HEADER HYDROLASE 30-MAR-07 2EPN
TITLE N-ACETYL-B-D-GLUCOSAMINIDASE (GCNA) FROM STREPTOCOCCUS GORDONII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-ACETYL-BETA-D-GLUCOSAMINIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GLYCOSIDE HYDROLASE;
COMPND 5 EC: 3.2.1.52;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS GORDONII;
SOURCE 3 ORGANISM_TAXID: 1302;
SOURCE 4 STRAIN: FSS2;
SOURCE 5 GENE: GCNA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHAR101
KEYWDS GLYCOSIDE HYDROLASE, FAMILY 20, GLUCOSAMINIDASE, GCNA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.B.LANGLEY
REVDAT 5 25-OCT-23 2EPN 1 REMARK
REVDAT 4 11-OCT-17 2EPN 1 REMARK
REVDAT 3 13-JUL-11 2EPN 1 VERSN
REVDAT 2 24-FEB-09 2EPN 1 VERSN
REVDAT 1 11-MAR-08 2EPN 0
JRNL AUTH D.B.LANGLEY,D.W.S.HARTY,N.A.JACQUES,N.HUNTER,J.M.GUSS,
JRNL AUTH 2 C.A.COLLYER
JRNL TITL STRUCTURE OF N-ACETYL-BETA-D-GLUCOSAMINIDASE (GCNA) FROM THE
JRNL TITL 2 ENDOCARDITIS PATHOGEN STREPTOCOCCUS GORDONII AND ITS COMPLEX
JRNL TITL 3 WITH THE MECHANISM-BASED INHIBITOR NAG-THIAZOLINE
JRNL REF J.MOL.BIOL. V. 377 104 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18237743
JRNL DOI 10.1016/J.JMB.2007.09.028
REMARK 2
REMARK 2 RESOLUTION. 1.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 161033
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8028
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.61
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.65
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10515
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE SET COUNT : 528
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10132
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 777
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.03000
REMARK 3 B22 (A**2) : -0.23000
REMARK 3 B33 (A**2) : -0.80000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.087
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.089
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.055
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.535
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10420 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 9256 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14092 ; 1.330 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 21526 ; 0.805 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1256 ; 5.853 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 550 ;33.804 ;24.691
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1847 ;12.090 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;16.349 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1520 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11654 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2169 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2189 ; 0.216 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 9802 ; 0.178 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5222 