HEADER ISOMERASE 03-FEB-07 2JFP
TITLE CRYSTAL STRUCTURE OF ENTEROCOCCUS FAECALIS GLUTAMATE RACEMASE IN
TITLE 2 COMPLEX WITH D- GLUTAMATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RACEMASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 5.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS FAECALIS;
SOURCE 3 ORGANISM_TAXID: 1351;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLUTAMATE RACEMASE, PEPTIDOGLYCAN BIOSYNTHESIS, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.LUNDQVIST
REVDAT 4 13-DEC-23 2JFP 1 LINK
REVDAT 3 17-JAN-18 2JFP 1 REMARK
REVDAT 2 24-FEB-09 2JFP 1 VERSN
REVDAT 1 03-JUL-07 2JFP 0
JRNL AUTH T.LUNDQVIST,S.L.FISHER,G.KERN,R.H.A.FOLMER,Y.XUE,D.T.NEWTON,
JRNL AUTH 2 T.A.KEATING,R.A.ALM,B.L.M.DE JONGE
JRNL TITL EXPLOITATION OF STRUCTURAL AND REGULATORY DIVERSITY IN
JRNL TITL 2 GLUTAMATE RACEMASES
JRNL REF NATURE V. 447 817 2007
JRNL REFN ISSN 0028-0836
JRNL PMID 17568739
JRNL DOI 10.1038/NATURE05689
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2002.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 35820
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 + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1793
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 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 : 4040
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 503
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.87200
REMARK 3 B22 (A**2) : 2.34300
REMARK 3 B33 (A**2) : 2.52900
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 8.61300
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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.272
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 : 0.41
REMARK 3 BSOL : 46.20
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 2JFP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1290031342.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAY-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.089
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36578
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 34.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.25000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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: PDB ENTRY 2JFO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN FORMULATED AT 10 MG/ML WITH
REMARK 280 200MM AMMONIUM ACETATE PH 7.4, 5MM D-L GLUTAMATE, 1 MM TCEP AND
REMARK 280 CRYSTALLISED WITH 0.1 M TRIS PH 7.5 0.2 MM CACL2 AND 20-25% PEG
REMARK 280 3350, PH 7.50
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 37.33500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ASN A 270
REMARK 465 GLU A 271
REMARK 465 ASN A 272
REMARK 465 ASP A 273
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ASN B 270
REMARK 465 GLU B 271
REMARK 465 ASN B 272
REMARK 465 ASP B 273
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLY A 269 CA C O
REMARK 470 GLY B 269 CA C O
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 ALA A 73 46.88 -76.09
REMARK 500 ALA B 73 48.59 -79.13
REMARK 500 ALA B 125 15.36 59.77
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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2037 DISTANCE = 6.48 ANGSTROMS
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 CA A1271 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 119 N
REMARK 620 2 HOH A2050 O 137.6
REMARK 620 3 HOH A2242 O 128.9 92.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1271 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU B 119 N
REMARK 620 2 HOH B2068 O 139.7
REMARK 620 3 HOH B2261 O 128.2 91.0
REMARK 620 N 1 2
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGL A1270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGL B1270
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2JFN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E. COLI GLUTAMATE RACEMASE IN COMPLEX WITH L-
REMARK 900 GLUTAMATE AND ACTIVATOR UDP-MURNAC-ALA
REMARK 900 RELATED ID: 2JFO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E. FAECALIS GLUTAMATE RACEMASE IN COMPLEX WITH
REMARK 900 D- AND L- GLUTAMATE
REMARK 900 RELATED ID: 2JFQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S. AUREUS GLUTAMATE RACEMASE IN COMPLEX WITH D-
REMARK 900 GLUTAMATE
REMARK 900 RELATED ID: 2JFU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E. FAECIUM GLUTAMATE RACEMASE IN COMPLEX WITH
REMARK 900 PHOSPHATE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 DATABASE REFERENCE GENESEQP ADR04180 (PATENT DATABASE).
