A 255
SITE 2 AC3 7 HIS A 256 PHE A 290 HOH A 654
SITE 1 AC4 12 CYS A 69 SER A 70 ASN A 104 TYR A 105
SITE 2 AC4 12 SER A 130 ASN A 132 ASN A 170 LYS A 234
SITE 3 AC4 12 THR A 235 GLY A 236 SER A 237 HOH A 552
CRYST1 72.799 72.799 99.467 90.00 90.00 120.00 P 32 2 1 6
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 0.013736 0.007931 0.000000 0.00000
SCALE2 0.000000 0.015861 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010054 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
