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HEADER HYDROLASE 09-JUN-09 3HRH
TITLE CRYSTAL STRUCTURE OF ANTIGEN 85C AND GLYCEROL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIGEN 85-C;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ANTIGEN 85 COMPLEX C, AG85C, 85C, MYCOLYL TRANSFERASE 85C,
COMPND 5 FIBRONECTIN-BINDING PROTEIN C;
COMPND 6 EC: 2.3.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: FBPC, FBPC2, MPT45, MT0137, MTCI5.03C, RV0129C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS ALPHA/BETA HYDROLASE, ACYLTRANSFERASE, SECRETED, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.BOUCAU,A.K SANKI,F.E.UMESIRI,S.J.SUCHECK,D.R.RONNING
REVDAT 2 13-JUL-11 3HRH 1 VERSN
REVDAT 1 29-SEP-09 3HRH 0
JRNL AUTH A.K.SANKI,J.BOUCAU,F.E.UMESIRI,D.R.RONNING,S.J.SUCHECK
JRNL TITL DESIGN, SYNTHESIS AND BIOLOGICAL EVALUATION OF SUGAR-DERIVED
JRNL TITL 2 ESTERS, ALPHA-KETOESTERS AND ALPHA-KETOAMIDES AS INHIBITORS
JRNL TITL 3 FOR MYCOBACTERIUM TUBERCULOSIS ANTIGEN 85C.
JRNL REF MOL BIOSYST V. 5 945 2009
JRNL REFN ISSN 1742-206X
JRNL PMID 19668859
JRNL DOI 10.1039/B902284H
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 85706.770
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 32389
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) : 0.190
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1634
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4732
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 272
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4304
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 120
REMARK 3 SOLVENT ATOMS : 103
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.70000
REMARK 3 B22 (A**2) : -6.38000
REMARK 3 B33 (A**2) : 2.68000
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) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.19
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) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.26
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.83
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) : 1.170 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.840 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.000 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.860 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 32.44
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 : GOL.PAR
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : GOL.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3HRH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUN-09.
REMARK 100 THE RCSB ID CODE IS RCSB053493.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 48.440
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.13800
REMARK 200 FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1DQY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA ACETATE AND 15% PEG 4000, PH
