HEADER HYDROLASE 25-JAN-07 2JF4
TITLE FAMILY 37 TREHALASE FROM ESCHERICHIA COLI IN COMPLEX WITH
TITLE 2 VALIDOXYLAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PERIPLASMIC TREHALASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 31-565;
COMPND 5 SYNONYM: TREHALASE, ALPHA-ALPHA-TREHALASE,
COMPND 6 ALPHA-ALPHA-TREHALOSE GLUCOHYDROLASE;
COMPND 7 EC: 3.2.1.28;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS FAMILY 37, HYDROLASE, INHIBITOR, TREHALASE, GLYCOSIDE
KEYWDS 2 HYDROLASE, PERIPLASMIC, GLYCOSIDASE, VALIDOXYLAMINE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.P.GIBSON,T.M.GLOSTER,S.ROBERTS,R.A.J.WARREN,
AUTHOR 2 I.STORCH DE GRACIA,A.GARCIA,J.L.CHIARA,G.J.DAVIES
REVDAT 2 24-FEB-09 2JF4 1 VERSN
REVDAT 1 13-FEB-07 2JF4 0
JRNL AUTH R.P.GIBSON,T.M.GLOSTER,S.ROBERTS,R.A.J.WARREN,
JRNL AUTH 2 I.STORCH DE GRACIA,A.GARCIA,J.L.CHIARA,G.J.DAVIES
JRNL TITL MOLECULAR BASIS FOR TREHALASE INHIBITION REVEALED
JRNL TITL 2 BY THE STRUCTURE OF TREHALASE IN COMPLEX WITH
JRNL TITL 3 POTENT INHIBITORS.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 46 4115 2007
JRNL REFN ISSN 1433-7851
JRNL PMID 17455176
JRNL DOI 10.1002/ANIE.200604825
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 25985
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1384
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1891
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1730
REMARK 3 BIN FREE R VALUE SET COUNT : 98
REMARK 3 BIN FREE R VALUE : 0.2540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3907
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 135
REMARK 3 SOLVENT ATOMS : 296
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.79000
REMARK 3 B22 (A**2) : 1.29000
REMARK 3 B33 (A**2) : -0.50000
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): 0.259
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.196
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.122
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.672
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4161 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5682 ; 1.290 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 512 ; 5.080 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 212 ;36.102 ;24.623
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 657 ;14.724 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;13.517 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 599 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3273 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1892 ; 0.194 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2841 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 258 ; 0.129 ; 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): 19 ; 0.224 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 17 ; 0.135 ; 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): 2590 ; 1.144 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4050 ; 1.297 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1846 ; 2.134 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1625 ; 3.130 ; 4.500
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. NO ELECTRON DENSITY CAN BE OBSERVED FOR THE
REMARK 3 CHAIN BETWEEN 101 AND 113.
REMARK 4
REMARK 4 2JF4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-JAN-07.
