HEADER HYDROLASE 12-JUN-07 2Q93
TITLE E. COLI METHIONINE AMINOPEPTIDASE MN-FORM WITH INHIBITOR B21
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHIONINE AMINOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MAP, PEPTIDASE M;
COMPND 5 EC: 3.4.11.18;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: MAP;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEMEX-1
KEYWDS AMINOPEPTIDASE, HYDROLASE, DINUCLEAR, MN(II)-FORM, ENZYME-INHIBITOR
KEYWDS 2 COMPLEX, METALLOENZYME
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.-Z.YE
REVDAT 3 30-AUG-23 2Q93 1 REMARK LINK
REVDAT 2 24-FEB-09 2Q93 1 VERSN
REVDAT 1 01-JAN-08 2Q93 0
JRNL AUTH Z.Q.MA,S.X.XIE,Q.Q.HUANG,F.J.NAN,T.D.HURLEY,Q.Z.YE
JRNL TITL STRUCTURAL ANALYSIS OF INHIBITION OF E. COLI METHIONINE
JRNL TITL 2 AMINOPEPTIDASE: IMPLICATION OF LOOP FLEXIBILITY IN SELECTIVE
JRNL TITL 3 INHIBITION OF BACTERIAL ENZYMES.
JRNL REF BMC STRUCT.BIOL. V. 7 84 2007
JRNL REFN ESSN 1472-6807
JRNL PMID 18093325
JRNL DOI 10.1186/1472-6807-7-84
REMARK 2
REMARK 2 RESOLUTION. 1.60 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.9
REMARK 3 NUMBER OF REFLECTIONS : 29277
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) : 0.226
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.300
REMARK 3 FREE R VALUE TEST SET COUNT : 2918
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 : 50
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.61
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 443
REMARK 3 BIN R VALUE (WORKING SET) : 0.5170
REMARK 3 BIN FREE R VALUE : 0.5290
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 70
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 : 2044
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 224
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.50200
REMARK 3 B22 (A**2) : -0.30700
REMARK 3 B33 (A**2) : -0.19500
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.24600
REMARK 3 B23 (A**2) : 0.00000
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) : 0.005
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) : 1.007 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.372 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.895 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.649 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 28.63
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : YE2.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : CNS_TOPPAR:PROTEIN_1.TOP
REMARK 3 TOPOLOGY FILE 2 : CNS_TOPPAR:DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : CNS_TOPPAR:WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : CNS_TOPPAR:ION.TOP
REMARK 3 TOPOLOGY FILE 5 : YE2.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2Q93 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000043303.
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 : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29294
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 19.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.2
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.03000
REMARK 200 R SYM (I) : 0.03000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.09900
REMARK 200 R SYM FOR SHELL (I) : 0.09900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.700
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: 1XNZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-15% PEG 20000, 0.1 M MES (PH 6.5),
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
