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HEADER HYDROLASE 05-MAR-18 6FW5
TITLE TESA A MAJOR THIOESTERASE FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE THIOESTERASE TESA;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.2.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS CDC1551;
SOURCE 3 ORGANISM_TAXID: 83331;
SOURCE 4 GENE: TESA, MT2998;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS THIOESTERASE, MYCOBACTERIUM TUBERCULOSIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CAMBILLAU,V.S.NGUYEN,S.CANAAN
REVDAT 1 24-OCT-18 6FW5 0
JRNL AUTH P.C.NGUYEN,V.S.NGUYEN,B.P.MARTIN,P.FOURQUET,L.CAMOIN,
JRNL AUTH 2 C.D.SPILLING,J.F.CAVALIER,C.CAMBILLAU,S.CANAAN
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF TESA, A MAJOR
JRNL TITL 2 THIOESTERASE REQUIRED FOR OUTER-ENVELOPE LIPID BIOSYNTHESIS
JRNL TITL 3 IN MYCOBACTERIUM TUBERCULOSIS.
JRNL REF J. MOL. BIOL. 2018
JRNL REFN ESSN 1089-8638
JRNL PMID 30292819
JRNL DOI 10.1016/J.JMB.2018.09.017
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 24306
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) : 0.272
REMARK 3 R VALUE (WORKING SET) : 0.271
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1216
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 12
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.19
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3026
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2942
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2874
REMARK 3 BIN R VALUE (WORKING SET) : 0.2933
REMARK 3 BIN FREE R VALUE : 0.3118
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.02
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 152
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6762
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 80
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 145.6
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 133.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.18160
REMARK 3 B22 (A**2) : 5.81830
REMARK 3 B33 (A**2) : -5.63670
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) : 0.590
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.411
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.920
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6985 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 9525 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2212 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 1193 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6985 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 932 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 8324 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.23
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.73
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 23.34
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -43.5001 71.2773 -16.7180
REMARK 3 T TENSOR
REMARK 3 T11: -0.1111 T22: 0.0262
REMARK 3 T33: 0.0161 T12: 0.0303
REMARK 3 T13: -0.0544 T23: 0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 1.1516 L22: 0.8333
REMARK 3 L33: 1.6917 L12: -0.5924
REMARK 3 L13: 0.7331 L23: -0.1689
REMARK 3 S TENSOR
REMARK 3 S11: 0.0017 S12: -0.0199 S13: -0.0265
REMARK 3 S21: -0.0884 S22: 0.0264 S23: 0.0279
REMARK 3 S31: -0.0202 S32: 0.0091 S33: -0.0281
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -33.5261 33.9504 -16.6032