REMARK 999 CLOSEST PUBLIC REFERENCE IS GENPEPT NP_814851 HAS 2
REMARK 999 DIFFERENCES AT RESIDUE 157 AND 164 (THR AND ASP IN
REMARK 999 NP_814851). THESE ARE TRUE DIFFERENCES CORRESPONDING TO
REMARK 999 DIFFERENCES BETWEEN DIFFERENT STRAINS OF THE BACTERIA
DBREF 2JFP A -19 0 PDB 2JFP 2JFP -19 0
DBREF 2JFP A 1 273 UNP Q836J0 Q836J0_ENTFA 1 273
DBREF 2JFP B -19 0 PDB 2JFP 2JFP -19 0
DBREF 2JFP B 1 273 UNP Q836J0 Q836J0_ENTFA 1 273
SEQADV 2JFP ALA A 144 UNP Q836J0 ASP 144 CONFLICT
SEQADV 2JFP ALA B 144 UNP Q836J0 ASP 144 CONFLICT
SEQADV 2JFP ALA A 137 UNP Q836J0 THR 137 CONFLICT
SEQADV 2JFP ALA B 137 UNP Q836J0 THR 137 CONFLICT
SEQRES 1 A 293 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 293 LEU VAL PRO ARG GLY SER HIS MET SER ASN GLN GLU ALA
SEQRES 3 A 293 ILE GLY LEU ILE ASP SER GLY VAL GLY GLY LEU THR VAL
SEQRES 4 A 293 LEU LYS GLU ALA LEU LYS GLN LEU PRO ASN GLU ARG LEU
SEQRES 5 A 293 ILE TYR LEU GLY ASP THR ALA ARG CYS PRO TYR GLY PRO
SEQRES 6 A 293 ARG PRO ALA GLU GLN VAL VAL GLN PHE THR TRP GLU MET
SEQRES 7 A 293 ALA ASP PHE LEU LEU LYS LYS ARG ILE LYS MET LEU VAL
SEQRES 8 A 293 ILE ALA CYS ASN THR ALA THR ALA VAL ALA LEU GLU GLU
SEQRES 9 A 293 ILE LYS ALA ALA LEU PRO ILE PRO VAL VAL GLY VAL ILE
SEQRES 10 A 293 LEU PRO GLY ALA ARG ALA ALA VAL LYS VAL THR LYS ASN
SEQRES 11 A 293 ASN LYS ILE GLY VAL ILE GLY THR LEU GLY THR ILE LYS
SEQRES 12 A 293 SER ALA SER TYR GLU ILE ALA ILE LYS SER LYS ALA PRO
SEQRES 13 A 293 ALA ILE GLU VAL THR SER LEU ALA CYS PRO LYS PHE VAL
SEQRES 14 A 293 PRO ILE VAL GLU SER ASN GLN TYR ARG SER SER VAL ALA
SEQRES 15 A 293 LYS LYS ILE VAL ALA GLU THR LEU GLN ALA LEU GLN LEU
SEQRES 16 A 293 LYS GLY LEU ASP THR LEU ILE LEU GLY CYS THR HIS TYR
SEQRES 17 A 293 PRO LEU LEU ARG PRO VAL ILE GLN ASN VAL MET GLY SER
SEQRES 18 A 293 HIS VAL THR LEU ILE ASP SER GLY ALA GLU THR VAL GLY
SEQRES 19 A 293 GLU VAL SER MET LEU LEU ASP TYR PHE ASP ILE ALA HIS
SEQRES 20 A 293 THR PRO GLU ALA PRO THR GLN PRO HIS GLU PHE TYR THR
SEQRES 21 A 293 THR GLY SER ALA LYS MET PHE GLU GLU ILE ALA SER SER
SEQRES 22 A 293 TRP LEU GLY ILE GLU ASN LEU LYS ALA GLN GLN ILE HIS
SEQRES 23 A 293 LEU GLY GLY ASN GLU ASN ASP
SEQRES 1 B 293 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 293 LEU VAL PRO ARG GLY SER HIS MET SER ASN GLN GLU ALA
SEQRES 3 B 293 ILE GLY LEU ILE ASP SER GLY VAL GLY GLY LEU THR VAL
