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HEADER HYDROLASE 20-JUL-13 4BYM
TITLE STRUCTURE OF PHAZ7 PHB DEPOLYMERASE Y105E MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHB DEPOLYMERASE PHAZ7;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHB DEPOLYMERASE;
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, SUBSTRATE-BINDING CAVITY, BINDING
KEYWDS 2 CAVITY, 3HB TRIMER BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HERMAWAN,B.SUBEDI,A.C.PAPAGEORGIOU,D.JENDROSSEK
REVDAT 1 18-SEP-13 4BYM 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. 1.60 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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.598
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.843
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.99
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.13
REMARK 3 NUMBER OF REFLECTIONS : 85301
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1497
REMARK 3 R VALUE (WORKING SET) : 0.1484
REMARK 3 FREE R VALUE : 0.1743
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 4266
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 19.8448 - 4.9409 0.95 2663 141 0.1370 0.1465
REMARK 3 2 4.9409 - 3.9317 0.96 2661 140 0.1158 0.1426
REMARK 3 3 3.9317 - 3.4377 0.97 2655 140 0.1241 0.1385
REMARK 3 4 3.4377 - 3.1247 0.98 2709 142 0.1370 0.1412
REMARK 3 5 3.1247 - 2.9015 0.98 2692 142 0.1430 0.1575
REMARK 3 6 2.9015 - 2.7308 0.98 2713 143 0.1416 0.1626
REMARK 3 7 2.7308 - 2.5944 0.99 2689 141 0.1428 0.1691
REMARK 3 8 2.5944 - 2.4817 0.98 2730 144 0.1420 0.1520
REMARK 3 9 2.4817 - 2.3863 0.98 2729 143 0.1442 0.1700
REMARK 3 10 2.3863 - 2.3041 0.99 2702 143 0.1462 0.1760
REMARK 3 11 2.3041 - 2.2321 0.98 2728 143 0.1449 0.1868
REMARK 3 12 2.2321 - 2.1684 0.99 2747 145 0.1437 0.1726
REMARK 3 13 2.1684 - 2.1114 0.99 2687 141 0.1438 0.1985
REMARK 3 14 2.1114 - 2.0599 0.99 2747 145 0.1481 0.1850
REMARK 3 15 2.0599 - 2.0132 0.99 2710 142 0.1479 0.2015
REMARK 3 16 2.0132 - 1.9703 1.00 2755 145 0.1494 0.1535
REMARK 3 17 1.9703 - 1.9310 0.99 2722 144 0.1554 0.1912
REMARK 3 18 1.9310 - 1.8946 1.00 2749 144 0.1605 0.2048
REMARK 3 19 1.8946 - 1.8607 0.99 2666 141 0.1665 0.2145
REMARK 3 20 1.8607 - 1.8292 0.99 2823 148 0.1641 0.2091
REMARK 3 21 1.8292 - 1.7997 1.00 2668 141 0.1683 0.1954
REMARK 3 22 1.7997 - 1.7721 0.99 2762 145 0.1675 0.1813
REMARK 3 23 1.7721 - 1.7460 0.99 2768 146 0.1702 0.1884
REMARK 3 24 1.7460 - 1.7214 1.00 2661 140 0.1727 0.2304
REMARK 3 25 1.7214 - 1.6982 0.99 2786 147 0.1824 0.1976
REMARK 3 26 1.6982 - 1.6762 1.00 2738 144 0.1822 0.2235
REMARK 3 27 1.6762 - 1.6552 1.00 2694 141 0.1927 0.2322
REMARK 3 28 1.6552 - 1.6353 0.99 2813 148 0.2054 0.2158
REMARK 3 29 1.6353 - 1.6163 1.00 2707 143 0.2215 0.2815
REMARK 3 30 1.6163 - 1.5981 0.80 2161 114 0.2452 0.2893
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) : 0.16
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.24
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.8
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 5335
REMARK 3 ANGLE : 1.037 7261
REMARK 3 CHIRALITY : 0.070 768
REMARK 3 PLANARITY : 0.005 943
REMARK 3 DIHEDRAL : 12.199 1843
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 4BYM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUL-13.