REMARK 100 THE PDBE ID CODE IS EBI-31240.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97931
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111) OR
REMARK 200 SI(311)
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27378
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
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: SAD
REMARK 200 SOFTWARE USED: AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.2
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 MG/ML PROTEIN. 25% PEG3350
REMARK 280 AND 0.1 M BIS-TRIS HCL, PH 6.5.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 24.69950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.58700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.34800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.58700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.69950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.34800
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 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 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 GLU A 31
REMARK 465 GLU A 32
REMARK 465 THR A 33
REMARK 465 PRO A 34
REMARK 465 VAL A 35
REMARK 465 THR A 36
REMARK 465 LYS A 102
REMARK 465 GLU A 103
REMARK 465 GLY A 104
REMARK 465 GLU A 105
REMARK 465 LYS A 106
REMARK 465 TYR A 107
REMARK 465 VAL A 108
REMARK 465 PRO A 109
REMARK 465 PRO A 110
REMARK 465 GLU A 111
REMARK 465 GLY A 112
REMARK 465 THR A 548
REMARK 465 VAL A 549
REMARK 465 LYS A 550
REMARK 465 SER A 551
REMARK 465 ALA A 552
REMARK 465 THR A 553
REMARK 465 THR A 554
REMARK 465 GLN A 555
REMARK 465 PRO A 556
REMARK 465 SER A 557
REMARK 465 THR A 558
REMARK 465 LYS A 559
REMARK 465 GLU A 560
REMARK 465 ALA A 561
REMARK 465 GLN A 562
REMARK 465 PRO A 563
REMARK 465 THR A 564
REMARK 465 PRO A 565
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 GLU A 134 CG CD OE1 OE2
REMARK 470 LYS A 135 CG CD CE NZ
REMARK 470 LYS A 176 CD CE NZ
REMARK 470 LYS A 535 CB CG CD CE NZ
REMARK 470 GLU A 536 CB CG CD OE1 OE2
REMARK 470 GLN A 537 CB CG CD OE1 NE2
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 TYR A 158 -70.49 -65.54
REMARK 500 SER A 206 -142.70 -115.72
REMARK 500 LYS A 255 -117.87 51.99
REMARK 500 SER A 280 44.88 -142.90
REMARK 500 ARG A 328 59.62 -144.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 TRP A 159 25.0 L L OUTSIDE RANGE
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VDM A1548
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FIRST 30 RESIDUES CORRESPOND TO A SIGNAL PEPTIDE THAT
REMARK 999 IS PREDICTED TO HAVE CLEAVED DURING EXPRESSION OF THE
REMARK 999 PROTEIN.
