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HEADER HYDROLASE 19-SEP-17 6EIC
TITLE CRYSTAL STRUKTURE OF RV0183, A MONOGLYCERIDE LIPASE FROM MYCOBACTERIUM
TITLE 2 TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYCOBACTERIUM TUBERCULOSIS MONOGLYCERIDE LIPASE;
COMPND 3 CHAIN: C, A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS H37RV;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 GENE: RV0183;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MONOGLYCERID LIPASE, HYDROLASE, LIPASE, ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.ASCHAUER,T.PAVKOV-KELLER,M.OBERER
REVDAT 1 27-JUN-18 6EIC 0
JRNL AUTH P.ASCHAUER,R.ZIMMERMANN,R.BREINBAUER,T.PAVKOV-KELLER,
JRNL AUTH 2 M.OBERER
JRNL TITL THE CRYSTAL STRUCTURE OF MONOACYLGLYCEROL LIPASE FROM M.
JRNL TITL 2 TUBERCULOSIS REVEALS THE BASIS FOR SPECIFIC INHIBITION.
JRNL REF SCI REP V. 8 8948 2018
JRNL REFN ESSN 2045-2322
JRNL PMID 29895832
JRNL DOI 10.1038/S41598-018-27051-7
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.21
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 77233
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 3805
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 24.0291 - 4.8737 0.95 3824 208 0.2103 0.2284
REMARK 3 2 4.8737 - 3.8736 0.95 3716 201 0.1736 0.2111
REMARK 3 3 3.8736 - 3.3855 0.96 3706 170 0.1814 0.2077
REMARK 3 4 3.3855 - 3.0766 0.95 3673 201 0.1994 0.2156
REMARK 3 5 3.0766 - 2.8565 0.95 3674 191 0.2092 0.2454
REMARK 3 6 2.8565 - 2.6883 0.95 3667 201 0.2189 0.2631
REMARK 3 7 2.6883 - 2.5538 0.95 3657 205 0.2257 0.2463
REMARK 3 8 2.5538 - 2.4428 0.95 3643 179 0.2246 0.2507
REMARK 3 9 2.4428 - 2.3488 0.95 3682 206 0.2290 0.2663
REMARK 3 10 2.3488 - 2.2678 0.95 3640 188 0.2331 0.2710
REMARK 3 11 2.2678 - 2.1970 0.95 3620 209 0.2314 0.2731
REMARK 3 12 2.1970 - 2.1342 0.95 3664 212 0.2380 0.2586
REMARK 3 13 2.1342 - 2.0781 0.95 3649 189 0.2428 0.2795
REMARK 3 14 2.0781 - 2.0274 0.95 3634 179 0.2515 0.2924
REMARK 3 15 2.0274 - 1.9813 0.95 3634 210 0.2582 0.3188
REMARK 3 16 1.9813 - 1.9392 0.96 3659 166 0.2607 0.2809
REMARK 3 17 1.9392 - 1.9004 0.95 3640 190 0.2899 0.3138
REMARK 3 18 1.9004 - 1.8646 0.96 3642 168 0.3088 0.3397
REMARK 3 19 1.8646 - 1.8313 0.96 3646 169 0.3292 0.3381
REMARK 3 20 1.8313 - 1.8002 0.96 3689 163 0.3710 0.4373
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.910
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 6478
REMARK 3 ANGLE : 1.010 8841
REMARK 3 CHIRALITY : 0.043 1020
REMARK 3 PLANARITY : 0.004 1161
REMARK 3 DIHEDRAL : 22.324 2356
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6EIC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1200006622.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97895
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 : SCALA
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77304
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 49.209
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.600
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.70
REMARK 200 R MERGE FOR SHELL (I) : 0.85300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.03M SODIUM NITRATE, 0.03M DI-SODIUM
REMARK 280 HYDROGENPHOSPHATE, 0.03M AMMONIUM SULFATE, 0.1M MOPS/HEPES, 12%
REMARK 280 2-METHYL 2,4 PENTANDIOL, 12% PEG1000, 12% PEG3350. MICROSEEDING,
REMARK 280 PH 7.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 1 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -Y,-X,-Z+2/3
REMARK 290 5555 -X+Y,Y,-Z+1/3
REMARK 290 6555 X,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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.66000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 131.32000
REMARK 290 SMTRY1 4 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 131.32000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 65.66000
REMARK 290 SMTRY1 6 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 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 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: 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: 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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C 517 LIES ON A SPECIAL POSITION.
