HEADER TRANSFERASE 18-JAN-16 5FTW
TITLE CRYSTAL STRUCTURE OF GLUTAMATE O-METHYLTRANSFERASE IN COMPLEX WITH S-
TITLE 2 ADENOSYL-L-HOMOCYSTEINE (SAH) FROM BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHEMOTAXIS PROTEIN METHYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SAH BINDING DOMAIN, UNP RESIDUES 1-256;
COMPND 5 SYNONYM: CHER METHYLTRANSFERASE;
COMPND 6 EC: 2.1.1.80;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: ROSETTA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET28C;
SOURCE 10 OTHER_DETAILS: MTCC
KEYWDS TRANSFERASE, METHYLTRANSFERASE, SAH
EXPDTA X-RAY DIFFRACTION
AUTHOR R.SHARMA,S.DHINDWAL,M.BATRA,M.AGGARWAL,P.KUMAR,S.TOMAR
REVDAT 3 10-JAN-24 5FTW 1 REMARK
REVDAT 2 07-DEC-16 5FTW 1 JRNL
REVDAT 1 05-OCT-16 5FTW 0
JRNL AUTH M.BATRA,R.SHARMA,A.MALIK,S.DHINDWAL,P.KUMAR,S.TOMAR
JRNL TITL CRYSTAL STRUCTURE OF PENTAPEPTIDE-INDEPENDENT CHEMOTAXIS
JRNL TITL 2 RECEPTOR METHYLTRANSFERASE (CHER) REVEALS IDIOSYNCRATIC
JRNL TITL 3 STRUCTURAL DETERMINANTS FOR RECEPTOR RECOGNITION.
JRNL REF J.STRUCT.BIOL. V. 196 364 2016
JRNL REFN ISSN 1047-8477
JRNL PMID 27544050
JRNL DOI 10.1016/J.JSB.2016.08.005
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 21799
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1183
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1470
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.2870
REMARK 3 BIN FREE R VALUE SET COUNT : 66
REMARK 3 BIN FREE R VALUE : 0.3520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2105
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 293
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.57000
REMARK 3 B22 (A**2) : -0.40000
REMARK 3 B33 (A**2) : -0.17000
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): 0.151
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.149
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.109
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.568
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2261 ; 0.017 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3055 ; 2.150 ; 1.998
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 264 ; 6.704 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 107 ;37.760 ;24.579
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 421 ;16.874 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;24.313 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 337 ; 0.169 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1658 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 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 RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 5FTW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1290066069.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 : BRUKER AXS MICROSTAR-H
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
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 : 23011
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.790
REMARK 200 RESOLUTION RANGE LOW (A) : 41.580
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.15000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.60000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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 1BC5
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M SODIUM
REMARK 280 ACETATE TRIHYDRATE
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 20.79000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.93000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.43500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.93000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.79000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.43500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 MET A 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 2024 O HOH A 2053 1.97
REMARK 500 O HOH A 2135 O HOH A 2287 2.00
REMARK 500 NH1 ARG A 30 O HOH A 2056 2.02
REMARK 500 CD ARG A 29 O HOH A 2053 2.04
REMARK 500 O HOH A 2064 O HOH A 2159 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 2125 O HOH A 2176 1655 1.65
REMARK 500 O HOH A 2164 O HOH A 2211 4555 1.86
REMARK 500
REMARK 500 REMARK: NULL
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 147 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 201 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 201 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 MET A 219 CG - SD - CE ANGL. DEV. = -22.3 DEGREES
REMARK 500 LYS A 224 CD - CE - NZ ANGL. DEV. = 13.9 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 74 72.52 62.62
REMARK 500 ALA A 101 66.80 81.75
REMARK 500 SER A 103 -132.86 47.31
REMARK 500 ALA A 188 -20.85 -140.97
REMARK 500 ASN A 226 -4.27 66.18
