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HEADER HYDROLASE 19-JUN-13 4BTV
TITLE STRUCTURE OF PHAZ7 PHB DEPOLYMERASE IN COMPLEX WITH 3HB TRIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHB DEPOLYMERASE PHAZ7;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 39-380;
COMPND 5 EC: 3.1.1.75;
COMPND 6 ENGINEERED: YES;
COMPND 7 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
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HERMAWAN,B.SUBEDI,A.C.PAPAGEORGIOU,D.JENDROSSEK
REVDAT 1 18-SEP-13 4BTV 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 2
REMARK 2 RESOLUTION. 1.59 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) : 1.594
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.848
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.99
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.63
REMARK 3 NUMBER OF REFLECTIONS : 83783
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1339
REMARK 3 R VALUE (WORKING SET) : 0.1327
REMARK 3 FREE R VALUE : 0.1575
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 4190
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 19.8500 - 4.9295 0.93 2600 137 0.1620 0.1685
REMARK 3 2 4.9295 - 3.9226 0.96 2645 139 0.1156 0.1212
REMARK 3 3 3.9226 - 3.4296 0.96 2614 138 0.1198 0.1203
REMARK 3 4 3.4296 - 3.1174 0.98 2685 141 0.1195 0.1567
REMARK 3 5 3.1174 - 2.8947 0.97 2697 142 0.1229 0.1240
REMARK 3 6 2.8947 - 2.7245 0.98 2687 142 0.1164 0.1552
REMARK 3 7 2.7245 - 2.5883 0.98 2669 140 0.1120 0.1216
REMARK 3 8 2.5883 - 2.4759 0.98 2716 143 0.1156 0.1458
REMARK 3 9 2.4759 - 2.3807 0.98 2723 144 0.1190 0.1319
REMARK 3 10 2.3807 - 2.2987 0.98 2668 140 0.1266 0.1593
REMARK 3 11 2.2987 - 2.2269 0.95 2596 137 0.1534 0.1932
REMARK 3 12 2.2269 - 2.1633 0.98 2713 142 0.1245 0.1378
REMARK 3 13 2.1633 - 2.1064 0.98 2682 142 0.1193 0.1422
REMARK 3 14 2.1064 - 2.0551 0.99 2688 141 0.1191 0.1398
REMARK 3 15 2.0551 - 2.0084 0.98 2678 141 0.1254 0.1494
REMARK 3 16 2.0084 - 1.9657 0.99 2729 144 0.1282 0.1702
REMARK 3 17 1.9657 - 1.9264 0.98 2689 141 0.1469 0.1556
REMARK 3 18 1.9264 - 1.8901 0.97 2652 140 0.1659 0.2053
REMARK 3 19 1.8901 - 1.8564 0.99 2687 141 0.1368 0.1834
REMARK 3 20 1.8564 - 1.8249 0.98 2753 145 0.1442 0.1730
REMARK 3 21 1.8249 - 1.7955 0.98 2612 137 0.1452 0.2041
REMARK 3 22 1.7955 - 1.7679 0.98 2740 145 0.1457 0.2195
REMARK 3 23 1.7679 - 1.7419 0.98 2724 143 0.1581 0.1934
REMARK 3 24 1.7419 - 1.7174 0.98 2638 139 0.1583 0.1992
REMARK 3 25 1.7174 - 1.6942 0.99 2739 144 0.1520 0.2058
REMARK 3 26 1.6942 - 1.6722 0.98 2686 141 0.1542 0.2020
REMARK 3 27 1.6722 - 1.6513 0.98 2636 139 0.1605 0.1873
REMARK 3 28 1.6513 - 1.6314 0.98 2751 145 0.1625 0.2127
REMARK 3 29 1.6314 - 1.6125 0.98 2698 142 0.1729 0.2132
REMARK 3 30 1.6125 - 1.5944 0.67 1798 95 0.1870 0.2160
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 : 0.80
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.13
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.94
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.7
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.4
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 : 0.007 5124
REMARK 3 ANGLE : 1.090 6962
REMARK 3 CHIRALITY : 0.060 736
REMARK 3 PLANARITY : 0.005 898
REMARK 3 DIHEDRAL : 15.409 1782
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 4BTV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUN-13.
REMARK 100 THE PDBE ID CODE IS EBI-57187.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-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
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83783
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.60
REMARK 200 RESOLUTION RANGE LOW (A) : 19.60
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 2.1
REMARK 200 R MERGE (I) : 0.04
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.1
REMARK 200 R MERGE FOR SHELL (I) : 0.21
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.2
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP VAPOUR DIFFUSION.
