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HEADER BIOSYNTHETIC PROTEIN 24-MAY-24 9BYU
TITLE STRUCTURE AND STABILITY OF AN APO THERMOPHILIC ESTERASE THAT
TITLE 2 HYDROLYZES POLYHYDROXYBUTYRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE, PHB DEPOLYMERASE FAMILY;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: POLYHYDROXYBUTYRATE DEPOLYMERASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LIHUAXUELLA THERMOPHILA;
SOURCE 3 ORGANISM_TAXID: 1173111;
SOURCE 4 GENE: SAMN05444955_11823;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BIOPLASTIC, ENZYMOLOGY, POLYHYDROXYALKANOATES, POLYMER HYDROLYSIS,
KEYWDS 2 THERMOPHILE, POLYHYDROXYBUTYRATE DEPOLYMERASE, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.M.THOMAS,S.QUIRK,D.J.E.HUARD,R.L.LIEBERMAN
REVDAT 1 06-NOV-24 9BYU 0
JRNL AUTH G.M.THOMAS,S.QUIRK,R.L.LIEBERMAN
JRNL TITL STRUCTURE AND STABILITY OF AN APO THERMOPHILIC ESTERASE THAT
JRNL TITL 2 HYDROLYZES POLYHYDROXYBUTYRATE.
JRNL REF ACTA CRYSTALLOGR D STRUCT 2024
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 39441250
JRNL DOI 10.1107/S2059798324009707
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 76.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.450
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.0
REMARK 3 NUMBER OF REFLECTIONS : 20110
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.146
REMARK 3 R VALUE (WORKING SET) : 0.141
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.870
REMARK 3 FREE R VALUE TEST SET COUNT : 1985
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 76.7200 - 4.2200 1.00 1512 162 0.1289 0.1656
REMARK 3 2 4.2200 - 3.3500 1.00 1461 164 0.1156 0.1518
REMARK 3 3 3.3500 - 2.9300 1.00 1465 161 0.1345 0.1908
REMARK 3 4 2.9300 - 2.6600 1.00 1463 162 0.1463 0.1937
REMARK 3 5 2.6600 - 2.4700 1.00 1436 164 0.1452 0.1966
REMARK 3 6 2.4700 - 2.3200 1.00 1461 156 0.1392 0.1853
REMARK 3 7 2.3200 - 2.2100 1.00 1463 152 0.1417 0.2073
REMARK 3 8 2.2100 - 2.1100 1.00 1438 165 0.1396 0.1929
REMARK 3 9 2.1100 - 2.0300 1.00 1458 159 0.1503 0.2318
REMARK 3 10 2.0300 - 1.9600 0.97 1376 153 0.1566 0.2191
REMARK 3 11 1.9600 - 1.9000 0.87 1269 130 0.1580 0.2641
REMARK 3 12 1.9000 - 1.8400 0.76 1082 120 0.1929 0.2666
REMARK 3 13 1.8400 - 1.7900 0.54 781 87 0.2251 0.3273
REMARK 3 14 1.7900 - 1.7500 0.32 460 50 0.2850 0.3537
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) : 0.193
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.867
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.75
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.60
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 : 0.008 2428
REMARK 3 ANGLE : 0.868 3326
REMARK 3 CHIRALITY : 0.058 342
REMARK 3 PLANARITY : 0.008 453
REMARK 3 DIHEDRAL : 6.263 359
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 9BYU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAY-24.
REMARK 100 THE DEPOSITION ID IS D_1000284398.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-OCT-23
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 : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : SI FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20114
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 76.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.0300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.15280
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 29.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 120 MM MGCL2, 60 MM TRIS, 14% PEG 4K,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 298.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 16.60567
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.21133
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 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 16.60567
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 33.21133
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 HOH A 553 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 737 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 747 LIES ON A SPECIAL POSITION.
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 VAL A 223
REMARK 465 ASP A 224
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD1 ASN A 76 NH1 ARG A 114 6554 1.93
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 THR A 41 -9.89 72.25
