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HEADER HYDROLASE 26-JUN-13 4BVK
TITLE STRUCTURE OF Y190E MUTANT OF PHAZ7 PHB DEPOLYMERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHB DEPOLYMERASE PHAZ7;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 39-380;
COMPND 5 SYNONYM: PHB DEPOLYMERASE;
COMPND 6 EC: 3.1.1.75;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PAUCIMONAS LEMOIGNEI;
SOURCE 3 ORGANISM_TAXID: 29443;
SOURCE 4 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 1423;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: WB800
KEYWDS HYDROLASE, CATALYTIC TRIAD, BIOPOLYMER BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HERMAWAN,B.SUBEDI,A.C.PAPAGEORGIOU,D.JENDROSSEK
REVDAT 1 18-SEP-13 4BVK 0
JRNL AUTH D.JENDROSSEK,S.HERMAWAN,B.SUBEDI,A.C.PAPAGEORGIOU
JRNL TITL BIOCHEMICAL ANALYSIS AND STRUCTURE DETERMINATION OF
JRNL TITL 2 PAUCIMONAS LEMOIGNEI POLY(3-HYDROXYBUTYRATE) (PHB)
JRNL TITL 3 DEPOLYMERASE PHAZ7 MUTEINS REVEAL THE PHB BINDING SITE AND
JRNL TITL 4 DETAILS OF SUBSTRATE-ENZYME INTERACTIONS.
JRNL REF MOL.MICROBIOL. 2013
JRNL REFN ESSN 1365-2958
JRNL PMID 24007310
JRNL DOI 10.1111/MMI.12391
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.C.PAPAGEORGIOU,S.HERMAWAN,C.B.SINGH,D.JENDROSSEK
REMARK 1 TITL STRUCTURAL BASIS OF POLY(3-HYDROXYBUTYRATE) HYDROLYSIS BY
REMARK 1 TITL 2 PHAZ7 DEPOLYMERASE FROM PAUCIMONAS LEMOIGNEI.
REMARK 1 REF J.MOL.BIOL. V. 382 1184 2008
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 18706425
REMARK 1 DOI 10.1016/J.JMB.2008.07.078
REMARK 2
REMARK 2 RESOLUTION. 1.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 1.606
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.776
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.00
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.83
REMARK 3 NUMBER OF REFLECTIONS : 81141
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1366
REMARK 3 R VALUE (WORKING SET) : 0.1348
REMARK 3 FREE R VALUE : 0.1701
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 4058
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 19.7777 - 4.9098 0.90 2537 134 0.1654 0.1833
REMARK 3 2 4.9098 - 3.9069 0.93 2599 137 0.1185 0.1250
REMARK 3 3 3.9069 - 3.4159 0.95 2639 139 0.1184 0.1568
REMARK 3 4 3.4159 - 3.1049 0.96 2679 141 0.1346 0.1760
REMARK 3 5 3.1049 - 2.8831 0.97 2697 142 0.1304 0.1569
REMARK 3 6 2.8831 - 2.7135 0.97 2715 143 0.1232 0.1664
REMARK 3 7 2.7135 - 2.5779 0.98 2688 141 0.1241 0.1595
REMARK 3 8 2.5779 - 2.4659 0.98 2718 143 0.1237 0.1579
REMARK 3 9 2.4659 - 2.3712 0.97 2755 145 0.1315 0.1767
REMARK 3 10 2.3712 - 2.2895 0.98 2688 142 0.1286 0.1686
REMARK 3 11 2.2895 - 2.2180 0.99 2715 142 0.1268 0.1562
REMARK 3 12 2.2180 - 2.1547 0.97 2759 146 0.1273 0.1652