REMARK 280 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 33.88850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.41750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.13900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.41750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.88850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.13900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 MET A 0
REMARK 465 PHE A 1
REMARK 465 SER A 2
REMARK 465 ARG A 3
REMARK 465 PRO A 4
REMARK 465 GLY A 5
REMARK 465 LEU A 6
REMARK 465 ALA A 283
REMARK 465 THR A 284
REMARK 465 PRO A 285
REMARK 465 PRO A 286
REMARK 465 ALA A 287
REMARK 465 ALA A 288
REMARK 465 PRO A 289
REMARK 465 ALA A 290
REMARK 465 ALA A 291
REMARK 465 PRO A 292
REMARK 465 ALA A 293
REMARK 465 ALA A 294
REMARK 465 LEU A 295
REMARK 465 GLU A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 MET B 500
REMARK 465 PHE B 501
REMARK 465 SER B 502
REMARK 465 ARG B 503
REMARK 465 PRO B 504
REMARK 465 GLY B 505
REMARK 465 ALA B 783
REMARK 465 THR B 784
REMARK 465 PRO B 785
REMARK 465 PRO B 786
REMARK 465 ALA B 787
REMARK 465 ALA B 788
REMARK 465 PRO B 789
REMARK 465 ALA B 790
REMARK 465 ALA B 791
REMARK 465 PRO B 792
REMARK 465 ALA B 793
REMARK 465 ALA B 794
REMARK 465 LEU B 795
REMARK 465 GLU B 796
REMARK 465 HIS B 797
REMARK 465 HIS B 798
REMARK 465 HIS B 799
REMARK 465 HIS B 800
REMARK 465 HIS B 801
REMARK 465 HIS B 802
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 ARG A 41 35.14 -97.57
REMARK 500 PRO A 54 31.56 -93.28
REMARK 500 SER A 86 -42.52 171.08
REMARK 500 ARG A 101 -68.09 -124.20
REMARK 500 SER A 124 -118.84 47.71
REMARK 500 ASN A 152 52.49 -149.95
REMARK 500 SER A 169 77.89 -101.63
REMARK 500 SER A 215 -164.23 -118.61
REMARK 500 PHE A 254 71.66 -118.25
REMARK 500 PRO A 256 38.61 -79.47
REMARK 500 ARG B 541 32.09 -95.02
REMARK 500 PRO B 554 35.20 -90.88
REMARK 500 SER B 586 -43.52 176.09
REMARK 500 ARG B 601 -62.35 -134.67
REMARK 500 SER B 624 -120.61 50.72
REMARK 500 ASN B 652 56.01 -148.42
REMARK 500 SER B 669 78.55 -101.23
REMARK 500 MET B 677 -70.47 -75.67
REMARK 500 SER B 715 -162.94 -114.64
REMARK 500 ARG B 748 14.74 -142.41
REMARK 500 PRO B 756 45.13 -84.29
REMARK 500 ASN B 781 -66.12 -108.69
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 GOL A 862
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 874
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 875
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 878
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 861
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 863
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 865
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 866
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 868
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 869
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 870
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 871
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 872
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 873
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 876
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 877
