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HEADER HYDROLASE 05-JUN-13 4BRS
TITLE STRUCTURE OF WILD TYPE PHAZ7 PHB DEPOLYMERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHB DEPOLYMERASE PHAZ7;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.75;
COMPND 5 ENGINEERED: 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 4BRS 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) : 1.600
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.923
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.05
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.62
REMARK 3 NUMBER OF REFLECTIONS : 81057
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1336
REMARK 3 R VALUE (WORKING SET) : 0.1317
REMARK 3 FREE R VALUE : 0.1704
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 4053
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 21.9246 - 4.8981 0.96 2729 143 0.1591 0.1713
REMARK 3 2 4.8981 - 3.8949 0.94 2670 141 0.1106 0.1289
REMARK 3 3 3.8949 - 3.4046 0.95 2662 140 0.1156 0.1453
REMARK 3 4 3.4046 - 3.0942 0.97 2735 144 0.1196 0.1728
REMARK 3 5 3.0942 - 2.8730 0.97 2737 144 0.1241 0.1671
REMARK 3 6 2.8730 - 2.7039 0.97 2730 144 0.1213 0.1465
REMARK 3 7 2.7039 - 2.5687 0.97 2705 142 0.1171 0.1756
REMARK 3 8 2.5687 - 2.4571 0.97 2710 143 0.1233 0.1641
REMARK 3 9 2.4571 - 2.3626 0.98 2817 148 0.1264 0.1694
REMARK 3 10 2.3626 - 2.2811 0.97 2733 144 0.1244 0.1847
REMARK 3 11 2.2811 - 2.2099 0.97 2677 141 0.1223 0.1479
REMARK 3 12 2.2099 - 2.1468 0.99 2812 148 0.1226 0.1645
REMARK 3 13 2.1468 - 2.0903 0.98 2741 144 0.1292 0.1815
REMARK 3 14 2.0903 - 2.0393 0.98 2752 145 0.1366 0.1789
REMARK 3 15 2.0393 - 1.9930 0.98 2726 143 0.1358 0.1714
REMARK 3 16 1.9930 - 1.9506 0.98 2766 146 0.1376 0.1754
REMARK 3 17 1.9506 - 1.9116 0.96 2701 142 0.1369 0.1642
REMARK 3 18 1.9116 - 1.8756 0.97 2711 143 0.1431 0.1831
REMARK 3 19 1.8756 - 1.8421 0.96 2664 140 0.1451 0.1917
REMARK 3 20 1.8421 - 1.8109 0.95 2699 142 0.1489 0.2098
REMARK 3 21 1.8109 - 1.7817 0.95 2652 140 0.1541 0.2106
REMARK 3 22 1.7817 - 1.7543 0.94 2638 138 0.1504 0.1940
REMARK 3 23 1.7543 - 1.7285 0.94 2587 137 0.1598 0.2031
REMARK 3 24 1.7285 - 1.7042 0.91 2583 135 0.1543 0.1999
REMARK 3 25 1.7042 - 1.6811 0.91 2568 136 0.1563 0.2029
REMARK 3 26 1.6811 - 1.6593 0.90 2476 130 0.1546 0.1936
REMARK 3 27 1.6593 - 1.6386 0.89 2537 133 0.1618 0.2186
REMARK 3 28 1.6386 - 1.6188 0.88 2455 130 0.1685 0.2078
REMARK 3 29 1.6188 - 1.6000 0.74 2031 107 0.1755 0.2360
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) : 0.15
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.12
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.35
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 : 0.012 5182
REMARK 3 ANGLE : 1.282 7037
REMARK 3 CHIRALITY : 0.078 743
REMARK 3 PLANARITY : 0.007 913
REMARK 3 DIHEDRAL : 12.300 1752
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 4BRS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-JUN-13.