REMARK 3 T TENSOR
REMARK 3 T11: -0.1030 T22: -0.0428
REMARK 3 T33: 0.0543 T12: 0.0465
REMARK 3 T13: -0.0487 T23: -0.0882
REMARK 3 L TENSOR
REMARK 3 L11: 0.0723 L22: 2.1841
REMARK 3 L33: 0.6769 L12: -0.2235
REMARK 3 L13: 0.0785 L23: 0.6302
REMARK 3 S TENSOR
REMARK 3 S11: -0.0090 S12: -0.0456 S13: -0.0260
REMARK 3 S21: -0.0168 S22: 0.0043 S23: 0.0336
REMARK 3 S31: 0.0067 S32: -0.0127 S33: 0.0047
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -24.7006 13.7677 -39.9609
REMARK 3 T TENSOR
REMARK 3 T11: 0.0594 T22: -0.0886
REMARK 3 T33: 0.0060 T12: -0.0299
REMARK 3 T13: 0.0732 T23: -0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 1.7706
REMARK 3 L33: 0.7841 L12: 0.0498
REMARK 3 L13: -0.9614 L23: 0.6060
REMARK 3 S TENSOR
REMARK 3 S11: 0.0059 S12: -0.0268 S13: -0.0024
REMARK 3 S21: -0.0550 S22: -0.0023 S23: -0.0326
REMARK 3 S31: -0.0242 S32: -0.0157 S33: -0.0036
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -64.9224 20.3277 -39.2455
REMARK 3 T TENSOR
REMARK 3 T11: 0.0856 T22: -0.0470
REMARK 3 T33: -0.0675 T12: -0.0341
REMARK 3 T13: 0.1092 T23: -0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 1.9027
REMARK 3 L33: 1.0612 L12: 0.2104
REMARK 3 L13: -0.9807 L23: 0.7230
REMARK 3 S TENSOR
REMARK 3 S11: -0.0041 S12: -0.0487 S13: -0.0317
REMARK 3 S21: -0.0543 S22: 0.0301 S23: -0.0194
REMARK 3 S31: -0.0234 S32: -0.0100 S33: -0.0260
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6FW5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009039.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24307
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 43.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 1.00000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.400
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 45% PEG 600, 0.1 M HEPES PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 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 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z+1/2
REMARK 290 7555 -X,Y+1/2,-Z+1/2
REMARK 290 8555 X,-Y+1/2,-Z+1/2
REMARK 290 9555 X+1/2,Y,Z+1/2
REMARK 290 10555 -X+1/2,-Y,Z+1/2
REMARK 290 11555 -X+1/2,Y,-Z+1/2
REMARK 290 12555 X+1/2,-Y,-Z+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z
REMARK 290 14555 -X+1/2,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y+1/2,-Z
REMARK 290 16555 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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 112.32500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 113.31000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 112.32500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 113.31000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 112.32500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 113.31000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 112.32500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 113.31000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 38.79000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 113.31000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 38.79000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 113.31000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 38.79000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 113.31000
REMARK 290 SMTRY1 12 1.000000 0.000000 0.000000 38.79000