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 879
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 880
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 881
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 882
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DQY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ANTIGEN 85C FROM MYCOBACTERIUM
REMARK 900 TUBERCULOSIS WITH DIETHYL PHOSPHATE INHIBITOR
REMARK 900 RELATED ID: 1DQZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ANTIGEN 85C FROM MYCOBACTERIUM
REMARK 900 TUBERCULOSIS
REMARK 900 RELATED ID: 1SFR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MYCOBACTERIUM TUBERCULOSIS ANTIGEN
REMARK 900 85A PROTEIN
REMARK 900 RELATED ID: 1F0N RELATED DB: PDB
REMARK 900 MYCOBACTERIUM TUBERCULOSIS ANTIGEN 85B
REMARK 900 RELATED ID: 1F0P RELATED DB: PDB
REMARK 900 MYCOBACTERIUM TUBERCULOSIS ANTIGEN 85B WITH TREHALOSE
REMARK 900 RELATED ID: 1VA5 RELATED DB: PDB
REMARK 900 ANTIGEN 85C WITH OCTYLTHIOGLUCOSIDE IN ACTIVE SITE
DBREF 3HRH A 1 294 UNP P0A4V4 A85C_MYCTU 47 340
DBREF 3HRH B 501 794 UNP P0A4V4 A85C_MYCTU 47 340
SEQADV 3HRH MET A 0 UNP P0A4V4 EXPRESSION TAG
SEQADV 3HRH LEU A 295 UNP P0A4V4 EXPRESSION TAG
SEQADV 3HRH GLU A 296 UNP P0A4V4 EXPRESSION TAG
SEQADV 3HRH HIS A 297 UNP P0A4V4 EXPRESSION TAG
SEQADV 3HRH HIS A 298 UNP P0A4V4 EXPRESSION TAG
SEQADV 3HRH HIS A 299 UNP P0A4V4 EXPRESSION TAG
SEQADV 3HRH HIS A 300 UNP P0A4V4 EXPRESSION TAG
SEQADV 3HRH HIS A 301 UNP P0A4V4 EXPRESSION TAG
SEQADV 3HRH HIS A 302 UNP P0A4V4 EXPRESSION TAG
SEQADV 3HRH MET B 500 UNP P0A4V4 EXPRESSION TAG
SEQADV 3HRH LEU B 795 UNP P0A4V4 EXPRESSION TAG
SEQADV 3HRH GLU B 796 UNP P0A4V4 EXPRESSION TAG
SEQADV 3HRH HIS B 797 UNP P0A4V4 EXPRESSION TAG
SEQADV 3HRH HIS B 798 UNP P0A4V4 EXPRESSION TAG
SEQADV 3HRH HIS B 799 UNP P0A4V4 EXPRESSION TAG
SEQADV 3HRH HIS B 800 UNP P0A4V4 EXPRESSION TAG
SEQADV 3HRH HIS B 801 UNP P0A4V4 EXPRESSION TAG
SEQADV 3HRH HIS B 802 UNP P0A4V4 EXPRESSION TAG
SEQRES 1 A 303 MET PHE SER ARG PRO GLY LEU PRO VAL GLU TYR LEU GLN
SEQRES 2 A 303 VAL PRO SER ALA SER MET GLY ARG ASP ILE LYS VAL GLN
SEQRES 3 A 303 PHE GLN GLY GLY GLY PRO HIS ALA VAL TYR LEU LEU ASP
SEQRES 4 A 303 GLY LEU ARG ALA GLN ASP ASP TYR ASN GLY TRP ASP ILE
SEQRES 5 A 303 ASN THR PRO ALA PHE GLU GLU TYR TYR GLN SER GLY LEU
SEQRES 6 A 303 SER VAL ILE MET PRO VAL GLY GLY GLN SER SER PHE TYR
SEQRES 7 A 303 THR ASP TRP TYR GLN PRO SER GLN SER ASN GLY GLN ASN
SEQRES 8 A 303 TYR THR TYR LYS TRP GLU THR PHE LEU THR ARG GLU MET
SEQRES 9 A 303 PRO ALA TRP LEU GLN ALA ASN LYS GLY VAL SER PRO THR
SEQRES 10 A 303 GLY ASN ALA ALA VAL GLY LEU SER MET SER GLY GLY SER
SEQRES 11 A 303 ALA LEU ILE LEU ALA ALA TYR TYR PRO GLN GLN PHE PRO
SEQRES 12 A 303 TYR ALA ALA SER LEU SER GLY PHE LEU ASN PRO SER GLU
SEQRES 13 A 303 GLY TRP TRP PRO THR LEU ILE GLY LEU ALA MET ASN ASP
SEQRES 14 A 303 SER GLY GLY TYR ASN ALA ASN SER MET TRP GLY PRO SER
SEQRES 15 A 303 SER ASP PRO ALA TRP LYS ARG ASN ASP PRO MET VAL GLN
SEQRES 16 A 303 ILE PRO ARG LEU VAL ALA ASN ASN THR ARG ILE TRP VAL