REMARK 280 0.1 M NAOAC (PH 5.0), 0.2 M NACL, 20% W/V PEG 6000
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 99.68700
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 THR A 281
REMARK 465 GLN A 282
REMARK 465 ALA A 283
REMARK 465 ASP A 284
REMARK 465 TYR A 285
REMARK 465 ASP A 286
REMARK 465 TRP A 287
REMARK 465 ALA A 288
REMARK 465 ASP A 289
REMARK 465 GLY A 290
REMARK 465 MET A 291
REMARK 465 PRO A 292
REMARK 465 TYR A 293
REMARK 465 ASN A 294
REMARK 465 THR B 281
REMARK 465 GLN B 282
REMARK 465 ALA B 283
REMARK 465 ASP B 284
REMARK 465 TYR B 285
REMARK 465 ASP B 286
REMARK 465 TRP B 287
REMARK 465 ALA B 288
REMARK 465 ASP B 289
REMARK 465 GLY B 290
REMARK 465 MET B 291
REMARK 465 PRO B 292
REMARK 465 TYR B 293
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 ASN A 279 CG OD1 ND2
REMARK 470 ASN B 343 CA C O CB 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 OE2 GLU A 333 O HOH A 2508 2.15
REMARK 500 O HOH A 2049 O HOH A 2065 2.11
REMARK 500 O HOH A 2060 O HOH A 2135 2.19
REMARK 500 O HOH A 2125 O HOH A 2241 2.18
REMARK 500 O HOH A 2148 O HOH A 2174 2.15
REMARK 500 O HOH A 2156 O HOH A 2284 2.10
REMARK 500 O HOH A 2160 O HOH A 2170 2.12
REMARK 500 O HOH A 2171 O HOH A 2309 2.18
REMARK 500 O HOH A 2238 O HOH A 2243 2.18
REMARK 500 O HOH A 2304 O HOH A 2305 2.13
REMARK 500 O HOH A 2305 O HOH A 2518 2.20
REMARK 500 O HOH A 2348 O HOH A 2380 2.13
REMARK 500 O HOH A 2415 O HOH A 2421 2.11
REMARK 500 O HOH A 2469 O HOH A 2470 2.10
REMARK 500 O HOH A 2522 O HOH A 2523 2.14
REMARK 500 O HOH B 2009 O HOH B 2023 2.19
REMARK 500 O HOH B 2018 O HOH B 2271 2.15
REMARK 500 O HOH B 2027 O HOH B 2031 2.16
REMARK 500 O HOH B 2039 O HOH B 2083 2.14
REMARK 500 O HOH B 2078 O HOH B 2154 2.19
REMARK 500 O HOH B 2130 O HOH B 2244 2.19
REMARK 500 O HOH B 2162 O HOH B 2322 2.11
REMARK 500 O HOH B 2162 O HOH B 2348 1.98
REMARK 500 O HOH B 2175 O HOH B 2177 2.04
REMARK 500 O HOH B 2210 O HOH B 2520 2.14
REMARK 500 O HOH B 2258 O HOH B 2458 2.11
REMARK 500 O HOH B 2258 O HOH B 2261 2.09
REMARK 500 O HOH B 2261 O HOH B 2263 2.18
REMARK 500 O HOH B 2267 O HOH B 2268 2.16
REMARK 500 O HOH B 2267 O HOH B 2482 2.07
REMARK 500 O HOH B 2267 O HOH B 2269 2.17
REMARK 500 O HOH B 2313 O HOH B 2314 2.15
REMARK 500 O HOH B 2321 O HOH B 2329 2.15
REMARK 500 O HOH B 2340 O HOH B 2341 2.19
REMARK 500 O HOH B 2385 O HOH B 2465 2.04
REMARK 500 O HOH B 2458 O HOH B 2459 2.11
REMARK 500 O HOH B 2470 O HOH B 2509 2.08
REMARK 500 O HOH B 2531 O HOH B 2532 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 O HOH A 2095 O HOH A 2418 1556 2.17
REMARK 500 O HOH B 2039 O HOH B 2332 1554 2.06
REMARK 500 O HOH B 2259 O HOH B 2525 1455 2.18
REMARK 500 O HOH B 2263 O HOH B 2269 1455 2.11
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 ALA A 23 84.16 -151.27
REMARK 500 CYS A 36 -177.97 -172.42
REMARK 500 ALA A 136 -125.97 56.47
REMARK 500 ALA A 177 44.83 -140.85
REMARK 500 ALA A 181 59.62 -156.16
REMARK 500 SER A 186 -153.66 -86.39
REMARK 500 ASN A 210 82.68 -160.37
REMARK 500 ALA B 23 82.74 -152.72
REMARK 500 ALA B 136 -128.71 56.96
REMARK 500 ARG B 156 -62.09 -97.51
REMARK 500 ALA B 181 60.77 -150.90
REMARK 500 SER B 186 -154.60 -84.71
REMARK 500 ASN B 210 82.10 -155.43
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 A2228 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH A2250 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A2290 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH A2391 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH B2194 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH B2251 DISTANCE = 5.72 ANGSTROMS