REMARK 290 SMTRY2 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 113.31000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 38.79000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 112.32500
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 38.79000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 112.32500
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 38.79000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 112.32500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 38.79000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 112.32500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 350
REMARK 350 BIOMOLECULE: 3
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: C
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
REMARK 350 BIOMOLECULE: 4
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: D
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 LEU A 2
REMARK 465 ALA A 3
REMARK 465 ARG A 4
REMARK 465 HIS A 5
REMARK 465 GLY A 6
REMARK 465 PRO A 7
REMARK 465 ARG A 8
REMARK 465 TYR A 9
REMARK 465 GLY A 10
REMARK 465 GLY A 11
REMARK 465 SER A 12
REMARK 465 VAL A 13
REMARK 465 ASN A 14
REMARK 465 GLY A 15
REMARK 465 HIS A 16
REMARK 465 SER A 17
REMARK 465 ASP A 18
REMARK 465 ASP A 19
REMARK 465 SER A 20
REMARK 465 SER A 21
REMARK 465 GLY A 22
REMARK 465 ASP A 23
REMARK 465 ALA A 24
REMARK 465 LYS A 25
REMARK 465 GLN A 26
REMARK 465 ALA A 27
REMARK 465 ALA A 261
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 ALA B 3
REMARK 465 ARG B 4
REMARK 465 HIS B 5
REMARK 465 GLY B 6
REMARK 465 PRO B 7
REMARK 465 ARG B 8
REMARK 465 TYR B 9
REMARK 465 GLY B 10
REMARK 465 GLY B 11
REMARK 465 SER B 12
REMARK 465 VAL B 13
REMARK 465 ASN B 14
REMARK 465 GLY B 15
REMARK 465 HIS B 16
REMARK 465 SER B 17
REMARK 465 ASP B 18
REMARK 465 ASP B 19
REMARK 465 SER B 20
REMARK 465 SER B 21
REMARK 465 GLY B 22
REMARK 465 ASP B 23
REMARK 465 ALA B 24
REMARK 465 LYS B 25
REMARK 465 GLN B 26
REMARK 465 GLN B 65
REMARK 465 HIS B 66
REMARK 465 ASP B 67
REMARK 465 ARG B 68
REMARK 465 SER B 69
REMARK 465 GLY B 70
REMARK 465 LEU B 71
REMARK 465 PRO B 72
REMARK 465 PRO B 73
REMARK 465 LEU B 74
REMARK 465 ARG B 260
REMARK 465 ALA B 261
REMARK 465 MET C 1
REMARK 465 LEU C 2
REMARK 465 ALA C 3
REMARK 465 ARG C 4
REMARK 465 HIS C 5
REMARK 465 GLY C 6
REMARK 465 PRO C 7
REMARK 465 ARG C 8
REMARK 465 TYR C 9
REMARK 465 GLY C 10
REMARK 465 GLY C 11
REMARK 465 SER C 12
REMARK 465 VAL C 13
REMARK 465 ASN C 14
REMARK 465 GLY C 15
REMARK 465 HIS C 16
REMARK 465 SER C 17
REMARK 465 ASP C 18
REMARK 465 ASP C 19
REMARK 465 SER C 20
REMARK 465 SER C 21
REMARK 465 GLY C 22
REMARK 465 ASP C 23
REMARK 465 ALA C 24
REMARK 465 LYS C 25
REMARK 465 GLY C 64
REMARK 465 GLN C 65
REMARK 465 HIS C 66
REMARK 465 ASP C 67
REMARK 465 ARG C 68
REMARK 465 SER C 69
REMARK 465 GLY C 70
REMARK 465 LEU C 71
REMARK 465 PRO C 72
REMARK 465 PRO C 73
REMARK 465 LEU C 74
REMARK 465 GLY C 160
REMARK 465 MET C 161
REMARK 465 ASN C 162
REMARK 465 PRO C 163
REMARK 465 ASP C 164
REMARK 465 PHE C 165
REMARK 465 PHE C 166
REMARK 465 THR C 167
REMARK 465 ASP C 168
REMARK 465 ASP C 169
REMARK 465 GLU C 170
REMARK 465 PHE C 171
REMARK 465 PHE C 172
REMARK 465 VAL C 173
REMARK 465 ASP C 259
REMARK 465 ARG C 260
REMARK 465 ALA C 261
REMARK 465 MET D 1
REMARK 465 LEU D 2
REMARK 465 ALA D 3
REMARK 465 ARG D 4
REMARK 465 HIS D 5