REMARK 3 13 2.1547 - 2.0980 0.98 2664 140 0.1328 0.1516
REMARK 3 14 2.0980 - 2.0469 0.98 2764 145 0.1348 0.1885
REMARK 3 15 2.0469 - 2.0004 0.98 2684 142 0.1277 0.1765
REMARK 3 16 2.0004 - 1.9579 0.98 2713 142 0.1324 0.1610
REMARK 3 17 1.9579 - 1.9187 0.98 2704 143 0.1352 0.1745
REMARK 3 18 1.9187 - 1.8825 0.98 2707 142 0.1403 0.1668
REMARK 3 19 1.8825 - 1.8489 0.97 2693 142 0.1416 0.1977
REMARK 3 20 1.8489 - 1.8176 0.96 2682 141 0.1443 0.1921
REMARK 3 21 1.8176 - 1.7883 0.98 2690 142 0.1474 0.2154
REMARK 3 22 1.7883 - 1.7608 0.95 2657 140 0.1436 0.2107
REMARK 3 23 1.7608 - 1.7349 0.97 2669 140 0.1459 0.1777
REMARK 3 24 1.7349 - 1.7105 0.96 2663 140 0.1504 0.1871
REMARK 3 25 1.7105 - 1.6874 0.95 2663 140 0.1547 0.2067
REMARK 3 26 1.6874 - 1.6655 0.96 2594 137 0.1616 0.2153
REMARK 3 27 1.6655 - 1.6447 0.95 2611 137 0.1667 0.2110
REMARK 3 28 1.6447 - 1.6249 0.94 2667 141 0.1698 0.1942
REMARK 3 29 1.6249 - 1.6060 0.75 2069 109 0.1859 0.2233
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.50
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.14
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.17
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.84
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.5
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 : 0.009 5285
REMARK 3 ANGLE : 1.180 7183
REMARK 3 CHIRALITY : 0.068 761
REMARK 3 PLANARITY : 0.006 935
REMARK 3 DIHEDRAL : 12.774 1796
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 4BVK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUN-13.
REMARK 100 THE PDBE ID CODE IS EBI-57479.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8123
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (SX-165)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81143
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.60
REMARK 200 RESOLUTION RANGE LOW (A) : 19.80
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 2.9
REMARK 200 R MERGE (I) : 0.04
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.6
REMARK 200 R MERGE FOR SHELL (I) : 0.23
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.70
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: PDB ENTRY 4BRS
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOUR DIFFUSION HANGING DROP.
REMARK 280 PROTEIN CONCENTRATION 10 MG/ML. 0.1 M NAOAC (PH 5.0), 0.2
REMARK 280 M MGCL2, 18% W/V PEG6000.
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 99.66000
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 PHE A 251
REMARK 465 TYR A 293
REMARK 465 ASN A 294
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 TYR B 293 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN B 294 CG OD1 ND2
REMARK 470 ASN B 343 CG OD1 ND2