SEQRES 4 B 293 LEU LYS GLU ALA LEU LYS GLN LEU PRO ASN GLU ARG LEU
SEQRES 5 B 293 ILE TYR LEU GLY ASP THR ALA ARG CYS PRO TYR GLY PRO
SEQRES 6 B 293 ARG PRO ALA GLU GLN VAL VAL GLN PHE THR TRP GLU MET
SEQRES 7 B 293 ALA ASP PHE LEU LEU LYS LYS ARG ILE LYS MET LEU VAL
SEQRES 8 B 293 ILE ALA CYS ASN THR ALA THR ALA VAL ALA LEU GLU GLU
SEQRES 9 B 293 ILE LYS ALA ALA LEU PRO ILE PRO VAL VAL GLY VAL ILE
SEQRES 10 B 293 LEU PRO GLY ALA ARG ALA ALA VAL LYS VAL THR LYS ASN
SEQRES 11 B 293 ASN LYS ILE GLY VAL ILE GLY THR LEU GLY THR ILE LYS
SEQRES 12 B 293 SER ALA SER TYR GLU ILE ALA ILE LYS SER LYS ALA PRO
SEQRES 13 B 293 ALA ILE GLU VAL THR SER LEU ALA CYS PRO LYS PHE VAL
SEQRES 14 B 293 PRO ILE VAL GLU SER ASN GLN TYR ARG SER SER VAL ALA
SEQRES 15 B 293 LYS LYS ILE VAL ALA GLU THR LEU GLN ALA LEU GLN LEU
SEQRES 16 B 293 LYS GLY LEU ASP THR LEU ILE LEU GLY CYS THR HIS TYR
SEQRES 17 B 293 PRO LEU LEU ARG PRO VAL ILE GLN ASN VAL MET GLY SER
SEQRES 18 B 293 HIS VAL THR LEU ILE ASP SER GLY ALA GLU THR VAL GLY
SEQRES 19 B 293 GLU VAL SER MET LEU LEU ASP TYR PHE ASP ILE ALA HIS
SEQRES 20 B 293 THR PRO GLU ALA PRO THR GLN PRO HIS GLU PHE TYR THR
SEQRES 21 B 293 THR GLY SER ALA LYS MET PHE GLU GLU ILE ALA SER SER
SEQRES 22 B 293 TRP LEU GLY ILE GLU ASN LEU LYS ALA GLN GLN ILE HIS
SEQRES 23 B 293 LEU GLY GLY ASN GLU ASN ASP
HET DGL A1270 10
HET CA A1271 1
HET DGL B1270 10
HET CA B1271 1
HETNAM DGL D-GLUTAMIC ACID
HETNAM CA CALCIUM ION
FORMUL 3 DGL 2(C5 H9 N O4)
FORMUL 4 CA 2(CA 2+)
FORMUL 7 HOH *503(H2 O)
HELIX 1 1 GLY A 16 LEU A 27 1 12
HELIX 2 2 THR A 38 CYS A 41 5 4
HELIX 3 3 PRO A 47 LYS A 64 1 18
HELIX 4 4 CYS A 74 LEU A 89 1 16
HELIX 5 5 VAL A 96 THR A 108 1 13
HELIX 6 6 THR A 118 ALA A 125 1 8
HELIX 7 7 ALA A 125 SER A 133 1 9
HELIX 8 8 LYS A 147 SER A 154 1 8
HELIX 9 9 SER A 159 LEU A 170 1 12
HELIX 10 10 GLN A 171 GLN A 174 5 4
HELIX 11 11 HIS A 187 LEU A 190 5 4
HELIX 12 12 LEU A 191 GLY A 200 1 10
HELIX 13 13 SER A 208 PHE A 223 1 16
HELIX 14 14 SER A 243 GLY A 256 1 14
HELIX 15 15 GLY B 16 LEU B 27 1 12
HELIX 16 16 THR B 38 CYS B 41 5 4
HELIX 17 17 PRO B 47 LYS B 64 1 18
HELIX 18 18 CYS B 74 LEU B 89 1 16
HELIX 19 19 VAL B 96 THR B 108 1 13
HELIX 20 20 THR B 118 ALA B 125 1 8
HELIX 21 21 ALA B 125 SER B 133 1 9
HELIX 22 22 LYS B 147 SER B 154 1 8
HELIX 23 23 SER B 159 GLN B 171 1 13
HELIX 24 24 ALA B 172 GLN B 174 5 3