REMARK 465 GLY D 6
REMARK 465 PRO D 7
REMARK 465 ARG D 8
REMARK 465 TYR D 9
REMARK 465 GLY D 10
REMARK 465 GLY D 11
REMARK 465 SER D 12
REMARK 465 VAL D 13
REMARK 465 ASN D 14
REMARK 465 GLY D 15
REMARK 465 HIS D 16
REMARK 465 SER D 17
REMARK 465 ASP D 18
REMARK 465 ASP D 19
REMARK 465 SER D 20
REMARK 465 SER D 21
REMARK 465 GLY D 22
REMARK 465 ASP D 23
REMARK 465 ALA D 24
REMARK 465 LYS D 25
REMARK 465 GLN D 26
REMARK 465 ASP D 67
REMARK 465 ARG D 68
REMARK 465 SER D 69
REMARK 465 GLY D 70
REMARK 465 LEU D 71
REMARK 465 PRO D 72
REMARK 465 ALA D 175
REMARK 465 HIS D 258
REMARK 465 ASP D 259
REMARK 465 ARG D 260
REMARK 465 ALA D 261
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 LYS A 42 CG CD CE NZ
REMARK 470 LYS A 56 CD CE NZ
REMARK 470 ARG A 93 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 141 CG CD CE NZ
REMARK 470 GLN A 144 CG CD OE1 NE2
REMARK 470 LEU A 146 CG CD1 CD2
REMARK 470 ASP A 148 CG OD1 OD2
REMARK 470 GLU A 150 CG CD OE1 OE2
REMARK 470 MET A 151 CG SD CE
REMARK 470 LEU A 154 CG CD1 CD2
REMARK 470 PHE A 155 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 165 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 166 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 176 CG CD1 CD2
REMARK 470 ARG A 180 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 42 CG CD CE NZ
REMARK 470 ARG B 123 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 144 CG CD OE1 NE2
REMARK 470 LEU B 146 CG CD1 CD2
REMARK 470 GLU B 150 CG CD OE1 OE2
REMARK 470 MET B 151 CG SD CE
REMARK 470 PHE B 155 CD1 CD2 CE1 CE2 CZ
REMARK 470 MET B 161 CG SD CE
REMARK 470 ASN B 162 CG OD1 ND2
REMARK 470 PHE B 165 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE B 166 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP B 169 CG OD1 OD2
REMARK 470 GLU B 170 CG CD OE1 OE2
REMARK 470 PHE B 171 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 255 CG CD1 CD2
REMARK 470 GLN B 256 CG CD OE1 NE2
REMARK 470 LYS C 42 CG CD CE NZ
REMARK 470 GLU C 50 CG CD OE1 OE2
REMARK 470 GLN C 118 CG CD OE1 NE2
REMARK 470 ARG C 123 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 144 CG CD OE1 NE2
REMARK 470 ARG C 180 CG CD NE CZ NH1 NH2
REMARK 470 SER C 189 OG
REMARK 470 LYS C 195 CG CD CE NZ
REMARK 470 LYS C 207 CG CD CE NZ
REMARK 470 ASP C 217 CG OD1 OD2
REMARK 470 ARG C 230 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 245 CD OE1 OE2
REMARK 470 LYS D 42 CG CD CE NZ
REMARK 470 GLU D 50 CG CD OE1 OE2
REMARK 470 ILE D 77 CG1 CG2 CD1
REMARK 470 ARG D 93 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 118 CG CD OE1 NE2
REMARK 470 LYS D 141 CG CD CE NZ
REMARK 470 GLN D 144 CG CD OE1 NE2
REMARK 470 LEU D 146 CG CD1 CD2
REMARK 470 ARG D 149 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 150 CG CD OE1 OE2
REMARK 470 MET D 151 CG SD CE
REMARK 470 PHE D 155 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 157 CG CD NE CZ NH1 NH2
REMARK 470 MET D 158 CG SD CE
REMARK 470 MET D 161 CG SD CE
REMARK 470 ASP D 164 CG OD1 OD2
REMARK 470 PHE D 165 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE D 166 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP D 168 CG OD1 OD2
REMARK 470 ASP D 169 CG OD1 OD2
REMARK 470 GLU D 170 CG CD OE1 OE2
REMARK 470 PHE D 171 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE D 172 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 180 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 183 CG CD NE CZ NH1 NH2