REMARK 100 THE PDBE ID CODE IS EBI-56707.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-APR-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 : 81064
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.60
REMARK 200 RESOLUTION RANGE LOW (A) : 21.92
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 200 DATA REDUNDANCY : 2.5
REMARK 200 R MERGE (I) : 0.02
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 27.39
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 (%) : 81.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.1
REMARK 200 R MERGE FOR SHELL (I) : 0.12
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.63
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 2VTV
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NAOAC (PH 5.0), 0.2 M
REMARK 280 MGCL2 AND 18 % 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 99.85000
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 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 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 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 A 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 O TYR A 66 O HOH A 2217 2.09
REMARK 500 O SER A 170 O HOH A 2387 2.06
REMARK 500 NH2 ARG B 71 O HOH A 2138 2.17
REMARK 500 O HOH A 2019 O HOH A 2100 2.11
REMARK 500 O HOH A 2023 O HOH A 2033 2.20
REMARK 500 O HOH A 2049 O HOH A 2525 2.16
REMARK 500 O HOH A 2061 O HOH A 2062 2.16
REMARK 500 O HOH A 2073 O HOH A 2149 2.14
REMARK 500 O HOH A 2099 O HOH A 2106 2.09
REMARK 500 O HOH A 2100 O HOH A 2105 2.14
REMARK 500 O HOH A 2116 O HOH A 2118 2.19
REMARK 500 O HOH A 2128 O HOH A 2137 2.07
REMARK 500 O HOH A 2134 O HOH A 2135 2.19
REMARK 500 O HOH A 2157 O HOH A 2272 2.14
REMARK 500 O HOH A 2163 O HOH A 2285 2.17
REMARK 500 O HOH A 2181 O HOH A 2345 2.10
REMARK 500 O HOH A 2215 O HOH A 2217 2.07
REMARK 500 O HOH A 2216 O HOH A 2217 2.09
REMARK 500 O HOH A 2228 O HOH A 2403 2.11
REMARK 500 O HOH A 2229 O HOH A 2243 2.17
REMARK 500 O HOH A 2249 O HOH A 2250 2.20
REMARK 500 O HOH A 2305 O HOH A 2307 1.96
REMARK 500 O HOH A 2342 O HOH A 2345 2.07
REMARK 500 O HOH A 2354 O HOH A 2355 2.16
REMARK 500 O HOH A 2399 O HOH A 2400 2.16
REMARK 500 O HOH A 2414 O HOH A 2416 2.13
REMARK 500 O HOH A 2417 O HOH A 2418 2.15
REMARK 500 O HOH A 2474 O HOH A 2477 2.07
REMARK 500 O HOH A 2520 O HOH A 2521 2.19
REMARK 500 O HOH B 2020 O HOH B 2030 2.14
REMARK 500 O HOH B 2027 O HOH B 2053 2.16
REMARK 500 O HOH B 2050 O HOH B 2106 2.15
REMARK 500 O HOH B 2062 O HOH B 2130 2.07
REMARK 500 O HOH B 2063 O HOH B 2543 2.18
REMARK 500 O HOH B 2084 O HOH B 2162 2.20
REMARK 500 O HOH B 2099 O HOH B 2100 2.16
REMARK 500 O HOH B 2158 O HOH B 2304 2.11
REMARK 500 O HOH B 2159 O HOH B 2167 2.09
REMARK 500 O HOH B 2180 O HOH B 2252 2.19
REMARK 500 O HOH B 2194 O HOH B 2498 2.19
REMARK 500 O HOH B 2220 O HOH B 2230 2.10
REMARK 500 O HOH B 2222 O HOH B 2382 2.13
REMARK 500 O HOH B 2227 O HOH B 2391 2.12
REMARK 500 O HOH B 2234 O HOH B 2246 2.16
REMARK 500 O HOH B 2236 O HOH B 2405 2.19
REMARK 500 O HOH B 2248 O HOH B 2415 2.17
REMARK 500 O HOH B 2308 O HOH B 2326 2.18
REMARK 500 O HOH B 2315 O HOH B 2321 2.19
REMARK 500 O HOH B 2350 O HOH B 2351 2.19
REMARK 500 O HOH B 2361 O HOH B 2399 2.03
REMARK 500
REMARK 500 THIS ENTRY HAS 52 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 2135 O HOH B 2305 1656 2.11
REMARK 500 O HOH A 2163 O HOH A 2331 1554 2.08
REMARK 500 O HOH A 2280 O HOH A 2523 1455 2.20
