| 6ioh-pdb | HEADER TRANSFERASE 30-OCT-18 6IOH
TITLE CRYSTAL STRUCTURE OF HOMOSERINE O-ACETYLTRANSFERASE IN COMPLEX WITH
TITLE 2 HOMOSERINE FROM MYCOBACTERIUM SMEGMATIS ATCC 19420
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMOSERINE O-ACETYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HAT,HOMOSERINE TRANSACETYLASE,HTA;
COMPND 5 EC: 2.3.1.31;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;
SOURCE 3 ORGANISM_TAXID: 1772;
SOURCE 4 GENE: METX_1, METXA, ERS451418_01697;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21_T1R(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET30A
KEYWDS TRANSFERASE, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.-Y.SAGONG,K.-J.KIM
REVDAT 1 04-SEP-19 6IOH 0
JRNL AUTH H.Y.SAGONG,J.HONG,K.J.KIM
JRNL TITL CRYSTAL STRUCTURE AND BIOCHEMICAL CHARACTERIZATION OF
JRNL TITL 2 O-ACETYLHOMOSERINE ACETYLTRANSFERASE FROM MYCOBACTERIUM
JRNL TITL 3 SMEGMATIS ATCC 19420.
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 517 399 2019
JRNL REFN ESSN 1090-2104
JRNL PMID 31378370
JRNL DOI 10.1016/J.BBRC.2019.07.117
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 46999
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2416
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3322
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE SET COUNT : 170
REMARK 3 BIN FREE R VALUE : 0.2760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5492
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 133
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.85000
REMARK 3 B22 (A**2) : 1.16000
REMARK 3 B33 (A**2) : -3.01000
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): 0.184
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.157
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.110
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.942
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5628 ; 0.009 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 5156 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7681 ; 1.559 ; 1.641
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11900 ; 1.362 ; 1.578
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 739 ; 6.739 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 295 ;28.911 ;21.119
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 813 ;14.679 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 49 ;19.063 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 721 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6537 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1190 ; 0.001 ; 0.020
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 : NULL
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6IOH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1300009629.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49446
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 39.7900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 9.010
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: 6IOG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 34 % (V/V) POLYETHYLENE GLYCOL (PEG)
REMARK 280 400, 0.1 M SODIUM ACETATE/ACETIC ACID PH 5.5, 0.2 M CALCIUM