REMARK 500 SER A 121 -121.73 60.89
REMARK 500 SER A 121 -120.90 59.59
REMARK 500 ASP A 168 114.02 -36.85
REMARK 500 THR A 199 -64.08 -99.45
REMARK 500 ASN A 242 19.36 59.03
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 MG A 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 229 OD1
REMARK 620 2 GLN A 231 O 78.2
REMARK 620 3 ASP A 233 OD1 146.0 91.3
REMARK 620 4 ASP A 233 OD2 154.8 83.3 50.4
REMARK 620 5 HOH A 557 O 78.9 147.7 120.2 109.9
REMARK 620 6 HOH A 575 O 131.1 147.8 57.2 71.9 63.0
REMARK 620 7 HOH A 589 O 79.0 71.9 128.6 79.0 81.6 120.9
REMARK 620 N 1 2 3 4 5 6
DBREF1 9BYU A 3 302 UNP A0A1H8IKU3_9BACL
DBREF2 9BYU A A0A1H8IKU3 34 333
SEQADV 9BYU GLY A 1 UNP A0A1H8IKU EXPRESSION TAG
SEQADV 9BYU PRO A 2 UNP A0A1H8IKU EXPRESSION TAG
SEQRES 1 A 302 GLY PRO ALA GLY GLN PHE ILE ARG ASP THR ALA PRO ASP
SEQRES 2 A 302 GLY ARG VAL TYR LYS LEU TYR ILE PRO SER GLY TYR ASN
SEQRES 3 A 302 GLY SER THR PRO LEU PRO LEU VAL VAL MET LEU HIS GLY
SEQRES 4 A 302 CYS THR GLN ASN PRO ASP ASP PHE ALA ALA GLY THR GLU
SEQRES 5 A 302 MET ASN VAL TYR ALA GLU GLN ASN ASN PHE LEU VAL ALA
SEQRES 6 A 302 TYR PRO GLU GLN PRO SER SER ALA ASN LEU ASN LYS CYS
SEQRES 7 A 302 TRP ASN TRP PHE ASP SER ASN HIS GLN SER ARG GLY ARG
SEQRES 8 A 302 GLY GLU PRO ALA SER ILE ALA GLY VAL VAL GLU ASP VAL
SEQRES 9 A 302 LYS ARG ASN TYR SER VAL ASP SER ARG ARG VAL TYR ALA
SEQRES 10 A 302 ALA GLY LEU SER ALA GLY GLY ALA MET SER VAL ILE MET
SEQRES 11 A 302 GLY ALA THR TYR PRO ASP VAL PHE ALA ALA ILE GLY VAL
SEQRES 12 A 302 GLY SER GLY LEU GLU TYR LYS ALA ALA THR SER MET THR
SEQRES 13 A 302 SER ALA TYR MET ALA MET ILE ASN GLY GLY PRO ASP PRO
SEQRES 14 A 302 VAL GLN GLN GLY ASN LEU ALA TYR GLN ALA MET GLY SER
SEQRES 15 A 302 HIS ALA ARG VAL VAL PRO VAL ILE VAL PHE HIS GLY THR
SEQRES 16 A 302 SER ASP TYR THR VAL TYR PRO VAL ASN GLY HIS GLN VAL
SEQRES 17 A 302 ILE SER GLN TRP ALA GLN THR ASN ASP ARG ALA GLY ASP
SEQRES 18 A 302 GLY VAL ASP ASN ASN HIS ILE ASP ASP GLN ALA ASP VAL
SEQRES 19 A 302 THR MET ASN GLY SER VAL PRO ASN GLY ARG THR TYR THR
SEQRES 20 A 302 ARG TYR LEU TYR LYS ASP GLN ASN GLY ASN VAL VAL MET
SEQRES 21 A 302 GLU LYS ILE MET VAL ASN GLY MET GLY HIS ALA TRP SER
SEQRES 22 A 302 GLY GLY SER THR ALA GLY THR TYR THR ASP PRO ALA GLY
SEQRES 23 A 302 PRO GLU ALA SER SER MET MET TRP SER PHE PHE VAL ASN
SEQRES 24 A 302 HIS PRO LYS
HET TRS A 401 20
HET MG A 402 1
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM MG MAGNESIUM ION
HETSYN TRS TRIS BUFFER
FORMUL 2 TRS C4 H12 N O3 1+
FORMUL 3 MG MG 2+
FORMUL 4 HOH *261(H2 O)
HELIX 1 AA1 ASN A 43 GLU A 52 1 10
HELIX 2 AA2 GLU A 52 ASN A 61 1 10
HELIX 3 AA3 ASP A 83 GLN A 87 5 5
HELIX 4 AA4 ARG A 91 TYR A 108 1 18
HELIX 5 AA5 SER A 121 TYR A 134 1 14
HELIX 6 AA6 SER A 154 THR A 156 5 3
HELIX 7 AA7 SER A 157 GLY A 165 1 9
HELIX 8 AA8 ASP A 168 MET A 180 1 13
HELIX 9 AA9 GLY A 181 ALA A 184 5 4
HELIX 10 AB1 PRO A 202 GLY A 220 1 19
HELIX 11 AB2 GLU A 288 ASN A 299 1 12
SHEET 1 AA110 GLN A 5 THR A 10 0
SHEET 2 AA110 VAL A 16 ILE A 21 -1 O TYR A 17 N ASP A 9
SHEET 3 AA110 LEU A 63 PRO A 67 -1 O TYR A 66 N LYS A 18
SHEET 4 AA110 LEU A 31 LEU A 37 1 N MET A 36 O ALA A 65
SHEET 5 AA110 VAL A 110 LEU A 120 1 O ALA A 118 N LEU A 37
SHEET 6 AA110 ALA A 140 GLY A 144 1 O GLY A 144 N GLY A 119
SHEET 7 AA110 VAL A 189 GLY A 194 1 O ILE A 190 N VAL A 143
SHEET 8 AA110 VAL A 258 VAL A 265 1 O ILE A 263 N VAL A 191
SHEET 9 AA110 THR A 245 LYS A 252 -1 N TYR A 251 O VAL A 259
SHEET 10 AA110 VAL A 234 SER A 239 -1 N MET A 236 O ARG A 248
SHEET 1 AA2 2 TRP A 272 SER A 273 0
SHEET 2 AA2 2 THR A 282 ASP A 283 1 O ASP A 283 N TRP A 272
SSBOND 1 CYS A 40 CYS A 78 1555 1555 2.04
LINK OD1 ASP A 229 MG MG A 402 1555 1555 2.59
LINK O GLN A 231 MG MG A 402 1555 1555 2.76
LINK OD1 ASP A 233 MG MG A 402 1555 1555 2.71
LINK OD2 ASP A 233 MG MG A 402 1555 1555 2.42
LINK MG MG A 402 O HOH A 557 1555 1555 2.31
LINK MG MG A 402 O HOH A 575 1555 1555 2.91
LINK MG MG A 402 O HOH A 589 1555 1555 2.21
CRYST1 88.585 88.585 49.817 90.00 90.00 120.00 P 64 6
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 0.011289 0.006517 0.000000 0.00000
SCALE2 0.000000 0.013035 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020073 0.00000
TER 2349 LYS A 302
MASTER 287 0 2 11 12 0 0 6 2533 1 31 24
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