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 5889 ; 0.082 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 648 ; 0.105 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 17 ; 0.194 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 48 ; 0.172 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.112 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 8116 ; 2.347 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2547 ; 0.586 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9961 ; 2.577 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4975 ; 4.056 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4124 ; 5.594 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL PARAMETERS FOR MASK CACLULATION
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2EPN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-APR-07.
REMARK 100 THE DEPOSITION ID IS D_1000026952.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 161033
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.610
REMARK 200 RESOLUTION RANGE LOW (A) : 15.020
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 9.100
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : 8.40
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.510
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLECULAR REPLACEMENT
REMARK 200 STARTING MODEL: PDB ENTRY 2EPK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES, 2M AMMONIUM SULPHATE,
REMARK 280 0.5%(V/V) PEG400, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 53.78700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.16600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.78700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.16600
REMARK 290 SMTRY3 4 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: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
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 1
REMARK 465 THR A 33
REMARK 465 ASP A 34
REMARK 465 SER A 35
REMARK 465 MET B 1
REMARK 465 THR B 33
REMARK 465 ASP B 34
REMARK 465 SER B 35
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 ARG A 242 NE - CZ - NH2 ANGL. DEV. = -3.1 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 ASN A 96 -21.78 113.18
REMARK 500 THR A 126 44.63 -99.49
REMARK 500 LEU A 168 -72.59 -141.85
REMARK 500 ALA A 169 -163.57 -119.37
REMARK 500 ASP A 187 -66.51 -94.40
REMARK 500 GLU A 189 -124.68 51.26
REMARK 500 ALA A 225 61.24 -104.32
REMARK 500 ASP A 308 118.22 -164.36
REMARK 500 TRP A 338 94.96 -66.68
REMARK 500 ASP A 376 127.45 -28.78
REMARK 500 ASP A 431 -4.07 79.42
REMARK 500 ILE A 624 -32.11 -148.00
REMARK 500 ASN B 96 -28.76 105.92
REMARK 500 THR B 126 45.23 -92.96
REMARK 500 LEU B 168 -71.86 -144.30
REMARK 500 ALA B 169 -167.13 -118.56
REMARK 500 ASP B 187 -62.79 -90.79
REMARK 500 VAL B 188 146.22 -170.23
REMARK 500 GLU B 189 -122.26 50.59
REMARK 500 ALA B 225 62.95 -106.30
REMARK 500 ASP B 308 117.12 -163.86
