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HEADER HYDROLASE 30-JUN-21 7P0Y
TITLE CRYSTAL STRUCTURE OF MTBMGL K74A (SUBSTRATE ANALOG COMPLEX)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MGL;
COMPND 5 EC: 3.1.1.23;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 /
SOURCE 3 H37RV);
SOURCE 4 ORGANISM_TAXID: 83332;
SOURCE 5 STRAIN: ATCC 25618 / H37RV;
SOURCE 6 GENE: RV0183, LH57_01015;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS MYCOBACTERIUM TUBERCULOSIS, MONOACYLGLYCEROL LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.GRININGER,P.ASCHAUER,T.PAVKOV-KELLER,M.OBERER
REVDAT 1 15-SEP-21 7P0Y 0
JRNL AUTH C.GRININGER,M.LEYPOLD,P.ASCHAUER,T.PAVKOV-KELLER,
JRNL AUTH 2 L.RIEGLER-BERKET,R.BREINBAUER,M.OBERER
JRNL TITL STRUCTURAL CHANGES IN THE CAP OF RV0183/MTBMGL MODULATE THE
JRNL TITL 2 SHAPE OF THE BINDING POCKET
JRNL REF BIOMOLECULES V. 11 2021
JRNL REFN ESSN 2218-273X
JRNL DOI 10.3390/BIOM11091299
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 28118
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.256
REMARK 3 R VALUE (WORKING SET) : 0.253
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.110
REMARK 3 FREE R VALUE TEST SET COUNT : 3751
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 40.7800 - 6.7400 0.98 1804 137 0.2030 0.2006
REMARK 3 2 6.7400 - 5.3500 0.99 1822 137 0.2290 0.2131
REMARK 3 3 5.3500 - 4.6800 0.99 1823 137 0.2005 0.1998
REMARK 3 4 4.6800 - 4.2500 0.99 1796 143 0.2065 0.2456
REMARK 3 5 4.2500 - 3.9500 0.99 1805 135 0.2159 0.2627
REMARK 3 6 3.9500 - 3.7100 1.00 1827 138 0.2264 0.2842
REMARK 3 7 3.7100 - 3.5300 1.00 1836 143 0.2419 0.3161
REMARK 3 8 3.5300 - 3.3700 1.00 1822 138 0.2558 0.2990
REMARK 3 9 3.3700 - 3.2400 0.99 1813 140 0.2534 0.3177
REMARK 3 10 3.2400 - 3.1300 0.99 1829 135 0.2536 0.3732
REMARK 3 11 3.1300 - 3.0300 0.99 1832 141 0.3126 0.2933
REMARK 3 12 3.0300 - 2.9500 0.98 1764 135 0.2979 0.4097
REMARK 3 13 2.9500 - 2.8700 0.99 1824 136 0.2909 0.3339
REMARK 3 14 2.8700 - 2.8000 1.00 1833 143 0.2905 0.3807
REMARK 3 15 2.8000 - 2.7400 1.00 1844 141 0.2781 0.3912
REMARK 3 16 2.7400 - 2.6800 1.00 1804 141 0.2922 0.3535
REMARK 3 17 2.6800 - 2.6300 0.99 1827 142 0.3010 0.3032
REMARK 3 18 2.6300 - 2.5800 0.99 1816 141 0.2944 0.4389
REMARK 3 19 2.5800 - 2.5300 1.00 1806 140 0.2930 0.3681
REMARK 3 20 2.5300 - 2.4900 0.99 1810 142 0.3140 0.3486
REMARK 3 21 2.4900 - 2.4500 1.00 1814 142 0.3299 0.3633
REMARK 3 22 2.4500 - 2.4100 0.99 1804 142 0.3077 0.3475
REMARK 3 23 2.4100 - 2.3700 0.99 1808 134 0.3019 0.3705
REMARK 3 24 2.3700 - 2.3400 0.98 1830 138 0.3107 0.3450
REMARK 3 25 2.3400 - 2.3100 0.97 1780 131 0.3149 0.3828
REMARK 3 26 2.3100 - 2.2800 0.99 1805 137 0.3208 0.3488
REMARK 3 27 2.2800 - 2.2500 0.99 1838 142 0.3424 0.3453
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.381
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.814
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.18
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.60
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 4326
REMARK 3 ANGLE : 0.607 5892
REMARK 3 CHIRALITY : 0.042 676
REMARK 3 PLANARITY : 0.005 775
REMARK 3 DIHEDRAL : 18.762 1594
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 7P0Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-JUL-21.
