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HEADER HYDROLASE 21-JAN-22 7WOL
TITLE CRYSTAL STRUCTURE OF LIPASE TRLIPB FROM THERMOMOCROBIUM ROSEUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOMICROBIUM ROSEUM DSM 5159;
SOURCE 3 ORGANISM_TAXID: 309801;
SOURCE 4 STRAIN: ATCC 27502 / DSM 5159 / P-2;
SOURCE 5 GENE: TRD_1687;
SOURCE 6 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 1423
KEYWDS LIPID DEGRADATION, LIPID METABOLISM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.ZHANG,Y.FANG,Y.SHI,Z.GU,Y.XIN
REVDAT 1 25-JAN-23 7WOL 0
JRNL AUTH Y.FANG,Y.XIN,Y.SHI,Z.GU,L.ZHANG
JRNL TITL CRYSTAL STRUCTURE OF LIPASE TRLIPB FROM THERMOMOCROBIUM
JRNL TITL 2 ROSEUM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 70744
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.943
REMARK 3 FREE R VALUE TEST SET COUNT : 3497
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4911
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2300
REMARK 3 BIN FREE R VALUE SET COUNT : 270
REMARK 3 BIN FREE R VALUE : 0.2310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4948
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 110
REMARK 3 SOLVENT ATOMS : 417
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.71700
REMARK 3 B22 (A**2) : -1.71700
REMARK 3 B33 (A**2) : 3.43300
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): 0.112
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.108
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.894
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.962
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5190 ; 0.008 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 5005 ; 0.001 ; 0.015
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7055 ; 1.454 ; 1.649
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11461 ; 1.319 ; 1.570
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 641 ; 6.212 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 298 ;27.203 ;19.799
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 768 ;12.394 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 61 ;19.610 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 639 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5840 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1218 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1047 ; 0.209 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 46 ; 0.259 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2484 ; 0.161 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 379 ; 0.161 ; 0.200
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): 2555 ; 2.593 ; 3.838
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2554 ; 2.592 ; 3.836
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3190 ; 3.596 ; 5.741
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3191 ; 3.596 ; 5.743
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2635 ; 3.562 ; 4.356
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2636 ; 3.561 ; 4.357
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3862 ; 5.397 ; 6.329
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3863 ; 5.396 ; 6.331
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 BULK SOLVENT
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 7WOL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE DEPOSITION ID IS D_1300026937.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL45XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70819
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 45.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.40
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 22.8000