REMARK 280 ACETATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 26.97000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.93200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.51650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.93200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.97000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.51650
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
REMARK 350 TOTAL BURIED SURFACE AREA: 4620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 ARG B 368
REMARK 465 LEU B 369
REMARK 465 GLU B 370
REMARK 465 HIS B 371
REMARK 465 HIS B 372
REMARK 465 HIS B 373
REMARK 465 HIS B 374
REMARK 465 HIS B 375
REMARK 465 HIS B 376
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 GLY B 46 NH2 ARG B 170 2.09
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 B 271 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG B 271 NE - CZ - NH2 ANGL. DEV. = -4.7 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 SER A 152 -125.86 66.33
REMARK 500 ASP A 206 41.65 -106.05
REMARK 500 ALA A 240 -135.81 36.43
REMARK 500 ASP A 245 -105.74 19.06
REMARK 500 ARG A 271 -4.90 -140.09
REMARK 500 ASP A 288 97.96 -172.06
REMARK 500 TYR A 318 75.37 -118.28
REMARK 500 ALA B 54 -167.09 -100.36
REMARK 500 ASP B 67 55.35 37.81
REMARK 500 SER B 152 -127.64 62.43
REMARK 500 ALA B 240 -132.17 43.39
REMARK 500 ASP B 245 -120.06 48.56
REMARK 500 ASP B 288 93.74 -171.97
REMARK 500 TYR B 318 74.04 -116.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR B 95 ASN B 96 149.26
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 HSE A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HSE B 401
DBREF1 6IOH A 2 368 UNP A0A0D6HE46_MYCSM
DBREF2 6IOH A A0A0D6HE46 2 368
DBREF1 6IOH B 2 368 UNP A0A0D6HE46_MYCSM
DBREF2 6IOH B A0A0D6HE46 2 368
SEQADV 6IOH LEU A 369 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOH GLU A 370 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOH HIS A 371 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOH HIS A 372 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOH HIS A 373 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOH HIS A 374 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOH HIS A 375 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOH HIS A 376 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOH LEU B 369 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOH GLU B 370 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOH HIS B 371 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOH HIS B 372 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOH HIS B 373 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOH HIS B 374 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOH HIS B 375 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOH HIS B 376 UNP A0A0D6HE4 EXPRESSION TAG
SEQRES 1 A 375 ALA THR VAL PRO LEU PRO ALA GLU GLY GLU ILE GLY LEU
SEQRES 2 A 375 VAL HIS ILE GLY ALA LEU THR LEU GLU ASN GLY THR VAL
SEQRES 3 A 375 LEU PRO ASP VAL THR ILE ALA VAL GLN ARG TRP GLY GLU
SEQRES 4 A 375 LEU ALA PRO ASP ARG GLY ASN VAL VAL MET VAL LEU HIS
SEQRES 5 A 375 ALA LEU THR GLY ASP SER HIS VAL THR GLY PRO ALA GLY
SEQRES 6 A 375 ASP GLY HIS PRO THR ALA GLY TRP TRP ASP GLY VAL ALA