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
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 31.17000
REMARK 290 SMTRY3 2 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 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: 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 ASN A 74 -103.23 44.82
REMARK 500 HIS A 185 33.69 -97.49
REMARK 500 ASN A 192 74.01 -153.10
REMARK 500 GLU A 204 66.88 -152.89
REMARK 500 TRP A 221 -51.36 -133.88
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 A 500 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 74 O
REMARK 620 2 VAL A 76 O 101.8
REMARK 620 3 SER A 231 O 92.0 126.5
REMARK 620 4 HOH A 517 O 142.7 106.4 90.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 302 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 97 OD1
REMARK 620 2 ASP A 97 OD2 55.5
REMARK 620 3 ASP A 108 OD1 108.5 163.3
REMARK 620 4 GLU A 235 OE1 86.0 93.8 89.2
REMARK 620 5 B21 A 400 OAN 142.7 87.3 108.2 101.2
REMARK 620 6 HOH A 505 O 87.4 86.8 87.8 171.4 87.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 301 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 108 OD2
REMARK 620 2 GLU A 204 OE2 148.8
REMARK 620 3 GLU A 235 OE2 82.0 79.8
REMARK 620 4 B21 A 400 OAO 106.0 102.6 149.0
REMARK 620 5 B21 A 400 OAN 91.1 115.1 93.5 57.1
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B21 A 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XNZ RELATED DB: PDB
REMARK 900 E. COLI METHIONINE AMINOPEPTIDASE MN(II) FORM IN COMPLEX WITH 5-(2-
REMARK 900 CHLOROPHENYL)FURAN-2-CARBOXYLIC ACID
REMARK 900 RELATED ID: 2GTX RELATED DB: PDB
REMARK 900 E. COLI MONONUCLEAR METHIONINE AMINOPEPTIDASE CATALYSIS
REMARK 900 RELATED ID: 2EVM RELATED DB: PDB
REMARK 900 E. COLI METHIONINE AMINOPEPTIDASE IN COMPLEX WITH 5-(2,5-
REMARK 900 DICHLOROPHENYL)FURAN-2-CARBOXYLIC ACID
REMARK 900 RELATED ID: 2EVC RELATED DB: PDB
REMARK 900 E. COLI METHIONINE AMINOPEPTIDASE IN COMPLEX WITH 5-(2-
REMARK 900 (TRIFLUOROMETHYL)PHENYL)FURAN-2-CARBOXYLIC ACID
REMARK 900 RELATED ID: 2Q92 RELATED DB: PDB
REMARK 900 E. COLI METHIONINE AMINOPEPTIDASE MN-FORM WITH INHIBITOR 5-(2-
REMARK 900 NITROPHENYL)-2-FUROIC ACID
REMARK 900 RELATED ID: 2Q94 RELATED DB: PDB
REMARK 900 E. COLI METHIONINE AMINOPEPTIDASE MN-FORM WITH INHIBITOR 5-[2-
REMARK 900 (TRIFLUOROMETHOXY)PHENYL]-2-FUROIC ACID
REMARK 900 RELATED ID: 2Q95 RELATED DB: PDB
REMARK 900 E. COLI METHIONINE AMINOPEPTIDASE MN-FORM WITH INHIBITOR 5-(2-
REMARK 900 CHLORO-4-NITROPHENYL)-2-FUROIC ACID
REMARK 900 RELATED ID: 2Q96 RELATED DB: PDB
REMARK 900 E. COLI METHIONINE AMINOPEPTIDASE MN-FORM WITH INHIBITOR 5-(2-
REMARK 900 CHLOROBENZYL)-2-FUROIC ACID
DBREF 2Q93 A 2 264 UNP P0AE18 AMPM_ECOLI 2 264
SEQRES 1 A 263 ALA ILE SER ILE LYS THR PRO GLU ASP ILE GLU LYS MET
SEQRES 2 A 263 ARG VAL ALA GLY ARG LEU ALA ALA GLU VAL LEU GLU MET
SEQRES 3 A 263 ILE GLU PRO TYR VAL LYS PRO GLY VAL SER THR GLY GLU
SEQRES 4 A 263 LEU ASP ARG ILE CYS ASN ASP TYR ILE VAL ASN GLU GLN
SEQRES 5 A 263 HIS ALA VAL SER ALA CYS LEU GLY TYR HIS GLY TYR PRO
SEQRES 6 A 263 LYS SER VAL CYS ILE SER ILE ASN GLU VAL VAL CYS HIS
SEQRES 7 A 263 GLY ILE PRO ASP ASP ALA LYS LEU LEU LYS ASP GLY ASP
SEQRES 8 A 263 ILE VAL ASN ILE ASP VAL THR VAL ILE LYS ASP GLY PHE
SEQRES 9 A 263 HIS GLY ASP THR SER LYS MET PHE ILE VAL GLY LYS PRO
SEQRES 10 A 263 THR ILE MET GLY GLU ARG LEU CYS ARG ILE THR GLN GLU