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 GLN C 140
REMARK 465 ASP C 141
REMARK 465 LEU C 142
REMARK 465 VAL C 143
REMARK 465 MET A 1
REMARK 465 ALA A 138
REMARK 465 ALA A 139
REMARK 465 GLN A 140
REMARK 465 ASP A 141
REMARK 465 LEU A 142
REMARK 465 LEU A 279
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 OH TYR A 119 O HOH A 401 2.14
REMARK 500 O HOH B 500 O HOH B 523 2.18
REMARK 500 O HOH B 434 O HOH B 517 2.18
REMARK 500 OD1 ASP A 125 O HOH A 402 2.19
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 NE ARG B 236 NE ARG B 236 6555 2.19
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 C 26 36.17 -78.20
REMARK 500 GLU C 41 -150.02 -96.43
REMARK 500 VAL C 76 34.09 39.46
REMARK 500 SER C 110 -121.55 58.72
REMARK 500 ALA C 134 65.40 37.36
REMARK 500 ALA C 138 73.07 -117.74
REMARK 500 VAL C 163 -64.61 -131.94
REMARK 500 TYR C 255 -158.68 -95.97
REMARK 500 GLU A 41 -150.10 -93.50
REMARK 500 SER A 110 -118.29 57.87
REMARK 500 ALA A 134 64.30 31.22
REMARK 500 VAL A 163 -66.89 -126.61
REMARK 500 ASP A 225 32.75 -88.63
REMARK 500 TYR A 255 -149.08 -91.12
REMARK 500 GLU B 41 -155.87 -100.51
REMARK 500 VAL B 76 37.71 36.12
REMARK 500 SER B 110 -119.14 56.75
REMARK 500 LEU B 142 54.38 -91.25
REMARK 500 VAL B 163 -69.06 -121.72
REMARK 500 TYR B 255 -156.23 -90.44
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 A 544 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH A 545 DISTANCE = 7.60 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 B 302
DBREF 6EIC C 1 279 UNP O07427 MGLL_MYCTU 1 279
DBREF 6EIC A 1 279 UNP O07427 MGLL_MYCTU 1 279
DBREF 6EIC B 1 279 UNP O07427 MGLL_MYCTU 1 279
SEQRES 1 C 279 MET THR THR THR ARG THR GLU ARG ASN PHE ALA GLY ILE
SEQRES 2 C 279 GLY ASP VAL ARG ILE VAL TYR ASP VAL TRP THR PRO ASP
SEQRES 3 C 279 THR ALA PRO GLN ALA VAL VAL VAL LEU ALA HIS GLY LEU
SEQRES 4 C 279 GLY GLU HIS ALA ARG ARG TYR ASP HIS VAL ALA GLN ARG
SEQRES 5 C 279 LEU GLY ALA ALA GLY LEU VAL THR TYR ALA LEU ASP HIS
SEQRES 6 C 279 ARG GLY HIS GLY ARG SER GLY GLY LYS ARG VAL LEU VAL
SEQRES 7 C 279 ARG ASP ILE SER GLU TYR THR ALA ASP PHE ASP THR LEU
SEQRES 8 C 279 VAL GLY ILE ALA THR ARG GLU TYR PRO GLY CYS LYS ARG
SEQRES 9 C 279 ILE VAL LEU GLY HIS SER MET GLY GLY GLY ILE VAL PHE
SEQRES 10 C 279 ALA TYR GLY VAL GLU ARG PRO ASP ASN TYR ASP LEU MET
SEQRES 11 C 279 VAL LEU SER ALA PRO ALA VAL ALA ALA GLN ASP LEU VAL
SEQRES 12 C 279 SER PRO VAL VAL ALA VAL ALA ALA LYS LEU LEU GLY VAL
SEQRES 13 C 279 VAL VAL PRO GLY LEU PRO VAL GLN GLU LEU ASP PHE THR