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 A2078 DISTANCE = 6.80 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 1257
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1258
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1259
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1260
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 1263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1265
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1266
DBREF 5FTW A 1 256 UNP P31105 CHER_BACSU 1 256
SEQRES 1 A 256 MET ASP THR TYR SER VAL PHE THR THR LYS TRP LYS GLN
SEQRES 2 A 256 LEU THR GLY VAL ASP LEU THR LEU TYR LYS GLU ALA GLN
SEQRES 3 A 256 MET LYS ARG ARG LEU THR SER LEU TYR GLU LYS LYS GLY
SEQRES 4 A 256 PHE GLN SER PHE LYS ASP PHE ALA ALA ALA LEU GLU LYS
SEQRES 5 A 256 ASP GLN ALA LEU LEU ASN GLU THR LEU ASP ARG MET THR
SEQRES 6 A 256 ILE ASN VAL SER GLU PHE TYR ARG ASN TYR LYS ARG TRP
SEQRES 7 A 256 GLU VAL LEU GLU THR ALA ILE LEU PRO LEU ILE LYS THR
SEQRES 8 A 256 SER ARG PRO LEU LYS ILE TRP SER ALA ALA CYS SER THR
SEQRES 9 A 256 GLY GLU GLU PRO TYR THR LEU ALA MET LEU LEU ASP GLN
SEQRES 10 A 256 GLN LYS GLY LEU PRO GLY TYR GLN ILE LEU ALA THR ASP
SEQRES 11 A 256 ILE ASP GLU LYS ALA LEU GLU LYS ALA LYS LYS GLY VAL
SEQRES 12 A 256 TYR GLN GLU ARG SER LEU GLN GLU VAL PRO LEU SER VAL
SEQRES 13 A 256 LYS ASP ARG TYR PHE THR GLN ASN ALA ASN ARG SER TYR
SEQRES 14 A 256 GLU VAL LYS THR GLU ILE LYS LYS ASN ILE THR PHE LYS
SEQRES 15 A 256 LYS HIS ASN LEU LEU ALA ASP ARG TYR GLU GLN ASP PHE
SEQRES 16 A 256 ASP LEU ILE VAL CYS ARG ASN VAL PHE ILE TYR PHE THR
SEQRES 17 A 256 GLU SER ALA LYS GLU GLU LEU TYR LEU LYS MET ALA HIS
SEQRES 18 A 256 SER LEU LYS LYS ASN GLY VAL LEU PHE VAL GLY SER THR
SEQRES 19 A 256 GLU GLN ILE PHE ASN PRO GLU LYS PHE GLY LEU VAL PRO
SEQRES 20 A 256 ALA ASP THR PHE PHE TYR GLN LYS ARG
HET SAH A1257 26
HET SO4 A1258 5
HET SO4 A1259 5
HET SO4 A1260 5
HET SO4 A1261 5
HET SO4 A1262 5
HET TRS A1263 8
HET SO4 A1264 5
HET GOL A1265 6
HET GOL A1266 6
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM SO4 SULFATE ION
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM GOL GLYCEROL
HETSYN TRS TRIS BUFFER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 SAH C14 H20 N6 O5 S
FORMUL 3 SO4 6(O4 S 2-)
FORMUL 8 TRS C4 H12 N O3 1+
FORMUL 10 GOL 2(C3 H8 O3)
FORMUL 12 HOH *293(H2 O)
HELIX 1 1 ASP A 2 GLY A 16 1 15
HELIX 2 2 ASP A 18 LEU A 21 5 4
HELIX 3 3 LYS A 23 LYS A 38 1 16
HELIX 4 4 SER A 42 ASP A 53 1 12
HELIX 5 5 ASP A 53 ARG A 63 1 11
HELIX 6 6 ASN A 74 ILE A 85 1 12
HELIX 7 7 ILE A 85 LYS A 90 1 6
HELIX 8 8 GLY A 105 GLN A 117 1 13
HELIX 9 9 ASP A 132 GLY A 142 1 11
HELIX 10 10 ARG A 147 LEU A 149 5 3
HELIX 11 11 PRO A 153 TYR A 160 1 8
HELIX 12 12 LYS A 172 LYS A 177 1 6
HELIX 13 13 VAL A 203 TYR A 206 5 4
HELIX 14 14 THR A 208 SER A 222 1 15
HELIX 15 15 ASN A 239 PHE A 243 5 5
SHEET 1 AA 7 ILE A 179 LYS A 183 0
SHEET 2 AA 7 TYR A 124 ASP A 130 1 O ILE A 126 N THR A 180
SHEET 3 AA 7 LEU A 95 ALA A 100 1 O LEU A 95 N GLN A 125
SHEET 4 AA 7 PHE A 195 CYS A 200 1 N ASP A 196 O LYS A 96
SHEET 5 AA 7 LEU A 223 VAL A 231 1 N LYS A 224 O PHE A 195
SHEET 6 AA 7 PHE A 252 LYS A 255 -1 O TYR A 253 N LEU A 229
SHEET 7 AA 7 LEU A 245 ASP A 249 -1 O VAL A 246 N GLN A 254
SHEET 1 AB 3 VAL A 143 GLN A 145 0
SHEET 2 AB 3 SER A 168 VAL A 171 -1 O TYR A 169 N TYR A 144
SHEET 3 AB 3 PHE A 161 ALA A 165 -1 O THR A 162 N GLU A 170
SITE 1 AC1 21 TYR A 22 THR A 65 SER A 69 ARG A 73
SITE 2 AC1 21 ALA A 101 SER A 103 GLU A 107 ASP A 130
SITE 3 AC1 21 ILE A 131 ASP A 132 HIS A 184 ASN A 185
SITE 4 AC1 21 LEU A 186 LEU A 187 ARG A 201 ASN A 202
SITE 5 AC1 21 VAL A 203 HOH A2090 HOH A2101 HOH A2149
SITE 6 AC1 21 HOH A2151
SITE 1 AC2 5 LYS A 177 ASN A 239 HOH A2225 HOH A2226
SITE 2 AC2 5 HOH A2288
SITE 1 AC3 8 ARG A 29 ARG A 30 PHE A 40 ASP A 45
SITE 2 AC3 8 ILE A 66 HOH A2060 HOH A2066 HOH A2073
SITE 1 AC4 5 THR A 173 GLU A 174 LYS A 177 HOH A2218
SITE 2 AC4 5 HOH A2291
SITE 1 AC5 5 ASN A 74 LYS A 76 ARG A 77 SER A 233
SITE 2 AC5 5 HOH A2119
SITE 1 AC6 6 ARG A 147 ARG A 167 LYS A 218 HIS A 221
SITE 2 AC6 6 HOH A2188 HOH A2245
SITE 1 AC7 6 GLU A 146 GLN A 150 ARG A 167 HOH A2189
SITE 2 AC7 6 HOH A2236 HOH A2292
SITE 1 AC8 3 LYS A 23 THR A 91 SER A 92
SITE 1 AC9 5 ARG A 73 ASN A 74 ASN A 202 THR A 234
SITE 2 AC9 5 HOH A2118
SITE 1 BC1 7 THR A 3 TYR A 35 SER A 42 PHE A 43
SITE 2 BC1 7 LYS A 44 HOH A2006 HOH A2293
CRYST1 41.580 72.870 81.860 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 0.024050 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013723 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012216 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