SEQRES 7 A 375 GLY PRO GLY ALA PRO ILE ASP THR ASP HIS TRP CYS ALA
SEQRES 8 A 375 ILE ALA THR ASN VAL LEU GLY GLY CYS ARG GLY SER THR
SEQRES 9 A 375 GLY PRO GLY SER LEU ALA PRO ASP GLY LYS PRO TRP GLY
SEQRES 10 A 375 SER ARG PHE PRO GLN ILE THR ILE ARG ASP GLN VAL ALA
SEQRES 11 A 375 ALA ASP ARG ALA ALA LEU ALA ALA LEU GLY ILE THR GLU
SEQRES 12 A 375 VAL ALA ALA VAL VAL GLY GLY SER MET GLY GLY ALA ARG
SEQRES 13 A 375 ALA LEU GLU TRP LEU VAL THR HIS PRO ASP ASP VAL ARG
SEQRES 14 A 375 ALA GLY LEU VAL LEU ALA VAL GLY ALA ARG ALA THR ALA
SEQRES 15 A 375 ASP GLN ILE GLY THR GLN SER THR GLN VAL ALA ALA ILE
SEQRES 16 A 375 LYS ALA ASP PRO ASP TRP GLN GLY GLY ASP TYR HIS GLY
SEQRES 17 A 375 THR GLY ARG ALA PRO THR GLU GLY MET GLU ILE ALA ARG
SEQRES 18 A 375 ARG PHE ALA HIS LEU THR TYR ARG GLY GLU GLU GLU LEU
SEQRES 19 A 375 ASP ASP ARG PHE ALA ASN THR PRO GLN ASP ASP GLU ASP
SEQRES 20 A 375 PRO LEU THR GLY GLY ARG TYR ALA VAL GLN SER TYR LEU
SEQRES 21 A 375 GLU TYR GLN GLY GLY LYS LEU ALA ARG ARG PHE ASP PRO
SEQRES 22 A 375 GLY THR TYR VAL VAL LEU SER ASP ALA LEU SER SER HIS
SEQRES 23 A 375 ASP VAL GLY ARG GLY ARG GLY GLY VAL GLU ALA ALA LEU
SEQRES 24 A 375 ARG SER CYS PRO VAL PRO VAL VAL VAL GLY GLY ILE THR
SEQRES 25 A 375 SER ASP ARG LEU TYR PRO ILE ARG LEU GLN GLN GLU LEU
SEQRES 26 A 375 ALA GLU LEU LEU PRO GLY CYS GLN GLY LEU ASP VAL VAL
SEQRES 27 A 375 ASP SER ILE TYR GLY HIS ASP GLY PHE LEU VAL GLU THR
SEQRES 28 A 375 GLU LEU VAL GLY LYS LEU ILE ARG ARG THR LEU GLU LEU
SEQRES 29 A 375 ALA GLN ARG LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 375 ALA THR VAL PRO LEU PRO ALA GLU GLY GLU ILE GLY LEU
SEQRES 2 B 375 VAL HIS ILE GLY ALA LEU THR LEU GLU ASN GLY THR VAL
SEQRES 3 B 375 LEU PRO ASP VAL THR ILE ALA VAL GLN ARG TRP GLY GLU
SEQRES 4 B 375 LEU ALA PRO ASP ARG GLY ASN VAL VAL MET VAL LEU HIS
SEQRES 5 B 375 ALA LEU THR GLY ASP SER HIS VAL THR GLY PRO ALA GLY
SEQRES 6 B 375 ASP GLY HIS PRO THR ALA GLY TRP TRP ASP GLY VAL ALA
SEQRES 7 B 375 GLY PRO GLY ALA PRO ILE ASP THR ASP HIS TRP CYS ALA
SEQRES 8 B 375 ILE ALA THR ASN VAL LEU GLY GLY CYS ARG GLY SER THR
SEQRES 9 B 375 GLY PRO GLY SER LEU ALA PRO ASP GLY LYS PRO TRP GLY
SEQRES 10 B 375 SER ARG PHE PRO GLN ILE THR ILE ARG ASP GLN VAL ALA
SEQRES 11 B 375 ALA ASP ARG ALA ALA LEU ALA ALA LEU GLY ILE THR GLU
SEQRES 12 B 375 VAL ALA ALA VAL VAL GLY GLY SER MET GLY GLY ALA ARG
SEQRES 13 B 375 ALA LEU GLU TRP LEU VAL THR HIS PRO ASP ASP VAL ARG
SEQRES 14 B 375 ALA GLY LEU VAL LEU ALA VAL GLY ALA ARG ALA THR ALA
SEQRES 15 B 375 ASP GLN ILE GLY THR GLN SER THR GLN VAL ALA ALA ILE
SEQRES 16 B 375 LYS ALA ASP PRO ASP TRP GLN GLY GLY ASP TYR HIS GLY
SEQRES 17 B 375 THR GLY ARG ALA PRO THR GLU GLY MET GLU ILE ALA ARG
SEQRES 18 B 375 ARG PHE ALA HIS LEU THR TYR ARG GLY GLU GLU GLU LEU
SEQRES 19 B 375 ASP ASP ARG PHE ALA ASN THR PRO GLN ASP ASP GLU ASP
SEQRES 20 B 375 PRO LEU THR GLY GLY ARG TYR ALA VAL GLN SER TYR LEU
SEQRES 21 B 375 GLU TYR GLN GLY GLY LYS LEU ALA ARG ARG PHE ASP PRO
SEQRES 22 B 375 GLY THR TYR VAL VAL LEU SER ASP ALA LEU SER SER HIS
SEQRES 23 B 375 ASP VAL GLY ARG GLY ARG GLY GLY VAL GLU ALA ALA LEU
SEQRES 24 B 375 ARG SER CYS PRO VAL PRO VAL VAL VAL GLY GLY ILE THR
SEQRES 25 B 375 SER ASP ARG LEU TYR PRO ILE ARG LEU GLN GLN GLU LEU
