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HEADER HYDROLASE 19-APR-22 7ZM2
TITLE CRYSTAL STRUCTURE OF HSAD FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX
TITLE 2 WITH CYCLOPHOSTIN-LIKE INHIBITOR CYC8B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4,5:9,10-DISECO-3-HYDROXY-5,9,17-TRIOXOANDROSTA-1(10),2-
COMPND 3 DIENE-4-OATE HYDROLASE;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: 2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOATE HYDROLASE,HOPDA
COMPND 6 HYDROLASE,META-CLEAVAGE PRODUCT HYDROLASE,MCP HYDROLASE;
COMPND 7 EC: 3.7.1.17,3.7.1.8;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS H37RV;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 GENE: HSAD, BPHD, RV3569C;
SOURCE 5 EXPRESSION_SYSTEM: MYCOLICIBACTERIUM SMEGMATIS MC2 155;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 246196
KEYWDS HSAD, M. TUBERCULOSIS, CHOLESTEROL, INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BARELIER,V.ROIG-ZAMBONI,J.F.CAVALIER,G.SULZENBACHER
REVDAT 1 28-SEP-22 7ZM2 0
JRNL AUTH S.BARELIER,R.AVELLAN,G.R.GNAWALI,P.FOURQUET,V.ROIG-ZAMBONI,
JRNL AUTH 2 I.PONCIN,V.POINT,S.AUDEBERT,L.CAMOIN,C.D.SPILLING,S.CANAAN,
JRNL AUTH 3 J.F.CAVALIER,G.SULZENBACHER,Y.BOURNE
JRNL TITL DIRECT CAPTURE, INHIBITION AND CRYSTAL STRUCTURE OF HSAD
JRNL TITL 2 (RV3569C) FROM M. TUBERCULOSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 34964
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1853
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2545
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.63
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 131
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4388
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 108
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.44
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.80000
REMARK 3 B22 (A**2) : 0.29000
REMARK 3 B33 (A**2) : 0.51000
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): 0.204
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.180
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.134
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.451
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4524 ; 0.014 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4288 ; 0.001 ; 0.015
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6126 ; 1.808 ; 1.637
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9806 ; 1.389 ; 1.578
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 566 ; 7.071 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 248 ;29.786 ;20.645
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 712 ;13.847 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;16.408 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 542 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5172 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1116 ; 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 : 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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7ZM2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-APR-22.