REMARK 100 THE PDBE ID CODE IS EBI-57355.
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
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 : 85362
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 (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.1
REMARK 200 R MERGE (I) : 0.05
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.30
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) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.9
REMARK 200 R MERGE FOR SHELL (I) : 0.37
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.90
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): 2.3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP VAPOUR DIFFUSION.
REMARK 280 PROTEIN CONCENTRATION 10 MG/ML. 0.1 M NAOAC (PH 5.0), 0.2
REMARK 280 M LICL, 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 100.17000
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 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 ASN B 294 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 OG SER A 136 O HOH A 2158 2.16
REMARK 500 OH TYR B 66 O HOH B 2216 2.20
REMARK 500 OG SER B 136 O HOH B 2177 2.02
REMARK 500 O TYR B 293 O HOH B 2577 2.00
REMARK 500 OE1A GLU B 333 O HOH A 2129 2.16
REMARK 500 OE2B GLU B 333 O HOH A 2129 1.94
REMARK 500 O HOH A 2046 O HOH A 2100 1.88
REMARK 500 O HOH A 2066 O HOH A 2540 2.15
REMARK 500 O HOH A 2112 O HOH A 2113 2.14
REMARK 500 O HOH A 2120 O HOH A 2121 2.05
REMARK 500 O HOH A 2121 O HOH A 2244 2.15
REMARK 500 O HOH A 2141 O HOH A 2265 2.05
REMARK 500 O HOH A 2158 O HOH A 2339 1.97
REMARK 500 O HOH A 2159 O HOH A 2160 2.10
REMARK 500 O HOH A 2179 O HOH A 2180 2.10
REMARK 500 O HOH A 2180 O HOH A 2346 2.03
REMARK 500 O HOH A 2298 O HOH A 2535 2.06
REMARK 500 O HOH A 2321 O HOH A 2322 2.17
REMARK 500 O HOH A 2321 O HOH A 2572 2.19
REMARK 500 O HOH A 2325 O HOH A 2326 2.13
REMARK 500 O HOH A 2357 O HOH A 2540 2.13
REMARK 500 O HOH A 2364 O HOH A 2365 2.12
REMARK 500 O HOH A 2448 O HOH A 2449 1.99
REMARK 500 O HOH A 2539 O HOH A 2540 2.19
REMARK 500 O HOH A 2565 O HOH A 2567 2.08
REMARK 500 O HOH A 2575 O HOH A 2578 2.12
REMARK 500 O HOH B 2011 O HOH B 2074 2.03
REMARK 500 O HOH B 2017 O HOH B 2025 2.14
REMARK 500 O HOH B 2020 O HOH B 2588 2.00
REMARK 500 O HOH B 2037 O HOH B 2059 2.11
REMARK 500 O HOH B 2038 O HOH B 2087 2.16
REMARK 500 O HOH B 2082 O HOH B 2147 2.10
REMARK 500 O HOH B 2083 O HOH B 2163 2.19
REMARK 500 O HOH B 2142 O HOH B 2282 2.14
REMARK 500 O HOH B 2142 O HOH B 2158 2.17
REMARK 500 O HOH B 2153 O HOH B 2154 1.97
REMARK 500 O HOH B 2166 O HOH B 2373 2.14
REMARK 500 O HOH B 2177 O HOH B 2380 2.15