SEQRES 11 A 263 SER LEU TYR LEU ALA LEU ARG MET VAL LYS PRO GLY ILE
SEQRES 12 A 263 ASN LEU ARG GLU ILE GLY ALA ALA ILE GLN LYS PHE VAL
SEQRES 13 A 263 GLU ALA GLU GLY PHE SER VAL VAL ARG GLU TYR CYS GLY
SEQRES 14 A 263 HIS GLY ILE GLY ARG GLY PHE HIS GLU GLU PRO GLN VAL
SEQRES 15 A 263 LEU HIS TYR ASP SER ARG GLU THR ASN VAL VAL LEU LYS
SEQRES 16 A 263 PRO GLY MET THR PHE THR ILE GLU PRO MET VAL ASN ALA
SEQRES 17 A 263 GLY LYS LYS GLU ILE ARG THR MET LYS ASP GLY TRP THR
SEQRES 18 A 263 VAL LYS THR LYS ASP ARG SER LEU SER ALA GLN TYR GLU
SEQRES 19 A 263 HIS THR ILE VAL VAL THR ASP ASN GLY CYS GLU ILE LEU
SEQRES 20 A 263 THR LEU ARG LYS ASP ASP THR ILE PRO ALA ILE ILE SER
SEQRES 21 A 263 HIS ASP GLU
HET MN A 301 1
HET MN A 302 1
HET NA A 500 1
HET B21 A 400 16
HETNAM MN MANGANESE (II) ION
HETNAM NA SODIUM ION
HETNAM B21 5-(2-METHOXYPHENYL)-2-FUROIC ACID
FORMUL 2 MN 2(MN 2+)
FORMUL 4 NA NA 1+
FORMUL 5 B21 C12 H10 O4
FORMUL 6 HOH *224(H2 O)
HELIX 1 1 THR A 7 GLU A 29 1 23
HELIX 2 2 PRO A 30 VAL A 32 5 3
HELIX 3 3 SER A 37 GLU A 52 1 16
HELIX 4 4 GLY A 61 TYR A 65 5 5
HELIX 5 5 THR A 119 ARG A 138 1 20
HELIX 6 6 ASN A 145 GLU A 160 1 16
SHEET 1 A 3 VAL A 56 SER A 57 0
SHEET 2 A 3 ILE A 93 LYS A 102 -1 O ILE A 101 N VAL A 56
SHEET 3 A 3 CYS A 70 ILE A 73 -1 N SER A 72 O ASN A 95
SHEET 1 B 3 VAL A 56 SER A 57 0
SHEET 2 B 3 ILE A 93 LYS A 102 -1 O ILE A 101 N VAL A 56
SHEET 3 B 3 PHE A 105 ILE A 114 -1 O THR A 109 N VAL A 98
SHEET 1 C 3 VAL A 76 CYS A 78 0
SHEET 2 C 3 VAL A 223 THR A 225 -1 O VAL A 223 N VAL A 77
SHEET 3 C 3 ILE A 214 THR A 216 -1 N ARG A 215 O LYS A 224
SHEET 1 D 3 SER A 163 VAL A 164 0
SHEET 2 D 3 MET A 206 ASN A 208 -1 O ASN A 208 N SER A 163
SHEET 3 D 3 SER A 231 GLN A 233 -1 O ALA A 232 N VAL A 207
SHEET 1 E 2 GLY A 170 GLY A 172 0
SHEET 2 E 2 GLU A 179 VAL A 183 -1 O VAL A 183 N GLY A 170
SHEET 1 F 4 THR A 200 ILE A 203 0
SHEET 2 F 4 HIS A 236 VAL A 240 -1 O ILE A 238 N PHE A 201
SHEET 3 F 4 GLY A 244 ILE A 247 -1 O GLU A 246 N VAL A 239
SHEET 4 F 4 ILE A 259 SER A 261 -1 O ILE A 260 N CYS A 245
LINK O ASN A 74 NA NA A 500 1555 1555 2.37
LINK O VAL A 76 NA NA A 500 1555 1555 2.37
LINK OD1 ASP A 97 MN MN A 302 1555 1555 2.17
LINK OD2 ASP A 97 MN MN A 302 1555 1555 2.49
LINK OD2 ASP A 108 MN MN A 301 1555 1555 2.20
LINK OD1 ASP A 108 MN MN A 302 1555 1555 2.15
LINK OE2 GLU A 204 MN MN A 301 1555 1555 2.24
LINK O SER A 231 NA NA A 500 1555 1555 2.42
LINK OE2 GLU A 235 MN MN A 301 1555 1555 2.18
LINK OE1 GLU A 235 MN MN A 302 1555 1555 2.08
LINK MN MN A 301 OAO B21 A 400 1555 1555 2.26
LINK MN MN A 301 OAN B21 A 400 1555 1555 2.37
LINK MN MN A 302 OAN B21 A 400 1555 1555 2.07
LINK MN MN A 302 O HOH A 505 1555 1555 2.28
LINK NA NA A 500 O HOH A 517 1555 1555 2.44
CISPEP 1 GLU A 180 PRO A 181 0 -0.06
SITE 1 AC1 6 ASP A 108 HIS A 171 GLU A 204 GLU A 235
SITE 2 AC1 6 MN A 302 B21 A 400
SITE 1 AC2 6 ASP A 97 ASP A 108 GLU A 235 MN A 301
SITE 2 AC2 6 B21 A 400 HOH A 505
SITE 1 AC3 4 ASN A 74 VAL A 76 SER A 231 HOH A 517
SITE 1 AC4 13 TYR A 62 TYR A 65 HIS A 79 ASP A 97
SITE 2 AC4 13 ASP A 108 HIS A 171 HIS A 178 GLU A 204
SITE 3 AC4 13 TRP A 221 GLU A 235 MN A 301 MN A 302
SITE 4 AC4 13 HOH A 505
CRYST1 39.107 62.340 52.441 90.00 108.80 90.00 P 1 21 1 2
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 0.025571 0.000000 0.008705 0.00000
SCALE2 0.000000 0.016041 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020144 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
