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HEADER HYDROLASE 26-JUN-13 4BVJ
TITLE STRUCTURE OF Y105A 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 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, BIOPOLYMER BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HERMAWAN,B.SUBEDI,A.C.PAPAGEORGIOU,D.JENDROSSEK
REVDAT 1 18-SEP-13 4BVJ 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. 1.60 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) : 1.599
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.005
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.99
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.94
REMARK 3 NUMBER OF REFLECTIONS : 84894
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1569
REMARK 3 R VALUE (WORKING SET) : 0.1553
REMARK 3 FREE R VALUE : 0.1887
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 4245
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 20.0066 - 4.9444 0.98 2688 142 0.1487 0.1718
REMARK 3 2 4.9444 - 3.9343 0.99 2692 142 0.1191 0.1364
REMARK 3 3 3.9343 - 3.4398 0.98 2670 140 0.1213 0.1475
REMARK 3 4 3.4398 - 3.1266 0.99 2697 142 0.1341 0.1736
REMARK 3 5 3.1266 - 2.9032 0.99 2700 142 0.1434 0.1751
REMARK 3 6 2.9032 - 2.7325 0.99 2685 142 0.1448 0.1596
REMARK 3 7 2.7325 - 2.5959 0.99 2689 141 0.1478 0.1605
REMARK 3 8 2.5959 - 2.4832 0.99 2743 145 0.1480 0.1956
REMARK 3 9 2.4832 - 2.3877 0.99 2723 143 0.1483 0.1839
REMARK 3 10 2.3877 - 2.3055 0.99 2633 138 0.1464 0.1778
REMARK 3 11 2.3055 - 2.2335 0.99 2739 145 0.1454 0.1875
REMARK 3 12 2.2335 - 2.1697 1.00 2696 141 0.1395 0.1603
REMARK 3 13 2.1697 - 2.1126 1.00 2671 141 0.1447 0.1879
REMARK 3 14 2.1126 - 2.0612 0.99 2739 144 0.1551 0.1867
REMARK 3 15 2.0612 - 2.0143 1.00 2687 142 0.1578 0.2155
REMARK 3 16 2.0143 - 1.9715 1.00 2724 143 0.1579 0.2101
REMARK 3 17 1.9715 - 1.9321 0.99 2676 141 0.1603 0.2058
REMARK 3 18 1.9321 - 1.8957 0.99 2726 143 0.1690 0.2294
REMARK 3 19 1.8957 - 1.8618 0.99 2677 141 0.1755 0.2302
REMARK 3 20 1.8618 - 1.8303 1.00 2734 144 0.1801 0.1965
REMARK 3 21 1.8303 - 1.8008 0.99 2664 140 0.1925 0.2273
REMARK 3 22 1.8008 - 1.7731 0.99 2697 142 0.1981 0.2474
REMARK 3 23 1.7731 - 1.7471 0.99 2721 143 0.1946 0.2322
REMARK 3 24 1.7471 - 1.7225 0.99 2625 139 0.2014 0.2333
REMARK 3 25 1.7225 - 1.6992 0.99 2727 143 0.2023 0.2410
REMARK 3 26 1.6992 - 1.6771 0.99 2710 143 0.2161 0.2594
REMARK 3 27 1.6771 - 1.6562 0.99 2632 138 0.2161 0.2501
REMARK 3 28 1.6562 - 1.6362 0.99 2720 143 0.2303 0.2681
REMARK 3 29 1.6362 - 1.6172 0.99 2711 143 0.2518 0.2930
REMARK 3 30 1.6172 - 1.5991 0.92 2453 129 0.2581 0.3142
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.17
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.23
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.2
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.1
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 5251
REMARK 3 ANGLE : 1.082 7136
REMARK 3 CHIRALITY : 0.074 755
REMARK 3 PLANARITY : 0.005 929
REMARK 3 DIHEDRAL : 12.491 1774
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 4BVJ 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-57421.