SEQRES 14 C 279 ALA ILE SER ARG ASP PRO GLU VAL VAL GLN ALA TYR ASN
SEQRES 15 C 279 THR ASP PRO LEU VAL HIS HIS GLY ARG VAL PRO ALA GLY
SEQRES 16 C 279 ILE GLY ARG ALA LEU LEU GLN VAL GLY GLU THR MET PRO
SEQRES 17 C 279 ARG ARG ALA PRO ALA LEU THR ALA PRO LEU LEU VAL LEU
SEQRES 18 C 279 HIS GLY THR ASP ASP ARG LEU ILE PRO ILE GLU GLY SER
SEQRES 19 C 279 ARG ARG LEU VAL GLU CYS VAL GLY SER ALA ASP VAL GLN
SEQRES 20 C 279 LEU LYS GLU TYR PRO GLY LEU TYR HIS GLU VAL PHE ASN
SEQRES 21 C 279 GLU PRO GLU ARG ASN GLN VAL LEU ASP ASP VAL VAL ALA
SEQRES 22 C 279 TRP LEU THR GLU ARG LEU
SEQRES 1 A 279 MET THR THR THR ARG THR GLU ARG ASN PHE ALA GLY ILE
SEQRES 2 A 279 GLY ASP VAL ARG ILE VAL TYR ASP VAL TRP THR PRO ASP
SEQRES 3 A 279 THR ALA PRO GLN ALA VAL VAL VAL LEU ALA HIS GLY LEU
SEQRES 4 A 279 GLY GLU HIS ALA ARG ARG TYR ASP HIS VAL ALA GLN ARG
SEQRES 5 A 279 LEU GLY ALA ALA GLY LEU VAL THR TYR ALA LEU ASP HIS
SEQRES 6 A 279 ARG GLY HIS GLY ARG SER GLY GLY LYS ARG VAL LEU VAL
SEQRES 7 A 279 ARG ASP ILE SER GLU TYR THR ALA ASP PHE ASP THR LEU
SEQRES 8 A 279 VAL GLY ILE ALA THR ARG GLU TYR PRO GLY CYS LYS ARG
SEQRES 9 A 279 ILE VAL LEU GLY HIS SER MET GLY GLY GLY ILE VAL PHE
SEQRES 10 A 279 ALA TYR GLY VAL GLU ARG PRO ASP ASN TYR ASP LEU MET
SEQRES 11 A 279 VAL LEU SER ALA PRO ALA VAL ALA ALA GLN ASP LEU VAL
SEQRES 12 A 279 SER PRO VAL VAL ALA VAL ALA ALA LYS LEU LEU GLY VAL
SEQRES 13 A 279 VAL VAL PRO GLY LEU PRO VAL GLN GLU LEU ASP PHE THR
SEQRES 14 A 279 ALA ILE SER ARG ASP PRO GLU VAL VAL GLN ALA TYR ASN
SEQRES 15 A 279 THR ASP PRO LEU VAL HIS HIS GLY ARG VAL PRO ALA GLY
SEQRES 16 A 279 ILE GLY ARG ALA LEU LEU GLN VAL GLY GLU THR MET PRO
SEQRES 17 A 279 ARG ARG ALA PRO ALA LEU THR ALA PRO LEU LEU VAL LEU
SEQRES 18 A 279 HIS GLY THR ASP ASP ARG LEU ILE PRO ILE GLU GLY SER
SEQRES 19 A 279 ARG ARG LEU VAL GLU CYS VAL GLY SER ALA ASP VAL GLN
SEQRES 20 A 279 LEU LYS GLU TYR PRO GLY LEU TYR HIS GLU VAL PHE ASN
SEQRES 21 A 279 GLU PRO GLU ARG ASN GLN VAL LEU ASP ASP VAL VAL ALA
SEQRES 22 A 279 TRP LEU THR GLU ARG LEU
SEQRES 1 B 279 MET THR THR THR ARG THR GLU ARG ASN PHE ALA GLY ILE
SEQRES 2 B 279 GLY ASP VAL ARG ILE VAL TYR ASP VAL TRP THR PRO ASP
SEQRES 3 B 279 THR ALA PRO GLN ALA VAL VAL VAL LEU ALA HIS GLY LEU
SEQRES 4 B 279 GLY GLU HIS ALA ARG ARG TYR ASP HIS VAL ALA GLN ARG
SEQRES 5 B 279 LEU GLY ALA ALA GLY LEU VAL THR TYR ALA LEU ASP HIS
SEQRES 6 B 279 ARG GLY HIS GLY ARG SER GLY GLY LYS ARG VAL LEU VAL
SEQRES 7 B 279 ARG ASP ILE SER GLU TYR THR ALA ASP PHE ASP THR LEU
