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HEADER HYDROLASE 10-JUL-25 9PID
TITLE CRYSTAL STRUCTURE OF AN ENGINEERED THERMOSTABLE MHETASE, MHT077, W148R
TITLE 2 VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA FOLD HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARMATIMONADOTA BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 2033014;
SOURCE 4 GENE: ENP40_11315;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: C41
KEYWDS MHETASE, W148R VARIANT, PET DEGRADING ENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.I.MATHEWS,N.P.MURPHY,R.GARCIA,R.SARANGI,J.MCGEEHAN,G.T.BECKHAM,
AUTHOR 2 N.P.GAUTHIER
REVDAT 1 15-JUL-26 9PID 0
JRNL AUTH N.P.MURPHY,J.E.GADO,I.I.MATHEWS,K.KOMP,E.L.BELL,
JRNL AUTH 2 B.NORTON-BAKER,M.CLARK,L.AVILAN,R.GARCIA,H.ALT,R.SARANGI,
JRNL AUTH 3 A.PICKFORD,J.E.MCGEEHAN,N.P.GAUTHIER,G.T.BECKHAM
JRNL TITL ENGINEERING THERMOSTABLE FERULIC ACID ESTERASES FOR MHET
JRNL TITL 2 HYDROLYSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.21.1_5286: ???)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.43
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 131235
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6563
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 35.4300 - 3.8500 1.00 4605 243 0.1500 0.1818
REMARK 3 2 3.8500 - 3.0600 0.97 4267 224 0.1611 0.1879
REMARK 3 3 3.0600 - 2.6700 1.00 4348 229 0.1738 0.2300
REMARK 3 4 2.6700 - 2.4300 1.00 4337 229 0.1726 0.2070
REMARK 3 5 2.4300 - 2.2500 1.00 4299 226 0.1648 0.1978
REMARK 3 6 2.2500 - 2.1200 0.99 4302 226 0.1709 0.2186
REMARK 3 7 2.1200 - 2.0100 0.99 4266 225 0.1784 0.2193
REMARK 3 8 2.0100 - 1.9300 0.96 4110 216 0.1772 0.2143
REMARK 3 9 1.9300 - 1.8500 0.98 4192 221 0.1948 0.2380
REMARK 3 10 1.8500 - 1.7900 0.99 4233 223 0.1833 0.2335
REMARK 3 11 1.7900 - 1.7300 0.99 4228 222 0.1954 0.2364
REMARK 3 12 1.7300 - 1.6800 0.99 4192 221 0.1849 0.1937
REMARK 3 13 1.6800 - 1.6400 0.98 4197 221 0.1767 0.2448
REMARK 3 14 1.6400 - 1.6000 0.98 4204 221 0.1785 0.2226
REMARK 3 15 1.6000 - 1.5600 0.98 4187 220 0.1756 0.2118
REMARK 3 16 1.5600 - 1.5300 0.98 4140 218 0.1769 0.2154
REMARK 3 17 1.5300 - 1.5000 0.97 4170 220 0.1874 0.2458
REMARK 3 18 1.5000 - 1.4700 0.97 4117 217 0.2047 0.2570
REMARK 3 19 1.4700 - 1.4400 0.97 4116 216 0.2023 0.2541
REMARK 3 20 1.4400 - 1.4200 0.95 4047 213 0.2175 0.2676
REMARK 3 21 1.4200 - 1.4000 0.97 4070 214 0.2233 0.2986
REMARK 3 22 1.4000 - 1.3800 0.96 4115 217 0.2497 0.2949
REMARK 3 23 1.3700 - 1.3500 0.96 4061 214 0.2581 0.2945
REMARK 3 24 1.3500 - 1.3400 0.96 4090 215 0.2502 0.2764
REMARK 3 25 1.3400 - 1.3200 0.95 4016 212 0.2575 0.2717
REMARK 3 26 1.3200 - 1.3000 0.94 3992 210 0.2917 0.2973
REMARK 3 27 1.3000 - 1.2800 0.93 3931 207 0.4076 0.4855
REMARK 3 28 1.2800 - 1.2700 0.94 3969 209 0.2710 0.3152
REMARK 3 29 1.2700 - 1.2500 0.93 3928 206 0.2846 0.3181
REMARK 3 30 1.2500 - 1.2400 0.93 3943 208 0.2936 0.2773
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.510
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 : 0.005 4141
REMARK 3 ANGLE : 0.782 5608
REMARK 3 CHIRALITY : 0.082 597
REMARK 3 PLANARITY : 0.009 755
REMARK 3 DIHEDRAL : 18.019 1568
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 9PID COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-25.