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 333 O HOH B 2433 2.06
REMARK 500 O HOH B 2154 O HOH B 2285 2.16
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 SER A 136 -126.63 52.55
REMARK 500 ARG A 156 -61.32 -91.35
REMARK 500 ALA A 181 59.60 -155.90
REMARK 500 SER A 186 -149.79 -82.47
REMARK 500 ASN A 210 82.58 -157.59
REMARK 500 ALA B 23 82.81 -151.85
REMARK 500 SER B 136 -128.10 53.36
REMARK 500 ARG B 156 -62.51 -95.08
REMARK 500 ALA B 181 59.52 -152.44
REMARK 500 SER B 186 -150.11 -85.25
REMARK 500 ASN B 210 82.40 -158.18
REMARK 500 ALA B 295 47.27 -109.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BTV RELATED DB: PDB
REMARK 900 STRUCTURE OF PHAZ7 PHB DEPOLYMERASE IN COMPLEX WITH
REMARK 900 3HB TRIMER
REMARK 900 RELATED ID: 4BVJ RELATED DB: PDB
REMARK 900 STRUCTURE OF Y105A MUTANT OF PHAZ7 PHB DEPOLYMERASE
REMARK 900 RELATED ID: 4BVL RELATED DB: PDB
REMARK 900 STRUCTURE OF 202-208 DELETION MUTANT OF PHAZ7 PHB
REMARK 900 DEPOLYMERASE
DBREF 4BVK A 1 342 UNP Q939Q9 Q939Q9_PSELE 39 380
DBREF 4BVK B 1 342 UNP Q939Q9 Q939Q9_PSELE 39 380
SEQADV 4BVK GLU A 190 UNP Q939Q9 TYR 228 ENGINEERED MUTATION
SEQADV 4BVK ASN A 343 UNP Q939Q9 EXPRESSION TAG
SEQADV 4BVK GLN A 344 UNP Q939Q9 EXPRESSION TAG
SEQADV 4BVK GLU B 190 UNP Q939Q9 TYR 228 ENGINEERED MUTATION
SEQADV 4BVK ASN B 343 UNP Q939Q9 EXPRESSION TAG
SEQADV 4BVK GLN B 344 UNP Q939Q9 EXPRESSION TAG
SEQRES 1 A 344 LEU THR CYS GLY THR ASN SER GLY PHE VAL CYS LYS GLY
SEQRES 2 A 344 THR GLN THR GLN TYR ALA GLY GLY PHE ALA PRO GLY VAL
SEQRES 3 A 344 GLY TYR GLY GLY PHE GLY GLY GLY SER CYS THR ALA THR
SEQRES 4 A 344 LYS THR PRO VAL ILE PHE ILE HIS GLY ASN GLY ASP ASN
SEQRES 5 A 344 ALA ILE SER PHE ASP MET PRO PRO GLY ASN VAL SER GLY
SEQRES 6 A 344 TYR GLY THR PRO ALA ARG SER VAL TYR ALA GLU LEU LYS
SEQRES 7 A 344 ALA ARG GLY TYR ASN ASP CYS GLU ILE PHE GLY VAL THR
SEQRES 8 A 344 TYR LEU SER SER SER GLU GLN GLY SER ALA GLN TYR ASN
SEQRES 9 A 344 TYR HIS SER SER THR LYS TYR ALA ILE ILE LYS THR PHE
SEQRES 10 A 344 ILE ASP LYS VAL LYS ALA TYR THR GLY LYS SER GLN VAL
SEQRES 11 A 344 ASP ILE VAL ALA HIS SER MET GLY VAL SER MET SER LEU
SEQRES 12 A 344 ALA THR LEU GLN TYR TYR ASN ASN TRP THR SER VAL ARG
SEQRES 13 A 344 LYS PHE ILE ASN LEU ALA GLY GLY ILE ARG GLY LEU TYR
SEQRES 14 A 344 SER CYS TYR TYR THR GLY TYR ALA ASN ALA ALA ALA PRO
SEQRES 15 A 344 THR CYS GLY SER GLN ASN TYR GLU ASN SER TYR THR PHE
SEQRES 16 A 344 GLY PHE PHE PRO GLU GLY TRP TYR TYR GLY VAL TRP VAL
SEQRES 17 A 344 SER ASN PRO TRP THR GLY SER GLY SER THR ASN SER MET
SEQRES 18 A 344 ARG ASP MET PRO ALA LYS ARG THR ALA VAL SER PHE TYR
SEQRES 19 A 344 THR LEU SER ALA GLY PHE LYS ASP GLN VAL GLY CYS ALA
SEQRES 20 A 344 THR ALA SER PHE TRP ALA GLY CYS ASP SER ALA ALA LYS
