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HEADER HYDROLASE 31-OCT-21 7Q4J
TITLE A THERMOSTABLE LIPASE FROM THERMOANAEROBACTER THERMOHYDROSULFURICUS IN
TITLE 2 COMPLEX A MONOACYLGLYCEROL INTERMEDIATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROLASE_4 DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: METHYLATES LYSINES, SELENO-METHIONINES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HYDROLASE_4 DOMAIN-CONTAINING PROTEIN;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOANAEROBACTER THERMOHYDROSULFURICUS;
SOURCE 3 ORGANISM_TAXID: 1516;
SOURCE 4 GENE: SAMN04324257_00243;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: THERMOANAEROBACTER THERMOHYDROSULFURICUS;
SOURCE 9 ORGANISM_TAXID: 1516;
SOURCE 10 GENE: SAMN04324257_00243;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA HYDROLASE, HYDROLASE, THERMOSTABLE, MONOACYLGLYCEROL,
KEYWDS 2 LIPASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.PINOTSIS,M.WILMANNS
REVDAT 1 10-MAY-23 7Q4J 0
JRNL AUTH N.PINOTSIS,M.WILMANNS
JRNL TITL A THERMOSTABLE LIPASE FROM THERMOANAEROBACTER
JRNL TITL 2 THERMOHYDROSULFURICUS IN COMPLEX A MONOACYLGLYCEROL
JRNL TITL 3 INTERMEDIATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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) : 1.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 49195
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1532
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 19.7500 - 4.2400 0.97 4599 132 0.1407 0.1537
REMARK 3 2 4.2300 - 3.3700 0.97 4425 152 0.1435 0.1753
REMARK 3 3 3.3700 - 2.9400 0.98 4386 153 0.1830 0.2296
REMARK 3 4 2.9400 - 2.6700 0.98 4408 156 0.1852 0.2016
REMARK 3 5 2.6700 - 2.4800 0.98 4390 138 0.1794 0.2154
REMARK 3 6 2.4800 - 2.3400 0.99 4373 138 0.1773 0.2119
REMARK 3 7 2.3400 - 2.2200 0.98 4344 154 0.1647 0.1923
REMARK 3 8 2.2200 - 2.1200 0.98 4334 125 0.1695 0.2512
REMARK 3 9 2.1200 - 2.0400 0.98 4310 141 0.1885 0.2339
REMARK 3 10 2.0400 - 1.9700 0.97 4291 147 0.2087 0.2607
REMARK 3 11 1.9700 - 1.9100 0.86 3803 96 0.2536 0.2199
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.166
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.538
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.26
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.20
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 : 0.004 4385
REMARK 3 ANGLE : 0.833 5856
REMARK 3 CHIRALITY : 0.047 633
REMARK 3 PLANARITY : 0.006 732
REMARK 3 DIHEDRAL : 15.198 1687
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 1:140 OR RESID 183:259)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6600 29.8547 4.5045
REMARK 3 T TENSOR
REMARK 3 T11: 0.2703 T22: 0.4023
REMARK 3 T33: 0.4254 T12: -0.0439
REMARK 3 T13: 0.0440 T23: -0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 2.1076 L22: 1.7485
REMARK 3 L33: 1.4024 L12: -0.3007
REMARK 3 L13: 0.1748 L23: 0.1123
REMARK 3 S TENSOR