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
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84896
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.60
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 2.6
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.70
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) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.3
REMARK 200 R MERGE FOR SHELL (I) : 0.48
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.00
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 NH4CL, 20% 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 100.02500
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 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 A 293 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN A 294 CG OD1 ND2
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 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 NZ LYS A 40 O HOH A 2158 1.99
REMARK 500 OH TYR A 148 O HOH A 2377 2.06
REMARK 500 OD1 ASN A 150 O HOH A 2383 2.01
REMARK 500 N GLY A 205 O HOH A 2454 2.11
REMARK 500 OH TYR B 148 O HOH B 2389 2.16
REMARK 500 OD1 ASN B 150 O HOH B 2397 2.18
REMARK 500 O TYR B 204 O HOH B 2468 2.20
REMARK 500 N ASN B 343 O HOH B 2518 2.19
REMARK 500 O HOH A 2039 O HOH A 2091 2.12
REMARK 500 O HOH A 2039 O HOH A 2040 2.16
REMARK 500 O HOH A 2040 O HOH A 2092 2.08
REMARK 500 O HOH A 2041 O HOH A 2093 2.02
REMARK 500 O HOH A 2055 O HOH A 2112 2.16
REMARK 500 O HOH A 2056 O HOH A 2059 2.07
REMARK 500 O HOH A 2059 O HOH A 2064 2.17
REMARK 500 O HOH A 2062 O HOH A 2179 1.97
REMARK 500 O HOH A 2072 O HOH B 2342 2.14
REMARK 500 O HOH A 2072 O HOH B 2602 2.04
REMARK 500 O HOH A 2075 O HOH A 2148 1.93
REMARK 500 O HOH A 2081 O HOH A 2156 1.98
REMARK 500 O HOH A 2096 O HOH A 2104 2.10
REMARK 500 O HOH A 2111 O HOH A 2112 1.92
REMARK 500 O HOH A 2121 O HOH A 2224 2.02
REMARK 500 O HOH A 2126 O HOH A 2129 2.09
REMARK 500 O HOH A 2144 O HOH A 2605 2.13
REMARK 500 O HOH A 2149 O HOH A 2295 1.27
REMARK 500 O HOH A 2150 O HOH A 2151 1.97
REMARK 500 O HOH A 2152 O HOH A 2293 2.18
REMARK 500 O HOH A 2171 O HOH A 2369 2.16
REMARK 500 O HOH A 2173 O HOH A 2367 2.18
REMARK 500 O HOH A 2173 O HOH A 2368 1.94
REMARK 500 O HOH A 2187 O HOH A 2188 2.12
REMARK 500 O HOH A 2218 O HOH A 2396 2.15
REMARK 500 O HOH A 2233 O HOH A 2237 1.73
REMARK 500 O HOH A 2242 O HOH A 2243 2.07
REMARK 500 O HOH A 2246 O HOH A 2378 1.92
REMARK 500 O HOH A 2253 O HOH A 2457 2.13
REMARK 500 O HOH A 2273 O HOH A 2274 2.01
REMARK 500 O HOH A 2283 O HOH A 2480 2.15
REMARK 500 O HOH A 2291 O HOH A 2538 1.98
REMARK 500 O HOH A 2302 O HOH A 2305 1.95
REMARK 500 O HOH A 2318 O HOH A 2549 2.02
REMARK 500 O HOH A 2319 O HOH A 2546 2.18
REMARK 500 O HOH A 2324 O HOH A 2326 2.04
REMARK 500 O HOH A 2325 O HOH A 2551 2.17
REMARK 500 O HOH A 2368 O HOH A 2369 2.05
REMARK 500 O HOH A 2397 O HOH A 2398 2.13
REMARK 500 O HOH A 2535 O HOH A 2536 2.11
REMARK 500 O HOH A 2548 O HOH A 2550 2.18
REMARK 500 O HOH A 2560 O HOH A 2561 1.93
REMARK 500
REMARK 500 THIS ENTRY HAS 92 CLOSE CONTACTS
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 2251 O HOH B 2439 2545 1.97
REMARK 500 O HOH B 2028 O HOH B 2377 1655 2.18
REMARK 500 O HOH B 2047 O HOH B 2220 1454 2.10
REMARK 500 O HOH B 2163 O HOH B 2577 1454 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 THR A 14 116.29 -39.63
REMARK 500 SER A 136 -128.05 55.49
