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HEADER HYDROLASE 12-JUL-25 9PJB
TITLE CRYSTAL STRUCTURE OF AN ENGINEERED THERMOSTABLE MHETASE, MHT043-5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MHETASE MHT043-5;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDATUS BATHYARCHAEOTA ARCHAEON;
SOURCE 3 ORGANISM_TAXID: 2026714;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_VARIANT: C41
KEYWDS MHETASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.I.MATHEWS,N.MURPHY,R.GARCIA,R.SARANGI,J.E.MCGEEHAN,G.T.BECKHAM,
AUTHOR 2 N.P.GAUTHIER
REVDAT 1 15-JUL-26 9PJB 0
JRNL AUTH N.MURPHY,I.I.MATHEWS,E.KOMP,E.BELL,B.NORTON-BAKER,M.CLARK,
JRNL AUTH 2 L.AVILAN,R.GARCIA,H.ALT,R.SARANGI,J.MCGEEHAN,N.P.GAUTHIER,
JRNL AUTH 3 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. 1.77 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) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 56156
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2806
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 39.3600 - 4.8000 0.99 2738 145 0.1567 0.1928
REMARK 3 2 4.8000 - 3.8100 0.98 2678 141 0.1320 0.1777
REMARK 3 3 3.8100 - 3.3300 0.99 2668 140 0.1530 0.2064
REMARK 3 4 3.3300 - 3.0300 1.00 2689 142 0.1639 0.2278
REMARK 3 5 3.0300 - 2.8100 1.00 2699 142 0.1605 0.2212
REMARK 3 6 2.8100 - 2.6400 0.99 2655 140 0.1583 0.2354
REMARK 3 7 2.6400 - 2.5100 0.98 2640 138 0.1553 0.2166
REMARK 3 8 2.5100 - 2.4000 0.97 2638 138 0.1494 0.2249
REMARK 3 9 2.4000 - 2.3100 0.99 2661 140 0.1450 0.2174
REMARK 3 10 2.3100 - 2.2300 0.99 2663 140 0.1512 0.2058
REMARK 3 11 2.2300 - 2.1600 0.99 2626 138 0.1714 0.2280
REMARK 3 12 2.1600 - 2.1000 1.00 2723 144 0.1726 0.2202
REMARK 3 13 2.1000 - 2.0400 0.99 2654 139 0.1791 0.2804
REMARK 3 14 2.0400 - 1.9900 1.00 2668 140 0.1880 0.2524
REMARK 3 15 1.9900 - 1.9500 1.00 2680 141 0.1958 0.2753
REMARK 3 16 1.9500 - 1.9100 1.00 2655 140 0.2041 0.2806
REMARK 3 17 1.9100 - 1.8700 0.99 2720 142 0.2307 0.2939
REMARK 3 18 1.8700 - 1.8300 1.00 2641 138 0.2519 0.3196
REMARK 3 19 1.8300 - 1.8000 1.00 2664 141 0.2830 0.3727
REMARK 3 20 1.8000 - 1.7700 0.96 2590 137 0.2927 0.3339
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.530
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 : 0.015 4381
REMARK 3 ANGLE : 1.254 5900
REMARK 3 CHIRALITY : 0.084 661
REMARK 3 PLANARITY : 0.012 757
REMARK 3 DIHEDRAL : 17.148 1662
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 9PJB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-25.
REMARK 100 THE DEPOSITION ID IS D_1000297941.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-25
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 : NULL
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 : 56203
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 39.360
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.3400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.71100
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M AMINOACIDS, 0.1M BUFFER SYSTEM 1,
REMARK 280 AND 30% PRECIPITANT MIX 1, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 40.59000