SEQRES 26 B 375 ALA GLU LEU LEU PRO GLY CYS GLN GLY LEU ASP VAL VAL
SEQRES 27 B 375 ASP SER ILE TYR GLY HIS ASP GLY PHE LEU VAL GLU THR
SEQRES 28 B 375 GLU LEU VAL GLY LYS LEU ILE ARG ARG THR LEU GLU LEU
SEQRES 29 B 375 ALA GLN ARG LEU GLU HIS HIS HIS HIS HIS HIS
HET HSE A 401 8
HET HSE B 401 8
HETNAM HSE L-HOMOSERINE
FORMUL 3 HSE 2(C4 H9 N O3)
FORMUL 5 HOH *133(H2 O)
HELIX 1 AA1 TRP A 117 PHE A 121 5 5
HELIX 2 AA2 THR A 125 LEU A 140 1 16
HELIX 3 AA3 SER A 152 HIS A 165 1 14
HELIX 4 AA4 THR A 182 ALA A 198 1 17
HELIX 5 AA5 ASP A 199 ASP A 206 5 8
HELIX 6 AA6 PRO A 214 ARG A 230 1 17
HELIX 7 AA7 GLY A 231 ALA A 240 1 10
HELIX 8 AA8 ASP A 248 GLY A 252 5 5
HELIX 9 AA9 TYR A 255 ARG A 270 1 16
HELIX 10 AB1 ASP A 273 SER A 286 1 14
HELIX 11 AB2 GLY A 295 SER A 302 1 8
HELIX 12 AB3 PRO A 319 LEU A 330 1 12
HELIX 13 AB4 TYR A 343 HIS A 345 5 3
HELIX 14 AB5 ASP A 346 GLU A 351 1 6
HELIX 15 AB6 GLU A 351 HIS A 372 1 22
HELIX 16 AB7 TRP B 117 PHE B 121 5 5
HELIX 17 AB8 THR B 125 LEU B 140 1 16
HELIX 18 AB9 SER B 152 HIS B 165 1 14
HELIX 19 AC1 THR B 182 ASP B 199 1 18
HELIX 20 AC2 PRO B 200 ASP B 206 5 7
HELIX 21 AC3 PRO B 214 ARG B 230 1 17
HELIX 22 AC4 GLY B 231 ALA B 240 1 10
HELIX 23 AC5 ASP B 248 GLY B 252 5 5
HELIX 24 AC6 TYR B 255 PHE B 272 1 18
HELIX 25 AC7 ASP B 273 SER B 286 1 14
HELIX 26 AC8 GLY B 295 SER B 302 1 8
HELIX 27 AC9 ILE B 320 LEU B 330 1 11
HELIX 28 AD1 ASP B 346 GLU B 351 1 6
HELIX 29 AD2 GLU B 351 GLN B 367 1 17
SHEET 1 AA1 8 GLY A 13 THR A 21 0
SHEET 2 AA1 8 VAL A 27 TRP A 38 -1 O LEU A 28 N LEU A 20
SHEET 3 AA1 8 CYS A 91 THR A 95 -1 O ALA A 92 N TRP A 38
SHEET 4 AA1 8 VAL A 48 LEU A 52 1 N VAL A 49 O ILE A 93
SHEET 5 AA1 8 VAL A 145 GLY A 151 1 O ALA A 147 N MET A 50
SHEET 6 AA1 8 VAL A 169 LEU A 175 1 O LEU A 173 N VAL A 148
SHEET 7 AA1 8 VAL A 307 ILE A 312 1 O VAL A 308 N GLY A 172
SHEET 8 AA1 8 LEU A 336 VAL A 339 1 O VAL A 339 N GLY A 311
SHEET 1 AA2 2 ALA A 79 GLY A 80 0
SHEET 2 AA2 2 ILE A 85 ASP A 86 1 O ILE A 85 N GLY A 80
SHEET 1 AA3 8 GLY B 13 THR B 21 0
SHEET 2 AA3 8 VAL B 27 TRP B 38 -1 O ILE B 33 N VAL B 15
SHEET 3 AA3 8 CYS B 91 THR B 95 -1 O ALA B 92 N TRP B 38
SHEET 4 AA3 8 VAL B 48 LEU B 52 1 N VAL B 51 O ILE B 93
SHEET 5 AA3 8 VAL B 145 GLY B 151 1 O ALA B 147 N MET B 50
SHEET 6 AA3 8 VAL B 169 LEU B 175 1 O LEU B 175 N GLY B 150
SHEET 7 AA3 8 VAL B 307 ILE B 312 1 O VAL B 308 N GLY B 172
SHEET 8 AA3 8 LEU B 336 VAL B 339 1 O VAL B 339 N GLY B 311
SHEET 1 AA4 2 ALA B 79 GLY B 80 0
SHEET 2 AA4 2 ILE B 85 ASP B 86 1 O ILE B 85 N GLY B 80
SITE 1 AC1 11 LEU A 55 THR A 56 SER A 152 ARG A 222
SITE 2 AC1 11 TYR A 229 HIS A 345 ASP A 346 HOH A 519
SITE 3 AC1 11 HOH A 534 HOH A 547 HOH A 565
SITE 1 AC2 10 LEU B 55 THR B 56 SER B 152 ARG B 222
SITE 2 AC2 10 TYR B 229 HIS B 345 ASP B 346 LEU B 349
SITE 3 AC2 10 HOH B 534 HOH B 538
CRYST1 53.940 95.033 141.864 90.00 90.00 90.00 P 21 21 21 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 0.018539 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010523 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007049 0.00000
TER 2791 HIS A 376
TER 5494 GLN B 367
MASTER 338 0 2 29 20 0 6 6 5641 2 16 58
END
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