REMARK 500 TRP B 338 98.15 -64.83
REMARK 500 ASP B 376 126.05 -24.90
REMARK 500 ASN B 377 41.60 70.01
REMARK 500 ASP B 431 -2.10 78.98
REMARK 500 ILE B 624 -29.06 -142.65
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 NGT A 1650
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGT B 2650
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2EPK RELATED DB: PDB
REMARK 900 RELATED ID: 2EPL RELATED DB: PDB
REMARK 900 RELATED ID: 2EPM RELATED DB: PDB
REMARK 900 RELATED ID: 2EPO RELATED DB: PDB
DBREF 2EPN A 1 627 UNP Q6ST21 Q6ST21_STRGN 1 627
DBREF 2EPN B 1 627 UNP Q6ST21 Q6ST21_STRGN 1 627
SEQRES 1 A 627 MET ALA THR PHE LEU GLY LEU SER SER LYS GLN GLU LYS
SEQRES 2 A 627 ALA LEU VAL ARG LEU ASP LYS TYR LEU ASN LEU GLY GLU
SEQRES 3 A 627 ILE ALA VAL SER LEU VAL THR ASP SER ALA THR SER ILE
SEQRES 4 A 627 LYS VAL GLU GLY ARG GLN GLY TYR TYR GLN VAL SER TYR
SEQRES 5 A 627 LYS GLN PRO HIS GLN LEU TYR ARG ALA LEU ALA LEU LEU
SEQRES 6 A 627 SER ALA ALA LEU ARG SER GLY GLN ASP GLU VAL GLN ILE
SEQRES 7 A 627 GLU GLU GLU ALA ALA TYR GLU ASP LEU ALA TYR MET ALA
SEQRES 8 A 627 ASP CYS SER ARG ASN ALA VAL LEU ASN LEU SER SER ALA
SEQRES 9 A 627 LYS LYS MET ILE GLU VAL LEU ALA LEU MET GLY TYR SER
SEQRES 10 A 627 THR PHE GLU LEU TYR MET GLU ASP THR TYR GLU ILE GLU
SEQRES 11 A 627 ASN GLN PRO TYR PHE GLY TYR PHE ARG GLY ARG TYR THR
SEQRES 12 A 627 VAL ALA GLU LEU GLN GLU ILE GLU ASP TYR ALA ALA ASP
SEQRES 13 A 627 PHE ASP MET SER PHE VAL PRO CYS ILE GLN THR LEU ALA
SEQRES 14 A 627 HIS LEU SER ALA PHE VAL LYS TRP GLY ILE LYS GLU VAL
SEQRES 15 A 627 GLN GLU LEU ARG ASP VAL GLU ASP ILE LEU LEU ILE GLY
SEQRES 16 A 627 GLU GLU LYS VAL TYR ASP LEU ILE GLU GLY MET PHE GLN
SEQRES 17 A 627 THR MET ALA HIS LEU HIS THR ARG LYS ILE ASN ILE GLY
SEQRES 18 A 627 MET ASP GLU ALA HIS LEU VAL GLY LEU GLY ARG TYR LEU
SEQRES 19 A 627 ILE LYS HIS GLY PHE GLN ASN ARG SER LEU LEU MET CYS
SEQRES 20 A 627 GLN HIS LEU GLU ARG VAL LEU ASP ILE ALA ASP LYS TYR
SEQRES 21 A 627 GLY PHE ASN CYS GLN MET TRP SER ASP MET PHE PHE LYS
SEQRES 22 A 627 LEU MET SER ALA ASP GLY GLN TYR ASP ARG ASP VAL GLU
SEQRES 23 A 627 ILE PRO GLU GLU THR ARG VAL TYR LEU ASP ARG LEU LYS
SEQRES 24 A 627 GLU ARG VAL THR LEU VAL TYR TRP ASP TYR TYR GLN ASP
SEQRES 25 A 627 SER GLU GLU LYS TYR ASN ARG ASN PHE GLN ASN HIS HIS
SEQRES 26 A 627 LYS ILE SER GLN ASP ILE ALA PHE ALA GLY GLY ALA TRP
SEQRES 27 A 627 LYS TRP ILE GLY PHE THR PRO HIS ASN HIS PHE SER ARG
SEQRES 28 A 627 LEU VAL ALA ILE GLU ALA ASN LYS ALA CYS ARG LYS ASN
SEQRES 29 A 627 GLN VAL LYS GLU VAL ILE VAL THR GLY TRP GLY ASP ASN
SEQRES 30 A 627 GLY GLY GLU THR SER GLN PHE SER VAL LEU PRO ALA LEU
SEQRES 31 A 627 GLN ILE TRP ALA GLU LEU ALA TYR ARG ASN ASP LEU LYS
SEQRES 32 A 627 LYS VAL SER GLU HIS PHE LEU VAL SER THR GLY LEU ASP
SEQRES 33 A 627 PHE ASP ASP PHE MET LYS ILE ASP LEU ALA ASN LEU LEU
SEQRES 34 A 627 PRO ASP LEU PRO ASP ASN LEU SER GLY ILE ASN PRO ASN