REMARK 500 O HOH B 2180 O HOH B 2361 2.11
REMARK 500 O HOH B 2194 O HOH B 2388 1.98
REMARK 500 O HOH B 2203 O HOH B 2402 1.96
REMARK 500 O HOH B 2251 O HOH A 2315 2.16
REMARK 500 O HOH B 2275 O HOH B 2282 2.14
REMARK 500 O HOH B 2293 O HOH B 2627 1.85
REMARK 500 O HOH B 2293 O HOH B 2628 2.09
REMARK 500 O HOH B 2299 O HOH B 2537 2.08
REMARK 500 O HOH B 2299 O HOH B 2534 2.19
REMARK 500 O HOH B 2337 O HOH B 2341 2.07
REMARK 500 O HOH B 2389 O HOH B 2390 2.03
REMARK 500 O HOH B 2460 O HOH B 2467 1.97
REMARK 500
REMARK 500 THIS ENTRY HAS 53 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 2117 O HOH B 2362 1656 2.08
REMARK 500 O HOH B 2045 O HOH B 2200 1655 2.04
REMARK 500 O HOH B 2190 O HOH B 2630 1455 2.20
REMARK 500 O HOH B 2214 O HOH B 2339 1656 2.18
REMARK 500 O HOH B 2529 O HOH B 2584 1455 2.03
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 -129.83 54.75
REMARK 500 ARG A 156 -61.25 -95.75
REMARK 500 ALA A 177 45.89 -142.96
REMARK 500 SER A 186 -157.93 -81.56
REMARK 500 TYR A 204 -115.40 54.13
REMARK 500 ASN A 210 83.25 -155.53
REMARK 500 ALA B 23 84.77 -151.99
REMARK 500 SER B 136 -133.00 58.21
REMARK 500 ARG B 156 -61.84 -92.01
REMARK 500 ALA B 177 40.07 -142.02
REMARK 500 ALA B 181 65.04 -150.25
REMARK 500 SER B 186 -155.83 -83.42
REMARK 500 TYR B 204 -119.27 53.31
REMARK 500 ASN B 210 81.65 -156.74
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 A2142 DISTANCE = 5.18 ANGSTROMS
REMARK 525 HOH A2575 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH A2576 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH A2578 DISTANCE = 7.96 ANGSTROMS
REMARK 525 HOH B2062 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH B2152 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH B2265 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH B2345 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH B2369 DISTANCE = 6.89 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 A1343 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 122 NZ
REMARK 620 2 HOH A2311 O 62.3
REMARK 620 3 HOH A2574 O 113.2 107.2
REMARK 620 4 HOH A2329 O 124.7 111.0 120.3
REMARK 620 5 SER A 128 O 89.7 143.8 104.7 65.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B1344 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 167 O
REMARK 620 2 HOH B2416 O 72.9
REMARK 620 3 HOH B2418 O 155.2 126.7
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1343
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B1344
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1343
DBREF 4BYM A 1 342 UNP Q939Q9 Q939Q9_PSELE 39 380
DBREF 4BYM B 1 342 UNP Q939Q9 Q939Q9_PSELE 39 380