REMARK 3 S11: -0.0559 S12: 0.0089 S13: -0.5009
REMARK 3 S21: -0.0237 S22: 0.0151 S23: 0.1469
REMARK 3 S31: 0.1173 S32: -0.2826 S33: 0.0385
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESID 141:182
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1197 48.6357 -8.3730
REMARK 3 T TENSOR
REMARK 3 T11: 0.4372 T22: 0.4628
REMARK 3 T33: 0.3414 T12: 0.0177
REMARK 3 T13: 0.0095 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 4.3232 L22: 1.9146
REMARK 3 L33: 0.9765 L12: 1.6528
REMARK 3 L13: 0.0720 L23: -0.5323
REMARK 3 S TENSOR
REMARK 3 S11: -0.1670 S12: 0.3583 S13: 0.3205
REMARK 3 S21: -0.3171 S22: 0.1500 S23: 0.1527
REMARK 3 S31: -0.2167 S32: -0.3240 S33: -0.0112
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN B AND (RESID 1:140 OR RESID 183:259)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8025 41.7670 18.8316
REMARK 3 T TENSOR
REMARK 3 T11: 0.2569 T22: 0.3445
REMARK 3 T33: 0.3322 T12: 0.0057
REMARK 3 T13: -0.0144 T23: 0.0612
REMARK 3 L TENSOR
REMARK 3 L11: 1.7069 L22: 2.3824
REMARK 3 L33: 1.5752 L12: 0.1810
REMARK 3 L13: -0.0207 L23: 0.3758
REMARK 3 S TENSOR
REMARK 3 S11: -0.0528 S12: -0.1407 S13: -0.2268
REMARK 3 S21: 0.1008 S22: 0.0577 S23: -0.3141
REMARK 3 S31: -0.0429 S32: 0.1463 S33: -0.0021
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND RESID 141:182
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8909 48.0164 31.6033
REMARK 3 T TENSOR
REMARK 3 T11: 0.3959 T22: 0.4753
REMARK 3 T33: 0.3058 T12: 0.0185
REMARK 3 T13: 0.0231 T23: 0.0776
REMARK 3 L TENSOR
REMARK 3 L11: 3.0979 L22: 1.4584
REMARK 3 L33: 0.7762 L12: 0.7690
REMARK 3 L13: -0.7791 L23: 0.6417
REMARK 3 S TENSOR
REMARK 3 S11: 0.0609 S12: -0.4872 S13: 0.0531
REMARK 3 S21: 0.3063 S22: -0.0735 S23: 0.1650
REMARK 3 S31: -0.0808 S32: 0.0268 S33: 0.0228
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 7Q4J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-NOV-21.
REMARK 100 THE DEPOSITION ID IS D_1292118970.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-SEP-09
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 : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97873, 0.97903
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49383
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.910
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.64200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.030
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: PARALLELEPIPED OF ABOUT 50 X 50 X 100 MICRO-M
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M AMMONIUM SULFATE, 0.1 M TRIS, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 33.89050
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 68.76300
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 68.76300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 50.83575
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 68.76300