REMARK 290 SMTRY3 2 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 HIS A 269
REMARK 465 HIS A 270
REMARK 465 HIS A 271
REMARK 465 HIS B 268
REMARK 465 HIS B 269
REMARK 465 HIS B 270
REMARK 465 HIS B 271
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 45 178.20 59.59
REMARK 500 SER A 115 -112.65 57.62
REMARK 500 GLU B 45 177.80 62.31
REMARK 500 SER B 115 -113.89 56.35
REMARK 500 LEU B 263 129.18 -171.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 304 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 466 O
REMARK 620 2 HOH B 512 O 85.2
REMARK 620 N 1
DBREF 9PJB A 1 271 PDB 9PJB 9PJB 1 271
DBREF 9PJB B 1 271 PDB 9PJB 9PJB 1 271
SEQRES 1 A 271 MET ILE LYS PRO VAL ILE PHE THR ASN LYS GLY GLN LYS
SEQRES 2 A 271 LEU VAL GLY ILE LEU HIS VAL PRO ASP ASN LEU GLU ARG
SEQRES 3 A 271 ASP GLU LYS ALA PRO ALA ILE VAL MET LEU HIS GLY PHE
SEQRES 4 A 271 THR GLY HIS LYS SER GLU ALA HIS ARG LEU PHE VAL HIS
SEQRES 5 A 271 VAL ALA ARG SER LEU CYS ASN ALA GLY PHE VAL VAL LEU
SEQRES 6 A 271 ARG PHE ASP PHE ARG GLY SER GLY ASP SER ASP GLY ASP
SEQRES 7 A 271 PHE GLU ASP MET THR VAL PRO GLY GLU VAL SER ASP ALA
SEQRES 8 A 271 GLU ARG ALA LEU ASP PHE LEU SER LYS LEU ARG ASN VAL
SEQRES 9 A 271 ASP LYS GLU ARG ILE GLY VAL ILE GLY LEU SER MET GLY
SEQRES 10 A 271 GLY ARG VAL ALA ALA ILE LEU ALA SER LYS ASP LYS ARG
SEQRES 11 A 271 VAL LYS PHE VAL VAL LEU TYR SER ALA ALA LEU ALA PRO
SEQRES 12 A 271 LEU ARG GLU ARG PHE LEU LYS ARG LEU GLY LYS GLU ASN
SEQRES 13 A 271 LEU GLU LYS LEU LYS LYS GLY GLU ALA VAL HIS ILE GLY
SEQRES 14 A 271 ASN GLY TRP TYR LEU LYS LYS ARG PHE PHE GLU THR ILE
SEQRES 15 A 271 ASP SER PRO VAL PRO LEU GLU VAL LEU ASP LYS ILE LYS
SEQRES 16 A 271 VAL PRO VAL LEU ILE VAL HIS GLY ASP SER ASP GLU VAL
SEQRES 17 A 271 VAL PRO LEU ASP GLU ALA LYS LYS GLY TYR GLU ILE ILE
SEQRES 18 A 271 LYS ASN LEU ASN SER LYS ASN GLU LEU TYR ILE VAL LYS
SEQRES 19 A 271 GLY GLY ASP HIS THR PHE SER LYS LYS GLU HIS THR GLN
SEQRES 20 A 271 GLU VAL ILE GLU LYS THR LEU ASN TRP LEU SER SER LEU
SEQRES 21 A 271 ASN LEU LEU LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 271 MET ILE LYS PRO VAL ILE PHE THR ASN LYS GLY GLN LYS
SEQRES 2 B 271 LEU VAL GLY ILE LEU HIS VAL PRO ASP ASN LEU GLU ARG
SEQRES 3 B 271 ASP GLU LYS ALA PRO ALA ILE VAL MET LEU HIS GLY PHE
SEQRES 4 B 271 THR GLY HIS LYS SER GLU ALA HIS ARG LEU PHE VAL HIS
SEQRES 5 B 271 VAL ALA ARG SER LEU CYS ASN ALA GLY PHE VAL VAL LEU
SEQRES 6 B 271 ARG PHE ASP PHE ARG GLY SER GLY ASP SER ASP GLY ASP
SEQRES 7 B 271 PHE GLU ASP MET THR VAL PRO GLY GLU VAL SER ASP ALA
SEQRES 8 B 271 GLU ARG ALA LEU ASP PHE LEU SER LYS LEU ARG ASN VAL
SEQRES 9 B 271 ASP LYS GLU ARG ILE GLY VAL ILE GLY LEU SER MET GLY
SEQRES 10 B 271 GLY ARG VAL ALA ALA ILE LEU ALA SER LYS ASP LYS ARG
SEQRES 11 B 271 VAL LYS PHE VAL VAL LEU TYR SER ALA ALA LEU ALA PRO
SEQRES 12 B 271 LEU ARG GLU ARG PHE LEU LYS ARG LEU GLY LYS GLU ASN
SEQRES 13 B 271 LEU GLU LYS LEU LYS LYS GLY GLU ALA VAL HIS ILE GLY
SEQRES 14 B 271 ASN GLY TRP TYR LEU LYS LYS ARG PHE PHE GLU THR ILE
SEQRES 15 B 271 ASP SER PRO VAL PRO LEU GLU VAL LEU ASP LYS ILE LYS
SEQRES 16 B 271 VAL PRO VAL LEU ILE VAL HIS GLY ASP SER ASP GLU VAL