DBREF 2JF4 A 31 565 UNP P13482 TREA_ECOLI 31 565
SEQRES 1 A 535 GLU GLU THR PRO VAL THR PRO GLN PRO PRO ASP ILE LEU
SEQRES 2 A 535 LEU GLY PRO LEU PHE ASN ASP VAL GLN ASN ALA LYS LEU
SEQRES 3 A 535 PHE PRO ASP GLN LYS THR PHE ALA ASP ALA VAL PRO ASN
SEQRES 4 A 535 SER ASP PRO LEU MSE ILE LEU ALA ASP TYR ARG MSE GLN
SEQRES 5 A 535 GLN ASN GLN SER GLY PHE ASP LEU ARG HIS PHE VAL ASN
SEQRES 6 A 535 VAL ASN PHE THR LEU PRO LYS GLU GLY GLU LYS TYR VAL
SEQRES 7 A 535 PRO PRO GLU GLY GLN SER LEU ARG GLU HIS ILE ASP GLY
SEQRES 8 A 535 LEU TRP PRO VAL LEU THR ARG SER THR GLU ASN THR GLU
SEQRES 9 A 535 LYS TRP ASP SER LEU LEU PRO LEU PRO GLU PRO TYR VAL
SEQRES 10 A 535 VAL PRO GLY GLY ARG PHE ARG GLU VAL TYR TYR TRP ASP
SEQRES 11 A 535 SER TYR PHE THR MSE LEU GLY LEU ALA GLU SER GLY HIS
SEQRES 12 A 535 TRP ASP LYS VAL ALA ASP MSE VAL ALA ASN PHE ALA HIS
SEQRES 13 A 535 GLU ILE ASP THR TYR GLY HIS ILE PRO ASN GLY ASN ARG
SEQRES 14 A 535 SER TYR TYR LEU SER ARG SER GLN PRO PRO PHE PHE ALA
SEQRES 15 A 535 LEU MSE VAL GLU LEU LEU ALA GLN HIS GLU GLY ASP ALA
SEQRES 16 A 535 ALA LEU LYS GLN TYR LEU PRO GLN MSE GLN LYS GLU TYR
SEQRES 17 A 535 ALA TYR TRP MSE ASP GLY VAL GLU ASN LEU GLN ALA GLY
SEQRES 18 A 535 GLN GLN GLU LYS ARG VAL VAL LYS LEU GLN ASP GLY THR
SEQRES 19 A 535 LEU LEU ASN ARG TYR TRP ASP ASP ARG ASP THR PRO ARG
SEQRES 20 A 535 PRO GLU SER TRP VAL GLU ASP ILE ALA THR ALA LYS SER
SEQRES 21 A 535 ASN PRO ASN ARG PRO ALA THR GLU ILE TYR ARG ASP LEU
SEQRES 22 A 535 ARG SER ALA ALA ALA SER GLY TRP ASP PHE SER SER ARG
SEQRES 23 A 535 TRP MSE ASP ASN PRO GLN GLN LEU ASN THR LEU ARG THR
SEQRES 24 A 535 THR SER ILE VAL PRO VAL ASP LEU ASN SER LEU MSE PHE
SEQRES 25 A 535 LYS MSE GLU LYS ILE LEU ALA ARG ALA SER LYS ALA ALA
SEQRES 26 A 535 GLY ASP ASN ALA MSE ALA ASN GLN TYR GLU THR LEU ALA
SEQRES 27 A 535 ASN ALA ARG GLN LYS GLY ILE GLU LYS TYR LEU TRP ASN
SEQRES 28 A 535 ASP GLN GLN GLY TRP TYR ALA ASP TYR ASP LEU LYS SER
SEQRES 29 A 535 HIS LYS VAL ARG ASN GLN LEU THR ALA ALA ALA LEU PHE
SEQRES 30 A 535 PRO LEU TYR VAL ASN ALA ALA ALA LYS ASP ARG ALA ASN
SEQRES 31 A 535 LYS MSE ALA THR ALA THR LYS THR HIS LEU LEU GLN PRO
SEQRES 32 A 535 GLY GLY LEU ASN THR THR SER VAL LYS SER GLY GLN GLN
SEQRES 33 A 535 TRP ASP ALA PRO ASN GLY TRP ALA PRO LEU GLN TRP VAL
SEQRES 34 A 535 ALA THR GLU GLY LEU GLN ASN TYR GLY GLN LYS GLU VAL
SEQRES 35 A 535 ALA MSE ASP ILE SER TRP HIS PHE LEU THR ASN VAL GLN
SEQRES 36 A 535 HIS THR TYR ASP ARG GLU LYS LYS LEU VAL GLU LYS TYR
SEQRES 37 A 535 ASP VAL SER THR THR GLY THR GLY GLY GLY GLY GLY GLU
SEQRES 38 A 535 TYR PRO LEU GLN ASP GLY PHE GLY TRP THR ASN GLY VAL