HELIX 25 25 HIS B 187 LEU B 190 5 4
HELIX 26 26 LEU B 191 MET B 199 1 9
HELIX 27 27 SER B 208 PHE B 223 1 16
HELIX 28 28 SER B 243 GLY B 256 1 14
SHEET 1 AA 6 VAL A 93 GLY A 95 0
SHEET 2 AA 6 MET A 69 ILE A 72 1 O LEU A 70 N VAL A 94
SHEET 3 AA 6 ILE A 7 ASP A 11 1 O GLY A 8 N VAL A 71
SHEET 4 AA 6 LEU A 32 GLY A 36 1 O ILE A 33 N LEU A 9
SHEET 5 AA 6 GLU A 237 THR A 240 1 O GLU A 237 N TYR A 34
SHEET 6 AA 6 GLN A 263 GLN A 264 1 O GLN A 263 N THR A 240
SHEET 1 AB 4 GLU A 139 ALA A 144 0
SHEET 2 AB 4 LYS A 112 GLY A 117 1 O ILE A 113 N THR A 141
SHEET 3 AB 4 THR A 180 LEU A 183 1 O THR A 180 N GLY A 114
SHEET 4 AB 4 THR A 204 ASP A 207 1 O THR A 204 N LEU A 181
SHEET 1 BA 6 VAL B 93 GLY B 95 0
SHEET 2 BA 6 MET B 69 ILE B 72 1 O LEU B 70 N VAL B 94
SHEET 3 BA 6 ILE B 7 ASP B 11 1 O GLY B 8 N VAL B 71
SHEET 4 BA 6 LEU B 32 GLY B 36 1 O ILE B 33 N LEU B 9
SHEET 5 BA 6 GLU B 237 THR B 240 1 O GLU B 237 N TYR B 34
SHEET 6 BA 6 ALA B 262 GLN B 264 1 O GLN B 263 N THR B 240
SHEET 1 BB 4 GLU B 139 ALA B 144 0
SHEET 2 BB 4 LYS B 112 GLY B 117 1 O ILE B 113 N THR B 141
SHEET 3 BB 4 THR B 180 LEU B 183 1 O THR B 180 N GLY B 114
SHEET 4 BB 4 THR B 204 ASP B 207 1 O THR B 204 N LEU B 181
LINK N LEU A 119 CA CA A1271 1555 1555 3.20
LINK CA CA A1271 O HOH A2050 1555 1555 2.91
LINK CA CA A1271 O HOH A2242 1555 1555 2.90
LINK N LEU B 119 CA CA B1271 1555 1555 3.18
LINK CA CA B1271 O HOH B2068 1555 1555 2.95
LINK CA CA B1271 O HOH B2261 1555 1555 3.06
CISPEP 1 CYS A 41 PRO A 42 0 0.15
CISPEP 2 CYS B 41 PRO B 42 0 0.19
SITE 1 AC1 6 GLY A 44 THR A 118 LEU A 119 PRO A 146
SITE 2 AC1 6 HOH A2050 HOH A2242
SITE 1 AC2 5 GLY B 44 THR B 118 LEU B 119 HOH B2068
SITE 2 AC2 5 HOH B2261
SITE 1 AC3 15 ASP A 11 SER A 12 PRO A 42 TYR A 43
SITE 2 AC3 15 GLY A 44 CYS A 74 ASN A 75 THR A 76
SITE 3 AC3 15 THR A 118 VAL A 149 CYS A 185 THR A 186
SITE 4 AC3 15 HIS A 187 HOH A2168 HOH A2242
SITE 1 AC4 15 ASP B 11 SER B 12 PRO B 42 TYR B 43
SITE 2 AC4 15 GLY B 44 CYS B 74 ASN B 75 THR B 76
SITE 3 AC4 15 THR B 118 VAL B 149 CYS B 185 THR B 186
SITE 4 AC4 15 HIS B 187 HOH B2188 HOH B2261
CRYST1 48.190 74.670 75.070 90.00 95.97 90.00 P 1 21 1 4
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 0.020751 0.000000 0.002170 0.00000
SCALE2 0.000000 0.013392 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013394 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