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) : 2.04
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.82100
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
REMARK 200 STARTING MODEL: 1LZK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M SUCCINIC ACID,0.1M HEPES,7,1%
REMARK 280 W/VPEG 2000 MME, VAPOR DIFFUSION, SITTING 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 61.39600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 64.70100
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 64.70100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 92.09400
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 64.70100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 64.70100
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 30.69800
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 64.70100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 64.70100
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 92.09400
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 64.70100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 64.70100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 30.69800
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 61.39600
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 18.0 KCAL/MOL
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 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 ALA A 324
REMARK 465 ALA A 325
REMARK 465 LEU A 326
REMARK 465 GLU A 327
REMARK 465 HIS A 328
REMARK 465 HIS A 329
REMARK 465 HIS A 330
REMARK 465 HIS A 331
REMARK 465 HIS A 332
REMARK 465 HIS A 333
REMARK 465 MET B 1
REMARK 465 ALA B 42
REMARK 465 LEU B 43
REMARK 465 ALA B 44
REMARK 465 SER B 45
REMARK 465 LEU B 46
REMARK 465 LEU B 47
REMARK 465 ALA B 324
REMARK 465 ALA B 325
REMARK 465 LEU B 326
REMARK 465 GLU B 327
REMARK 465 HIS B 328
REMARK 465 HIS B 329
REMARK 465 HIS B 330
REMARK 465 HIS B 331
REMARK 465 HIS B 332
REMARK 465 HIS B 333
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 TYR A 95 -4.29 74.94
REMARK 500 SER A 165 -121.89 59.63
REMARK 500 TYR A 193 64.29 27.71
REMARK 500 ILE A 214 -64.09 80.31
REMARK 500 LEU B 39 -71.11 -45.54
REMARK 500 TYR B 95 -4.20 74.85
REMARK 500 TYR B 131 136.40 -40.00
REMARK 500 SER B 165 -122.52 61.26
REMARK 500 TYR B 193 64.06 29.68
REMARK 500 ILE B 214 -62.14 83.19
REMARK 500 ALA B 299 57.81 -145.40
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7WOL A 1 320 UNP B9L0X7 B9L0X7_THERP 1 320
DBREF 7WOL B 1 320 UNP B9L0X7 B9L0X7_THERP 1 320
SEQADV 7WOL LYS A 321 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL LEU A 322 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL ALA A 323 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL ALA A 324 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL ALA A 325 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL LEU A 326 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL GLU A 327 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL HIS A 328 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL HIS A 329 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL HIS A 330 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL HIS A 331 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL HIS A 332 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL HIS A 333 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL LYS B 321 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL LEU B 322 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL ALA B 323 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL ALA B 324 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL ALA B 325 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL LEU B 326 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL GLU B 327 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL HIS B 328 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL HIS B 329 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL HIS B 330 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL HIS B 331 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL HIS B 332 UNP B9L0X7 EXPRESSION TAG