REMARK 100 THE DEPOSITION ID IS D_1000297879.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : RH COATED COLLIMATING MIRRORS, K
REMARK 200 -B FOCUSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 131248
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.240
REMARK 200 RESOLUTION RANGE LOW (A) : 39.160
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 10.50
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.6200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.27
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.77500
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE (PH 4.5), 22% PEG
REMARK 280 SMEAR BROAD, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 -1.000000 0.000000 0.000000 23.78500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.39500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.74000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.39500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.78500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.74000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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 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 1
REMARK 465 ILE A 2
REMARK 465 GLY B 1
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 B 225 O HOH B 401 1.90
REMARK 500 NH2 ARG B 243 O HOH B 401 2.16
REMARK 500 O GLY B 30 NH1 ARG B 105 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 3 CB - CG - CD1 ANGL. DEV. = -10.5 DEGREES
REMARK 500 ARG A 202 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
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 LYS A 17 -168.72 -125.87
REMARK 500 GLU A 47 178.52 60.41
REMARK 500 SER A 117 -120.33 61.78
REMARK 500 LYS B 17 -167.91 -119.64
REMARK 500 GLU B 47 178.18 60.80
REMARK 500 SER B 117 -120.88 61.76
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 638 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH A 639 DISTANCE = 6.32 ANGSTROMS
DBREF1 9PID A 1 252 UNP A0A7C2Z7G5_UNCAM
DBREF2 9PID A A0A7C2Z7G5 118 369
DBREF1 9PID B 1 252 UNP A0A7C2Z7G5_UNCAM
DBREF2 9PID B A0A7C2Z7G5 118 369
SEQADV 9PID MET A 60 UNP A0A7C2Z7G VAL 177 CONFLICT
SEQADV 9PID VAL A 65 UNP A0A7C2Z7G ILE 182 CONFLICT
SEQADV 9PID ARG A 148 UNP A0A7C2Z7G TRP 265 VARIANT
SEQADV 9PID ILE A 154 UNP A0A7C2Z7G VAL 271 CONFLICT
SEQADV 9PID TYR A 164 UNP A0A7C2Z7G ASN 281 CONFLICT
SEQADV 9PID MET A 165 UNP A0A7C2Z7G LEU 282 CONFLICT
SEQADV 9PID LYS A 187 UNP A0A7C2Z7G ARG 304 CONFLICT
SEQADV 9PID ASN A 215 UNP A0A7C2Z7G SER 332 CONFLICT
SEQADV 9PID GLU A 225 UNP A0A7C2Z7G ASP 342 CONFLICT
SEQADV 9PID MET B 60 UNP A0A7C2Z7G VAL 177 CONFLICT
SEQADV 9PID VAL B 65 UNP A0A7C2Z7G ILE 182 CONFLICT
SEQADV 9PID ARG B 148 UNP A0A7C2Z7G TRP 265 VARIANT