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 68.76300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 16.94525
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 68.76300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 68.76300
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 50.83575
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 68.76300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 68.76300
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 16.94525
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 33.89050
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: DIMERIC
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 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 ASP A 23 CG OD1 OD2
REMARK 470 LYS A 25 CG CD CE NZ
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 OE1 GLU A 239 O HOH A 401 2.17
REMARK 500 OG SER A 113 C1 STE A 301 2.18
REMARK 500 O2 SO4 A 309 O HOH A 402 2.18
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 GLU A 43 178.98 59.82
REMARK 500 HIS A 45 38.60 39.70
REMARK 500 SER A 113 -120.28 60.05
REMARK 500 LYS A 152 -169.38 -106.21
REMARK 500 GLU B 43 177.93 63.10
REMARK 500 HIS B 45 38.91 39.78
REMARK 500 SER B 113 -122.88 62.48
REMARK 500 ALA B 137 55.01 39.38
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 STE A 301
REMARK 610 STE B 301
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE ANTIBIOTIC
REMARK 630 MOLECULE NAME: NONANE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 DD9 B 306
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: NULL
REMARK 630 DETAILS: NULL
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE ANTIBIOTIC
REMARK 630 MOLECULE NAME: DECANE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 D10 B 307
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: NULL
REMARK 630 DETAILS: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7Q4H RELATED DB: PDB
REMARK 900 THE SAME STRUCTURE WITH PMSF
DBREF1 7Q4J A 1 259 UNP A0A1I1X7Z7_THETY
DBREF2 7Q4J A A0A1I1X7Z7 1 259
DBREF1 7Q4J B 1 259 UNP A0A1I1X7Z7_THETY
DBREF2 7Q4J B A0A1I1X7Z7 1 259
SEQRES 1 A 259 MSE GLN LYS ALA VAL GLU ILE THR TYR ASN GLY MLY THR
SEQRES 2 A 259 LEU ARG GLY MSE MSE HIS LEU PRO ASP ASP VAL LYS GLY
SEQRES 3 A 259 LYS VAL PRO MSE VAL ILE MSE PHE HIS GLY PHE THR GLY
SEQRES 4 A 259 ASN LYS VAL GLU SER HIS PHE ILE PHE VAL LYS MSE SER
SEQRES 5 A 259 ARG ALA LEU GLU LYS VAL GLY ILE GLY SER VAL ARG PHE
SEQRES 6 A 259 ASP PHE TYR GLY SER GLY GLU SER ASP GLY ASP PHE SER
SEQRES 7 A 259 GLU MSE THR PHE SER SER GLU LEU GLU ASP ALA ARG GLN
SEQRES 8 A 259 ILE LEU MLY PHE VAL MLY GLU GLN PRO THR THR ASP PRO
SEQRES 9 A 259 GLU ARG ILE GLY LEU LEU GLY LEU SER MSE GLY GLY ALA
SEQRES 10 A 259 ILE ALA GLY ILE VAL ALA ARG GLU TYR MLY ASP GLU ILE
SEQRES 11 A 259 LYS ALA LEU VAL LEU TRP ALA PRO ALA PHE ASN MSE PRO
SEQRES 12 A 259 GLU LEU ILE MSE ASN GLU SER VAL LYS GLN TYR GLY ALA
SEQRES 13 A 259 ILE MSE GLU GLN LEU GLY PHE VAL ASP ILE GLY GLY HIS