REMARK 100 THE DEPOSITION ID IS D_1292116705.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, DESY
REMARK 200 BEAMLINE : P11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
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 : DIALS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28192
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 40.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.14900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.9900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.72000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.190
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6EIC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30 % PEG300, 125 MM CALCIUM ACETATE,
REMARK 280 100 MM TRIS-HCL PH 8.5, 10 MG/ML PROTEIN, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21
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+1/2,-Y,-Z+1/2
REMARK 290 4555 -X+1/2,-Y,Z+1/2
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 37.34500
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.89000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 37.34500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 46.89000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 GLY A -4
REMARK 465 ALA A -3
REMARK 465 MET A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 GLY B -4
REMARK 465 ALA B -3
REMARK 465 MET B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 THR B 3
REMARK 465 THR B 4
REMARK 465 PRO B 252
REMARK 465 GLY B 253
REMARK 465 LEU B 254
REMARK 465 TYR B 255
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 GLU B 176 CG CD OE1 OE2
REMARK 470 VAL B 177 CG1 CG2
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 TYR B 20
REMARK 475 ASP B 225
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU B 263 CB CG CD OE1 OE2
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 GLU A 41 -160.02 -105.64
REMARK 500 VAL A 76 35.48 39.13
REMARK 500 SER A 110 -116.51 60.71
REMARK 500 ALA A 138 45.73 -143.50
REMARK 500 HIS A 189 32.77 -93.12
REMARK 500 TYR A 255 -158.23 -83.50
REMARK 500 GLU B 41 -150.13 -109.48
REMARK 500 VAL B 76 40.49 37.69
REMARK 500 SER B 110 -119.04 57.97
REMARK 500 ALA B 138 55.21 -143.87
REMARK 500 HIS B 222 117.68 -162.36
REMARK 500 GLU B 257 99.28 -68.98
REMARK 500 ASN B 260 10.95 -145.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7OZM RELATED DB: PDB
REMARK 900 7OZM CONTAINS THE SAME PROTEIN WITHOUT LIGAND, BUT CLOSED CAP
REMARK 900 CONFORMATION
DBREF 7P0Y A 1 279 UNP O07427 MGLL_MYCTU 1 279
DBREF 7P0Y B 1 279 UNP O07427 MGLL_MYCTU 1 279
SEQADV 7P0Y GLY A -4 UNP O07427 EXPRESSION TAG
SEQADV 7P0Y ALA A -3 UNP O07427 EXPRESSION TAG
SEQADV 7P0Y MET A -2 UNP O07427 EXPRESSION TAG
SEQADV 7P0Y GLY A -1 UNP O07427 EXPRESSION TAG
SEQADV 7P0Y SER A 0 UNP O07427 EXPRESSION TAG
SEQADV 7P0Y ALA A 74 UNP O07427 LYS 74 ENGINEERED MUTATION
SEQADV 7P0Y GLY B -4 UNP O07427 EXPRESSION TAG