SEQADV 7WOL HIS B 333 UNP B9L0X7 EXPRESSION TAG
SEQRES 1 A 333 MET SER VAL PHE ALA ARG LEU ASP PRO GLU LEU ALA ALA
SEQRES 2 A 333 ALA LEU ARG GLU ILE PRO GLU GLU PHE LEU LEU ASP LEU
SEQRES 3 A 333 ARG ASP ILE SER LEU ALA ARG ARG ARG LEU GLN ILE LEU
SEQRES 4 A 333 ARG GLU ALA LEU ALA SER LEU LEU PRO PRO LEU PRO SER
SEQRES 5 A 333 ASP VAL ALA VAL THR ASP GLU LEU ALA PRO ASN SER PHE
SEQRES 6 A 333 ASP GLY THR MET VAL ARG VAL ARG LEU TYR ARG PRO SER
SEQRES 7 A 333 GLU VAL THR GLY PRO LEU PRO VAL LEU LEU TRP ILE HIS
SEQRES 8 A 333 GLY GLY GLY TYR VAL MET GLY ALA PRO GLU MET ASN ASP
SEQRES 9 A 333 GLN GLN CYS ALA GLU LEU ALA GLN ARG ILE PRO ALA LEU
SEQRES 10 A 333 VAL ALA SER VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO
SEQRES 11 A 333 TYR PRO ALA PRO LEU GLU ASP CYS TYR ALA ALA LEU ARG
SEQRES 12 A 333 TRP VAL ALA GLU ARG ALA GLU GLN LEU GLY VAL ASP ARG
SEQRES 13 A 333 GLU ARG LEU ALA ILE ALA GLY ALA SER ALA GLY GLY GLY
SEQRES 14 A 333 LEU ALA ALA GLY LEU ALA LEU LEU ALA ARG ASP ARG GLY
SEQRES 15 A 333 GLU VAL PRO VAL ARG PHE GLN LEU LEU ILE TYR PRO MET
SEQRES 16 A 333 LEU ASP ASP ARG ASN GLN THR PRO SER SER TYR GLU ILE
SEQRES 17 A 333 THR ASP PRO ARG LEU ILE TRP THR ARG ASP TRP ASN LEU
SEQRES 18 A 333 ILE GLY TRP ARG ALA TYR LEU GLY ARG GLU PRO GLY SER
SEQRES 19 A 333 PRO ASP VAL PRO PRO TYR ALA ALA PRO ALA ARG ALA ASP
SEQRES 20 A 333 ASP LEU ALA GLY LEU PRO PRO ALA TYR VAL LEU VAL GLY
SEQRES 21 A 333 THR ALA ASP LEU PHE ARG ASP GLU ASP ILE ALA TYR ALA
SEQRES 22 A 333 GLN ARG LEU MET GLN ALA GLY VAL PRO THR GLU LEU HIS
SEQRES 23 A 333 VAL PHE ALA GLY ALA PHE HIS GLY PHE ASP VAL PHE ALA
SEQRES 24 A 333 PRO THR ALA TRP VAL SER GLN ARG ALA ASN ALA GLU VAL
SEQRES 25 A 333 LEU ALA VAL LEU GLN ARG ALA LEU LYS LEU ALA ALA ALA
SEQRES 26 A 333 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 333 MET SER VAL PHE ALA ARG LEU ASP PRO GLU LEU ALA ALA
SEQRES 2 B 333 ALA LEU ARG GLU ILE PRO GLU GLU PHE LEU LEU ASP LEU
SEQRES 3 B 333 ARG ASP ILE SER LEU ALA ARG ARG ARG LEU GLN ILE LEU
SEQRES 4 B 333 ARG GLU ALA LEU ALA SER LEU LEU PRO PRO LEU PRO SER
SEQRES 5 B 333 ASP VAL ALA VAL THR ASP GLU LEU ALA PRO ASN SER PHE
SEQRES 6 B 333 ASP GLY THR MET VAL ARG VAL ARG LEU TYR ARG PRO SER
SEQRES 7 B 333 GLU VAL THR GLY PRO LEU PRO VAL LEU LEU TRP ILE HIS
SEQRES 8 B 333 GLY GLY GLY TYR VAL MET GLY ALA PRO GLU MET ASN ASP
SEQRES 9 B 333 GLN GLN CYS ALA GLU LEU ALA GLN ARG ILE PRO ALA LEU
SEQRES 10 B 333 VAL ALA SER VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO
SEQRES 11 B 333 TYR PRO ALA PRO LEU GLU ASP CYS TYR ALA ALA LEU ARG
SEQRES 12 B 333 TRP VAL ALA GLU ARG ALA GLU GLN LEU GLY VAL ASP ARG
SEQRES 13 B 333 GLU ARG LEU ALA ILE ALA GLY ALA SER ALA GLY GLY GLY
SEQRES 14 B 333 LEU ALA ALA GLY LEU ALA LEU LEU ALA ARG ASP ARG GLY
SEQRES 15 B 333 GLU VAL PRO VAL ARG PHE GLN LEU LEU ILE TYR PRO MET
SEQRES 16 B 333 LEU ASP ASP ARG ASN GLN THR PRO SER SER TYR GLU ILE
SEQRES 17 B 333 THR ASP PRO ARG LEU ILE TRP THR ARG ASP TRP ASN LEU
SEQRES 18 B 333 ILE GLY TRP ARG ALA TYR LEU GLY ARG GLU PRO GLY SER
SEQRES 19 B 333 PRO ASP VAL PRO PRO TYR ALA ALA PRO ALA ARG ALA ASP