SEQRES 35 A 627 ARG TYR VAL LEU TYR GLN ASP VAL LEU CYS PRO LEU LEU
SEQRES 36 A 627 GLU GLN HIS ILE ARG PRO GLU LYS ASP LYS GLN HIS PHE
SEQRES 37 A 627 ALA SER SER ALA GLN GLN LEU GLY GLU ILE SER LYS ARG
SEQRES 38 A 627 ALA GLY GLU TYR ALA TYR ILE PHE GLU THR GLN ALA GLN
SEQRES 39 A 627 LEU ASN ALA LEU LEU ALA LEU LYS ILE SER ILE THR SER
SEQRES 40 A 627 GLY ILE GLN LYS ALA TYR ARG ASN GLY ASP LYS GLU HIS
SEQRES 41 A 627 LEU SER ALA LEU ALA GLU LYS ASP PHE PRO GLN LEU TYR
SEQRES 42 A 627 GLN MET VAL GLU ASP PHE SER ASP GLN PHE SER ARG GLN
SEQRES 43 A 627 TRP GLN GLN GLU ASN LYS ILE PHE GLY LEU ASP THR ILE
SEQRES 44 A 627 ASP ILE ARG PHE GLY GLY LEU LEU LYS ARG ILE LYS ARG
SEQRES 45 A 627 ALA GLN GLU ARG LEU GLU GLN PHE ILE SER GLY GLN ILE
SEQRES 46 A 627 ASP CYS VAL GLU GLU LEU GLU GLN GLU ILE LEU PRO PHE
SEQRES 47 A 627 ASN ASP PHE TYR LYS ASP GLN GLY LEU THR ALA THR THR
SEQRES 48 A 627 ALA ASN GLN TRP HIS LEU ILE ALA THR ALA SER THR ILE
SEQRES 49 A 627 TYR THR THR
SEQRES 1 B 627 MET ALA THR PHE LEU GLY LEU SER SER LYS GLN GLU LYS
SEQRES 2 B 627 ALA LEU VAL ARG LEU ASP LYS TYR LEU ASN LEU GLY GLU
SEQRES 3 B 627 ILE ALA VAL SER LEU VAL THR ASP SER ALA THR SER ILE
SEQRES 4 B 627 LYS VAL GLU GLY ARG GLN GLY TYR TYR GLN VAL SER TYR
SEQRES 5 B 627 LYS GLN PRO HIS GLN LEU TYR ARG ALA LEU ALA LEU LEU
SEQRES 6 B 627 SER ALA ALA LEU ARG SER GLY GLN ASP GLU VAL GLN ILE
SEQRES 7 B 627 GLU GLU GLU ALA ALA TYR GLU ASP LEU ALA TYR MET ALA
SEQRES 8 B 627 ASP CYS SER ARG ASN ALA VAL LEU ASN LEU SER SER ALA
SEQRES 9 B 627 LYS LYS MET ILE GLU VAL LEU ALA LEU MET GLY TYR SER
SEQRES 10 B 627 THR PHE GLU LEU TYR MET GLU ASP THR TYR GLU ILE GLU
SEQRES 11 B 627 ASN GLN PRO TYR PHE GLY TYR PHE ARG GLY ARG TYR THR
SEQRES 12 B 627 VAL ALA GLU LEU GLN GLU ILE GLU ASP TYR ALA ALA ASP
SEQRES 13 B 627 PHE ASP MET SER PHE VAL PRO CYS ILE GLN THR LEU ALA
SEQRES 14 B 627 HIS LEU SER ALA PHE VAL LYS TRP GLY ILE LYS GLU VAL
SEQRES 15 B 627 GLN GLU LEU ARG ASP VAL GLU ASP ILE LEU LEU ILE GLY
SEQRES 16 B 627 GLU GLU LYS VAL TYR ASP LEU ILE GLU GLY MET PHE GLN
SEQRES 17 B 627 THR MET ALA HIS LEU HIS THR ARG LYS ILE ASN ILE GLY
SEQRES 18 B 627 MET ASP GLU ALA HIS LEU VAL GLY LEU GLY ARG TYR LEU
SEQRES 19 B 627 ILE LYS HIS GLY PHE GLN ASN ARG SER LEU LEU MET CYS
SEQRES 20 B 627 GLN HIS LEU GLU ARG VAL LEU ASP ILE ALA ASP LYS TYR
SEQRES 21 B 627 GLY PHE ASN CYS GLN MET TRP SER ASP MET PHE PHE LYS
SEQRES 22 B 627 LEU MET SER ALA ASP GLY GLN TYR ASP ARG ASP VAL GLU
SEQRES 23 B 627 ILE PRO GLU GLU THR ARG VAL TYR LEU ASP ARG LEU LYS
SEQRES 24 B 627 GLU ARG VAL THR LEU VAL TYR TRP ASP TYR TYR GLN ASP
SEQRES 25 B 627 SER GLU GLU LYS TYR ASN ARG ASN PHE GLN ASN HIS HIS
SEQRES 26 B 627 LYS ILE SER GLN ASP ILE ALA PHE ALA GLY GLY ALA TRP
SEQRES 27 B 627 LYS TRP ILE GLY PHE THR PRO HIS ASN HIS PHE SER ARG
SEQRES 28 B 627 LEU VAL ALA ILE GLU ALA ASN LYS ALA CYS ARG LYS ASN
SEQRES 29 B 627 GLN VAL LYS GLU VAL ILE VAL THR GLY TRP GLY ASP ASN
