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HEADER HYDROLASE 30-OCT-21 7Q4H
TITLE A THERMOSTABLE LIPASE FROM THERMOANAEROBACTER THERMOHYDROSULFURICUS IN
TITLE 2 COMPLEX WITH PMSF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROLASE_4 DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: METHYLATED LYSINES;
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_COMMON: CLOSTRIDIUM THERMOHYDROSULFURICUM;
SOURCE 4 ORGANISM_TAXID: 1516;
SOURCE 5 GENE: SAMN04324257_00243;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: THERMOANAEROBACTER THERMOHYDROSULFURICUS;
SOURCE 10 ORGANISM_COMMON: CLOSTRIDIUM THERMOHYDROSULFURICUM;
SOURCE 11 ORGANISM_TAXID: 1516;
SOURCE 12 GENE: SAMN04324257_00243;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA HYDROLASE, HYDROLASE, THERMOSTABLE, PMSF
EXPDTA X-RAY DIFFRACTION
AUTHOR N.PINOTSIS,M.WILMANNS
REVDAT 1 10-MAY-23 7Q4H 0
JRNL AUTH N.PINOTSIS,M.WILMANNS
JRNL TITL A THERMOSTABLE LIPASE FROM THERMOANAEROBACTER
JRNL TITL 2 THERMOHYDROSULFURICUS IN COMPLEX WITH PMSF
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.400
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 38901
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.134
REMARK 3 FREE R VALUE TEST SET COUNT : 1219
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 29.9840 - 4.1569 1.00 4553 141 0.1499 0.1783
REMARK 3 2 4.1569 - 3.3008 1.00 4302 148 0.1613 0.2023
REMARK 3 3 3.3008 - 2.8840 1.00 4252 157 0.2014 0.2605
REMARK 3 4 2.8840 - 2.6205 1.00 4249 128 0.1991 0.2655
REMARK 3 5 2.6205 - 2.4327 1.00 4197 134 0.2006 0.2324
REMARK 3 6 2.4327 - 2.2894 1.00 4200 134 0.2165 0.2918
REMARK 3 7 2.2894 - 2.1747 1.00 4160 119 0.2327 0.2762
REMARK 3 8 2.1747 - 2.0801 0.98 4153 124 0.2714 0.3516
REMARK 3 9 2.0801 - 2.0100 0.87 3616 134 0.3149 0.3513
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) : 0.268
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.243
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.38
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.00
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 : 0.005 4260
REMARK 3 ANGLE : 0.937 5712
REMARK 3 CHIRALITY : 0.035 621
REMARK 3 PLANARITY : 0.003 721
REMARK 3 DIHEDRAL : 16.249 1602
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 1:140) OR (RESSEQ 183:259))
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0791 -14.9436 3.3440
REMARK 3 T TENSOR
REMARK 3 T11: 0.2270 T22: 0.3328
REMARK 3 T33: 0.3145 T12: -0.0908
REMARK 3 T13: -0.0180 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 1.0028 L22: 0.9232
REMARK 3 L33: 0.8224 L12: -0.0481
REMARK 3 L13: -0.0567 L23: -0.1282
REMARK 3 S TENSOR
REMARK 3 S11: -0.0841 S12: 0.0444 S13: 0.3174
REMARK 3 S21: -0.0183 S22: 0.0600 S23: 0.1337
REMARK 3 S31: -0.2746 S32: 0.3575 S33: 0.0261
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 1:140) OR (RESSEQ 183:259))
REMARK 3 ORIGIN FOR THE GROUP (A): 11.0689 -41.3773 18.6544
REMARK 3 T TENSOR
REMARK 3 T11: 0.2311 T22: 0.3548
REMARK 3 T33: 0.2733 T12: -0.0047
REMARK 3 T13: 0.0493 T23: 0.0768
REMARK 3 L TENSOR
REMARK 3 L11: 1.0823 L22: 1.7453
REMARK 3 L33: 0.6343 L12: 0.2398
REMARK 3 L13: 0.4779 L23: -0.3750
REMARK 3 S TENSOR
REMARK 3 S11: 0.1510 S12: -0.5124 S13: -0.1441
REMARK 3 S21: 0.4038 S22: -0.0005 S23: 0.2704