SEQRES 20 B 333 ASP LEU ALA GLY LEU PRO PRO ALA TYR VAL LEU VAL GLY
SEQRES 21 B 333 THR ALA ASP LEU PHE ARG ASP GLU ASP ILE ALA TYR ALA
SEQRES 22 B 333 GLN ARG LEU MET GLN ALA GLY VAL PRO THR GLU LEU HIS
SEQRES 23 B 333 VAL PHE ALA GLY ALA PHE HIS GLY PHE ASP VAL PHE ALA
SEQRES 24 B 333 PRO THR ALA TRP VAL SER GLN ARG ALA ASN ALA GLU VAL
SEQRES 25 B 333 LEU ALA VAL LEU GLN ARG ALA LEU LYS LEU ALA ALA ALA
SEQRES 26 B 333 LEU GLU HIS HIS HIS HIS HIS HIS
HET SIN A 401 8
HET GOL A 402 6
HET PEG A 403 7
HET PEG A 404 7
HET GOL A 405 6
HET GOL A 406 6
HET EDO A 407 4
HET GOL A 408 6
HET EDO A 409 4
HET EDO A 410 4
HET EDO A 411 4
HET SIN B 401 8
HET PEG B 402 7
HET EDO B 403 4
HET PEG B 404 7
HET EDO B 405 4
HET EDO B 406 4
HET EDO B 407 4
HET GOL B 408 6
HET EDO B 409 4
HETNAM SIN SUCCINIC ACID
HETNAM GOL GLYCEROL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 SIN 2(C4 H6 O4)
FORMUL 4 GOL 5(C3 H8 O3)
FORMUL 5 PEG 4(C4 H10 O3)
FORMUL 9 EDO 9(C2 H6 O2)
FORMUL 23 HOH *417(H2 O)
HELIX 1 AA1 ASP A 8 GLU A 17 1 10
HELIX 2 AA2 ILE A 18 LEU A 23 5 6
HELIX 3 AA3 ASP A 28 LEU A 46 1 19
HELIX 4 AA4 ALA A 99 MET A 102 5 4
HELIX 5 AA5 ASN A 103 ILE A 114 1 12
HELIX 6 AA6 PRO A 132 GLY A 153 1 22
HELIX 7 AA7 SER A 165 GLY A 182 1 18
HELIX 8 AA8 PRO A 203 ILE A 208 1 6
HELIX 9 AA9 ASP A 210 ILE A 214 5 5
HELIX 10 AB1 THR A 216 GLY A 229 1 14
HELIX 11 AB2 ALA A 242 ALA A 246 5 5
HELIX 12 AB3 PHE A 265 ALA A 279 1 15
HELIX 13 AB4 GLY A 294 ALA A 299 1 6
HELIX 14 AB5 ALA A 302 LYS A 321 1 20
HELIX 15 AB6 ASP B 8 GLU B 17 1 10
HELIX 16 AB7 ILE B 18 LEU B 23 5 6
HELIX 17 AB8 ASP B 28 GLU B 41 1 14
HELIX 18 AB9 ALA B 99 MET B 102 5 4
HELIX 19 AC1 ASN B 103 ILE B 114 1 12
HELIX 20 AC2 PRO B 132 ARG B 148 1 17
HELIX 21 AC3 ARG B 148 GLY B 153 1 6
HELIX 22 AC4 SER B 165 GLY B 182 1 18
HELIX 23 AC5 THR B 202 ILE B 208 1 7
HELIX 24 AC6 ASP B 210 ILE B 214 5 5
HELIX 25 AC7 THR B 216 GLY B 229 1 14
HELIX 26 AC8 ALA B 242 ALA B 246 5 5
HELIX 27 AC9 PHE B 265 ALA B 279 1 15
HELIX 28 AD1 GLY B 294 ALA B 299 1 6
HELIX 29 AD2 ALA B 302 LYS B 321 1 20
SHEET 1 AA116 VAL A 54 PRO A 62 0
SHEET 2 AA116 MET A 69 PRO A 77 -1 O VAL A 70 N ALA A 61
SHEET 3 AA116 LEU A 117 VAL A 121 -1 O SER A 120 N ARG A 73
SHEET 4 AA116 LEU A 84 ILE A 90 1 N LEU A 87 O ALA A 119
SHEET 5 AA116 VAL A 154 ALA A 164 1 O ALA A 160 N LEU A 88
SHEET 6 AA116 PHE A 188 ILE A 192 1 O ILE A 192 N GLY A 163
SHEET 7 AA116 ALA A 255 ALA A 262 1 O TYR A 256 N LEU A 191
SHEET 8 AA116 THR A 283 PHE A 292 1 O GLU A 284 N VAL A 257
SHEET 9 AA116 THR B 283 PHE B 292 -1 O LEU B 285 N VAL A 287
SHEET 10 AA116 ALA B 255 ALA B 262 1 N VAL B 257 O HIS B 286
SHEET 11 AA116 PHE B 188 ILE B 192 1 N LEU B 191 O TYR B 256
SHEET 12 AA116 VAL B 154 ALA B 164 1 N GLY B 163 O ILE B 192
SHEET 13 AA116 LEU B 84 ILE B 90 1 N LEU B 88 O ALA B 160
SHEET 14 AA116 LEU B 117 VAL B 121 1 O ALA B 119 N LEU B 87
SHEET 15 AA116 MET B 69 PRO B 77 -1 N ARG B 73 O SER B 120
SHEET 16 AA116 VAL B 54 PRO B 62 -1 N THR B 57 O LEU B 74
CISPEP 1 ILE A 114 PRO A 115 0 -11.15
CISPEP 2 ALA A 126 PRO A 127 0 -2.31
CISPEP 3 TYR A 131 PRO A 132 0 2.71
CISPEP 4 ILE B 114 PRO B 115 0 -10.70
CISPEP 5 ALA B 126 PRO B 127 0 -1.38
CISPEP 6 TYR B 131 PRO B 132 0 2.30
CRYST1 129.402 129.402 122.792 90.00 90.00 90.00 P 43 21 2 16
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 0.007728 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007728 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008144 0.00000
TER 2511 ALA A 323
TER 4974 ALA B 323
MASTER 318 0 20 29 16 0 0 6 5475 2 110 52
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