SEQRES 14 A 259 MLY LEU SER LYS ASP PHE VAL GLU ASP ILE SER LYS LEU
SEQRES 15 A 259 ASN ILE PHE GLU LEU SER LYS GLY TYR ASP LYS MLZ VAL
SEQRES 16 A 259 LEU ILE VAL HIS GLY THR ASN ASP GLU ALA VAL GLU TYR
SEQRES 17 A 259 MLZ VAL SER ASP ARG ILE LEU LYS GLU VAL TYR GLY ASP
SEQRES 18 A 259 ASN ALA THR ARG VAL THR ILE GLU ASN ALA ASP HIS THR
SEQRES 19 A 259 PHE MLY SER LEU GLU TRP GLU MLZ MLY ALA ILE GLU GLU
SEQRES 20 A 259 SER VAL GLU PHE PHE MLZ LYS GLU LEU LEU LYS GLY
SEQRES 1 B 259 MSE GLN MLY ALA VAL GLU ILE THR TYR ASN GLY LYS THR
SEQRES 2 B 259 LEU ARG GLY MSE MSE HIS LEU PRO ASP ASP VAL MLY GLY
SEQRES 3 B 259 LYS VAL PRO MSE VAL ILE MSE PHE HIS GLY PHE THR GLY
SEQRES 4 B 259 ASN LYS VAL GLU SER HIS PHE ILE PHE VAL LYS MSE SER
SEQRES 5 B 259 ARG ALA LEU GLU MLY VAL GLY ILE GLY SER VAL ARG PHE
SEQRES 6 B 259 ASP PHE TYR GLY SER GLY GLU SER ASP GLY ASP PHE SER
SEQRES 7 B 259 GLU MSE THR PHE SER SER GLU LEU GLU ASP ALA ARG GLN
SEQRES 8 B 259 ILE LEU MLZ PHE VAL LYS GLU GLN PRO THR THR ASP PRO
SEQRES 9 B 259 GLU ARG ILE GLY LEU LEU GLY LEU SER MSE GLY GLY ALA
SEQRES 10 B 259 ILE ALA GLY ILE VAL ALA ARG GLU TYR MLY ASP GLU ILE
SEQRES 11 B 259 MLZ ALA LEU VAL LEU TRP ALA PRO ALA PHE ASN MSE PRO
SEQRES 12 B 259 GLU LEU ILE MSE ASN GLU SER VAL MLZ GLN TYR GLY ALA
SEQRES 13 B 259 ILE MSE GLU GLN LEU GLY PHE VAL ASP ILE GLY GLY HIS
SEQRES 14 B 259 MLY LEU SER LYS ASP PHE VAL GLU ASP ILE SER LYS LEU
SEQRES 15 B 259 ASN ILE PHE GLU LEU SER LYS GLY TYR ASP MLY MLZ VAL
SEQRES 16 B 259 LEU ILE VAL HIS GLY THR ASN ASP GLU ALA VAL GLU TYR
SEQRES 17 B 259 MLY VAL SER ASP ARG ILE LEU LYS GLU VAL TYR GLY ASP
SEQRES 18 B 259 ASN ALA THR ARG VAL THR ILE GLU ASN ALA ASP HIS THR
SEQRES 19 B 259 PHE MLY SER LEU GLU TRP GLU LYS MLY ALA ILE GLU GLU
SEQRES 20 B 259 SER VAL GLU PHE PHE MLZ MLZ GLU LEU LEU LYS GLY
MODRES 7Q4J MSE A 1 MET MODIFIED RESIDUE
MODRES 7Q4J MLY A 12 LYS MODIFIED RESIDUE
MODRES 7Q4J MSE A 17 MET MODIFIED RESIDUE
MODRES 7Q4J MSE A 18 MET MODIFIED RESIDUE
MODRES 7Q4J MSE A 30 MET MODIFIED RESIDUE
MODRES 7Q4J MSE A 33 MET MODIFIED RESIDUE
MODRES 7Q4J MSE A 51 MET MODIFIED RESIDUE
MODRES 7Q4J MSE A 80 MET MODIFIED RESIDUE
MODRES 7Q4J MLY A 94 LYS MODIFIED RESIDUE
MODRES 7Q4J MLY A 97 LYS MODIFIED RESIDUE
MODRES 7Q4J MSE A 114 MET MODIFIED RESIDUE
MODRES 7Q4J MLY A 127 LYS MODIFIED RESIDUE
MODRES 7Q4J MSE A 142 MET MODIFIED RESIDUE
MODRES 7Q4J MSE A 147 MET MODIFIED RESIDUE
MODRES 7Q4J MSE A 158 MET MODIFIED RESIDUE
MODRES 7Q4J MLY A 170 LYS MODIFIED RESIDUE
MODRES 7Q4J MLZ A 194 LYS MODIFIED RESIDUE
MODRES 7Q4J MLZ A 209 LYS MODIFIED RESIDUE
MODRES 7Q4J MLY A 236 LYS MODIFIED RESIDUE
MODRES 7Q4J MLZ A 242 LYS MODIFIED RESIDUE
MODRES 7Q4J MLY A 243 LYS MODIFIED RESIDUE
MODRES 7Q4J MLZ A 253 LYS MODIFIED RESIDUE
MODRES 7Q4J MSE B 1 MET MODIFIED RESIDUE
MODRES 7Q4J MLY B 3 LYS MODIFIED RESIDUE
MODRES 7Q4J MSE B 17 MET MODIFIED RESIDUE