SEQRES 17 B 271 VAL PRO LEU ASP GLU ALA LYS LYS GLY TYR GLU ILE ILE
SEQRES 18 B 271 LYS ASN LEU ASN SER LYS ASN GLU LEU TYR ILE VAL LYS
SEQRES 19 B 271 GLY GLY ASP HIS THR PHE SER LYS LYS GLU HIS THR GLN
SEQRES 20 B 271 GLU VAL ILE GLU LYS THR LEU ASN TRP LEU SER SER LEU
SEQRES 21 B 271 ASN LEU LEU LEU GLU HIS HIS HIS HIS HIS HIS
HET EDO A 301 4
HET CL A 302 1
HET CL A 303 1
HET NA A 304 1
HET EDO B 301 4
HET CL B 302 1
HET CL B 303 1
HET NA B 304 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 2(C2 H6 O2)
FORMUL 4 CL 4(CL 1-)
FORMUL 6 NA 2(NA 1+)
FORMUL 11 HOH *341(H2 O)
HELIX 1 AA1 GLU A 45 HIS A 47 5 3
HELIX 2 AA2 ARG A 48 ALA A 60 1 13
HELIX 3 AA3 ASP A 78 MET A 82 5 5
HELIX 4 AA4 THR A 83 LYS A 100 1 18
HELIX 5 AA5 SER A 115 ASP A 128 1 14
HELIX 6 AA6 LEU A 144 GLY A 153 1 10
HELIX 7 AA7 GLY A 153 LYS A 162 1 10
HELIX 8 AA8 LYS A 175 ILE A 182 1 8
HELIX 9 AA9 VAL A 186 ILE A 194 5 9
HELIX 10 AB1 PRO A 210 LYS A 222 1 13
HELIX 11 AB2 LYS A 242 SER A 258 1 17
HELIX 12 AB3 SER A 259 LEU A 264 5 6
HELIX 13 AB4 GLU B 45 HIS B 47 5 3
HELIX 14 AB5 ARG B 48 ALA B 60 1 13
HELIX 15 AB6 ASP B 78 MET B 82 5 5
HELIX 16 AB7 THR B 83 LYS B 100 1 18
HELIX 17 AB8 SER B 115 ASP B 128 1 14
HELIX 18 AB9 LEU B 144 ARG B 151 1 8
HELIX 19 AC1 GLY B 153 LYS B 162 1 10
HELIX 20 AC2 LYS B 175 ILE B 182 1 8
HELIX 21 AC3 VAL B 186 LEU B 191 1 6
HELIX 22 AC4 ASP B 192 ILE B 194 5 3
HELIX 23 AC5 PRO B 210 LYS B 222 1 13
HELIX 24 AC6 LYS B 242 LEU B 260 1 19
SHEET 1 AA1 8 ILE A 2 ASN A 9 0
SHEET 2 AA1 8 GLN A 12 HIS A 19 -1 O LEU A 14 N PHE A 7
SHEET 3 AA1 8 VAL A 63 PHE A 67 -1 O VAL A 64 N HIS A 19
SHEET 4 AA1 8 ALA A 30 LEU A 36 1 N ILE A 33 O LEU A 65
SHEET 5 AA1 8 VAL A 104 LEU A 114 1 O ILE A 112 N LEU A 36
SHEET 6 AA1 8 VAL A 134 TYR A 137 1 O TYR A 137 N GLY A 113
SHEET 7 AA1 8 VAL A 198 GLY A 203 1 O LEU A 199 N LEU A 136
SHEET 8 AA1 8 GLU A 229 VAL A 233 1 O TYR A 231 N ILE A 200
SHEET 1 AA2 2 VAL A 166 GLY A 169 0
SHEET 2 AA2 2 TRP A 172 LEU A 174 -1 O TRP A 172 N ILE A 168
SHEET 1 AA3 8 ILE B 2 ASN B 9 0
SHEET 2 AA3 8 GLN B 12 HIS B 19 -1 O LEU B 14 N PHE B 7
SHEET 3 AA3 8 VAL B 63 PHE B 67 -1 O ARG B 66 N ILE B 17
SHEET 4 AA3 8 ALA B 30 LEU B 36 1 N ILE B 33 O LEU B 65
SHEET 5 AA3 8 VAL B 104 LEU B 114 1 O ASP B 105 N ALA B 30
SHEET 6 AA3 8 VAL B 134 TYR B 137 1 O TYR B 137 N GLY B 113
SHEET 7 AA3 8 VAL B 198 GLY B 203 1 O LEU B 199 N LEU B 136
SHEET 8 AA3 8 GLU B 229 VAL B 233 1 O TYR B 231 N ILE B 200
SHEET 1 AA4 2 VAL B 166 GLY B 169 0
SHEET 2 AA4 2 TRP B 172 LEU B 174 -1 O LEU B 174 N VAL B 166
LINK NA NA A 304 O HOH A 466 1555 1555 3.12
LINK NA NA A 304 O HOH B 512 1555 1555 3.09
LINK NA NA B 304 O HOH B 480 1555 1555 2.87
CISPEP 1 SER A 184 PRO A 185 0 2.64
CISPEP 2 SER B 184 PRO B 185 0 -3.92
CRYST1 47.380 81.180 79.920 90.00 106.06 90.00 P 1 21 1 4
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 0.021106 0.000000 0.006075 0.00000
SCALE2 0.000000 0.012318 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013020 0.00000
TER 2157 HIS A 268
TER 4290 HIS B 267
MASTER 254 0 8 24 20 0 0 6 4593 2 13 42
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