SEQRES 21 A 344 PHE ALA SER THR THR SER ASN VAL LYS ALA GLN ILE ASN
SEQRES 22 A 344 VAL GLY ALA GLY SER ASN ALA THR GLN ALA ASP TYR ASP
SEQRES 23 A 344 TRP ALA ASP GLY MET PRO TYR ASN ALA GLY GLY GLY ASP
SEQRES 24 A 344 THR THR ASN GLY VAL GLY HIS PHE ARG THR LYS THR ASN
SEQRES 25 A 344 THR GLY ALA ILE ILE GLN ARG MET LEU LEU THR THR CYS
SEQRES 26 A 344 THR GLY LEU ASP CYS ALA ALA GLU TYR THR THR GLY PRO
SEQRES 27 A 344 LYS ALA ALA TYR ASN GLN
SEQRES 1 B 344 LEU THR CYS GLY THR ASN SER GLY PHE VAL CYS LYS GLY
SEQRES 2 B 344 THR GLN THR GLN TYR ALA GLY GLY PHE ALA PRO GLY VAL
SEQRES 3 B 344 GLY TYR GLY GLY PHE GLY GLY GLY SER CYS THR ALA THR
SEQRES 4 B 344 LYS THR PRO VAL ILE PHE ILE HIS GLY ASN GLY ASP ASN
SEQRES 5 B 344 ALA ILE SER PHE ASP MET PRO PRO GLY ASN VAL SER GLY
SEQRES 6 B 344 TYR GLY THR PRO ALA ARG SER VAL TYR ALA GLU LEU LYS
SEQRES 7 B 344 ALA ARG GLY TYR ASN ASP CYS GLU ILE PHE GLY VAL THR
SEQRES 8 B 344 TYR LEU SER SER SER GLU GLN GLY SER ALA GLN TYR ASN
SEQRES 9 B 344 TYR HIS SER SER THR LYS TYR ALA ILE ILE LYS THR PHE
SEQRES 10 B 344 ILE ASP LYS VAL LYS ALA TYR THR GLY LYS SER GLN VAL
SEQRES 11 B 344 ASP ILE VAL ALA HIS SER MET GLY VAL SER MET SER LEU
SEQRES 12 B 344 ALA THR LEU GLN TYR TYR ASN ASN TRP THR SER VAL ARG
SEQRES 13 B 344 LYS PHE ILE ASN LEU ALA GLY GLY ILE ARG GLY LEU TYR
SEQRES 14 B 344 SER CYS TYR TYR THR GLY TYR ALA ASN ALA ALA ALA PRO
SEQRES 15 B 344 THR CYS GLY SER GLN ASN TYR GLU ASN SER TYR THR PHE
SEQRES 16 B 344 GLY PHE PHE PRO GLU GLY TRP TYR TYR GLY VAL TRP VAL
SEQRES 17 B 344 SER ASN PRO TRP THR GLY SER GLY SER THR ASN SER MET
SEQRES 18 B 344 ARG ASP MET PRO ALA LYS ARG THR ALA VAL SER PHE TYR
SEQRES 19 B 344 THR LEU SER ALA GLY PHE LYS ASP GLN VAL GLY CYS ALA
SEQRES 20 B 344 THR ALA SER PHE TRP ALA GLY CYS ASP SER ALA ALA LYS
SEQRES 21 B 344 PHE ALA SER THR THR SER ASN VAL LYS ALA GLN ILE ASN
SEQRES 22 B 344 VAL GLY ALA GLY SER ASN ALA THR GLN ALA ASP TYR ASP
SEQRES 23 B 344 TRP ALA ASP GLY MET PRO TYR ASN ALA GLY GLY GLY ASP
SEQRES 24 B 344 THR THR ASN GLY VAL GLY HIS PHE ARG THR LYS THR ASN
SEQRES 25 B 344 THR GLY ALA ILE ILE GLN ARG MET LEU LEU THR THR CYS
SEQRES 26 B 344 THR GLY LEU ASP CYS ALA ALA GLU TYR THR THR GLY PRO
SEQRES 27 B 344 LYS ALA ALA TYR ASN GLN
FORMUL 3 HOH *896(H2 O)
HELIX 1 1 ASN A 52 MET A 58 5 7
HELIX 2 2 SER A 72 ARG A 80 1 9
HELIX 3 3 SER A 94 GLY A 99 1 6
HELIX 4 4 SER A 100 ASN A 104 5 5
HELIX 5 5 SER A 107 GLY A 126 1 20
HELIX 6 6 SER A 136 ASN A 150 1 15
HELIX 7 7 ASN A 151 THR A 153 5 3
HELIX 8 8 SER A 170 GLY A 175 1 6
HELIX 9 9 ALA A 181 GLY A 185 5 5
HELIX 10 10 SER A 220 ARG A 222 5 3
HELIX 11 11 ASP A 223 ARG A 228 1 6
HELIX 12 12 ALA A 238 ASP A 242 5 5
HELIX 13 13 GLY A 254 ALA A 258 5 5