MODRES 7Q4J MSE B 18 MET MODIFIED RESIDUE
MODRES 7Q4J MLY B 25 LYS MODIFIED RESIDUE
MODRES 7Q4J MSE B 30 MET MODIFIED RESIDUE
MODRES 7Q4J MSE B 33 MET MODIFIED RESIDUE
MODRES 7Q4J MSE B 51 MET MODIFIED RESIDUE
MODRES 7Q4J MLY B 57 LYS MODIFIED RESIDUE
MODRES 7Q4J MSE B 80 MET MODIFIED RESIDUE
MODRES 7Q4J MLZ B 94 LYS MODIFIED RESIDUE
MODRES 7Q4J MSE B 114 MET MODIFIED RESIDUE
MODRES 7Q4J MLY B 127 LYS MODIFIED RESIDUE
MODRES 7Q4J MLZ B 131 LYS MODIFIED RESIDUE
MODRES 7Q4J MSE B 142 MET MODIFIED RESIDUE
MODRES 7Q4J MSE B 147 MET MODIFIED RESIDUE
MODRES 7Q4J MLZ B 152 LYS MODIFIED RESIDUE
MODRES 7Q4J MSE B 158 MET MODIFIED RESIDUE
MODRES 7Q4J MLY B 170 LYS MODIFIED RESIDUE
MODRES 7Q4J MLY B 193 LYS MODIFIED RESIDUE
MODRES 7Q4J MLZ B 194 LYS MODIFIED RESIDUE
MODRES 7Q4J MLY B 209 LYS MODIFIED RESIDUE
MODRES 7Q4J MLY B 236 LYS MODIFIED RESIDUE
MODRES 7Q4J MLY B 243 LYS MODIFIED RESIDUE
MODRES 7Q4J MLZ B 253 LYS MODIFIED RESIDUE
MODRES 7Q4J MLZ B 254 LYS MODIFIED RESIDUE
HET MSE A 1 8
HET MLY A 12 11
HET MSE A 17 8
HET MSE A 18 8
HET MSE A 30 8
HET MSE A 33 8
HET MSE A 51 8
HET MSE A 80 8
HET MLY A 94 11
HET MLY A 97 11
HET MSE A 114 8
HET MLY A 127 11
HET MSE A 142 8
HET MSE A 147 8
HET MSE A 158 8
HET MLY A 170 11
HET MLZ A 194 10
HET MLZ A 209 10
HET MLY A 236 11
HET MLZ A 242 10
HET MLY A 243 11
HET MLZ A 253 10
HET MSE B 1 8
HET MLY B 3 11
HET MSE B 17 8
HET MSE B 18 8
HET MLY B 25 11
HET MSE B 30 8
HET MSE B 33 8
HET MSE B 51 8
HET MLY B 57 11
HET MSE B 80 8
HET MLZ B 94 10
HET MSE B 114 8
HET MLY B 127 11
HET MLZ B 131 10
HET MSE B 142 8
HET MSE B 147 8
HET MLZ B 152 10
HET MSE B 158 8
HET MLY B 170 11
HET MLY B 193 11
HET MLZ B 194 10
HET MLY B 209 11
HET MLY B 236 11
HET MLY B 243 11
HET MLZ B 253 10
HET MLZ B 254 10
HET STE A 301 19
HET OCT A 302 8
HET OCT A 303 8
HET GOL A 304 6
HET GOL A 305 6
HET GOL A 306 6
HET SO4 A 307 5
HET SO4 A 308 5
HET SO4 A 309 5
HET SO4 A 310 5
HET CL A 311 1
HET STE B 301 19
HET GOL B 302 6
HET GOL B 303 6
HET GOL B 304 6
HET GOL B 305 6
HET DD9 B 306 9
HET D10 B 307 10
HETNAM MSE SELENOMETHIONINE
HETNAM MLY N-DIMETHYL-LYSINE
HETNAM MLZ N-METHYL-LYSINE
HETNAM STE STEARIC ACID
HETNAM OCT N-OCTANE
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM DD9 NONANE
HETNAM D10 DECANE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 22(C5 H11 N O2 SE)
FORMUL 1 MLY 16(C8 H18 N2 O2)
FORMUL 1 MLZ 10(C7 H16 N2 O2)
FORMUL 3 STE 2(C18 H36 O2)
FORMUL 4 OCT 2(C8 H18)
FORMUL 6 GOL 7(C3 H8 O3)
FORMUL 9 SO4 4(O4 S 2-)
FORMUL 13 CL CL 1-
FORMUL 19 DD9 C9 H20
FORMUL 20 D10 C10 H22
FORMUL 21 HOH *287(H2 O)
HELIX 1 AA1 GLU A 43 HIS A 45 5 3
HELIX 2 AA2 PHE A 46 VAL A 58 1 13
HELIX 3 AA3 ASP A 76 MSE A 80 5 5
HELIX 4 AA4 THR A 81 GLU A 98 1 18
HELIX 5 AA5 SER A 113 TYR A 126 1 14
HELIX 6 AA6 ASN A 141 SER A 150 1 10
HELIX 7 AA7 LYS A 152 GLY A 162 1 11
HELIX 8 AA8 LYS A 173 LYS A 181 1 9
HELIX 9 AA9 ASN A 183 LYS A 189 1 7
