| content |
HEADER HYDROLASE 10-JUL-25 9PIC
TITLE CRYSTAL STRUCTURE OF AN ENGINEERED THERMOSTABLE MHETASE, MHT077
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA FOLD HYDROLASE;
COMPND 3 CHAIN: A;
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, PET DEGRADATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.I.MATHEWS,N.P.MURPHY,R.GARCIA,R.SARANGI,J.E.MCGEEHAN,G.T.BECKHAM,
AUTHOR 2 N.P.GAUTHIER
REVDAT 1 15-JUL-26 9PIC 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. 1.16 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.21.2_5419: ???)
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) : 1.16
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 80457
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.166
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4023
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 39.5900 - 3.5600 1.00 2929 154 0.1452 0.1537
REMARK 3 2 3.5600 - 2.8300 1.00 2811 148 0.1489 0.1409
REMARK 3 3 2.8300 - 2.4700 1.00 2796 147 0.1523 0.1777
REMARK 3 4 2.4700 - 2.2400 1.00 2797 146 0.1404 0.1634
REMARK 3 5 2.2400 - 2.0800 1.00 2750 145 0.1408 0.1585
REMARK 3 6 2.0800 - 1.9600 0.99 2736 144 0.1397 0.1570
REMARK 3 7 1.9600 - 1.8600 1.00 2746 144 0.1354 0.1588
REMARK 3 8 1.8600 - 1.7800 1.00 2761 146 0.1422 0.1627
REMARK 3 9 1.7800 - 1.7100 1.00 2731 143 0.1383 0.1625
REMARK 3 10 1.7100 - 1.6500 1.00 2728 144 0.1334 0.1997
REMARK 3 11 1.6500 - 1.6000 1.00 2752 145 0.1293 0.1463
REMARK 3 12 1.6000 - 1.5600 1.00 2733 144 0.1226 0.1482
REMARK 3 13 1.5600 - 1.5200 1.00 2732 144 0.1246 0.1429
REMARK 3 14 1.5200 - 1.4800 0.99 2720 143 0.1287 0.1527
REMARK 3 15 1.4800 - 1.4500 0.99 2697 142 0.1360 0.1729
REMARK 3 16 1.4500 - 1.4100 1.00 2722 143 0.1323 0.1683
REMARK 3 17 1.4100 - 1.3900 1.00 2708 143 0.1437 0.1517
REMARK 3 18 1.3900 - 1.3600 1.00 2721 143 0.1437 0.1549
REMARK 3 19 1.3600 - 1.3400 1.00 2738 144 0.1547 0.1881
REMARK 3 20 1.3400 - 1.3100 1.00 2724 144 0.1545 0.2028
REMARK 3 21 1.3100 - 1.2900 1.00 2684 141 0.1522 0.1596
REMARK 3 22 1.2900 - 1.2700 1.00 2734 144 0.1660 0.2171
REMARK 3 23 1.2700 - 1.2500 0.98 2658 140 0.1980 0.2230
REMARK 3 24 1.2500 - 1.2400 0.94 2572 136 0.2269 0.2243
REMARK 3 25 1.2400 - 1.2200 0.89 2417 127 0.2679 0.2818
REMARK 3 26 1.2200 - 1.2000 0.84 2295 121 0.2695 0.2533
REMARK 3 27 1.2000 - 1.1900 0.80 2151 113 0.2923 0.3338
REMARK 3 28 1.1900 - 1.1700 0.75 2039 108 0.2986 0.3317
REMARK 3 29 1.1700 - 1.1600 0.68 1852 97 0.3298 0.3203
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) : 0.100
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.890
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 : 0.004 2106
REMARK 3 ANGLE : 0.817 2852
REMARK 3 CHIRALITY : 0.088 301
REMARK 3 PLANARITY : 0.011 383
REMARK 3 DIHEDRAL : 15.656 793
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 9PIC 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_1000297691.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-FEB-24
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 : 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 : 80496
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.160
REMARK 200 RESOLUTION RANGE LOW (A) : 39.590
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 10.80
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.3900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.16
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.19
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.54100
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 (%): 42.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.075M KSCN, 0.075M SODIUM FORMATE,
REMARK 280 0.025M SODIUM CITRATE (PH 5.8), 0.025M CACODYLATE (PH 6.5),
REMARK 280 0.025M HEPES (PH 7.4), 0.025M TRIS (PH 8.0), 25% PEG1500, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.21500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.21500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 23.92000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.55500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 23.92000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.55500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 46.21500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 23.92000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 54.55500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 46.21500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 23.92000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 54.55500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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: 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 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 CL CL A 305 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 470 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 642 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 647 LIES ON A SPECIAL POSITION.
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 -169.58 -126.89
REMARK 500 GLU A 47 177.94 62.60
REMARK 500 ARG A 110 62.76 -119.92
REMARK 500 SER A 117 -121.06 64.90
REMARK 500 SER A 117 -111.23 60.07
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 691 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH A 692 DISTANCE = 6.12 ANGSTROMS
DBREF1 9PIC A 1 252 UNP A0A7C2Z7G5_UNCAM
DBREF2 9PIC A A0A7C2Z7G5 118 369
SEQADV 9PIC MET A 60 UNP A0A7C2Z7G VAL 177 CONFLICT
SEQADV 9PIC VAL A 65 UNP A0A7C2Z7G ILE 182 CONFLICT
SEQADV 9PIC ILE A 154 UNP A0A7C2Z7G VAL 271 CONFLICT
SEQADV 9PIC TYR A 164 UNP A0A7C2Z7G ASN 281 CONFLICT
SEQADV 9PIC MET A 165 UNP A0A7C2Z7G LEU 282 CONFLICT
SEQADV 9PIC LYS A 187 UNP A0A7C2Z7G ARG 304 CONFLICT
SEQADV 9PIC ASN A 215 UNP A0A7C2Z7G SER 332 CONFLICT
SEQADV 9PIC GLU A 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 TRP 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
HET EDO A 301 4
HET EDO A 302 4
HET SCN A 303 3
HET SCN A 304 3
HET CL A 305 1
HET CL A 306 2
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SCN THIOCYANATE ION
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO 2(C2 H6 O2)
FORMUL 4 SCN 2(C N S 1-)
FORMUL 6 CL 2(CL 1-)
FORMUL 8 HOH *292(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 PHE A 213 1 12
HELIX 12 AB3 GLN A 233 VAL A 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 LEU A 114 N LEU A 36
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
CRYST1 47.840 109.110 92.430 90.00 90.00 90.00 C 2 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 0.020903 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009165 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010819 0.00000
TER 2042 VAL A 252
MASTER 281 0 6 12 10 0 0 6 2280 1 14 20
END |