SEQADV 7P0Y ALA B -3 UNP O07427 EXPRESSION TAG
SEQADV 7P0Y MET B -2 UNP O07427 EXPRESSION TAG
SEQADV 7P0Y GLY B -1 UNP O07427 EXPRESSION TAG
SEQADV 7P0Y SER B 0 UNP O07427 EXPRESSION TAG
SEQADV 7P0Y ALA B 74 UNP O07427 LYS 74 ENGINEERED MUTATION
SEQRES 1 A 284 GLY ALA MET GLY SER MET THR THR THR ARG THR GLU ARG
SEQRES 2 A 284 ASN PHE ALA GLY ILE GLY ASP VAL ARG ILE VAL TYR ASP
SEQRES 3 A 284 VAL TRP THR PRO ASP THR ALA PRO GLN ALA VAL VAL VAL
SEQRES 4 A 284 LEU ALA HIS GLY LEU GLY GLU HIS ALA ARG ARG TYR ASP
SEQRES 5 A 284 HIS VAL ALA GLN ARG LEU GLY ALA ALA GLY LEU VAL THR
SEQRES 6 A 284 TYR ALA LEU ASP HIS ARG GLY HIS GLY ARG SER GLY GLY
SEQRES 7 A 284 ALA ARG VAL LEU VAL ARG ASP ILE SER GLU TYR THR ALA
SEQRES 8 A 284 ASP PHE ASP THR LEU VAL GLY ILE ALA THR ARG GLU TYR
SEQRES 9 A 284 PRO GLY CYS LYS ARG ILE VAL LEU GLY HIS SER MET GLY
SEQRES 10 A 284 GLY GLY ILE VAL PHE ALA TYR GLY VAL GLU ARG PRO ASP
SEQRES 11 A 284 ASN TYR ASP LEU MET VAL LEU SER ALA PRO ALA VAL ALA
SEQRES 12 A 284 ALA GLN ASP LEU VAL SER PRO VAL VAL ALA VAL ALA ALA
SEQRES 13 A 284 LYS LEU LEU GLY VAL VAL VAL PRO GLY LEU PRO VAL GLN
SEQRES 14 A 284 GLU LEU ASP PHE THR ALA ILE SER ARG ASP PRO GLU VAL
SEQRES 15 A 284 VAL GLN ALA TYR ASN THR ASP PRO LEU VAL HIS HIS GLY
SEQRES 16 A 284 ARG VAL PRO ALA GLY ILE GLY ARG ALA LEU LEU GLN VAL
SEQRES 17 A 284 GLY GLU THR MET PRO ARG ARG ALA PRO ALA LEU THR ALA
SEQRES 18 A 284 PRO LEU LEU VAL LEU HIS GLY THR ASP ASP ARG LEU ILE
SEQRES 19 A 284 PRO ILE GLU GLY SER ARG ARG LEU VAL GLU CYS VAL GLY
SEQRES 20 A 284 SER ALA ASP VAL GLN LEU LYS GLU TYR PRO GLY LEU TYR
SEQRES 21 A 284 HIS GLU VAL PHE ASN GLU PRO GLU ARG ASN GLN VAL LEU
SEQRES 22 A 284 ASP ASP VAL VAL ALA TRP LEU THR GLU ARG LEU
SEQRES 1 B 284 GLY ALA MET GLY SER MET THR THR THR ARG THR GLU ARG
SEQRES 2 B 284 ASN PHE ALA GLY ILE GLY ASP VAL ARG ILE VAL TYR ASP
SEQRES 3 B 284 VAL TRP THR PRO ASP THR ALA PRO GLN ALA VAL VAL VAL
SEQRES 4 B 284 LEU ALA HIS GLY LEU GLY GLU HIS ALA ARG ARG TYR ASP
SEQRES 5 B 284 HIS VAL ALA GLN ARG LEU GLY ALA ALA GLY LEU VAL THR
SEQRES 6 B 284 TYR ALA LEU ASP HIS ARG GLY HIS GLY ARG SER GLY GLY
SEQRES 7 B 284 ALA ARG VAL LEU VAL ARG ASP ILE SER GLU TYR THR ALA
SEQRES 8 B 284 ASP PHE ASP THR LEU VAL GLY ILE ALA THR ARG GLU TYR
SEQRES 9 B 284 PRO GLY CYS LYS ARG ILE VAL LEU GLY HIS SER MET GLY
SEQRES 10 B 284 GLY GLY ILE VAL PHE ALA TYR GLY VAL GLU ARG PRO ASP
SEQRES 11 B 284 ASN TYR ASP LEU MET VAL LEU SER ALA PRO ALA VAL ALA
SEQRES 12 B 284 ALA GLN ASP LEU VAL SER PRO VAL VAL ALA VAL ALA ALA
SEQRES 13 B 284 LYS LEU LEU GLY VAL VAL VAL PRO GLY LEU PRO VAL GLN
SEQRES 14 B 284 GLU LEU ASP PHE THR ALA ILE SER ARG ASP PRO GLU VAL
SEQRES 15 B 284 VAL GLN ALA TYR ASN THR ASP PRO LEU VAL HIS HIS GLY
SEQRES 16 B 284 ARG VAL PRO ALA GLY ILE GLY ARG ALA LEU LEU GLN VAL
SEQRES 17 B 284 GLY GLU THR MET PRO ARG ARG ALA PRO ALA LEU THR ALA