HELIX 10 AB1 TYR A 208 VAL A 218 1 11
HELIX 11 AB2 SER A 237 LYS A 258 1 22
HELIX 12 AB3 GLU B 43 HIS B 45 5 3
HELIX 13 AB4 PHE B 46 VAL B 58 1 13
HELIX 14 AB5 ASP B 76 MSE B 80 5 5
HELIX 15 AB6 THR B 81 GLU B 98 1 18
HELIX 16 AB7 SER B 113 TYR B 126 1 14
HELIX 17 AB8 ASN B 141 GLU B 149 1 9
HELIX 18 AB9 MLZ B 152 GLY B 162 1 11
HELIX 19 AC1 LYS B 173 SER B 180 1 8
HELIX 20 AC2 ASN B 183 LYS B 189 1 7
HELIX 21 AC3 TYR B 208 VAL B 218 1 11
HELIX 22 AC4 SER B 237 LEU B 257 1 21
SHEET 1 AA1 8 GLN A 2 TYR A 9 0
SHEET 2 AA1 8 MLY A 12 HIS A 19 -1 O LEU A 14 N ILE A 7
SHEET 3 AA1 8 GLY A 61 PHE A 65 -1 O SER A 62 N HIS A 19
SHEET 4 AA1 8 VAL A 28 PHE A 34 1 N PRO A 29 O GLY A 61
SHEET 5 AA1 8 THR A 102 LEU A 112 1 O GLY A 108 N MSE A 30
SHEET 6 AA1 8 ALA A 132 TRP A 136 1 O TRP A 136 N GLY A 111
SHEET 7 AA1 8 MLZ A 194 GLY A 200 1 O LEU A 196 N LEU A 135
SHEET 8 AA1 8 ALA A 223 ILE A 228 1 O VAL A 226 N ILE A 197
SHEET 1 AA2 2 PHE A 163 ASP A 165 0
SHEET 2 AA2 2 MLY A 170 SER A 172 -1 O LEU A 171 N VAL A 164
SHEET 1 AA3 8 GLN B 2 TYR B 9 0
SHEET 2 AA3 8 LYS B 12 HIS B 19 -1 O LEU B 14 N ILE B 7
SHEET 3 AA3 8 GLY B 61 PHE B 65 -1 O SER B 62 N HIS B 19
SHEET 4 AA3 8 VAL B 28 PHE B 34 1 N PRO B 29 O GLY B 61
SHEET 5 AA3 8 THR B 102 LEU B 112 1 O LEU B 110 N ILE B 32
SHEET 6 AA3 8 ALA B 132 TRP B 136 1 O TRP B 136 N GLY B 111
SHEET 7 AA3 8 MLZ B 194 GLY B 200 1 O VAL B 198 N LEU B 135
SHEET 8 AA3 8 ALA B 223 ILE B 228 1 O VAL B 226 N ILE B 197
SHEET 1 AA4 2 PHE B 163 ASP B 165 0
SHEET 2 AA4 2 MLY B 170 SER B 172 -1 O LEU B 171 N VAL B 164
LINK C MSE A 1 N GLN A 2 1555 1555 1.33
LINK C GLY A 11 N MLY A 12 1555 1555 1.33
LINK C MLY A 12 N THR A 13 1555 1555 1.33
LINK C GLY A 16 N MSE A 17 1555 1555 1.33
LINK C MSE A 17 N MSE A 18 1555 1555 1.32
LINK C MSE A 18 N HIS A 19 1555 1555 1.33
LINK C PRO A 29 N MSE A 30 1555 1555 1.33
LINK C MSE A 30 N VAL A 31 1555 1555 1.33
LINK C ILE A 32 N MSE A 33 1555 1555 1.33
LINK C MSE A 33 N PHE A 34 1555 1555 1.33
LINK C LYS A 50 N MSE A 51 1555 1555 1.33
LINK C MSE A 51 N SER A 52 1555 1555 1.34
LINK C GLU A 79 N MSE A 80 1555 1555 1.33
LINK C MSE A 80 N THR A 81 1555 1555 1.33
LINK C LEU A 93 N MLY A 94 1555 1555 1.33
LINK C MLY A 94 N PHE A 95 1555 1555 1.33
LINK C VAL A 96 N MLY A 97 1555 1555 1.33
LINK C MLY A 97 N GLU A 98 1555 1555 1.33
LINK C SER A 113 N MSE A 114 1555 1555 1.33
LINK C MSE A 114 N GLY A 115 1555 1555 1.34
LINK C TYR A 126 N MLY A 127 1555 1555 1.33
LINK C MLY A 127 N ASP A 128 1555 1555 1.33
LINK C ASN A 141 N MSE A 142 1555 1555 1.33
LINK C MSE A 142 N PRO A 143 1555 1555 1.35
LINK C ILE A 146 N MSE A 147 1555 1555 1.33
LINK C MSE A 147 N ASN A 148 1555 1555 1.34
LINK C ILE A 157 N MSE A 158 1555 1555 1.33
LINK C MSE A 158 N GLU A 159 1555 1555 1.33
LINK C HIS A 169 N MLY A 170 1555 1555 1.33
LINK C MLY A 170 N LEU A 171 1555 1555 1.33
LINK C LYS A 193 N MLZ A 194 1555 1555 1.33
LINK C MLZ A 194 N VAL A 195 1555 1555 1.33