REMARK 3 S31: 0.1240 S32: 0.0434 S33: 0.2658
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 141:182))
REMARK 3 ORIGIN FOR THE GROUP (A): 26.2188 -34.1327 -9.8339
REMARK 3 T TENSOR
REMARK 3 T11: 0.3950 T22: 0.6082
REMARK 3 T33: 0.2806 T12: 0.0364
REMARK 3 T13: 0.0412 T23: -0.0328
REMARK 3 L TENSOR
REMARK 3 L11: 0.7472 L22: 2.8073
REMARK 3 L33: 1.3935 L12: 1.0362
REMARK 3 L13: 0.4639 L23: -0.1467
REMARK 3 S TENSOR
REMARK 3 S11: -0.1257 S12: 0.3091 S13: -0.1256
REMARK 3 S21: -0.6488 S22: 0.1902 S23: -0.3972
REMARK 3 S31: 0.3665 S32: 0.6972 S33: -0.0425
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 141:182))
REMARK 3 ORIGIN FOR THE GROUP (A): 29.3914 -31.2190 30.7206
REMARK 3 T TENSOR
REMARK 3 T11: 0.4926 T22: 0.6610
REMARK 3 T33: 0.3040 T12: -0.0697
REMARK 3 T13: -0.0476 T23: -0.0362
REMARK 3 L TENSOR
REMARK 3 L11: 0.1487 L22: 0.1265
REMARK 3 L33: 0.0116 L12: -0.0067
REMARK 3 L13: 0.0003 L23: 0.0370
REMARK 3 S TENSOR
REMARK 3 S11: 0.2885 S12: -0.2332 S13: -0.0050
REMARK 3 S21: 0.3862 S22: -0.0420 S23: -0.3053
REMARK 3 S31: 0.0076 S32: 0.0002 S33: 0.0008
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 7Q4H 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_1292118940.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-OCT-07
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) : 0.95372
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 : 38930
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08200
REMARK 200 FOR THE DATA SET : 24.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.51400
REMARK 200 FOR SHELL : 4.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: APO STRUCTURE
REMARK 200
REMARK 200 REMARK: LONG, VERY THIN RODS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4M AMMONIUM SULFATE, 0.1M TRIS, PH
REMARK 280 7.5, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 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,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+1/4
REMARK 290 8555 -Y,-X,-Z+3/4
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 78.74200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 118.11300
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 39.37100
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 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 78.74200
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 39.37100
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 118.11300
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 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 A 422 LIES ON A SPECIAL POSITION.
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 470 GLU A 186 CD OE1 OE2
REMARK 470 LYS A 216 CG CD CE NZ
REMARK 470 GLU A 229 CG CD OE1 OE2
REMARK 470 GLU A 239 CD OE1 OE2
REMARK 470 LYS A 254 CD CE NZ
REMARK 470 LYS A 258 CG CD CE NZ
REMARK 470 ASP B 23 CG OD1 OD2
REMARK 470 LYS B 216 CE NZ
REMARK 470 LYS B 258 CG CD CE NZ
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 43 173.10 63.99
REMARK 500 HIS A 45 40.97 38.31
REMARK 500 SEB A 113 -114.15 55.06
REMARK 500 ASN A 230 -14.49 75.58
REMARK 500 LYS A 258 -56.15 -134.50
REMARK 500 GLU B 43 176.18 59.79
REMARK 500 HIS B 45 39.03 39.48
REMARK 500 ARG B 106 53.60 -116.99
REMARK 500 SEB B 113 -114.15 51.91
REMARK 500 GLU B 129 17.04 -141.06