REMARK 500 ARG A 156 -62.93 -93.39
REMARK 500 ALA A 177 43.77 -140.19
REMARK 500 ALA A 181 63.66 -151.84
REMARK 500 ASN A 210 82.27 -157.99
REMARK 500 PHE A 251 48.47 -140.93
REMARK 500 ALA B 23 84.91 -155.59
REMARK 500 SER B 136 -128.76 58.38
REMARK 500 ARG B 156 -60.75 -93.41
REMARK 500 ALA B 177 36.22 -146.49
REMARK 500 ALA B 181 65.54 -153.15
REMARK 500 SER B 186 -153.97 -88.30
REMARK 500 ASN B 210 84.44 -156.91
REMARK 500 ARG B 228 64.23 -119.25
REMARK 500 ALA B 295 50.60 -110.85
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 A2608 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH A2609 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH A2610 DISTANCE = 7.17 ANGSTROMS
REMARK 525 HOH A2611 DISTANCE = 9.31 ANGSTROMS
REMARK 525 HOH B2066 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH B2077 DISTANCE = 7.31 ANGSTROMS
REMARK 525 HOH B2266 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH B2619 DISTANCE = 7.73 ANGSTROMS
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 601 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2606 O
REMARK 620 2 HOH A2605 O 101.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 501 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2616 O
REMARK 620 2 HOH B2618 O 100.1
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 501
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: 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 4BVJ A 1 342 UNP Q939Q9 Q939Q9_PSELE 39 380
DBREF 4BVJ B 1 342 UNP Q939Q9 Q939Q9_PSELE 39 380
SEQADV 4BVJ ALA A 105 UNP Q939Q9 TYR 143 ENGINEERED MUTATION
SEQADV 4BVJ ASN A 343 UNP Q939Q9 EXPRESSION TAG
SEQADV 4BVJ ALA B 105 UNP Q939Q9 TYR 143 ENGINEERED MUTATION
SEQADV 4BVJ ASN B 343 UNP Q939Q9 EXPRESSION TAG
SEQRES 1 A 343 LEU THR CYS GLY THR ASN SER GLY PHE VAL CYS LYS GLY
SEQRES 2 A 343 THR GLN THR GLN TYR ALA GLY GLY PHE ALA PRO GLY VAL
SEQRES 3 A 343 GLY TYR GLY GLY PHE GLY GLY GLY SER CYS THR ALA THR
SEQRES 4 A 343 LYS THR PRO VAL ILE PHE ILE HIS GLY ASN GLY ASP ASN
SEQRES 5 A 343 ALA ILE SER PHE ASP MET PRO PRO GLY ASN VAL SER GLY
SEQRES 6 A 343 TYR GLY THR PRO ALA ARG SER VAL TYR ALA GLU LEU LYS
SEQRES 7 A 343 ALA ARG GLY TYR ASN ASP CYS GLU ILE PHE GLY VAL THR
SEQRES 8 A 343 TYR LEU SER SER SER GLU GLN GLY SER ALA GLN TYR ASN
SEQRES 9 A 343 ALA HIS SER SER THR LYS TYR ALA ILE ILE LYS THR PHE
SEQRES 10 A 343 ILE ASP LYS VAL LYS ALA TYR THR GLY LYS SER GLN VAL
SEQRES 11 A 343 ASP ILE VAL ALA HIS SER MET GLY VAL SER MET SER LEU
SEQRES 12 A 343 ALA THR LEU GLN TYR TYR ASN ASN TRP THR SER VAL ARG
SEQRES 13 A 343 LYS PHE ILE ASN LEU ALA GLY GLY ILE ARG GLY LEU TYR
SEQRES 14 A 343 SER CYS TYR TYR THR GLY TYR ALA ASN ALA ALA ALA PRO
SEQRES 15 A 343 THR CYS GLY SER GLN ASN TYR TYR ASN SER TYR THR PHE
SEQRES 16 A 343 GLY PHE PHE PRO GLU GLY TRP TYR TYR GLY VAL TRP VAL
SEQRES 17 A 343 SER ASN PRO TRP THR GLY SER GLY SER THR ASN SER MET
SEQRES 18 A 343 ARG ASP MET PRO ALA LYS ARG THR ALA VAL SER PHE TYR
SEQRES 19 A 343 THR LEU SER ALA GLY PHE LYS ASP GLN VAL GLY CYS ALA
SEQRES 20 A 343 THR ALA SER PHE TRP ALA GLY CYS ASP SER ALA ALA LYS
SEQRES 21 A 343 PHE ALA SER THR THR SER ASN VAL LYS ALA GLN ILE ASN
SEQRES 22 A 343 VAL GLY ALA GLY SER ASN ALA THR GLN ALA ASP TYR ASP
SEQRES 23 A 343 TRP ALA ASP GLY MET PRO TYR ASN ALA GLY GLY GLY ASP
SEQRES 24 A 343 THR THR ASN GLY VAL GLY HIS PHE ARG THR LYS THR ASN
