HEADER TRANSCRIPTION REGULATOR 23-FEB-07 2EFP
TITLE CRYSTAL STRUCTURE OF TYR77 TO ALA OF ST1022-GLUTAMINE COMPLEX FROM
TITLE 2 SULOLOBUS TOKODAII 7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 150AA LONG HYPOTHETICAL TRANSCRIPTIONAL REGULATOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ST1022;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS TOKODAII;
SOURCE 3 ORGANISM_TAXID: 111955;
SOURCE 4 GENE: ST1022;
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: PET21A
KEYWDS TRANSCRIPTIONAL REGULATOR, LRP/ASNC FAMILY GLN BINDING, ST1022,
KEYWDS 2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL
KEYWDS 3 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, TRANSCRIPTION REGULATOR
EXPDTA X-RAY DIFFRACTION
AUTHOR T.S.KUMAREVEL,P.KARTHE,N.NAKANO,A.SHINKAI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 7 25-OCT-23 2EFP 1 REMARK
REVDAT 6 10-NOV-21 2EFP 1 REMARK SEQADV
REVDAT 5 11-OCT-17 2EFP 1 REMARK
REVDAT 4 13-JUL-11 2EFP 1 VERSN
REVDAT 3 17-MAR-09 2EFP 1 JRNL
REVDAT 2 24-FEB-09 2EFP 1 VERSN
REVDAT 1 26-FEB-08 2EFP 0
JRNL AUTH T.S.KUMAREVEL,N.NAKANO,K.PONNURAJ,S.C.GOPINATH,K.SAKAMOTO,
JRNL AUTH 2 A.SHINKAI,P.K.KUMAR,S.YOKOYAMA
JRNL TITL CRYSTAL STRUCTURE OF GLUTAMINE RECEPTOR PROTEIN FROM
JRNL TITL 2 SULFOLOBUS TOKODAII STRAIN 7 IN COMPLEX WITH ITS EFFECTOR
JRNL TITL 3 L-GLUTAMINE: IMPLICATIONS OF EFFECTOR BINDING IN MOLECULAR
JRNL TITL 4 ASSOCIATION AND DNA BINDING.
JRNL REF NUCLEIC ACIDS RES. V. 36 4808 2008
JRNL REFN ISSN 0305-1048
JRNL PMID 18653535
JRNL DOI 10.1093/NAR/GKN456
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1934373.570
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 10634
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 SET) : 0.232
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 540
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.011
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1650
REMARK 3 BIN R VALUE (WORKING SET) : 0.2840
REMARK 3 BIN FREE R VALUE : 0.3650
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 98
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.037
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1226
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 43
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.04000
REMARK 3 B22 (A**2) : -9.04000
REMARK 3 B33 (A**2) : 18.08000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.27
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.34
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.700
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.570 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.580 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.420 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.770 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 45.89
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : DNA-RNA_REP.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2EFP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000026607.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 180
REMARK 200 PH : 6.2
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 VII
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10689
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 9.100
REMARK 200 R MERGE (I) : 0.05000
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) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.20
REMARK 200 R MERGE FOR SHELL (I) : 0.45500
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: MOLREP
REMARK 200 STARTING MODEL: 2E7W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% POLYPROPYLENEGLYCOL, 30%
REMARK 280 ISOPROPANOL, 0.07M SODIUM CITRATE, 10MM TAURINE, PH 6.2, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 51.84350
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 51.84350
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 37.47100
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 51.84350
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 51.84350
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 37.47100
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 51.84350
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 51.84350