SEQADV 4BYM GLU A 105 UNP Q939Q9 TYR 143 ENGINEERED MUTATION
SEQADV 4BYM GLU B 105 UNP Q939Q9 TYR 143 ENGINEERED MUTATION
SEQRES 1 A 342 LEU THR CYS GLY THR ASN SER GLY PHE VAL CYS LYS GLY
SEQRES 2 A 342 THR GLN THR GLN TYR ALA GLY GLY PHE ALA PRO GLY VAL
SEQRES 3 A 342 GLY TYR GLY GLY PHE GLY GLY GLY SER CYS THR ALA THR
SEQRES 4 A 342 LYS THR PRO VAL ILE PHE ILE HIS GLY ASN GLY ASP ASN
SEQRES 5 A 342 ALA ILE SER PHE ASP MET PRO PRO GLY ASN VAL SER GLY
SEQRES 6 A 342 TYR GLY THR PRO ALA ARG SER VAL TYR ALA GLU LEU LYS
SEQRES 7 A 342 ALA ARG GLY TYR ASN ASP CYS GLU ILE PHE GLY VAL THR
SEQRES 8 A 342 TYR LEU SER SER SER GLU GLN GLY SER ALA GLN TYR ASN
SEQRES 9 A 342 GLU HIS SER SER THR LYS TYR ALA ILE ILE LYS THR PHE
SEQRES 10 A 342 ILE ASP LYS VAL LYS ALA TYR THR GLY LYS SER GLN VAL
SEQRES 11 A 342 ASP ILE VAL ALA HIS SER MET GLY VAL SER MET SER LEU
SEQRES 12 A 342 ALA THR LEU GLN TYR TYR ASN ASN TRP THR SER VAL ARG
SEQRES 13 A 342 LYS PHE ILE ASN LEU ALA GLY GLY ILE ARG GLY LEU TYR
SEQRES 14 A 342 SER CYS TYR TYR THR GLY TYR ALA ASN ALA ALA ALA PRO
SEQRES 15 A 342 THR CYS GLY SER GLN ASN TYR TYR ASN SER TYR THR PHE
SEQRES 16 A 342 GLY PHE PHE PRO GLU GLY TRP TYR TYR GLY VAL TRP VAL
SEQRES 17 A 342 SER ASN PRO TRP THR GLY SER GLY SER THR ASN SER MET
SEQRES 18 A 342 ARG ASP MET PRO ALA LYS ARG THR ALA VAL SER PHE TYR
SEQRES 19 A 342 THR LEU SER ALA GLY PHE LYS ASP GLN VAL GLY CYS ALA
SEQRES 20 A 342 THR ALA SER PHE TRP ALA GLY CYS ASP SER ALA ALA LYS
SEQRES 21 A 342 PHE ALA SER THR THR SER ASN VAL LYS ALA GLN ILE ASN
SEQRES 22 A 342 VAL GLY ALA GLY SER ASN ALA THR GLN ALA ASP TYR ASP
SEQRES 23 A 342 TRP ALA ASP GLY MET PRO TYR ASN ALA GLY GLY GLY ASP
SEQRES 24 A 342 THR THR ASN GLY VAL GLY HIS PHE ARG THR LYS THR ASN
SEQRES 25 A 342 THR GLY ALA ILE ILE GLN ARG MET LEU LEU THR THR CYS
SEQRES 26 A 342 THR GLY LEU ASP CYS ALA ALA GLU TYR THR THR GLY PRO
SEQRES 27 A 342 LYS ALA ALA TYR
SEQRES 1 B 342 LEU THR CYS GLY THR ASN SER GLY PHE VAL CYS LYS GLY
SEQRES 2 B 342 THR GLN THR GLN TYR ALA GLY GLY PHE ALA PRO GLY VAL
SEQRES 3 B 342 GLY TYR GLY GLY PHE GLY GLY GLY SER CYS THR ALA THR
SEQRES 4 B 342 LYS THR PRO VAL ILE PHE ILE HIS GLY ASN GLY ASP ASN
SEQRES 5 B 342 ALA ILE SER PHE ASP MET PRO PRO GLY ASN VAL SER GLY
SEQRES 6 B 342 TYR GLY THR PRO ALA ARG SER VAL TYR ALA GLU LEU LYS
SEQRES 7 B 342 ALA ARG GLY TYR ASN ASP CYS GLU ILE PHE GLY VAL THR
SEQRES 8 B 342 TYR LEU SER SER SER GLU GLN GLY SER ALA GLN TYR ASN
SEQRES 9 B 342 GLU HIS SER SER THR LYS TYR ALA ILE ILE LYS THR PHE
SEQRES 10 B 342 ILE ASP LYS VAL LYS ALA TYR THR GLY LYS SER GLN VAL
SEQRES 11 B 342 ASP ILE VAL ALA HIS SER MET GLY VAL SER MET SER LEU