SEQRES 30 B 627 GLY GLY GLU THR SER GLN PHE SER VAL LEU PRO ALA LEU
SEQRES 31 B 627 GLN ILE TRP ALA GLU LEU ALA TYR ARG ASN ASP LEU LYS
SEQRES 32 B 627 LYS VAL SER GLU HIS PHE LEU VAL SER THR GLY LEU ASP
SEQRES 33 B 627 PHE ASP ASP PHE MET LYS ILE ASP LEU ALA ASN LEU LEU
SEQRES 34 B 627 PRO ASP LEU PRO ASP ASN LEU SER GLY ILE ASN PRO ASN
SEQRES 35 B 627 ARG TYR VAL LEU TYR GLN ASP VAL LEU CYS PRO LEU LEU
SEQRES 36 B 627 GLU GLN HIS ILE ARG PRO GLU LYS ASP LYS GLN HIS PHE
SEQRES 37 B 627 ALA SER SER ALA GLN GLN LEU GLY GLU ILE SER LYS ARG
SEQRES 38 B 627 ALA GLY GLU TYR ALA TYR ILE PHE GLU THR GLN ALA GLN
SEQRES 39 B 627 LEU ASN ALA LEU LEU ALA LEU LYS ILE SER ILE THR SER
SEQRES 40 B 627 GLY ILE GLN LYS ALA TYR ARG ASN GLY ASP LYS GLU HIS
SEQRES 41 B 627 LEU SER ALA LEU ALA GLU LYS ASP PHE PRO GLN LEU TYR
SEQRES 42 B 627 GLN MET VAL GLU ASP PHE SER ASP GLN PHE SER ARG GLN
SEQRES 43 B 627 TRP GLN GLN GLU ASN LYS ILE PHE GLY LEU ASP THR ILE
SEQRES 44 B 627 ASP ILE ARG PHE GLY GLY LEU LEU LYS ARG ILE LYS ARG
SEQRES 45 B 627 ALA GLN GLU ARG LEU GLU GLN PHE ILE SER GLY GLN ILE
SEQRES 46 B 627 ASP CYS VAL GLU GLU LEU GLU GLN GLU ILE LEU PRO PHE
SEQRES 47 B 627 ASN ASP PHE TYR LYS ASP GLN GLY LEU THR ALA THR THR
SEQRES 48 B 627 ALA ASN GLN TRP HIS LEU ILE ALA THR ALA SER THR ILE
SEQRES 49 B 627 TYR THR THR
HET NGT A1650 14
HET NGT B2650 14
HETNAM NGT 3AR,5R,6S,7R,7AR-5-HYDROXYMETHYL-2-METHYL-5,6,7,7A-
HETNAM 2 NGT TETRAHYDRO-3AH-PYRANO[3,2-D]THIAZOLE-6,7-DIOL
FORMUL 3 NGT 2(C8 H13 N O4 S)
FORMUL 5 HOH *777(H2 O)
HELIX 1 1 SER A 8 ASN A 23 1 16
HELIX 2 2 HIS A 56 SER A 71 1 16
HELIX 3 3 ASN A 100 GLY A 115 1 16
HELIX 4 4 THR A 143 PHE A 157 1 15
HELIX 5 5 LEU A 171 LYS A 176 1 6
HELIX 6 6 ILE A 179 GLU A 184 1 6
HELIX 7 7 GLU A 196 ALA A 211 1 16
HELIX 8 8 GLY A 231 GLY A 238 1 8
HELIX 9 9 ASN A 241 TYR A 260 1 20
HELIX 10 10 SER A 268 SER A 276 1 9
HELIX 11 11 PRO A 288 LYS A 299 1 12
HELIX 12 12 SER A 313 LYS A 326 1 14
HELIX 13 13 HIS A 346 ASN A 364 1 19
HELIX 14 14 VAL A 386 ASN A 400 1 15
HELIX 15 15 LYS A 404 GLY A 414 1 11
HELIX 16 16 ASP A 416 LYS A 422 1 7
HELIX 17 17 ILE A 423 LEU A 428 5 6
HELIX 18 18 ASN A 440 GLN A 448 1 9
HELIX 19 19 LEU A 455 ILE A 459 5 5
HELIX 20 20 ARG A 460 SER A 479 1 20
HELIX 21 21 LYS A 480 GLU A 484 5 5
HELIX 22 22 TYR A 485 GLY A 516 1 32
HELIX 23 23 ASP A 517 LYS A 527 1 11
HELIX 24 24 LYS A 527 ASN A 551 1 25
HELIX 25 25 GLY A 555 SER A 582 1 28
HELIX 26 26 VAL A 588 GLN A 593 1 6
HELIX 27 27 TYR A 602 GLY A 606 5 5
HELIX 28 28 GLN A 614 ALA A 619 1 6
HELIX 29 29 SER B 8 ASN B 23 1 16
HELIX 30 30 HIS B 56 SER B 71 1 16
HELIX 31 31 ASN B 100 GLY B 115 1 16
HELIX 32 32 THR B 143 PHE B 157 1 15
HELIX 33 33 LEU B 171 LYS B 176 1 6
HELIX 34 34 ILE B 179 GLU B 184 1 6
HELIX 35 35 GLU B 196 ALA B 211 1 16
HELIX 36 36 GLY B 231 GLY B 238 1 8
HELIX 37 37 ASN B 241 TYR B 260 1 20
HELIX 38 38 SER B 268 MET B 275 1 8
HELIX 39 39 PRO B 288 LYS B 299 1 12