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 37.47100
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 51.84350
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 51.84350
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 37.47100
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 51.84350
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 51.84350
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 37.47100
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 51.84350
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 51.84350
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 37.47100
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 51.84350
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 51.84350
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 37.47100
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 51.84350
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 51.84350
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 37.47100
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 33510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -212.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 6 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 7 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1043 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1022 O HOH A 1022 7555 1.28
REMARK 500 MG MG A 1001 MG MG A 1001 7555 1.53
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 LYS A 75 -133.99 42.14
REMARK 500 PHE A 119 -66.05 -105.98
REMARK 500 GLU A 143 82.24 -151.10
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 GLN A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN A 1003
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2E7W RELATED DB: PDB
REMARK 900 WILD TYPE
REMARK 900 RELATED ID: 2E7X RELATED DB: PDB
REMARK 900 COMPLEXED WITH GLN
REMARK 900 RELATED ID: 2EFN RELATED DB: PDB
REMARK 900 S32A MUTANT
REMARK 900 RELATED ID: 2EFO RELATED DB: PDB
REMARK 900 Y77A MUTANT
REMARK 900 RELATED ID: 2EFQ RELATED DB: PDB
REMARK 900 T134A COMPLEXED WITH GLUTAMINE
REMARK 900 RELATED ID: STO001001022.5 RELATED DB: TARGETDB
DBREF 2EFP A 1 150 UNP Q972W6 Q972W6_SULTO 1 150
SEQADV 2EFP ALA A 77 UNP Q972W6 TYR 77 ENGINEERED MUTATION
SEQRES 1 A 150 MET ASP GLU ILE ASP LEU ARG ILE LEU LYS ILE LEU GLN
SEQRES 2 A 150 TYR ASN ALA LYS TYR SER LEU ASP GLU ILE ALA ARG GLU
SEQRES 3 A 150 ILE ARG ILE PRO LYS SER THR LEU SER TYR ARG ILE LYS
SEQRES 4 A 150 LYS LEU GLU LYS ASP GLY VAL ILE LYS GLY TYR TYR ALA
SEQRES 5 A 150 TYR ILE ASN PRO ALA SER LEU ASN LEU ASP TYR ILE VAL
SEQRES 6 A 150 ILE THR SER VAL LYS ALA LYS TYR GLY LYS ASN ALA HIS
SEQRES 7 A 150 VAL GLU LEU GLY ASN LYS LEU ALA GLN ILE PRO GLY VAL
SEQRES 8 A 150 TRP GLY VAL TYR PHE VAL LEU GLY ASP ASN ASP PHE ILE
SEQRES 9 A 150 VAL MET ALA ARG TYR LYS THR ARG GLU GLU PHE MET GLU
SEQRES 10 A 150 LYS PHE LEU GLU ARG VAL MET SER ILE PRO GLU VAL GLU
SEQRES 11 A 150 ARG THR SER THR GLN VAL VAL VAL LYS ILE ILE LYS GLU
SEQRES 12 A 150 SER PRO ASN ILE VAL ILE PHE
HET MG A1001 1
HET GLN A1002 10
HET GLN A1003 10
HETNAM MG MAGNESIUM ION
HETNAM GLN GLUTAMINE
FORMUL 2 MG MG 2+
FORMUL 3 GLN 2(C5 H10 N2 O3)
FORMUL 5 HOH *43(H2 O)
HELIX 1 1 ASP A 2 GLN A 13 1 12
HELIX 2 2 SER A 19 ARG A 28 1 10
HELIX 3 3 PRO A 30 ASP A 44 1 15
HELIX 4 4 PRO A 56 ASN A 60 5 5
HELIX 5 5 ASN A 76 GLN A 87 1 12
HELIX 6 6 THR A 111 PHE A 119 1 9
HELIX 7 7 PHE A 119 ILE A 126 1 8
SHEET 1 A 4 VAL A 91 PHE A 96 0
SHEET 2 A 4 PHE A 103 TYR A 109 -1 O MET A 106 N GLY A 93
SHEET 3 A 4 TYR A 63 ALA A 71 -1 N THR A 67 O VAL A 105
SHEET 4 A 4 VAL A 129 VAL A 137 -1 O ARG A 131 N LYS A 70
SITE 1 AC1 4 PRO A 30 LYS A 31 SER A 32 LYS A 39
SITE 1 AC2 11 THR A 67 LEU A 98 GLY A 99 ASP A 100
SITE 2 AC2 11 ASN A 101 ASP A 102 LEU A 120 ARG A 131
SITE 3 AC2 11 THR A 132 SER A 133 THR A 134
CRYST1 103.687 103.687 74.942 90.00 90.00 90.00 I 4 2 2 16
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 0.009644 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009644 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013344 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