SEQADV 9PID ILE B 154 UNP A0A7C2Z7G VAL 271 CONFLICT
SEQADV 9PID TYR B 164 UNP A0A7C2Z7G ASN 281 CONFLICT
SEQADV 9PID MET B 165 UNP A0A7C2Z7G LEU 282 CONFLICT
SEQADV 9PID LYS B 187 UNP A0A7C2Z7G ARG 304 CONFLICT
SEQADV 9PID ASN B 215 UNP A0A7C2Z7G SER 332 CONFLICT
SEQADV 9PID GLU B 225 UNP A0A7C2Z7G ASP 342 CONFLICT
SEQRES 1 A 252 GLY ILE LEU ASN ALA MET GLU GLU LEU LEU TRP ILE PRO
SEQRES 2 A 252 SER ARG GLY LYS ARG MET ALA ALA VAL LEU HIS LEU PRO
SEQRES 3 A 252 GLU GLY ARG GLY ARG ALA PRO ALA VAL LEU MET CYS HIS
SEQRES 4 A 252 GLY PHE THR GLY HIS LYS ALA GLU ALA HIS ARG LEU PHE
SEQRES 5 A 252 VAL HIS THR ALA ARG ARG LEU MET GLN GLU GLY LEU VAL
SEQRES 6 A 252 VAL LEU ARG PHE ASP PHE LEU GLY SER GLY ASP SER GLU
SEQRES 7 A 252 GLY LEU PHE GLU GLU MET THR ILE ARG GLY GLU VAL GLU
SEQRES 8 A 252 ASP ALA LEU ASN ALA LEU ALA PHE LEU ARG GLY HIS GLY
SEQRES 9 A 252 ARG VAL ASP ALA ALA ARG VAL ALA MET LEU GLY PHE SER
SEQRES 10 A 252 LEU GLY GLY CYS VAL VAL ALA LEU SER LEU PRO ARG ALA
SEQRES 11 A 252 GLY ALA VAL LYS THR LEU VAL LEU TRP ALA PRO VAL SER
SEQRES 12 A 252 ASN PRO MET ARG ARG MET PRO PRO THR GLY ILE PRO ASP
SEQRES 13 A 252 LYS PRO GLN ASN ARG GLY GLY TYR MET VAL GLY VAL ASN
SEQRES 14 A 252 PHE PHE ARG GLU LEU PRO ASP LEU LYS PRO LEU GLU SER
SEQRES 15 A 252 VAL ARG ASP TYR LYS GLY THR VAL LEU VAL LEU HIS GLY
SEQRES 16 A 252 SER ALA ASP GLU ALA VAL ARG PRO ASP GLU GLY ARG ALA
SEQRES 17 A 252 TYR GLU ARG ALA PHE THR ASN ALA GLN ARG PHE GLU PHE
SEQRES 18 A 252 HIS LEU ILE GLU GLY ALA ASP HIS THR PHE THR GLN PRO
SEQRES 19 A 252 ASP ALA GLU ARG ARG LEU ILE GLU ARG THR THR GLU TRP
SEQRES 20 A 252 LEU ARG ALA GLN VAL
SEQRES 1 B 252 GLY ILE LEU ASN ALA MET GLU GLU LEU LEU TRP ILE PRO
SEQRES 2 B 252 SER ARG GLY LYS ARG MET ALA ALA VAL LEU HIS LEU PRO
SEQRES 3 B 252 GLU GLY ARG GLY ARG ALA PRO ALA VAL LEU MET CYS HIS
SEQRES 4 B 252 GLY PHE THR GLY HIS LYS ALA GLU ALA HIS ARG LEU PHE
SEQRES 5 B 252 VAL HIS THR ALA ARG ARG LEU MET GLN GLU GLY LEU VAL
SEQRES 6 B 252 VAL LEU ARG PHE ASP PHE LEU GLY SER GLY ASP SER GLU
SEQRES 7 B 252 GLY LEU PHE GLU GLU MET THR ILE ARG GLY GLU VAL GLU
SEQRES 8 B 252 ASP ALA LEU ASN ALA LEU ALA PHE LEU ARG GLY HIS GLY
SEQRES 9 B 252 ARG VAL ASP ALA ALA ARG VAL ALA MET LEU GLY PHE SER
SEQRES 10 B 252 LEU GLY GLY CYS VAL VAL ALA LEU SER LEU PRO ARG ALA
SEQRES 11 B 252 GLY ALA VAL LYS THR LEU VAL LEU TRP ALA PRO VAL SER
SEQRES 12 B 252 ASN PRO MET ARG ARG MET PRO PRO THR GLY ILE PRO ASP
SEQRES 13 B 252 LYS PRO GLN ASN ARG GLY GLY TYR MET VAL GLY VAL ASN
SEQRES 14 B 252 PHE PHE ARG GLU LEU PRO ASP LEU LYS PRO LEU GLU SER
SEQRES 15 B 252 VAL ARG ASP TYR LYS GLY THR VAL LEU VAL LEU HIS GLY
SEQRES 16 B 252 SER ALA ASP GLU ALA VAL ARG PRO ASP GLU GLY ARG ALA