HELIX 40 40 SER B 313 SER B 328 1 16
HELIX 41 41 HIS B 346 ASN B 364 1 19
HELIX 42 42 VAL B 386 ASN B 400 1 15
HELIX 43 43 LYS B 404 GLY B 414 1 11
HELIX 44 44 ASP B 416 LYS B 422 1 7
HELIX 45 45 ILE B 423 LEU B 428 5 6
HELIX 46 46 ASN B 440 GLN B 448 1 9
HELIX 47 47 LEU B 455 ILE B 459 5 5
HELIX 48 48 GLU B 462 LYS B 480 1 19
HELIX 49 49 ARG B 481 GLU B 484 5 4
HELIX 50 50 TYR B 485 ASN B 515 1 31
HELIX 51 51 ASP B 517 LYS B 527 1 11
HELIX 52 52 LYS B 527 ASN B 551 1 25
HELIX 53 53 GLY B 555 SER B 582 1 28
HELIX 54 54 VAL B 588 GLN B 593 5 6
HELIX 55 55 TYR B 602 GLY B 606 5 5
HELIX 56 56 GLN B 614 THR B 620 1 7
SHEET 1 A 5 THR A 3 LEU A 5 0
SHEET 2 A 5 ALA A 28 LEU A 31 1 O VAL A 29 N THR A 3
SHEET 3 A 5 TYR A 47 TYR A 52 1 O VAL A 50 N SER A 30
SHEET 4 A 5 ILE A 39 ARG A 44 -1 N GLU A 42 O GLN A 49
SHEET 5 A 5 VAL A 76 GLU A 80 -1 O ILE A 78 N VAL A 41
SHEET 1 B 9 ASP A 86 ASP A 92 0
SHEET 2 B 9 THR A 118 TYR A 122 1 O TYR A 122 N ALA A 91
SHEET 3 B 9 SER A 160 CYS A 164 1 O CYS A 164 N LEU A 121
SHEET 4 B 9 LYS A 217 ASN A 219 1 O ASN A 219 N PRO A 163
SHEET 5 B 9 ASN A 263 TRP A 267 1 O GLN A 265 N ILE A 218
SHEET 6 B 9 VAL A 302 TRP A 307 1 O VAL A 305 N MET A 266
SHEET 7 B 9 ILE A 331 GLY A 336 1 O ALA A 332 N TYR A 306
SHEET 8 B 9 GLU A 368 GLY A 373 1 O THR A 372 N GLY A 335
SHEET 9 B 9 ASP A 86 ASP A 92 1 N ALA A 88 O VAL A 371
SHEET 1 C 2 ARG A 186 VAL A 188 0
SHEET 2 C 2 ILE A 191 LEU A 192 -1 O ILE A 191 N VAL A 188
SHEET 1 D 5 THR B 3 LEU B 5 0
SHEET 2 D 5 ALA B 28 LEU B 31 1 O LEU B 31 N LEU B 5
SHEET 3 D 5 TYR B 47 TYR B 52 1 O TYR B 48 N SER B 30
SHEET 4 D 5 ILE B 39 ARG B 44 -1 N GLU B 42 O GLN B 49
SHEET 5 D 5 VAL B 76 GLU B 80 -1 O ILE B 78 N VAL B 41
SHEET 1 E 9 ASP B 86 ASP B 92 0
SHEET 2 E 9 THR B 118 TYR B 122 1 O TYR B 122 N ALA B 91
SHEET 3 E 9 SER B 160 CYS B 164 1 O CYS B 164 N LEU B 121
SHEET 4 E 9 LYS B 217 ASN B 219 1 O ASN B 219 N PRO B 163
SHEET 5 E 9 ASN B 263 TRP B 267 1 O GLN B 265 N ILE B 218
SHEET 6 E 9 VAL B 302 TRP B 307 1 O VAL B 305 N MET B 266
SHEET 7 E 9 ILE B 331 GLY B 336 1 O ALA B 332 N LEU B 304
SHEET 8 E 9 GLU B 368 GLY B 373 1 O THR B 372 N GLY B 335
SHEET 9 E 9 ASP B 86 ASP B 92 1 N ALA B 88 O VAL B 371
SHEET 1 F 2 ARG B 186 VAL B 188 0
SHEET 2 F 2 ILE B 191 LEU B 192 -1 O ILE B 191 N ASP B 187
SITE 1 AC1 13 ARG A 95 HIS A 170 ASP A 223 GLU A 224
SITE 2 AC1 13 TRP A 267 TRP A 307 TYR A 309 TRP A 340
SITE 3 AC1 13 TRP A 374 ASP A 376 HOH A1676 HOH A1755
SITE 4 AC1 13 HOH A1968
SITE 1 AC2 12 ARG B 95 HIS B 170 ASP B 223 GLU B 224
SITE 2 AC2 12 TRP B 267 TRP B 307 TYR B 309 TRP B 374
SITE 3 AC2 12 ASP B 376 HOH B2659 HOH B2828 HOH B2953
CRYST1 107.574 112.332 103.127 90.00 90.00 90.00 P 21 21 2 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 0.009296 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008902 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009697 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