REMARK 470 SER D 189 OG
REMARK 470 GLU D 245 CD OE1 OE2
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 NH1 ARG A 220 NH1 ARG B 220 1.77
REMARK 500 CD GLN D 65 OE2 GLU D 83 2.10
REMARK 500 OG SER A 147 NH2 ARG A 183 2.13
REMARK 500 CA ARG C 116 OG SER C 119 2.17
REMARK 500 OE1 GLN D 65 OE2 GLU D 83 2.18
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 OD2 ASP A 164 OE2 GLU A 170 3455 1.62
REMARK 500 NH2 ARG A 157 CZ2 TRP A 209 3455 1.87
REMARK 500 NH1 ARG B 157 CZ PHE B 237 3455 1.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER A 48 C SER A 48 O 0.169
REMARK 500 ARG A 49 CA ARG A 49 C -0.218
REMARK 500 ARG A 49 CA ARG A 49 C -0.185
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 49 CA - C - O ANGL. DEV. = -13.1 DEGREES
REMARK 500 ARG A 49 CA - C - O ANGL. DEV. = -12.9 DEGREES
REMARK 500 GLU A 50 C - N - CA ANGL. DEV. = 20.4 DEGREES
REMARK 500 GLU A 50 N - CA - CB ANGL. DEV. = -12.8 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 ASP A 54 48.83 -77.43
REMARK 500 PRO A 63 90.20 -64.62
REMARK 500 GLN A 65 72.57 43.29
REMARK 500 ASP A 67 20.10 -70.61
REMARK 500 ARG A 68 109.17 -36.27
REMARK 500 ASP A 95 -66.50 -152.45
REMARK 500 PRO A 97 144.69 -30.06
REMARK 500 SER A 104 -119.47 59.57
REMARK 500 ARG A 123 73.58 60.08
REMARK 500 ALA A 131 48.80 39.00
REMARK 500 GLU A 170 -53.36 5.06
REMARK 500 PHE A 171 -53.28 -17.12
REMARK 500 PRO A 218 9.63 -65.54
REMARK 500 GLU A 225 -143.03 -104.78
REMARK 500 ASP A 235 -141.71 -104.16
REMARK 500 SER B 104 -119.71 59.55
REMARK 500 ALA B 131 48.33 39.19
REMARK 500 LYS B 141 87.18 -156.68
REMARK 500 SER B 147 -132.96 53.43
REMARK 500 ALA B 175 69.41 -156.63
REMARK 500 PRO B 218 7.70 -66.92
REMARK 500 GLU B 225 -145.73 -105.56
REMARK 500 PHE B 237 57.73 -98.41
REMARK 500 SER C 52 -126.94 52.27
REMARK 500 ALA C 53 -127.23 45.42
REMARK 500 SER C 104 -119.76 59.40
REMARK 500 ARG C 139 -4.84 82.75
REMARK 500 GLN C 144 46.65 -77.95
REMARK 500 PRO C 177 88.44 -63.57
REMARK 500 ARG C 180 -6.08 -57.50
REMARK 500 THR C 194 96.51 -68.75
REMARK 500 PRO C 218 12.81 -69.41
REMARK 500 GLU C 225 -141.06 -108.90
REMARK 500 ASP C 235 -151.37 -87.23
REMARK 500 PHE C 237 61.15 -101.09
REMARK 500 PHE D 51 -71.36 -60.33
REMARK 500 ILE D 94 23.62 -66.46
REMARK 500 SER D 104 -119.96 58.14
REMARK 500 ARG D 139 -3.13 85.73
REMARK 500 LEU D 146 -14.46 -144.68
REMARK 500 MET D 158 -116.62 74.00
REMARK 500 PRO D 218 10.05 -67.99
REMARK 500 GLU D 226 156.86 -48.70
REMARK 500 ASP D 235 -154.58 -82.25
REMARK 500 PHE D 237 50.09 -100.75
REMARK 500 ASN D 242 61.33 -114.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLU A 170 10.35
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 B 422 DISTANCE = 8.66 ANGSTROMS
REMARK 525 HOH C 410 DISTANCE = 6.74 ANGSTROMS
REMARK 525 HOH D 411 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH D 412 DISTANCE = 6.44 ANGSTROMS
REMARK 525 HOH D 413 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH D 414 DISTANCE = 8.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ARG B 157 and PHE B
REMARK 800 237
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PO4 B 301 and SER B
REMARK 800 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PO4 C 301 and SER C
REMARK 800 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PO4 D 301 and SER D