SEQRES 17 B 252 TYR GLU ARG ALA PHE THR ASN ALA GLN ARG PHE GLU PHE
SEQRES 18 B 252 HIS LEU ILE GLU GLY ALA ASP HIS THR PHE THR GLN PRO
SEQRES 19 B 252 ASP ALA GLU ARG ARG LEU ILE GLU ARG THR THR GLU TRP
SEQRES 20 B 252 LEU ARG ALA GLN VAL
HET EDO A 301 4
HET CL A 302 1
HET EDO B 301 8
HET CL B 302 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 2(C2 H6 O2)
FORMUL 4 CL 2(CL 1-)
FORMUL 7 HOH *455(H2 O)
HELIX 1 AA1 GLU A 47 HIS A 49 5 3
HELIX 2 AA2 ARG A 50 GLU A 62 1 13
HELIX 3 AA3 LEU A 80 MET A 84 5 5
HELIX 4 AA4 THR A 85 GLY A 102 1 18
HELIX 5 AA5 SER A 117 LEU A 127 1 11
HELIX 6 AA6 PRO A 128 ALA A 130 5 3
HELIX 7 AA7 ASN A 144 MET A 149 5 6
HELIX 8 AA8 GLY A 167 LEU A 174 1 8
HELIX 9 AA9 PRO A 175 LEU A 177 5 3
HELIX 10 AB1 LYS A 178 VAL A 183 1 6
HELIX 11 AB2 ARG A 202 ALA A 208 1 7
HELIX 12 AB3 TYR A 209 ALA A 212 5 4
HELIX 13 AB4 GLN A 233 VAL A 252 1 20
HELIX 14 AB5 GLU B 47 HIS B 49 5 3
HELIX 15 AB6 ARG B 50 GLU B 62 1 13
HELIX 16 AB7 LEU B 80 MET B 84 5 5
HELIX 17 AB8 THR B 85 HIS B 103 1 19
HELIX 18 AB9 SER B 117 GLY B 131 1 15
HELIX 19 AC1 ASN B 144 MET B 149 5 6
HELIX 20 AC2 GLY B 167 LEU B 174 1 8
HELIX 21 AC3 PRO B 175 LEU B 177 5 3
HELIX 22 AC4 LYS B 178 VAL B 183 1 6
HELIX 23 AC5 ARG B 202 ALA B 208 1 7
HELIX 24 AC6 ALA B 208 PHE B 213 1 6
HELIX 25 AC7 GLN B 233 VAL B 252 1 20
SHEET 1 AA1 8 MET A 6 SER A 14 0
SHEET 2 AA1 8 LYS A 17 LEU A 25 -1 O LEU A 25 N MET A 6
SHEET 3 AA1 8 VAL A 65 PHE A 69 -1 O VAL A 66 N HIS A 24
SHEET 4 AA1 8 ALA A 32 CYS A 38 1 N MET A 37 O LEU A 67
SHEET 5 AA1 8 VAL A 106 PHE A 116 1 O ASP A 107 N ALA A 32
SHEET 6 AA1 8 THR A 135 TRP A 139 1 O TRP A 139 N GLY A 115
SHEET 7 AA1 8 THR A 189 GLY A 195 1 O LEU A 191 N LEU A 138
SHEET 8 AA1 8 ARG A 218 ILE A 224 1 O GLU A 220 N VAL A 192
SHEET 1 AA2 2 GLN A 159 ARG A 161 0
SHEET 2 AA2 2 TYR A 164 VAL A 166 -1 O VAL A 166 N GLN A 159
SHEET 1 AA3 8 MET B 6 SER B 14 0
SHEET 2 AA3 8 LYS B 17 LEU B 25 -1 O LEU B 25 N MET B 6
SHEET 3 AA3 8 VAL B 65 PHE B 69 -1 O VAL B 66 N HIS B 24
SHEET 4 AA3 8 ALA B 32 CYS B 38 1 N MET B 37 O LEU B 67
SHEET 5 AA3 8 VAL B 106 PHE B 116 1 O LEU B 114 N LEU B 36
SHEET 6 AA3 8 THR B 135 TRP B 139 1 O TRP B 139 N GLY B 115
SHEET 7 AA3 8 THR B 189 GLY B 195 1 O LEU B 191 N LEU B 138
SHEET 8 AA3 8 ARG B 218 ILE B 224 1 O GLU B 220 N VAL B 192
SHEET 1 AA4 2 GLN B 159 ARG B 161 0
SHEET 2 AA4 2 TYR B 164 VAL B 166 -1 O VAL B 166 N GLN B 159
CRYST1 47.570 85.480 116.790 90.00 90.00 90.00 P 21 21 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 0.021022 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011699 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008562 0.00000
TER 2020 VAL A 252
TER 4034 VAL B 252
MASTER 303 0 4 25 20 0 0 6 4389 2 12 40
END |