SEQRES 25 A 343 THR GLY ALA ILE ILE GLN ARG MET LEU LEU THR THR CYS
SEQRES 26 A 343 THR GLY LEU ASP CYS ALA ALA GLU TYR THR THR GLY PRO
SEQRES 27 A 343 LYS ALA ALA TYR ASN
SEQRES 1 B 343 LEU THR CYS GLY THR ASN SER GLY PHE VAL CYS LYS GLY
SEQRES 2 B 343 THR GLN THR GLN TYR ALA GLY GLY PHE ALA PRO GLY VAL
SEQRES 3 B 343 GLY TYR GLY GLY PHE GLY GLY GLY SER CYS THR ALA THR
SEQRES 4 B 343 LYS THR PRO VAL ILE PHE ILE HIS GLY ASN GLY ASP ASN
SEQRES 5 B 343 ALA ILE SER PHE ASP MET PRO PRO GLY ASN VAL SER GLY
SEQRES 6 B 343 TYR GLY THR PRO ALA ARG SER VAL TYR ALA GLU LEU LYS
SEQRES 7 B 343 ALA ARG GLY TYR ASN ASP CYS GLU ILE PHE GLY VAL THR
SEQRES 8 B 343 TYR LEU SER SER SER GLU GLN GLY SER ALA GLN TYR ASN
SEQRES 9 B 343 ALA HIS SER SER THR LYS TYR ALA ILE ILE LYS THR PHE
SEQRES 10 B 343 ILE ASP LYS VAL LYS ALA TYR THR GLY LYS SER GLN VAL
SEQRES 11 B 343 ASP ILE VAL ALA HIS SER MET GLY VAL SER MET SER LEU
SEQRES 12 B 343 ALA THR LEU GLN TYR TYR ASN ASN TRP THR SER VAL ARG
SEQRES 13 B 343 LYS PHE ILE ASN LEU ALA GLY GLY ILE ARG GLY LEU TYR
SEQRES 14 B 343 SER CYS TYR TYR THR GLY TYR ALA ASN ALA ALA ALA PRO
SEQRES 15 B 343 THR CYS GLY SER GLN ASN TYR TYR ASN SER TYR THR PHE
SEQRES 16 B 343 GLY PHE PHE PRO GLU GLY TRP TYR TYR GLY VAL TRP VAL
SEQRES 17 B 343 SER ASN PRO TRP THR GLY SER GLY SER THR ASN SER MET
SEQRES 18 B 343 ARG ASP MET PRO ALA LYS ARG THR ALA VAL SER PHE TYR
SEQRES 19 B 343 THR LEU SER ALA GLY PHE LYS ASP GLN VAL GLY CYS ALA
SEQRES 20 B 343 THR ALA SER PHE TRP ALA GLY CYS ASP SER ALA ALA LYS
SEQRES 21 B 343 PHE ALA SER THR THR SER ASN VAL LYS ALA GLN ILE ASN
SEQRES 22 B 343 VAL GLY ALA GLY SER ASN ALA THR GLN ALA ASP TYR ASP
SEQRES 23 B 343 TRP ALA ASP GLY MET PRO TYR ASN ALA GLY GLY GLY ASP
SEQRES 24 B 343 THR THR ASN GLY VAL GLY HIS PHE ARG THR LYS THR ASN
SEQRES 25 B 343 THR GLY ALA ILE ILE GLN ARG MET LEU LEU THR THR CYS
SEQRES 26 B 343 THR GLY LEU ASP CYS ALA ALA GLU TYR THR THR GLY PRO
SEQRES 27 B 343 LYS ALA ALA TYR ASN
HET NA A 501 1
HET NA A 601 1
HET NA B 501 1
HETNAM NA SODIUM ION
FORMUL 2 NA 3(NA 1+)
FORMUL 3 HOH *1230(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 LEU A 168 TYR A 172 5 5
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 LYS B 241 5 4
HELIX 30 30 ASP B 242 ALA B 247 1 6
HELIX 31 31 GLY B 254 ALA B 258 5 5
HELIX 32 32 ASP B 286 GLY B 290 5 5
HELIX 33 33 PHE B 307 ASN B 312 1 6
HELIX 34 34 THR B 313 THR B 323 1 11
HELIX 35 35 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 2.04
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 2.02
SSBOND 6 CYS B 3 CYS B 11 1555 1555 2.04
SSBOND 7 CYS B 36 CYS B 85 1555 1555 2.03
SSBOND 8 CYS B 171 CYS B 184 1555 1555 2.04
SSBOND 9 CYS B 246 CYS B 255 1555 1555 2.04
SSBOND 10 CYS B 325 CYS B 330 1555 1555 2.02
LINK NA NA A 601 O HOH A2606 1555 1555 2.95
LINK NA NA A 601 O HOH A2605 1555 1555 3.01
LINK NA NA B 501 O HOH B2618 1555 1555 3.18
LINK NA NA B 501 O HOH B2616 1555 1555 3.04
SITE 1 AC1 2 ASN A 83 ASP A 84
SITE 1 AC2 4 CYS A 36 THR A 37 HOH A2605 HOH A2606
SITE 1 AC3 4 ALA B 23 PRO B 24 GLY B 25 HOH B2616
CRYST1 41.370 200.050 44.180 90.00 114.28 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 0.024172 0.000000 0.010904 0.00000
SCALE2 0.000000 0.004999 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024831 0.00000
TER 2561 ASN A 343
TER 5104 ASN B 343
MASTER 417 0 3 35 22 0 3 6 6335 2 26 54
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