SEQRES 17 A 303 TYR CYS GLY ASN GLY THR PRO SER ASP LEU GLY GLY ASP
SEQRES 18 A 303 ASN ILE PRO ALA LYS PHE LEU GLU GLY LEU THR LEU ARG
SEQRES 19 A 303 THR ASN GLN THR PHE ARG ASP THR TYR ALA ALA ASP GLY
SEQRES 20 A 303 GLY ARG ASN GLY VAL PHE ASN PHE PRO PRO ASN GLY THR
SEQRES 21 A 303 HIS SER TRP PRO TYR TRP ASN GLU GLN LEU VAL ALA MET
SEQRES 22 A 303 LYS ALA ASP ILE GLN HIS VAL LEU ASN GLY ALA THR PRO
SEQRES 23 A 303 PRO ALA ALA PRO ALA ALA PRO ALA ALA LEU GLU HIS HIS
SEQRES 24 A 303 HIS HIS HIS HIS
SEQRES 1 B 303 MET PHE SER ARG PRO GLY LEU PRO VAL GLU TYR LEU GLN
SEQRES 2 B 303 VAL PRO SER ALA SER MET GLY ARG ASP ILE LYS VAL GLN
SEQRES 3 B 303 PHE GLN GLY GLY GLY PRO HIS ALA VAL TYR LEU LEU ASP
SEQRES 4 B 303 GLY LEU ARG ALA GLN ASP ASP TYR ASN GLY TRP ASP ILE
SEQRES 5 B 303 ASN THR PRO ALA PHE GLU GLU TYR TYR GLN SER GLY LEU
SEQRES 6 B 303 SER VAL ILE MET PRO VAL GLY GLY GLN SER SER PHE TYR
SEQRES 7 B 303 THR ASP TRP TYR GLN PRO SER GLN SER ASN GLY GLN ASN
SEQRES 8 B 303 TYR THR TYR LYS TRP GLU THR PHE LEU THR ARG GLU MET
SEQRES 9 B 303 PRO ALA TRP LEU GLN ALA ASN LYS GLY VAL SER PRO THR
SEQRES 10 B 303 GLY ASN ALA ALA VAL GLY LEU SER MET SER GLY GLY SER
SEQRES 11 B 303 ALA LEU ILE LEU ALA ALA TYR TYR PRO GLN GLN PHE PRO
SEQRES 12 B 303 TYR ALA ALA SER LEU SER GLY PHE LEU ASN PRO SER GLU
SEQRES 13 B 303 GLY TRP TRP PRO THR LEU ILE GLY LEU ALA MET ASN ASP
SEQRES 14 B 303 SER GLY GLY TYR ASN ALA ASN SER MET TRP GLY PRO SER
SEQRES 15 B 303 SER ASP PRO ALA TRP LYS ARG ASN ASP PRO MET VAL GLN
SEQRES 16 B 303 ILE PRO ARG LEU VAL ALA ASN ASN THR ARG ILE TRP VAL
SEQRES 17 B 303 TYR CYS GLY ASN GLY THR PRO SER ASP LEU GLY GLY ASP
SEQRES 18 B 303 ASN ILE PRO ALA LYS PHE LEU GLU GLY LEU THR LEU ARG
SEQRES 19 B 303 THR ASN GLN THR PHE ARG ASP THR TYR ALA ALA ASP GLY
SEQRES 20 B 303 GLY ARG ASN GLY VAL PHE ASN PHE PRO PRO ASN GLY THR
SEQRES 21 B 303 HIS SER TRP PRO TYR TRP ASN GLU GLN LEU VAL ALA MET
SEQRES 22 B 303 LYS ALA ASP ILE GLN HIS VAL LEU ASN GLY ALA THR PRO
SEQRES 23 B 303 PRO ALA ALA PRO ALA ALA PRO ALA ALA LEU GLU HIS HIS
SEQRES 24 B 303 HIS HIS HIS HIS
HET GOL A 862 6
HET GOL A 874 6
HET GOL A 875 6
HET GOL A 878 6
HET GOL B 861 6
HET GOL B 863 6
HET GOL B 865 6
HET GOL B 866 6
HET GOL B 868 6
HET GOL B 869 6
HET GOL B 870 6
HET GOL B 871 6
HET GOL B 872 6
HET GOL B 873 6
HET GOL B 876 6
HET GOL B 877 6
HET GOL B 879 6
HET GOL B 880 6
HET GOL B 881 6
HET GOL B 882 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 20(C3 H8 O3)
FORMUL 23 HOH *103(H2 O)
HELIX 1 1 ASN A 47 THR A 53 1 7
HELIX 2 2 PRO A 54 TYR A 59 1 6
HELIX 3 3 LYS A 94 ARG A 101 1 8
HELIX 4 4 ARG A 101 GLY A 112 1 12
HELIX 5 5 SER A 124 TYR A 137 1 14
HELIX 6 6 TRP A 157 SER A 169 1 13
HELIX 7 7 ASN A 173 GLY A 179 1 7
HELIX 8 8 PRO A 184 ASN A 189 1 6
HELIX 9 9 GLN A 194 ASN A 201 1 8
HELIX 10 10 ASN A 221 ASP A 245 1 25
HELIX 11 11 SER A 261 MET A 272 1 12
HELIX 12 12 MET A 272 ASN A 281 1 10
HELIX 13 13 ASN B 547 THR B 553 1 7
HELIX 14 14 PRO B 554 TYR B 559 1 6
HELIX 15 15 LYS B 594 ARG B 601 1 8