REMARK 800 104
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6FVJ RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEX
DBREF 6FW5 A 1 261 UNP P9WQD4 TESA_MYCTO 1 261
DBREF 6FW5 B 1 261 UNP P9WQD4 TESA_MYCTO 1 261
DBREF 6FW5 C 1 261 UNP P9WQD4 TESA_MYCTO 1 261
DBREF 6FW5 D 1 261 UNP P9WQD4 TESA_MYCTO 1 261
SEQRES 1 A 261 MET LEU ALA ARG HIS GLY PRO ARG TYR GLY GLY SER VAL
SEQRES 2 A 261 ASN GLY HIS SER ASP ASP SER SER GLY ASP ALA LYS GLN
SEQRES 3 A 261 ALA ALA PRO THR LEU TYR ILE PHE PRO HIS ALA GLY GLY
SEQRES 4 A 261 THR ALA LYS ASP TYR VAL ALA PHE SER ARG GLU PHE SER
SEQRES 5 A 261 ALA ASP VAL LYS ARG ILE ALA VAL GLN TYR PRO GLY GLN
SEQRES 6 A 261 HIS ASP ARG SER GLY LEU PRO PRO LEU GLU SER ILE PRO
SEQRES 7 A 261 THR LEU ALA ASP GLU ILE PHE ALA MET MET LYS PRO SER
SEQRES 8 A 261 ALA ARG ILE ASP ASP PRO VAL ALA PHE PHE GLY HIS SER
SEQRES 9 A 261 MET GLY GLY MET LEU ALA PHE GLU VAL ALA LEU ARG TYR
SEQRES 10 A 261 GLN SER ALA GLY HIS ARG VAL LEU ALA PHE PHE VAL SER
SEQRES 11 A 261 ALA CYS SER ALA PRO GLY HIS ILE ARG TYR LYS GLN LEU
SEQRES 12 A 261 GLN ASP LEU SER ASP ARG GLU MET LEU ASP LEU PHE THR
SEQRES 13 A 261 ARG MET THR GLY MET ASN PRO ASP PHE PHE THR ASP ASP
SEQRES 14 A 261 GLU PHE PHE VAL GLY ALA LEU PRO THR LEU ARG ALA VAL
SEQRES 15 A 261 ARG ALA ILE ALA GLY TYR SER CYS PRO PRO GLU THR LYS
SEQRES 16 A 261 LEU SER CYS PRO ILE TYR ALA PHE ILE GLY ASP LYS ASP
SEQRES 17 A 261 TRP ILE ALA THR GLN ASP ASP MET ASP PRO TRP ARG ASP
SEQRES 18 A 261 ARG THR THR GLU GLU PHE SER ILE ARG VAL PHE PRO GLY
SEQRES 19 A 261 ASP HIS PHE TYR LEU ASN ASP ASN LEU PRO GLU LEU VAL
SEQRES 20 A 261 SER ASP ILE GLU ASP LYS THR LEU GLN TRP HIS ASP ARG
SEQRES 21 A 261 ALA
SEQRES 1 B 261 MET LEU ALA ARG HIS GLY PRO ARG TYR GLY GLY SER VAL
SEQRES 2 B 261 ASN GLY HIS SER ASP ASP SER SER GLY ASP ALA LYS GLN
SEQRES 3 B 261 ALA ALA PRO THR LEU TYR ILE PHE PRO HIS ALA GLY GLY
SEQRES 4 B 261 THR ALA LYS ASP TYR VAL ALA PHE SER ARG GLU PHE SER
SEQRES 5 B 261 ALA ASP VAL LYS ARG ILE ALA VAL GLN TYR PRO GLY GLN
SEQRES 6 B 261 HIS ASP ARG SER GLY LEU PRO PRO LEU GLU SER ILE PRO
SEQRES 7 B 261 THR LEU ALA ASP GLU ILE PHE ALA MET MET LYS PRO SER
SEQRES 8 B 261 ALA ARG ILE ASP ASP PRO VAL ALA PHE PHE GLY HIS SER
SEQRES 9 B 261 MET GLY GLY MET LEU ALA PHE GLU VAL ALA LEU ARG TYR
SEQRES 10 B 261 GLN SER ALA GLY HIS ARG VAL LEU ALA PHE PHE VAL SER
SEQRES 11 B 261 ALA CYS SER ALA PRO GLY HIS ILE ARG TYR LYS GLN LEU
SEQRES 12 B 261 GLN ASP LEU SER ASP ARG GLU MET LEU ASP LEU PHE THR
SEQRES 13 B 261 ARG MET THR GLY MET ASN PRO ASP PHE PHE THR ASP ASP
SEQRES 14 B 261 GLU PHE PHE VAL GLY ALA LEU PRO THR LEU ARG ALA VAL
SEQRES 15 B 261 ARG ALA ILE ALA GLY TYR SER CYS PRO PRO GLU THR LYS
SEQRES 16 B 261 LEU SER CYS PRO ILE TYR ALA PHE ILE GLY ASP LYS ASP
SEQRES 17 B 261 TRP ILE ALA THR GLN ASP ASP MET ASP PRO TRP ARG ASP
SEQRES 18 B 261 ARG THR THR GLU GLU PHE SER ILE ARG VAL PHE PRO GLY
SEQRES 19 B 261 ASP HIS PHE TYR LEU ASN ASP ASN LEU PRO GLU LEU VAL
SEQRES 20 B 261 SER ASP ILE GLU ASP LYS THR LEU GLN TRP HIS ASP ARG
SEQRES 21 B 261 ALA
SEQRES 1 C 261 MET LEU ALA ARG HIS GLY PRO ARG TYR GLY GLY SER VAL
SEQRES 2 C 261 ASN GLY HIS SER ASP ASP SER SER GLY ASP ALA LYS GLN
SEQRES 3 C 261 ALA ALA PRO THR LEU TYR ILE PHE PRO HIS ALA GLY GLY
SEQRES 4 C 261 THR ALA LYS ASP TYR VAL ALA PHE SER ARG GLU PHE SER