SEQRES 18 B 284 PRO LEU LEU VAL LEU HIS GLY THR ASP ASP ARG LEU ILE
SEQRES 19 B 284 PRO ILE GLU GLY SER ARG ARG LEU VAL GLU CYS VAL GLY
SEQRES 20 B 284 SER ALA ASP VAL GLN LEU LYS GLU TYR PRO GLY LEU TYR
SEQRES 21 B 284 HIS GLU VAL PHE ASN GLU PRO GLU ARG ASN GLN VAL LEU
SEQRES 22 B 284 ASP ASP VAL VAL ALA TRP LEU THR GLU ARG LEU
HET 4E0 A 301 23
HET 4E0 B 301 23
HETNAM 4E0 1-[BUTYL(FLUORANYL)PHOSPHORYL]OXYHEXADECANE
FORMUL 3 4E0 2(C20 H42 F O2 P)
FORMUL 5 HOH *141(H2 O)
HELIX 1 AA1 ILE A 13 ASP A 15 5 3
HELIX 2 AA2 HIS A 42 ARG A 45 5 4
HELIX 3 AA3 TYR A 46 ALA A 55 1 10
HELIX 4 AA4 ASP A 80 TYR A 99 1 20
HELIX 5 AA5 SER A 110 ARG A 123 1 14
HELIX 6 AA6 ALA A 138 VAL A 143 5 6
HELIX 7 AA7 SER A 144 VAL A 158 1 15
HELIX 8 AA8 ASP A 167 ILE A 171 5 5
HELIX 9 AA9 ASP A 174 THR A 183 1 10
HELIX 10 AB1 ALA A 194 ALA A 211 1 18
HELIX 11 AB2 PRO A 212 LEU A 214 5 3
HELIX 12 AB3 ILE A 231 VAL A 241 1 11
HELIX 13 AB4 GLU A 257 PRO A 262 5 6
HELIX 14 AB5 GLU A 263 LEU A 279 1 17
HELIX 15 AB6 ILE B 13 ASP B 15 5 3
HELIX 16 AB7 HIS B 42 ARG B 45 5 4
HELIX 17 AB8 TYR B 46 ALA B 55 1 10
HELIX 18 AB9 ASP B 80 TYR B 99 1 20
HELIX 19 AC1 SER B 110 ARG B 123 1 14
HELIX 20 AC2 ALA B 138 LEU B 142 5 5
HELIX 21 AC3 SER B 144 VAL B 158 1 15
HELIX 22 AC4 ASP B 174 ASP B 184 1 11
HELIX 23 AC5 ALA B 194 ALA B 211 1 18
HELIX 24 AC6 PRO B 212 LEU B 214 5 3
HELIX 25 AC7 PRO B 230 GLU B 239 1 10
HELIX 26 AC8 GLU B 263 GLU B 277 1 15
SHEET 1 AA1 8 THR A 3 ALA A 11 0
SHEET 2 AA1 8 ARG A 17 PRO A 25 -1 O ILE A 18 N PHE A 10
SHEET 3 AA1 8 LEU A 58 LEU A 63 -1 O ALA A 62 N ASP A 21
SHEET 4 AA1 8 ALA A 31 ALA A 36 1 N VAL A 33 O TYR A 61
SHEET 5 AA1 8 LYS A 103 HIS A 109 1 O ILE A 105 N VAL A 34
SHEET 6 AA1 8 LEU A 129 SER A 133 1 O SER A 133 N GLY A 108
SHEET 7 AA1 8 LEU A 218 GLY A 223 1 O LEU A 219 N LEU A 132
SHEET 8 AA1 8 VAL A 246 TYR A 251 1 O LYS A 249 N VAL A 220
SHEET 1 AA2 2 PRO A 162 GLN A 164 0
SHEET 2 AA2 2 VAL A 192 PRO A 193 -1 O VAL A 192 N GLN A 164
SHEET 1 AA3 8 THR B 6 ALA B 11 0
SHEET 2 AA3 8 ARG B 17 TRP B 23 -1 O ILE B 18 N PHE B 10
SHEET 3 AA3 8 LEU B 58 LEU B 63 -1 O THR B 60 N TRP B 23
SHEET 4 AA3 8 ALA B 31 ALA B 36 1 N LEU B 35 O TYR B 61
SHEET 5 AA3 8 ARG B 104 HIS B 109 1 O LEU B 107 N VAL B 34
SHEET 6 AA3 8 LEU B 129 SER B 133 1 O SER B 133 N GLY B 108
SHEET 7 AA3 8 LEU B 218 GLY B 223 1 O LEU B 219 N LEU B 132
SHEET 8 AA3 8 VAL B 246 TYR B 251 1 O GLN B 247 N VAL B 220
SHEET 1 AA4 2 PRO B 162 GLN B 164 0
SHEET 2 AA4 2 VAL B 192 PRO B 193 -1 O VAL B 192 N GLN B 164
LINK OG SER A 110 P18 4E0 A 301 1555 1555 1.56
LINK OG SER B 110 P18 4E0 B 301 1555 1555 1.56
CRYST1 74.690 82.603 93.780 90.00 90.00 90.00 P 21 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 0.013389 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012106 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010663 0.00000
TER 2131 LEU A 279
TER 4196 LEU B 279
MASTER 311 0 2 26 20 0 0 6 4373 2 48 44
END |