LINK C TYR A 208 N MLZ A 209 1555 1555 1.33
LINK C MLZ A 209 N VAL A 210 1555 1555 1.33
LINK C PHE A 235 N MLY A 236 1555 1555 1.33
LINK C MLY A 236 N SER A 237 1555 1555 1.33
LINK C GLU A 241 N MLZ A 242 1555 1555 1.33
LINK C MLZ A 242 N MLY A 243 1555 1555 1.33
LINK C MLY A 243 N ALA A 244 1555 1555 1.33
LINK C PHE A 252 N MLZ A 253 1555 1555 1.33
LINK C MLZ A 253 N LYS A 254 1555 1555 1.33
LINK C MSE B 1 N GLN B 2 1555 1555 1.33
LINK C GLN B 2 N MLY B 3 1555 1555 1.33
LINK C MLY B 3 N ALA B 4 1555 1555 1.33
LINK C GLY B 16 N MSE B 17 1555 1555 1.33
LINK C MSE B 17 N MSE B 18 1555 1555 1.33
LINK C MSE B 18 N HIS B 19 1555 1555 1.33
LINK C VAL B 24 N MLY B 25 1555 1555 1.33
LINK C MLY B 25 N GLY B 26 1555 1555 1.33
LINK C PRO B 29 N MSE B 30 1555 1555 1.33
LINK C MSE B 30 N VAL B 31 1555 1555 1.33
LINK C ILE B 32 N MSE B 33 1555 1555 1.33
LINK C MSE B 33 N PHE B 34 1555 1555 1.33
LINK C LYS B 50 N MSE B 51 1555 1555 1.33
LINK C MSE B 51 N SER B 52 1555 1555 1.34
LINK C GLU B 56 N MLY B 57 1555 1555 1.33
LINK C MLY B 57 N VAL B 58 1555 1555 1.33
LINK C GLU B 79 N MSE B 80 1555 1555 1.33
LINK C MSE B 80 N THR B 81 1555 1555 1.33
LINK C LEU B 93 N MLZ B 94 1555 1555 1.33
LINK C MLZ B 94 N PHE B 95 1555 1555 1.33
LINK C SER B 113 N MSE B 114 1555 1555 1.33
LINK C MSE B 114 N GLY B 115 1555 1555 1.34
LINK C TYR B 126 N MLY B 127 1555 1555 1.33
LINK C MLY B 127 N AASP B 128 1555 1555 1.33
LINK C MLY B 127 N BASP B 128 1555 1555 1.33
LINK C ILE B 130 N MLZ B 131 1555 1555 1.33
LINK C MLZ B 131 N ALA B 132 1555 1555 1.33
LINK C ASN B 141 N MSE B 142 1555 1555 1.33
LINK C MSE B 142 N PRO B 143 1555 1555 1.35
LINK C ILE B 146 N MSE B 147 1555 1555 1.33
LINK C MSE B 147 N ASN B 148 1555 1555 1.34
LINK C VAL B 151 N MLZ B 152 1555 1555 1.33
LINK C MLZ B 152 N GLN B 153 1555 1555 1.33
LINK C ILE B 157 N MSE B 158 1555 1555 1.33
LINK C MSE B 158 N GLU B 159 1555 1555 1.34
LINK C HIS B 169 N MLY B 170 1555 1555 1.33
LINK C MLY B 170 N LEU B 171 1555 1555 1.33
LINK C AASP B 192 N MLY B 193 1555 1555 1.33
LINK C BASP B 192 N MLY B 193 1555 1555 1.33
LINK C MLY B 193 N MLZ B 194 1555 1555 1.33
LINK C MLZ B 194 N VAL B 195 1555 1555 1.33
LINK C TYR B 208 N MLY B 209 1555 1555 1.33
LINK C MLY B 209 N VAL B 210 1555 1555 1.33
LINK C PHE B 235 N MLY B 236 1555 1555 1.33
LINK C MLY B 236 N SER B 237 1555 1555 1.33
LINK C LYS B 242 N MLY B 243 1555 1555 1.33
LINK C MLY B 243 N ALA B 244 1555 1555 1.33
LINK C PHE B 252 N MLZ B 253 1555 1555 1.33
LINK C MLZ B 253 N MLZ B 254 1555 1555 1.33
LINK C MLZ B 254 N GLU B 255 1555 1555 1.33
CRYST1 137.526 137.526 67.781 90.00 90.00 90.00 P 43 21 2 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 0.007271 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007271 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014753 0.00000
TER 2087 GLY A 259
TER 4187 GLY B 259
MASTER 353 0 66 22 20 0 0 6 4558 2 673 40
END |