REMARK 100 THE DEPOSITION ID IS D_1292122335.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980114
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.7
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36843
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 45.260
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.40
REMARK 200 R MERGE (I) : 0.15700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 11.40
REMARK 200 R MERGE FOR SHELL (I) : 1.34900
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.3
REMARK 200 STARTING MODEL: 7ZJT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES NA 0.1 M NH4SO4 1.656 M PEG400
REMARK 280 5.76%, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-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 52.95700
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 52.95700
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
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -193.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 153.66800
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 158.87100
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 153.66800
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 174.37400
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 52.95700
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 174.37400
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 105.91400
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 THR A 2
REMARK 465 ALA A 3
REMARK 465 THR A 4
REMARK 465 GLU A 5
REMARK 465 GLU A 6
REMARK 465 ARG A 291
REMARK 465 LYS A 292
REMARK 465 LEU A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 THR B 4
REMARK 465 GLU B 5
REMARK 465 GLU B 6
REMARK 465 ARG B 291
REMARK 465 LYS B 292
REMARK 465 LEU B 293
REMARK 465 HIS B 294
REMARK 465 HIS B 295
REMARK 465 HIS B 296
REMARK 465 HIS B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
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 GLU A 218 CD GLU A 218 OE2 0.067
REMARK 500 GLU B 278 CD GLU B 278 OE1 0.080
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 224 NE - CZ - NH2 ANGL. DEV. = -3.9 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 GLN A 87 118.98 -39.57
REMARK 500 SER A 114 -118.67 55.48
REMARK 500 THR A 198 140.01 -37.32
REMARK 500 ALA A 213 65.77 -108.44
REMARK 500 SER B 114 -117.35 60.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 9SW A 301
REMARK 610 9SW B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7ZJT RELATED DB: PDB
REMARK 900 7ZJT CONTAINS THE NATIVE STRUCTURE
REMARK 900 RELATED ID: 7ZM1 RELATED DB: PDB
DBREF 7ZM2 A 1 291 UNP P9WNH5 HSAD_MYCTU 1 291
DBREF 7ZM2 B 1 291 UNP P9WNH5 HSAD_MYCTU 1 291
SEQADV 7ZM2 LYS A 292 UNP P9WNH5 EXPRESSION TAG
SEQADV 7ZM2 LEU A 293 UNP P9WNH5 EXPRESSION TAG
SEQADV 7ZM2 HIS A 294 UNP P9WNH5 EXPRESSION TAG
SEQADV 7ZM2 HIS A 295 UNP P9WNH5 EXPRESSION TAG
SEQADV 7ZM2 HIS A 296 UNP P9WNH5 EXPRESSION TAG
SEQADV 7ZM2 HIS A 297 UNP P9WNH5 EXPRESSION TAG
SEQADV 7ZM2 HIS A 298 UNP P9WNH5 EXPRESSION TAG
SEQADV 7ZM2 HIS A 299 UNP P9WNH5 EXPRESSION TAG
SEQADV 7ZM2 LYS B 292 UNP P9WNH5 EXPRESSION TAG
SEQADV 7ZM2 LEU B 293 UNP P9WNH5 EXPRESSION TAG