SEQRES 8 B 279 VAL GLY ILE ALA THR ARG GLU TYR PRO GLY CYS LYS ARG
SEQRES 9 B 279 ILE VAL LEU GLY HIS SER MET GLY GLY GLY ILE VAL PHE
SEQRES 10 B 279 ALA TYR GLY VAL GLU ARG PRO ASP ASN TYR ASP LEU MET
SEQRES 11 B 279 VAL LEU SER ALA PRO ALA VAL ALA ALA GLN ASP LEU VAL
SEQRES 12 B 279 SER PRO VAL VAL ALA VAL ALA ALA LYS LEU LEU GLY VAL
SEQRES 13 B 279 VAL VAL PRO GLY LEU PRO VAL GLN GLU LEU ASP PHE THR
SEQRES 14 B 279 ALA ILE SER ARG ASP PRO GLU VAL VAL GLN ALA TYR ASN
SEQRES 15 B 279 THR ASP PRO LEU VAL HIS HIS GLY ARG VAL PRO ALA GLY
SEQRES 16 B 279 ILE GLY ARG ALA LEU LEU GLN VAL GLY GLU THR MET PRO
SEQRES 17 B 279 ARG ARG ALA PRO ALA LEU THR ALA PRO LEU LEU VAL LEU
SEQRES 18 B 279 HIS GLY THR ASP ASP ARG LEU ILE PRO ILE GLU GLY SER
SEQRES 19 B 279 ARG ARG LEU VAL GLU CYS VAL GLY SER ALA ASP VAL GLN
SEQRES 20 B 279 LEU LYS GLU TYR PRO GLY LEU TYR HIS GLU VAL PHE ASN
SEQRES 21 B 279 GLU PRO GLU ARG ASN GLN VAL LEU ASP ASP VAL VAL ALA
SEQRES 22 B 279 TRP LEU THR GLU ARG LEU
HET SO4 C 301 5
HET MPD C 302 8
HET MPD A 301 8
HET MPD B 301 8
HET NO3 B 302 4
HETNAM SO4 SULFATE ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM NO3 NITRATE ION
FORMUL 4 SO4 O4 S 2-
FORMUL 5 MPD 3(C6 H14 O2)
FORMUL 8 NO3 N O3 1-
FORMUL 9 HOH *459(H2 O)
HELIX 1 AA1 ILE C 13 ASP C 15 5 3
HELIX 2 AA2 HIS C 42 ARG C 45 5 4
HELIX 3 AA3 TYR C 46 ALA C 56 1 11
HELIX 4 AA4 ASP C 80 TYR C 99 1 20
HELIX 5 AA5 SER C 110 ARG C 123 1 14
HELIX 6 AA6 PRO C 145 VAL C 158 1 14
HELIX 7 AA7 ASP C 167 ILE C 171 5 5
HELIX 8 AA8 ASP C 174 THR C 183 1 10
HELIX 9 AA9 ALA C 194 ALA C 211 1 18
HELIX 10 AB1 PRO C 212 LEU C 214 5 3
HELIX 11 AB2 PRO C 230 VAL C 241 1 12
HELIX 12 AB3 GLU C 263 GLU C 277 1 15
HELIX 13 AB4 ILE A 13 ASP A 15 5 3
HELIX 14 AB5 HIS A 42 ARG A 45 5 4
HELIX 15 AB6 TYR A 46 ALA A 56 1 11
HELIX 16 AB7 ASP A 80 TYR A 99 1 20
HELIX 17 AB8 SER A 110 ARG A 123 1 14
HELIX 18 AB9 SER A 144 VAL A 158 1 15
HELIX 19 AC1 ASP A 167 ILE A 171 5 5
HELIX 20 AC2 ASP A 174 THR A 183 1 10
HELIX 21 AC3 ALA A 194 GLU A 205 1 12
HELIX 22 AC4 ARG A 210 LEU A 214 5 5
HELIX 23 AC5 ILE A 231 VAL A 241 1 11
HELIX 24 AC6 GLU A 263 GLU A 277 1 15
HELIX 25 AC7 ILE B 13 ASP B 15 5 3
HELIX 26 AC8 HIS B 42 ARG B 45 5 4
HELIX 27 AC9 TYR B 46 ALA B 56 1 11
HELIX 28 AD1 ASP B 80 TYR B 99 1 20
HELIX 29 AD2 SER B 110 ARG B 123 1 14
HELIX 30 AD3 SER B 144 VAL B 158 1 15
HELIX 31 AD4 ASP B 167 SER B 172 5 6
HELIX 32 AD5 ASP B 174 ASP B 184 1 11
HELIX 33 AD6 ALA B 194 THR B 206 1 13