SEQRES 5 C 261 ALA ASP VAL LYS ARG ILE ALA VAL GLN TYR PRO GLY GLN
SEQRES 6 C 261 HIS ASP ARG SER GLY LEU PRO PRO LEU GLU SER ILE PRO
SEQRES 7 C 261 THR LEU ALA ASP GLU ILE PHE ALA MET MET LYS PRO SER
SEQRES 8 C 261 ALA ARG ILE ASP ASP PRO VAL ALA PHE PHE GLY HIS SER
SEQRES 9 C 261 MET GLY GLY MET LEU ALA PHE GLU VAL ALA LEU ARG TYR
SEQRES 10 C 261 GLN SER ALA GLY HIS ARG VAL LEU ALA PHE PHE VAL SER
SEQRES 11 C 261 ALA CYS SER ALA PRO GLY HIS ILE ARG TYR LYS GLN LEU
SEQRES 12 C 261 GLN ASP LEU SER ASP ARG GLU MET LEU ASP LEU PHE THR
SEQRES 13 C 261 ARG MET THR GLY MET ASN PRO ASP PHE PHE THR ASP ASP
SEQRES 14 C 261 GLU PHE PHE VAL GLY ALA LEU PRO THR LEU ARG ALA VAL
SEQRES 15 C 261 ARG ALA ILE ALA GLY TYR SER CYS PRO PRO GLU THR LYS
SEQRES 16 C 261 LEU SER CYS PRO ILE TYR ALA PHE ILE GLY ASP LYS ASP
SEQRES 17 C 261 TRP ILE ALA THR GLN ASP ASP MET ASP PRO TRP ARG ASP
SEQRES 18 C 261 ARG THR THR GLU GLU PHE SER ILE ARG VAL PHE PRO GLY
SEQRES 19 C 261 ASP HIS PHE TYR LEU ASN ASP ASN LEU PRO GLU LEU VAL
SEQRES 20 C 261 SER ASP ILE GLU ASP LYS THR LEU GLN TRP HIS ASP ARG
SEQRES 21 C 261 ALA
SEQRES 1 D 261 MET LEU ALA ARG HIS GLY PRO ARG TYR GLY GLY SER VAL
SEQRES 2 D 261 ASN GLY HIS SER ASP ASP SER SER GLY ASP ALA LYS GLN
SEQRES 3 D 261 ALA ALA PRO THR LEU TYR ILE PHE PRO HIS ALA GLY GLY
SEQRES 4 D 261 THR ALA LYS ASP TYR VAL ALA PHE SER ARG GLU PHE SER
SEQRES 5 D 261 ALA ASP VAL LYS ARG ILE ALA VAL GLN TYR PRO GLY GLN
SEQRES 6 D 261 HIS ASP ARG SER GLY LEU PRO PRO LEU GLU SER ILE PRO
SEQRES 7 D 261 THR LEU ALA ASP GLU ILE PHE ALA MET MET LYS PRO SER
SEQRES 8 D 261 ALA ARG ILE ASP ASP PRO VAL ALA PHE PHE GLY HIS SER
SEQRES 9 D 261 MET GLY GLY MET LEU ALA PHE GLU VAL ALA LEU ARG TYR
SEQRES 10 D 261 GLN SER ALA GLY HIS ARG VAL LEU ALA PHE PHE VAL SER
SEQRES 11 D 261 ALA CYS SER ALA PRO GLY HIS ILE ARG TYR LYS GLN LEU
SEQRES 12 D 261 GLN ASP LEU SER ASP ARG GLU MET LEU ASP LEU PHE THR
SEQRES 13 D 261 ARG MET THR GLY MET ASN PRO ASP PHE PHE THR ASP ASP
SEQRES 14 D 261 GLU PHE PHE VAL GLY ALA LEU PRO THR LEU ARG ALA VAL
SEQRES 15 D 261 ARG ALA ILE ALA GLY TYR SER CYS PRO PRO GLU THR LYS
SEQRES 16 D 261 LEU SER CYS PRO ILE TYR ALA PHE ILE GLY ASP LYS ASP
SEQRES 17 D 261 TRP ILE ALA THR GLN ASP ASP MET ASP PRO TRP ARG ASP
SEQRES 18 D 261 ARG THR THR GLU GLU PHE SER ILE ARG VAL PHE PRO GLY
SEQRES 19 D 261 ASP HIS PHE TYR LEU ASN ASP ASN LEU PRO GLU LEU VAL
SEQRES 20 D 261 SER ASP ILE GLU ASP LYS THR LEU GLN TRP HIS ASP ARG
SEQRES 21 D 261 ALA
HET PO4 A 301 5
HET PO4 B 301 5
HET PO4 C 301 5
HET PO4 D 301 5
HETNAM PO4 PHOSPHATE ION
FORMUL 5 PO4 4(O4 P 3-)
FORMUL 9 HOH *80(H2 O)
HELIX 1 AA1 TYR A 44 GLU A 50 1 7
HELIX 2 AA2 SER A 76 LYS A 89 1 14
HELIX 3 AA3 PRO A 90 ALA A 92 5 3
HELIX 4 AA4 SER A 104 SER A 119 1 16
HELIX 5 AA5 LEU A 146 MET A 158 1 13
HELIX 6 AA6 MET A 161 THR A 167 1 7
HELIX 7 AA7 GLU A 170 TYR A 188 1 19
HELIX 8 AA8 THR A 212 ASP A 217 1 6
HELIX 9 AA9 PRO A 218 THR A 223 5 6
HELIX 10 AB1 PHE A 237 ASP A 241 5 5
HELIX 11 AB2 ASN A 242 ASP A 259 1 18
HELIX 12 AB3 TYR B 44 ARG B 49 1 6
HELIX 13 AB4 SER B 76 LYS B 89 1 14
HELIX 14 AB5 PRO B 90 ALA B 92 5 3
HELIX 15 AB6 MET B 105 SER B 119 1 15
HELIX 16 AB7 SER B 147 LEU B 154 1 8
HELIX 17 AB8 MET B 161 PHE B 166 1 6
HELIX 18 AB9 GLU B 170 LEU B 176 1 7
HELIX 19 AC1 LEU B 176 TYR B 188 1 13
HELIX 20 AC2 THR B 212 ASP B 217 1 6