HELIX 16 16 ARG B 601 GLY B 612 1 12
HELIX 17 17 SER B 624 TYR B 637 1 14
HELIX 18 18 TRP B 657 SER B 669 1 13
HELIX 19 19 ASN B 673 GLY B 679 1 7
HELIX 20 20 ASP B 683 ASN B 689 1 7
HELIX 21 21 GLN B 694 ASN B 701 1 8
HELIX 22 22 ASN B 721 ASP B 745 1 25
HELIX 23 23 SER B 761 ASN B 781 1 21
SHEET 1 A 8 GLU A 9 SER A 15 0
SHEET 2 A 8 ARG A 20 GLN A 27 -1 O ILE A 22 N VAL A 13
SHEET 3 A 8 SER A 65 PRO A 69 -1 O MET A 68 N GLN A 25
SHEET 4 A 8 ALA A 33 LEU A 36 1 N VAL A 34 O SER A 65
SHEET 5 A 8 ALA A 119 LEU A 123 1 O ALA A 119 N TYR A 35
SHEET 6 A 8 TYR A 143 LEU A 147 1 O ALA A 145 N ALA A 120
SHEET 7 A 8 ARG A 204 TYR A 208 1 O TRP A 206 N SER A 146
SHEET 8 A 8 GLY A 250 ASN A 253 1 O VAL A 251 N ILE A 205
SHEET 1 B 8 VAL B 508 SER B 515 0
SHEET 2 B 8 ARG B 520 GLN B 527 -1 O PHE B 526 N GLU B 509
SHEET 3 B 8 SER B 565 PRO B 569 -1 O VAL B 566 N GLN B 527
SHEET 4 B 8 ALA B 533 LEU B 536 1 N LEU B 536 O ILE B 567
SHEET 5 B 8 ALA B 619 LEU B 623 1 O ALA B 619 N TYR B 535
SHEET 6 B 8 TYR B 643 LEU B 647 1 O ALA B 645 N ALA B 620
SHEET 7 B 8 ARG B 704 TYR B 708 1 O TRP B 706 N SER B 646
SHEET 8 B 8 GLY B 750 ASN B 753 1 O VAL B 751 N VAL B 707
SITE 1 AC1 6 GLY A 39 LEU A 40 ARG A 41 SER A 124
SITE 2 AC1 6 TRP A 262 GOL A 878
SITE 1 AC2 6 PHE A 76 TYR A 77 THR A 78 GLU A 96
SITE 2 AC2 6 LEU A 133 ASN A 189
SITE 1 AC3 5 PRO A 159 GLY A 163 ASN A 175 GLY A 179
SITE 2 AC3 5 TRP A 186
SITE 1 AC4 6 ASP A 38 ARG A 41 ALA A 42 GLN A 43
SITE 2 AC4 6 ASN A 52 GOL A 862
SITE 1 AC5 6 GLY B 539 LEU B 540 ARG B 541 SER B 624
SITE 2 AC5 6 TRP B 762 GOL B 863
SITE 1 AC6 5 ASP B 538 ARG B 541 GLN B 543 ASN B 552
SITE 2 AC6 5 GOL B 861
SITE 1 AC7 6 VAL A 199 ASP A 245 GLY A 246 TYR B 546
SITE 2 AC7 6 ASP B 550 GOL B 869
SITE 1 AC8 6 ARG B 520 ASP B 521 ILE B 522 LYS B 523
SITE 2 AC8 6 VAL B 570 TYR B 591
SITE 1 AC9 8 PRO B 507 ARG B 739 TYR B 742 GLY B 747
SITE 2 AC9 8 ARG B 748 ASN B 749 GLY B 750 PHE B 752
SITE 1 BC1 4 ARG A 248 TYR B 510 ASP B 550 GOL B 865
SITE 1 BC2 2 GLU B 767 GOL B 882
SITE 1 BC3 10 PHE B 576 MET B 625 GLY B 628 SER B 629
SITE 2 BC3 10 PHE B 650 PRO B 653 TRP B 678 ASN B 689
SITE 3 BC3 10 GOL B 872 HOH B1001
SITE 1 BC4 9 PHE B 576 TYR B 577 THR B 578 GLU B 596
SITE 2 BC4 9 ILE B 632 LEU B 633 TRP B 678 ASN B 689
SITE 3 BC4 9 GOL B 871
SITE 1 BC5 4 ALA B 609 TYR B 708 SER B 715 GLU B 767
SITE 1 BC6 6 PRO B 507 GLU B 509 GLY B 528 LYS B 611
SITE 2 BC6 6 ARG B 739 PHE B 752
SITE 1 BC7 3 ARG B 541 ALA B 542 GLN B 543
SITE 1 BC8 3 ASN A 221 ILE A 222 ARG B 541
SITE 1 BC9 3 ASN A 167 THR B 713 LYS B 725
SITE 1 CC1 3 GLU B 557 GLU B 558 HOH B1119
SITE 1 CC2 6 ALA B 605 TRP B 606 ALA B 609 ASN B 610
SITE 2 CC2 6 ALA B 771 GOL B 870
CRYST1 67.777 80.278 136.835 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 0.014754 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012457 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007308 0.00000
TER 2149 GLY A 282
TER 4306 GLY B 782
MASTER 429 0 20 23 16 0 35 6 4527 2 120 48
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