HELIX 14 14 ASP A 286 GLY A 290 5 5
HELIX 15 15 PHE A 307 ASN A 312 1 6
HELIX 16 16 THR A 313 THR A 323 1 11
HELIX 17 17 THR A 326 ALA A 332 5 7
HELIX 18 18 ASN B 52 MET B 58 5 7
HELIX 19 19 SER B 72 ARG B 80 1 9
HELIX 20 20 SER B 94 GLY B 99 1 6
HELIX 21 21 SER B 100 ASN B 104 5 5
HELIX 22 22 SER B 107 GLY B 126 1 20
HELIX 23 23 SER B 136 ASN B 150 1 15
HELIX 24 24 ASN B 151 THR B 153 5 3
HELIX 25 25 LEU B 168 TYR B 172 5 5
HELIX 26 26 ALA B 181 GLY B 185 5 5
HELIX 27 27 SER B 220 ARG B 222 5 3
HELIX 28 28 ASP B 223 ARG B 228 1 6
HELIX 29 29 ALA B 238 ASP B 242 5 5
HELIX 30 30 GLY B 254 ALA B 258 5 5
HELIX 31 31 ASP B 286 GLY B 290 5 5
HELIX 32 32 PHE B 307 ASN B 312 1 6
HELIX 33 33 THR B 313 THR B 323 1 11
HELIX 34 34 THR B 326 ALA B 332 5 7
SHEET 1 AA 9 THR A 16 TYR A 18 0
SHEET 2 AA 9 GLY A 30 GLY A 32 1 O GLY A 30 N GLN A 17
SHEET 3 AA 9 ILE A 87 VAL A 90 -1 O GLY A 89 N PHE A 31
SHEET 4 AA 9 VAL A 43 ILE A 46 1 O VAL A 43 N PHE A 88
SHEET 5 AA 9 VAL A 130 HIS A 135 1 O ASP A 131 N ILE A 44
SHEET 6 AA 9 VAL A 155 LEU A 161 1 N ARG A 156 O VAL A 130
SHEET 7 AA 9 SER A 232 SER A 237 1 O SER A 232 N PHE A 158
SHEET 8 AA 9 VAL A 268 ASN A 273 1 N LYS A 269 O PHE A 233
SHEET 9 AA 9 ALA A 340 ALA A 341 -1 O ALA A 340 N ASN A 273
SHEET 1 AB 2 GLY A 201 TYR A 203 0
SHEET 2 AB 2 VAL A 206 VAL A 208 -1 O VAL A 206 N TYR A 203
SHEET 1 BA 9 THR B 16 TYR B 18 0
SHEET 2 BA 9 GLY B 30 GLY B 32 1 O GLY B 30 N GLN B 17
SHEET 3 BA 9 ILE B 87 VAL B 90 -1 O GLY B 89 N PHE B 31
SHEET 4 BA 9 VAL B 43 ILE B 46 1 O VAL B 43 N PHE B 88
SHEET 5 BA 9 VAL B 130 HIS B 135 1 O ASP B 131 N ILE B 44
SHEET 6 BA 9 VAL B 155 LEU B 161 1 N ARG B 156 O VAL B 130
SHEET 7 BA 9 SER B 232 SER B 237 1 O SER B 232 N PHE B 158
SHEET 8 BA 9 VAL B 268 ASN B 273 1 N LYS B 269 O PHE B 233
SHEET 9 BA 9 ALA B 340 ALA B 341 -1 O ALA B 340 N ASN B 273
SHEET 1 BB 2 GLY B 201 TYR B 203 0
SHEET 2 BB 2 VAL B 206 VAL B 208 -1 O VAL B 206 N TYR B 203
SSBOND 1 CYS A 3 CYS A 11 1555 1555 2.04
SSBOND 2 CYS A 36 CYS A 85 1555 1555 2.04
SSBOND 3 CYS A 171 CYS A 184 1555 1555 2.04
SSBOND 4 CYS A 246 CYS A 255 1555 1555 2.04
SSBOND 5 CYS A 325 CYS A 330 1555 1555 2.04
SSBOND 6 CYS B 3 CYS B 11 1555 1555 2.04
SSBOND 7 CYS B 36 CYS B 85 1555 1555 2.04
SSBOND 8 CYS B 171 CYS B 184 1555 1555 2.04
SSBOND 9 CYS B 246 CYS B 255 1555 1555 2.05
SSBOND 10 CYS B 325 CYS B 330 1555 1555 2.03
CRYST1 41.410 199.320 44.310 90.00 114.39 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 0.024149 0.000000 0.010949 0.00000
SCALE2 0.000000 0.005017 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024780 0.00000
TER 2556 GLN A 344
TER 5137 GLN B 344
MASTER 295 0 0 34 22 0 0 6 6031 2 20 54
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