REMARK 500 O HOH A 2407 O HOH B 2409 2656 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 246 CB CYS A 246 SG 0.099
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 82.72 -153.66
REMARK 500 SER A 136 -125.34 52.80
REMARK 500 ARG A 156 -61.20 -93.08
REMARK 500 ALA A 177 31.53 -140.22
REMARK 500 SER A 186 -148.82 -82.73
REMARK 500 ASN A 210 83.33 -154.27
REMARK 500 ALA A 247 80.74 -68.29
REMARK 500 PHE A 251 47.59 -143.81
REMARK 500 ALA A 295 -97.51 -134.46
REMARK 500 PHE B 9 -35.19 -130.01
REMARK 500 THR B 14 115.06 -36.75
REMARK 500 ALA B 23 85.35 -151.05
REMARK 500 SER B 136 -126.50 54.70
REMARK 500 SER B 186 -145.42 -84.12
REMARK 500 ASN B 210 83.58 -153.83
REMARK 500 TYR B 293 74.25 -101.95
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 A2162 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH A2192 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH A2565 DISTANCE = 9.05 ANGSTROMS
REMARK 525 HOH A2566 DISTANCE = 8.33 ANGSTROMS
REMARK 525 HOH B2547 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH B2548 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH B2549 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH B2550 DISTANCE = 5.33 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 MG A1344 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 119 OD2
REMARK 620 2 HOH A2564 O 114.7
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 A1343
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1344
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B1344
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B1345
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1346
DBREF 4BRS A 1 342 UNP Q939Q9 Q939Q9_PSELE 39 380
DBREF 4BRS B 1 342 UNP Q939Q9 Q939Q9_PSELE 39 380
SEQADV 4BRS ASN A 343 UNP Q939Q9 EXPRESSION TAG
SEQADV 4BRS 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 TYR 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 TYR 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 A1343 1
HET MG A1344 1
HET NA B1344 1
HET NA B1345 1
HET CL B1346 1
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM MG MAGNESIUM ION
FORMUL 2 CL CL 1-
FORMUL 3 NA 3(NA 1+)
FORMUL 4 MG MG 2+
FORMUL 5 HOH *1114(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 SER B 170 GLY B 175 1 6
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 GLY B 296 THR B 301 5 6
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 2.06
SSBOND 2 CYS A 36 CYS A 85 1555 1555 2.03
SSBOND 3 CYS A 171 CYS A 184 1555 1555 2.05
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 2.03
SSBOND 7 CYS B 36 CYS B 85 1555 1555 2.05
SSBOND 8 CYS B 171 CYS B 184 1555 1555 2.06
SSBOND 9 CYS B 246 CYS B 255 1555 1555 2.05
SSBOND 10 CYS B 325 CYS B 330 1555 1555 2.04
LINK MG MG A1344 OD2 ASP A 119 1555 1555 2.93
LINK MG MG A1344 O HOH A2564 1555 1555 2.66
LINK NA NA B1345 O HOH B2543 1555 1555 2.95
SITE 1 AC1 2 ASN A 83 ASP A 84
SITE 1 AC2 5 GLY A 65 TYR A 66 THR A 116 ASP A 119
SITE 2 AC2 5 HOH A2564
SITE 1 AC3 2 THR B 41 GLN B 129
SITE 1 AC4 3 ASN B 83 ASP B 84 HOH B2543
SITE 1 AC5 3 ALA B 23 PRO B 24 GLY B 25
CRYST1 41.400 199.700 44.200 90.00 114.20 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 0.024155 0.000000 0.010856 0.00000
SCALE2 0.000000 0.005008 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024804 0.00000
TER 2554 ASN A 343
TER 5037 ASN B 343
MASTER 441 0 5 34 22 0 6 6 6154 2 25 54
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