REMARK 500 ALA B 137 54.96 39.24
REMARK 500 GLN B 153 -30.12 -149.57
REMARK 500 ASN B 230 -5.32 69.11
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7Q4H A 1 259 UNP A0A1I1X7Z7_THETY
DBREF2 7Q4H A A0A1I1X7Z7 1 259
DBREF1 7Q4H B 1 259 UNP A0A1I1X7Z7_THETY
DBREF2 7Q4H B A0A1I1X7Z7 1 259
SEQRES 1 A 259 MET GLN LYS ALA VAL GLU ILE THR TYR ASN GLY MLZ THR
SEQRES 2 A 259 LEU ARG GLY MET MET HIS LEU PRO ASP ASP VAL LYS GLY
SEQRES 3 A 259 LYS VAL PRO MET VAL ILE MET PHE HIS GLY PHE THR GLY
SEQRES 4 A 259 ASN LYS VAL GLU SER HIS PHE ILE PHE VAL LYS MET 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 MET THR PHE SER SER GLU LEU GLU ASP ALA ARG GLN
SEQRES 8 A 259 ILE LEU LYS PHE VAL LYS GLU GLN PRO THR THR ASP PRO
SEQRES 9 A 259 GLU ARG ILE GLY LEU LEU GLY LEU SEB MET GLY GLY ALA
SEQRES 10 A 259 ILE ALA GLY ILE VAL ALA ARG GLU TYR LYS ASP GLU ILE
SEQRES 11 A 259 LYS ALA LEU VAL LEU TRP ALA PRO ALA PHE ASN MET PRO
SEQRES 12 A 259 GLU LEU ILE MET ASN GLU SER VAL LYS GLN TYR GLY ALA
SEQRES 13 A 259 ILE MET GLU GLN LEU GLY PHE VAL ASP ILE GLY GLY HIS
SEQRES 14 A 259 LYS LEU SER LYS ASP PHE VAL GLU ASP ILE SER LYS LEU
SEQRES 15 A 259 ASN ILE PHE GLU LEU SER MLZ GLY TYR ASP MLY LYS VAL
SEQRES 16 A 259 LEU ILE VAL HIS GLY THR ASN ASP GLU ALA VAL GLU TYR
SEQRES 17 A 259 LYS 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 LYS LYS ALA ILE GLU GLU
SEQRES 20 A 259 SER VAL GLU PHE PHE MLZ LYS GLU LEU LEU LYS GLY
SEQRES 1 B 259 MET GLN MLY ALA VAL GLU ILE THR TYR ASN GLY LYS THR
SEQRES 2 B 259 LEU ARG GLY MET MET HIS LEU PRO ASP ASP VAL MLZ GLY
SEQRES 3 B 259 MLZ VAL PRO MET VAL ILE MET PHE HIS GLY PHE THR GLY
SEQRES 4 B 259 ASN LYS VAL GLU SER HIS PHE ILE PHE VAL LYS MET SER
SEQRES 5 B 259 ARG ALA LEU GLU LYS 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 MET THR PHE SER SER GLU LEU GLU ASP ALA ARG GLN
SEQRES 8 B 259 ILE LEU LYS PHE VAL LYS GLU GLN PRO THR THR ASP PRO
SEQRES 9 B 259 GLU ARG ILE GLY LEU LEU GLY LEU SEB MET GLY GLY ALA
SEQRES 10 B 259 ILE ALA GLY ILE VAL ALA ARG GLU TYR LYS ASP GLU ILE
SEQRES 11 B 259 MLY ALA LEU VAL LEU TRP ALA PRO ALA PHE ASN MET PRO
SEQRES 12 B 259 GLU LEU ILE MET ASN GLU SER VAL LYS GLN TYR GLY ALA
SEQRES 13 B 259 ILE MET GLU GLN LEU GLY PHE VAL ASP ILE GLY GLY HIS
SEQRES 14 B 259 LYS 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 LYS MLY VAL
SEQRES 16 B 259 LEU ILE VAL HIS GLY THR ASN ASP GLU ALA VAL GLU TYR
SEQRES 17 B 259 LYS 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 MLZ SER LEU GLU TRP GLU LYS LYS ALA ILE GLU GLU
SEQRES 20 B 259 SER VAL GLU PHE PHE MLY LYS GLU LEU LEU LYS GLY
MODRES 7Q4H MLZ A 12 LYS MODIFIED RESIDUE
MODRES 7Q4H SEB A 113 SER MODIFIED RESIDUE
MODRES 7Q4H MLZ A 189 LYS MODIFIED RESIDUE
MODRES 7Q4H MLY A 193 LYS MODIFIED RESIDUE
MODRES 7Q4H MLY A 236 LYS MODIFIED RESIDUE
MODRES 7Q4H MLZ A 253 LYS MODIFIED RESIDUE
MODRES 7Q4H MLY B 3 LYS MODIFIED RESIDUE
MODRES 7Q4H MLZ B 25 LYS MODIFIED RESIDUE
MODRES 7Q4H MLZ B 27 LYS MODIFIED RESIDUE
MODRES 7Q4H SEB B 113 SER MODIFIED RESIDUE
MODRES 7Q4H MLY B 131 LYS MODIFIED RESIDUE
MODRES 7Q4H MLY B 194 LYS MODIFIED RESIDUE
MODRES 7Q4H MLZ B 236 LYS MODIFIED RESIDUE
MODRES 7Q4H MLY B 253 LYS MODIFIED RESIDUE
HET MLZ A 12 10
HET SEB A 113 16
HET MLZ A 189 10
HET MLY A 193 11