REMARK 525 HOH B2291 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH B2576 DISTANCE = 5.10 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RB3 A1345
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RB3 B1343
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BVJ RELATED DB: PDB
REMARK 900 STRUCTURE OF Y105A MUTANT OF PHAZ7 PHB DEPOLYMERASE
REMARK 900 RELATED ID: 4BVK RELATED DB: PDB
REMARK 900 STRUCTURE OF Y190E 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 4BTV A 1 342 UNP Q939Q9 Q939Q9_PSELE 39 380
DBREF 4BTV B 1 342 UNP Q939Q9 Q939Q9_PSELE 39 380
SEQADV 4BTV ALA A 136 UNP Q939Q9 SER 174 ENGINEERED MUTATION
SEQADV 4BTV ALA B 136 UNP Q939Q9 SER 174 ENGINEERED MUTATION
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 ALA 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 TYR 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 ALA 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 TYR 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
HET RB3 A1345 20
HET RB3 B1343 20
HETNAM RB3 (1R)-3-{[(1R)-3-METHOXY-1-METHYL-3-OXOPROPYL]
HETNAM 2 RB3 OXY}-1-METHYL-3-OXOPROPYL (3R)-3-
HETNAM 3 RB3 HYDROXYBUTANOATE
HETSYN RB3 METHYL (3R)-3-{[(3R)-3-{[(3R)-3-
HETSYN 2 RB3 HYDROXYBUTANOYL]OXY}BUTANOYL]OXY}BUTANOATE
FORMUL 2 RB3 2(C13 H22 O7)
FORMUL 3 HOH *1103(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 ALA 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 ALA A 247 PHE A 251 5 5
HELIX 14 14 GLY A 254 ALA A 258 5 5
HELIX 15 15 GLY A 296 THR A 301 5 6
HELIX 16 16 PHE A 307 ASN A 312 1 6
HELIX 17 17 THR A 313 THR A 323 1 11
HELIX 18 18 THR A 326 ALA A 332 5 7
HELIX 19 19 ASN B 52 MET B 58 5 7
HELIX 20 20 SER B 72 ARG B 80 1 9
HELIX 21 21 SER B 94 GLY B 99 1 6
HELIX 22 22 SER B 100 ASN B 104 5 5
HELIX 23 23 SER B 107 GLY B 126 1 20
HELIX 24 24 ALA B 136 ASN B 150 1 15
HELIX 25 25 ASN B 151 THR B 153 5 3
HELIX 26 26 SER B 170 GLY B 175 1 6
HELIX 27 27 ALA B 181 GLY B 185 5 5
HELIX 28 28 SER B 220 ARG B 222 5 3
HELIX 29 29 ASP B 223 ARG B 228 1 6
HELIX 30 30 ALA B 238 ASP B 242 5 5
HELIX 31 31 ALA B 247 PHE B 251 5 5
HELIX 32 32 GLY B 254 ALA B 258 5 5
HELIX 33 33 GLY B 296 THR B 300 5 5
HELIX 34 34 PHE B 307 ASN B 312 1 6
HELIX 35 35 THR B 313 THR B 323 1 11
HELIX 36 36 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 2.03
SSBOND 2 CYS A 36 CYS A 85 1555 1555 2.03
SSBOND 3 CYS A 171 CYS A 184 1555 1555 2.04
SSBOND 4 CYS A 246 CYS A 255 1555 1555 2.06
SSBOND 5 CYS A 325 CYS A 330 1555 1555 2.04
SSBOND 6 CYS B 3 CYS B 11 1555 1555 2.05
SSBOND 7 CYS B 36 CYS B 85 1555 1555 2.01
SSBOND 8 CYS B 171 CYS B 184 1555 1555 2.03
SSBOND 9 CYS B 246 CYS B 255 1555 1555 2.05
SSBOND 10 CYS B 325 CYS B 330 1555 1555 2.05
SITE 1 AC1 9 TYR A 176 SER A 186 GLN A 187 ASN A 188
SITE 2 AC1 9 TYR A 189 TYR A 190 PHE A 195 GLY A 196
SITE 3 AC1 9 HOH A2527
SITE 1 AC2 10 TYR B 176 PRO B 182 SER B 186 ASN B 188
SITE 2 AC2 10 TYR B 189 TYR B 190 PHE B 195 GLY B 196
SITE 3 AC2 10 HOH B2423 HOH B2424
CRYST1 41.337 199.374 44.424 90.00 114.24 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 0.024191 0.000000 0.010892 0.00000
SCALE2 0.000000 0.005016 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024687 0.00000
TER 2480 GLN A 344
TER 4943 ASN B 343
MASTER 396 0 2 36 22 0 6 6 6084 2 60 54
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