SEQRES 12 B 342 ALA THR LEU GLN TYR TYR ASN ASN TRP THR SER VAL ARG
SEQRES 13 B 342 LYS PHE ILE ASN LEU ALA GLY GLY ILE ARG GLY LEU TYR
SEQRES 14 B 342 SER CYS TYR TYR THR GLY TYR ALA ASN ALA ALA ALA PRO
SEQRES 15 B 342 THR CYS GLY SER GLN ASN TYR TYR ASN SER TYR THR PHE
SEQRES 16 B 342 GLY PHE PHE PRO GLU GLY TRP TYR TYR GLY VAL TRP VAL
SEQRES 17 B 342 SER ASN PRO TRP THR GLY SER GLY SER THR ASN SER MET
SEQRES 18 B 342 ARG ASP MET PRO ALA LYS ARG THR ALA VAL SER PHE TYR
SEQRES 19 B 342 THR LEU SER ALA GLY PHE LYS ASP GLN VAL GLY CYS ALA
SEQRES 20 B 342 THR ALA SER PHE TRP ALA GLY CYS ASP SER ALA ALA LYS
SEQRES 21 B 342 PHE ALA SER THR THR SER ASN VAL LYS ALA GLN ILE ASN
SEQRES 22 B 342 VAL GLY ALA GLY SER ASN ALA THR GLN ALA ASP TYR ASP
SEQRES 23 B 342 TRP ALA ASP GLY MET PRO TYR ASN ALA GLY GLY GLY ASP
SEQRES 24 B 342 THR THR ASN GLY VAL GLY HIS PHE ARG THR LYS THR ASN
SEQRES 25 B 342 THR GLY ALA ILE ILE GLN ARG MET LEU LEU THR THR CYS
SEQRES 26 B 342 THR GLY LEU ASP CYS ALA ALA GLU TYR THR THR GLY PRO
SEQRES 27 B 342 LYS ALA ALA TYR
HET CL B1343 1
HET NA B1344 1
HET NA A1343 1
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
FORMUL 3 CL CL 1-
FORMUL 4 NA 2(NA 1+)
FORMUL 5 HOH *1210(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 228 5 9
HELIX 28 28 ALA B 238 ASP B 242 5 5
HELIX 29 29 GLY B 254 ALA B 258 5 5
HELIX 30 30 ASP B 286 GLY B 290 5 5
HELIX 31 31 PHE B 307 ASN B 312 1 6
HELIX 32 32 THR B 313 THR B 323 1 11
HELIX 33 33 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 2.05
SSBOND 5 CYS A 325 CYS A 330 1555 1555 2.04
SSBOND 6 CYS B 3 CYS B 11 1555 1555 2.03
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 2.05
SSBOND 10 CYS B 325 CYS B 330 1555 1555 2.03
LINK NA NA A1343 NZ LYS A 122 1555 1555 2.73
LINK NA NA A1343 O HOH A2311 1555 1555 2.90
LINK NA NA A1343 O HOH A2574 1555 1555 2.54
LINK NA NA A1343 O HOH A2329 1555 1555 2.01
LINK NA NA A1343 O SER A 128 1555 1555 3.03
LINK NA NA B1344 O HOH B2416 1555 1555 2.95
LINK NA NA B1344 O HOH B2418 1555 1555 2.71
LINK NA NA B1344 O GLY B 167 1555 1555 3.09
SITE 1 AC1 3 PHE B 240 ASN B 273 HOH B2517
SITE 1 AC2 6 ARG B 166 GLY B 167 TYR B 169 ALA B 258
SITE 2 AC2 6 HOH B2416 HOH B2418
SITE 1 AC3 5 LYS A 122 SER A 128 HOH A2311 HOH A2329
SITE 2 AC3 5 HOH A2574
CRYST1 41.560 200.340 44.520 90.00 114.57 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 0.024062 0.000000 0.011001 0.00000
SCALE2 0.000000 0.004992 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024698 0.00000
TER 2568 TYR A 342
TER 5164 TYR B 342
MASTER 398 0 3 33 22 0 5 6 6375 2 31 54
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