HELIX 21 AC3 PRO B 218 THR B 223 5 6
HELIX 22 AC4 LEU B 243 LEU B 255 1 13
HELIX 23 AC5 TYR C 44 GLU C 50 1 7
HELIX 24 AC6 SER C 76 LYS C 89 1 14
HELIX 25 AC7 PRO C 90 ALA C 92 5 3
HELIX 26 AC8 SER C 104 GLY C 121 1 18
HELIX 27 AC9 LEU C 146 MET C 158 1 13
HELIX 28 AD1 THR C 178 ARG C 180 5 3
HELIX 29 AD2 ALA C 181 GLY C 187 1 7
HELIX 30 AD3 THR C 212 ASP C 217 1 6
HELIX 31 AD4 PRO C 218 ASP C 221 5 4
HELIX 32 AD5 ASN C 242 HIS C 258 1 17
HELIX 33 AD6 TYR D 44 GLU D 50 1 7
HELIX 34 AD7 SER D 76 LYS D 89 1 14
HELIX 35 AD8 SER D 104 SER D 119 1 16
HELIX 36 AD9 ARG D 149 PHE D 155 1 7
HELIX 37 AE1 PRO D 163 GLY D 174 1 12
HELIX 38 AE2 THR D 178 TYR D 188 1 11
HELIX 39 AE3 THR D 212 ASP D 217 1 6
HELIX 40 AE4 PRO D 218 THR D 223 5 6
HELIX 41 AE5 PHE D 237 ASP D 241 5 5
HELIX 42 AE6 ASN D 242 GLN D 256 1 15
SHEET 1 AA1 6 LYS A 56 ALA A 59 0
SHEET 2 AA1 6 THR A 30 PHE A 34 1 N LEU A 31 O LYS A 56
SHEET 3 AA1 6 VAL A 98 HIS A 103 1 O PHE A 101 N TYR A 32
SHEET 4 AA1 6 VAL A 124 SER A 130 1 O LEU A 125 N VAL A 98
SHEET 5 AA1 6 ILE A 200 GLY A 205 1 O TYR A 201 N PHE A 127
SHEET 6 AA1 6 PHE A 227 PHE A 232 1 O PHE A 232 N ILE A 204
SHEET 1 AA2 6 ARG B 57 ALA B 59 0
SHEET 2 AA2 6 THR B 30 PHE B 34 1 N ILE B 33 O ILE B 58
SHEET 3 AA2 6 PRO B 97 HIS B 103 1 O PHE B 101 N TYR B 32
SHEET 4 AA2 6 ARG B 123 SER B 130 1 O PHE B 128 N PHE B 100
SHEET 5 AA2 6 ILE B 200 GLY B 205 1 O TYR B 201 N PHE B 127
SHEET 6 AA2 6 PHE B 227 PHE B 232 1 O PHE B 232 N ILE B 204
SHEET 1 AA3 6 LYS C 56 ALA C 59 0
SHEET 2 AA3 6 THR C 30 PHE C 34 1 N LEU C 31 O LYS C 56
SHEET 3 AA3 6 VAL C 98 HIS C 103 1 O PHE C 101 N TYR C 32
SHEET 4 AA3 6 VAL C 124 SER C 130 1 O PHE C 128 N PHE C 100
SHEET 5 AA3 6 ILE C 200 GLY C 205 1 O TYR C 201 N VAL C 129
SHEET 6 AA3 6 PHE C 227 PHE C 232 1 O PHE C 232 N ILE C 204
SHEET 1 AA4 6 LYS D 56 ALA D 59 0
SHEET 2 AA4 6 THR D 30 PHE D 34 1 N LEU D 31 O LYS D 56
SHEET 3 AA4 6 VAL D 98 HIS D 103 1 O PHE D 101 N TYR D 32
SHEET 4 AA4 6 VAL D 124 SER D 130 1 O LEU D 125 N VAL D 98
SHEET 5 AA4 6 ILE D 200 GLY D 205 1 O TYR D 201 N PHE D 127
SHEET 6 AA4 6 PHE D 227 PHE D 232 1 O SER D 228 N ALA D 202
LINK CB SER A 104 O3 PO4 A 301 1555 1555 1.46
LINK CB SER B 104 O2 PO4 B 301 1555 1555 1.52
LINK CB SER C 104 O1 PO4 C 301 1555 1555 1.42
LINK CB SER D 104 O1 PO4 D 301 1555 1555 1.42
LINK NH1 ARG B 157 CE2 PHE B 237 1555 3455 1.50
SITE 1 AC1 5 HIS A 36 ALA A 37 SER A 104 MET A 105
SITE 2 AC1 5 HIS A 236
SITE 1 AC2 9 ASP B 153 LEU B 154 PHE B 155 THR B 156
SITE 2 AC2 9 MET B 158 ASP B 235 HIS B 236 TYR B 238
SITE 3 AC2 9 LEU B 239
SITE 1 AC3 10 HIS B 36 ALA B 37 HIS B 103 MET B 105
SITE 2 AC3 10 GLY B 106 GLY B 107 SER B 130 ALA B 131
SITE 3 AC3 10 CYS B 132 HIS B 236
SITE 1 AC4 10 HIS C 36 ALA C 37 HIS C 103 MET C 105
SITE 2 AC4 10 GLY C 106 GLY C 107 SER C 130 ALA C 131
SITE 3 AC4 10 CYS C 132 HIS C 236
SITE 1 AC5 10 HIS D 36 ALA D 37 HIS D 103 MET D 105
SITE 2 AC5 10 GLY D 106 GLY D 107 SER D 130 ALA D 131
SITE 3 AC5 10 CYS D 132 HIS D 236
CRYST1 77.580 224.650 226.620 90.00 90.00 90.00 F 2 2 2 64
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 0.012890 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004451 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004413 0.00000
TER 1800 ARG A 260
TER 3505 ASP B 259
TER 5107 HIS C 258
TER 6774 TRP D 257
MASTER 793 0 4 42 24 0 14 6 6862 4 24 84
END |