HELIX 34 AD7 THR B 206 ALA B 211 1 6
HELIX 35 AD8 PRO B 212 LEU B 214 5 3
HELIX 36 AD9 PRO B 230 VAL B 241 1 12
HELIX 37 AE1 GLU B 263 GLU B 277 1 15
SHEET 1 AA1 8 THR C 3 ALA C 11 0
SHEET 2 AA1 8 ARG C 17 PRO C 25 -1 O ILE C 18 N PHE C 10
SHEET 3 AA1 8 LEU C 58 LEU C 63 -1 O ALA C 62 N ASP C 21
SHEET 4 AA1 8 ALA C 31 ALA C 36 1 N VAL C 33 O TYR C 61
SHEET 5 AA1 8 LYS C 103 HIS C 109 1 O ILE C 105 N VAL C 34
SHEET 6 AA1 8 LEU C 129 SER C 133 1 O SER C 133 N GLY C 108
SHEET 7 AA1 8 LEU C 218 GLY C 223 1 O LEU C 221 N LEU C 132
SHEET 8 AA1 8 VAL C 246 TYR C 251 1 O LYS C 249 N VAL C 220
SHEET 1 AA2 2 PRO C 162 GLN C 164 0
SHEET 2 AA2 2 VAL C 192 PRO C 193 -1 O VAL C 192 N GLN C 164
SHEET 1 AA3 8 THR A 3 ALA A 11 0
SHEET 2 AA3 8 ARG A 17 PRO A 25 -1 O ILE A 18 N PHE A 10
SHEET 3 AA3 8 LEU A 58 LEU A 63 -1 O ALA A 62 N ASP A 21
SHEET 4 AA3 8 ALA A 31 ALA A 36 1 N VAL A 33 O TYR A 61
SHEET 5 AA3 8 LYS A 103 HIS A 109 1 O LEU A 107 N VAL A 34
SHEET 6 AA3 8 LEU A 129 SER A 133 1 O SER A 133 N GLY A 108
SHEET 7 AA3 8 LEU A 218 GLY A 223 1 O LEU A 219 N LEU A 132
SHEET 8 AA3 8 VAL A 246 TYR A 251 1 O LYS A 249 N VAL A 220
SHEET 1 AA4 2 PRO A 162 GLN A 164 0
SHEET 2 AA4 2 VAL A 192 PRO A 193 -1 O VAL A 192 N GLN A 164
SHEET 1 AA5 8 THR B 3 ALA B 11 0
SHEET 2 AA5 8 ARG B 17 PRO B 25 -1 O ILE B 18 N PHE B 10
SHEET 3 AA5 8 LEU B 58 LEU B 63 -1 O THR B 60 N TRP B 23
SHEET 4 AA5 8 ALA B 31 ALA B 36 1 N VAL B 33 O TYR B 61
SHEET 5 AA5 8 LYS B 103 HIS B 109 1 O LEU B 107 N VAL B 34
SHEET 6 AA5 8 LEU B 129 SER B 133 1 O SER B 133 N GLY B 108
SHEET 7 AA5 8 LEU B 218 GLY B 223 1 O LEU B 219 N LEU B 132
SHEET 8 AA5 8 VAL B 246 TYR B 251 1 O LYS B 249 N VAL B 220
SHEET 1 AA6 2 PRO B 162 GLN B 164 0
SHEET 2 AA6 2 VAL B 192 PRO B 193 -1 O VAL B 192 N GLN B 164
SITE 1 AC1 3 LEU C 39 LEU C 166 HOH C 422
SITE 1 AC2 6 LEU C 39 GLU C 41 HIS C 109 SER C 110
SITE 2 AC2 6 HIS C 256 GLU C 257
SITE 1 AC3 7 LEU A 39 HIS A 109 SER A 110 TYR A 181
SITE 2 AC3 7 LEU A 228 HIS A 256 GLU A 257
SITE 1 AC4 7 GLY B 38 LEU B 39 ARG B 45 HIS B 109
SITE 2 AC4 7 TYR B 181 HIS B 256 GLU B 257
SITE 1 AC5 3 LEU B 39 LEU B 200 HOH B 428
CRYST1 85.825 85.825 196.980 90.00 90.00 120.00 P 31 1 2 18
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 0.011652 0.006727 0.000000 0.00000
SCALE2 0.000000 0.013454 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005077 0.00000
TER 2103 LEU C 279
TER 4186 ARG A 278
TER 6320 LEU B 279
MASTER 366 0 5 37 30 0 8 6 6809 3 33 66
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