SEQRES 39 A 535 THR LEU LYS MSE LEU ASP LEU ILE CYS PRO LYS GLU GLN
SEQRES 40 A 535 PRO CYS ASP ASN VAL PRO ALA THR ARG PRO THR VAL LYS
SEQRES 41 A 535 SER ALA THR THR GLN PRO SER THR LYS GLU ALA GLN PRO
SEQRES 42 A 535 THR PRO
MODRES 2JF4 MSE A 74 MET SELENOMETHIONINE
MODRES 2JF4 MSE A 81 MET SELENOMETHIONINE
MODRES 2JF4 MSE A 165 MET SELENOMETHIONINE
MODRES 2JF4 MSE A 180 MET SELENOMETHIONINE
MODRES 2JF4 MSE A 214 MET SELENOMETHIONINE
MODRES 2JF4 MSE A 234 MET SELENOMETHIONINE
MODRES 2JF4 MSE A 242 MET SELENOMETHIONINE
MODRES 2JF4 MSE A 318 MET SELENOMETHIONINE
MODRES 2JF4 MSE A 341 MET SELENOMETHIONINE
MODRES 2JF4 MSE A 344 MET SELENOMETHIONINE
MODRES 2JF4 MSE A 360 MET SELENOMETHIONINE
MODRES 2JF4 MSE A 422 MET SELENOMETHIONINE
MODRES 2JF4 MSE A 474 MET SELENOMETHIONINE
MODRES 2JF4 MSE A 528 MET SELENOMETHIONINE
HET MSE A 74 8
HET MSE A 81 8
HET MSE A 165 8
HET MSE A 180 8
HET MSE A 214 8
HET MSE A 234 8
HET MSE A 242 8
HET MSE A 318 8
HET MSE A 341 8
HET MSE A 344 8
HET MSE A 360 8
HET MSE A 422 8
HET MSE A 474 8
HET MSE A 528 8
HET VDM A1548 23
HETNAM MSE SELENOMETHIONINE
HETNAM VDM (1S,2S,3R,6S)-4-(HYDROXYMETHYL)-6-{[(1S,2S,
HETNAM 2 VDM 3S,4R,5R)-2,3,4-TRIHYDROXY-5-(HYDROXYMETHYL)
HETNAM 3 VDM CYCLOHEXYL]AMINO}CYCLOHEX-4-ENE-1,2,3-TRIOL
HETSYN VDM VALIDOXYLAMINE
FORMUL 1 MSE 14(C5 H11 N O2 SE)
FORMUL 2 VDM C14 H25 N O8
FORMUL 3 HOH *296(H2 O1)
HELIX 1 1 PRO A 39 LEU A 44 1 6
HELIX 2 2 LEU A 44 LYS A 55 1 12
HELIX 3 3 GLN A 60 ASP A 65 1 6
HELIX 4 4 ASP A 71 GLN A 83 1 13
HELIX 5 5 ASP A 89 ASN A 97 1 9
HELIX 6 6 SER A 114 LEU A 126 1 13
HELIX 7 7 TYR A 157 SER A 171 1 15
HELIX 8 8 HIS A 173 GLY A 192 1 20
HELIX 9 9 SER A 200 LEU A 203 5 4
HELIX 10 10 PHE A 210 GLY A 223 1 14
HELIX 11 11 GLY A 223 TYR A 230 1 8
HELIX 12 12 TYR A 230 MSE A 242 1 13
HELIX 13 13 ARG A 277 GLU A 279 5 3
HELIX 14 14 SER A 280 SER A 290 1 11
HELIX 15 15 PRO A 295 SER A 309 1 15
HELIX 16 16 SER A 314 TRP A 317 5 4
HELIX 17 17 GLN A 323 THR A 326 5 4
HELIX 18 18 ARG A 328 THR A 330 5 3
HELIX 19 19 PRO A 334 GLY A 356 1 23
HELIX 20 20 ASP A 357 LEU A 379 1 23
HELIX 21 21 ALA A 403 ALA A 405 5 3
HELIX 22 22 LEU A 406 VAL A 411 1 6
HELIX 23 23 ALA A 415 LEU A 430 1 16
HELIX 24 24 TRP A 453 ASN A 466 1 14
HELIX 25 25 GLN A 469 LYS A 492 1 24
HELIX 26 26 PHE A 518 CYS A 533 1 16
SHEET 1 AA 2 VAL A 67 PRO A 68 0
SHEET 2 AA 2 PHE A 98 THR A 99 -1 O THR A 99 N VAL A 67
SHEET 1 AB 2 THR A 127 ARG A 128 0
SHEET 2 AB 2 TYR A 146 VAL A 147 -1 O TYR A 146 N ARG A 128
SHEET 1 AC 3 GLN A 252 GLU A 254 0
SHEET 2 AC 3 VAL A 257 LYS A 259 -1 O VAL A 257 N GLU A 254