SEQADV 7ZM2 HIS B 294 UNP P9WNH5 EXPRESSION TAG
SEQADV 7ZM2 HIS B 295 UNP P9WNH5 EXPRESSION TAG
SEQADV 7ZM2 HIS B 296 UNP P9WNH5 EXPRESSION TAG
SEQADV 7ZM2 HIS B 297 UNP P9WNH5 EXPRESSION TAG
SEQADV 7ZM2 HIS B 298 UNP P9WNH5 EXPRESSION TAG
SEQADV 7ZM2 HIS B 299 UNP P9WNH5 EXPRESSION TAG
SEQRES 1 A 299 MET THR ALA THR GLU GLU LEU THR PHE GLU SER THR SER
SEQRES 2 A 299 ARG PHE ALA GLU VAL ASP VAL ASP GLY PRO LEU LYS LEU
SEQRES 3 A 299 HIS TYR HIS GLU ALA GLY VAL GLY ASN ASP GLN THR VAL
SEQRES 4 A 299 VAL LEU LEU HIS GLY GLY GLY PRO GLY ALA ALA SER TRP
SEQRES 5 A 299 THR ASN PHE SER ARG ASN ILE ALA VAL LEU ALA ARG HIS
SEQRES 6 A 299 PHE HIS VAL LEU ALA VAL ASP GLN PRO GLY TYR GLY HIS
SEQRES 7 A 299 SER ASP LYS ARG ALA GLU HIS GLY GLN PHE ASN ARG TYR
SEQRES 8 A 299 ALA ALA MET ALA LEU LYS GLY LEU PHE ASP GLN LEU GLY
SEQRES 9 A 299 LEU GLY ARG VAL PRO LEU VAL GLY ASN SER LEU GLY GLY
SEQRES 10 A 299 GLY THR ALA VAL ARG PHE ALA LEU ASP TYR PRO ALA ARG
SEQRES 11 A 299 ALA GLY ARG LEU VAL LEU MET GLY PRO GLY GLY LEU SER
SEQRES 12 A 299 ILE ASN LEU PHE ALA PRO ASP PRO THR GLU GLY VAL LYS
SEQRES 13 A 299 ARG LEU SER LYS PHE SER VAL ALA PRO THR ARG GLU ASN
SEQRES 14 A 299 LEU GLU ALA PHE LEU ARG VAL MET VAL TYR ASP LYS ASN
SEQRES 15 A 299 LEU ILE THR PRO GLU LEU VAL ASP GLN ARG PHE ALA LEU
SEQRES 16 A 299 ALA SER THR PRO GLU SER LEU THR ALA THR ARG ALA MET
SEQRES 17 A 299 GLY LYS SER PHE ALA GLY ALA ASP PHE GLU ALA GLY MET
SEQRES 18 A 299 MET TRP ARG GLU VAL TYR ARG LEU ARG GLN PRO VAL LEU
SEQRES 19 A 299 LEU ILE TRP GLY ARG GLU ASP ARG VAL ASN PRO LEU ASP
SEQRES 20 A 299 GLY ALA LEU VAL ALA LEU LYS THR ILE PRO ARG ALA GLN
SEQRES 21 A 299 LEU HIS VAL PHE GLY GLN CYS GLY HIS TRP VAL GLN VAL
SEQRES 22 A 299 GLU LYS PHE ASP GLU PHE ASN LYS LEU THR ILE GLU PHE
SEQRES 23 A 299 LEU GLY GLY GLY ARG LYS LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 299 MET THR ALA THR GLU GLU LEU THR PHE GLU SER THR SER
SEQRES 2 B 299 ARG PHE ALA GLU VAL ASP VAL ASP GLY PRO LEU LYS LEU
SEQRES 3 B 299 HIS TYR HIS GLU ALA GLY VAL GLY ASN ASP GLN THR VAL
SEQRES 4 B 299 VAL LEU LEU HIS GLY GLY GLY PRO GLY ALA ALA SER TRP
SEQRES 5 B 299 THR ASN PHE SER ARG ASN ILE ALA VAL LEU ALA ARG HIS
SEQRES 6 B 299 PHE HIS VAL LEU ALA VAL ASP GLN PRO GLY TYR GLY HIS
SEQRES 7 B 299 SER ASP LYS ARG ALA GLU HIS GLY GLN PHE ASN ARG TYR
SEQRES 8 B 299 ALA ALA MET ALA LEU LYS GLY LEU PHE ASP GLN LEU GLY
SEQRES 9 B 299 LEU GLY ARG VAL PRO LEU VAL GLY ASN SER LEU GLY GLY
SEQRES 10 B 299 GLY THR ALA VAL ARG PHE ALA LEU ASP TYR PRO ALA ARG
SEQRES 11 B 299 ALA GLY ARG LEU VAL LEU MET GLY PRO GLY GLY LEU SER
SEQRES 12 B 299 ILE ASN LEU PHE ALA PRO ASP PRO THR GLU GLY VAL LYS
SEQRES 13 B 299 ARG LEU SER LYS PHE SER VAL ALA PRO THR ARG GLU ASN
SEQRES 14 B 299 LEU GLU ALA PHE LEU ARG VAL MET VAL TYR ASP LYS ASN
SEQRES 15 B 299 LEU ILE THR PRO GLU LEU VAL ASP GLN ARG PHE ALA LEU
SEQRES 16 B 299 ALA SER THR PRO GLU SER LEU THR ALA THR ARG ALA MET
SEQRES 17 B 299 GLY LYS SER PHE ALA GLY ALA ASP PHE GLU ALA GLY MET
SEQRES 18 B 299 MET TRP ARG GLU VAL TYR ARG LEU ARG GLN PRO VAL LEU
SEQRES 19 B 299 LEU ILE TRP GLY ARG GLU ASP ARG VAL ASN PRO LEU ASP