HET MLY A 236 11
HET MLZ A 253 10
HET MLY B 3 11
HET MLZ B 25 10
HET MLZ B 27 10
HET SEB B 113 16
HET MLY B 131 11
HET MLY B 194 11
HET MLZ B 236 10
HET MLY B 253 11
HET CL A 301 1
HET GOL A 302 12
HET GOL A 303 6
HET GOL A 304 6
HET SO4 A 305 5
HET SO4 A 306 5
HET OLC B 301 25
HET GOL B 302 6
HET SO4 B 303 5
HETNAM MLZ N-METHYL-LYSINE
HETNAM SEB O-BENZYLSULFONYL-SERINE
HETNAM MLY N-DIMETHYL-LYSINE
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 1 MLZ 6(C7 H16 N2 O2)
FORMUL 1 SEB 2(C10 H13 N O5 S)
FORMUL 1 MLY 6(C8 H18 N2 O2)
FORMUL 3 CL CL 1-
FORMUL 4 GOL 4(C3 H8 O3)
FORMUL 7 SO4 3(O4 S 2-)
FORMUL 9 OLC C21 H40 O4
FORMUL 12 HOH *136(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 MET A 80 5 5
HELIX 4 AA4 THR A 81 GLU A 98 1 18
HELIX 5 AA5 SEB A 113 TYR A 126 1 14
HELIX 6 AA6 ASN A 141 GLY A 162 1 22
HELIX 7 AA7 LYS A 173 LYS A 181 1 9
HELIX 8 AA8 ASN A 183 MLZ A 189 1 7
HELIX 9 AA9 TYR A 208 VAL A 218 1 11
HELIX 10 AB1 SER A 237 LEU A 257 1 21
HELIX 11 AB2 GLU B 43 HIS B 45 5 3
HELIX 12 AB3 PHE B 46 VAL B 58 1 13
HELIX 13 AB4 ASP B 76 MET B 80 5 5
HELIX 14 AB5 THR B 81 GLU B 98 1 18
HELIX 15 AB6 SEB B 113 TYR B 126 1 14
HELIX 16 AB7 ASN B 141 GLN B 153 1 13
HELIX 17 AB8 GLN B 153 GLY B 162 1 10
HELIX 18 AB9 LYS B 173 LYS B 181 1 9
HELIX 19 AC1 ASN B 183 LYS B 189 1 7
HELIX 20 AC2 TYR B 208 VAL B 218 1 11
HELIX 21 AC3 SER B 237 LEU B 257 1 21
SHEET 1 AA1 8 GLN A 2 TYR A 9 0
SHEET 2 AA1 8 MLZ 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 LEU A 110 N ILE A 32
SHEET 6 AA1 8 ALA A 132 TRP A 136 1 O VAL A 134 N LEU A 109
SHEET 7 AA1 8 VAL A 195 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 LYS 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 MLY B 194 GLY B 200 1 O LEU B 196 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 LYS B 170 SER B 172 -1 O LEU B 171 N VAL B 164
LINK C GLY A 11 N MLZ A 12 1555 1555 1.33
LINK C MLZ A 12 N THR A 13 1555 1555 1.33
LINK C LEU A 112 N SEB A 113 1555 1555 1.33
LINK C SEB A 113 N MET A 114 1555 1555 1.33
LINK C SER A 188 N MLZ A 189 1555 1555 1.33
LINK C MLZ A 189 N GLY A 190 1555 1555 1.33
LINK C ASP A 192 N MLY A 193 1555 1555 1.33
LINK C MLY A 193 N LYS A 194 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 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 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 VAL B 24 N MLZ B 25 1555 1555 1.33
LINK C MLZ B 25 N GLY B 26 1555 1555 1.33
LINK C GLY B 26 N MLZ B 27 1555 1555 1.33
LINK C MLZ B 27 N VAL B 28 1555 1555 1.33
LINK C LEU B 112 N SEB B 113 1555 1555 1.33
LINK C SEB B 113 N MET B 114 1555 1555 1.33
LINK C ILE B 130 N MLY B 131 1555 1555 1.33
LINK C MLY B 131 N ALA B 132 1555 1555 1.33
LINK C LYS B 193 N MLY B 194 1555 1555 1.33
LINK C MLY B 194 N VAL B 195 1555 1555 1.33
LINK C PHE B 235 N MLZ B 236 1555 1555 1.33
LINK C MLZ B 236 N SER B 237 1555 1555 1.33
LINK C PHE B 252 N MLY B 253 1555 1555 1.33
LINK C MLY B 253 N LYS B 254 1555 1555 1.33
CRYST1 84.808 84.808 157.484 90.00 90.00 90.00 P 43 2 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 0.011791 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011791 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006350 0.00000
TER 2049 GLY A 259
TER 4121 GLY B 259
MASTER 326 0 23 21 20 0 0 6 4302 2 256 40
END |