SHEET 3 AC 3 LEU A 265 ASN A 267 -1 O LEU A 266 N VAL A 258
SHEET 1 AD 3 ILE A 332 VAL A 333 0
SHEET 2 AD 3 TYR A 390 ASP A 391 -1 O TYR A 390 N VAL A 333
SHEET 3 AD 3 LYS A 396 VAL A 397 -1 O LYS A 396 N ASP A 391
SHEET 1 AE 2 TRP A 380 ASN A 381 0
SHEET 2 AE 2 TRP A 386 TYR A 387 -1 O TRP A 386 N ASN A 381
SHEET 1 AF 2 LEU A 431 GLN A 432 0
SHEET 2 AF 2 GLY A 435 LEU A 436 -1 O GLY A 435 N GLN A 432
SHEET 1 AG 2 ASN A 451 GLY A 452 0
SHEET 2 AG 2 TYR A 498 ASP A 499 -1 O TYR A 498 N GLY A 452
SHEET 1 AH 2 LEU A 494 VAL A 495 0
SHEET 2 AH 2 ASP A 516 GLY A 517 -1 O GLY A 517 N LEU A 494
SSBOND 1 CYS A 533 CYS A 539 1555 1555 2.58
SSBOND 2 CYS A 533 CYS A 539 1555 1555 2.06
LINK C LEU A 73 N MSE A 74 1555 1555 1.32
LINK C MSE A 74 N ILE A 75 1555 1555 1.33
LINK C ARG A 80 N MSE A 81 1555 1555 1.33
LINK C MSE A 81 N GLN A 82 1555 1555 1.33
LINK C THR A 164 N MSE A 165 1555 1555 1.33
LINK C MSE A 165 N LEU A 166 1555 1555 1.33
LINK C ASP A 179 N MSE A 180 1555 1555 1.33
LINK C MSE A 180 N VAL A 181 1555 1555 1.33
LINK C LEU A 213 N MSE A 214 1555 1555 1.34
LINK C MSE A 214 N VAL A 215 1555 1555 1.34
LINK C GLN A 233 N MSE A 234 1555 1555 1.34
LINK C MSE A 234 N GLN A 235 1555 1555 1.33
LINK C TRP A 241 N MSE A 242 1555 1555 1.34
LINK C MSE A 242 N ASP A 243 1555 1555 1.33
LINK C TRP A 317 N MSE A 318 1555 1555 1.34
LINK C MSE A 318 N ASP A 319 1555 1555 1.33
LINK C LEU A 340 N MSE A 341 1555 1555 1.34
LINK C MSE A 341 N PHE A 342 1555 1555 1.33
LINK C LYS A 343 N MSE A 344 1555 1555 1.33
LINK C MSE A 344 N GLU A 345 1555 1555 1.33
LINK C ALA A 359 N MSE A 360 1555 1555 1.33
LINK C MSE A 360 N ALA A 361 1555 1555 1.33
LINK C LYS A 421 N MSE A 422 1555 1555 1.33
LINK C MSE A 422 N ALA A 423 1555 1555 1.33
LINK C ALA A 473 N MSE A 474 1555 1555 1.34
LINK C MSE A 474 N ASP A 475 1555 1555 1.33
LINK C LYS A 527 N MSE A 528 1555 1555 1.34
LINK C MSE A 528 N LEU A 529 1555 1555 1.33
CISPEP 1 ASP A 312 PHE A 313 0 0.25
CISPEP 2 ALA A 449 PRO A 450 0 -2.73
CISPEP 3 GLY A 517 PHE A 518 0 -4.24
SITE 1 AC1 23 ARG A 152 PHE A 153 TYR A 157 TRP A 159
SITE 2 AC1 23 ASP A 160 ASN A 196 TYR A 202 ARG A 205
SITE 3 AC1 23 GLN A 207 ARG A 277 GLU A 279 SER A 280
SITE 4 AC1 23 ALA A 307 GLY A 310 ASP A 312 GLN A 446
SITE 5 AC1 23 TRP A 447 GLU A 511 TYR A 512 PHE A 518
SITE 6 AC1 23 TRP A 520 HOH A2178 HOH A2263
CRYST1 49.399 102.696 103.174 90.00 90.00 90.00 P 21 21 21 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 0.020243 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009737 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009692 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