SEQRES 20 B 299 GLY ALA LEU VAL ALA LEU LYS THR ILE PRO ARG ALA GLN
SEQRES 21 B 299 LEU HIS VAL PHE GLY GLN CYS GLY HIS TRP VAL GLN VAL
SEQRES 22 B 299 GLU LYS PHE ASP GLU PHE ASN LYS LEU THR ILE GLU PHE
SEQRES 23 B 299 LEU GLY GLY GLY ARG LYS LEU HIS HIS HIS HIS HIS HIS
HET 9SW A 301 5
HET SO4 A 302 5
HET SO4 A 303 5
HET SO4 A 304 5
HET 9SW B 301 5
HET SO4 B 302 5
HET SO4 B 303 5
HETNAM 9SW METHOXY-[(3~{R})-3-[(2~{R})-1-METHOXY-1,3-
HETNAM 2 9SW BIS(OXIDANYLIDENE)BUTAN-2-YL]PENTADECYL]PHOSPHINIC
HETNAM 3 9SW ACID
HETNAM SO4 SULFATE ION
FORMUL 3 9SW 2(C21 H41 O6 P)
FORMUL 4 SO4 5(O4 S 2-)
FORMUL 10 HOH *108(H2 O)
HELIX 1 AA1 THR A 8 THR A 12 1 5
HELIX 2 AA2 ALA A 50 PHE A 55 1 6
HELIX 3 AA3 ASN A 58 ARG A 64 1 7
HELIX 4 AA4 GLN A 87 GLY A 104 1 18
HELIX 5 AA5 SER A 114 TYR A 127 1 14
HELIX 6 AA6 THR A 152 ALA A 164 1 13
HELIX 7 AA7 THR A 166 VAL A 176 1 11
HELIX 8 AA8 ASP A 180 ILE A 184 5 5
HELIX 9 AA9 THR A 185 THR A 198 1 14
HELIX 10 AB1 THR A 198 SER A 211 1 14
HELIX 11 AB2 ASP A 216 LEU A 229 5 14
HELIX 12 AB3 PRO A 245 GLY A 248 5 4
HELIX 13 AB4 ALA A 249 ILE A 256 1 8
HELIX 14 AB5 TRP A 270 LYS A 275 1 6
HELIX 15 AB6 LYS A 275 LEU A 287 1 13
HELIX 16 AB7 THR B 8 THR B 12 1 5
HELIX 17 AB8 ALA B 50 ARG B 64 1 15
HELIX 18 AB9 GLN B 87 LEU B 103 1 17
HELIX 19 AC1 SER B 114 TYR B 127 1 14
HELIX 20 AC2 THR B 152 ALA B 164 1 13
HELIX 21 AC3 THR B 166 VAL B 176 1 11
HELIX 22 AC4 ASP B 180 ILE B 184 5 5
HELIX 23 AC5 THR B 185 SER B 197 1 13
HELIX 24 AC6 THR B 198 ALA B 213 1 16
HELIX 25 AC7 ASP B 216 LEU B 229 5 14
HELIX 26 AC8 PRO B 245 GLY B 248 5 4
HELIX 27 AC9 ALA B 249 ILE B 256 1 8
HELIX 28 AD1 TRP B 270 LYS B 275 1 6
HELIX 29 AD2 LYS B 275 LEU B 287 1 13
SHEET 1 AA1 8 SER A 13 ASP A 19 0
SHEET 2 AA1 8 PRO A 23 ALA A 31 -1 O LEU A 24 N VAL A 18
SHEET 3 AA1 8 HIS A 67 VAL A 71 -1 O VAL A 68 N ALA A 31
SHEET 4 AA1 8 THR A 38 LEU A 42 1 N LEU A 41 O LEU A 69
SHEET 5 AA1 8 VAL A 108 ASN A 113 1 O VAL A 111 N VAL A 40
SHEET 6 AA1 8 ALA A 131 MET A 137 1 O VAL A 135 N GLY A 112
SHEET 7 AA1 8 VAL A 233 GLY A 238 1 O ILE A 236 N LEU A 136
SHEET 8 AA1 8 ALA A 259 PHE A 264 1 O GLN A 260 N LEU A 235
SHEET 1 AA2 8 SER B 13 ASP B 19 0
SHEET 2 AA2 8 PRO B 23 ALA B 31 -1 O LEU B 24 N VAL B 18
SHEET 3 AA2 8 HIS B 67 VAL B 71 -1 O ALA B 70 N HIS B 29
SHEET 4 AA2 8 THR B 38 LEU B 42 1 N LEU B 41 O LEU B 69
SHEET 5 AA2 8 VAL B 108 ASN B 113 1 O VAL B 111 N LEU B 42
SHEET 6 AA2 8 ALA B 131 MET B 137 1 O GLY B 132 N VAL B 108
SHEET 7 AA2 8 VAL B 233 GLY B 238 1 O LEU B 234 N LEU B 134
SHEET 8 AA2 8 ALA B 259 PHE B 264 1 O GLN B 260 N LEU B 235
LINK OG SER A 114 P01 9SW A 301 1555 1555 1.62
LINK OG SER B 114 P01 9SW B 301 1555 1555 1.58
CISPEP 1 ASP A 150 PRO A 151 0 2.45
CISPEP 2 ASP B 150 PRO B 151 0 -2.39
CRYST1 76.834 87.187 105.914 90.00 90.00 90.00 P 2 2 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 0.013015 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011470 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009442 0.00000
TER 2195 GLY A 290
TER 4390 GLY B 290
MASTER 360 0 7 29 16 0 0 6 4531 2 37 46
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