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HEADER HYDROLASE 01-OCT-19 6SZ0
TITLE THE GLUCURONOYL ESTERASE OTCE15A H408A VARIANT FROM OPITUTUS TERRAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCURONOYL ESTERASE OTCE15A;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OPITUTUS TERRAE PB90-1;
SOURCE 3 ORGANISM_TAXID: 452637;
SOURCE 4 GENE: OTER_0116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ESTERASE, COMPLEX, BIOMASS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MAZURKEWICH,J.C.NAVARRO POULSEN,J.LARSBRINK,L.LO LEGGIO
REVDAT 1 27-NOV-19 6SZ0 0
JRNL AUTH S.MAZURKEWICH,J.C.NAVARRO POULSEN,J.LARSBRINK,L.LO LEGGIO
JRNL TITL THE GLUCURONOYL ESTERASE OTCE15A H408A VARIANT FROM OPITUTUS
JRNL TITL 2 TERRAE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.15.2_3472
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.930
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 30727
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.146
REMARK 3 R VALUE (WORKING SET) : 0.142
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.500
REMARK 3 FREE R VALUE TEST SET COUNT : 2306
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 45.3900 - 4.3800 0.98 1845 150 0.1498 0.1863
REMARK 3 2 4.3800 - 3.4800 0.98 1859 151 0.1142 0.1583
REMARK 3 3 3.4800 - 3.0400 0.98 1843 149 0.1264 0.1748
REMARK 3 4 3.0400 - 2.7600 0.98 1828 148 0.1320 0.1725
REMARK 3 5 2.7600 - 2.5600 0.97 1826 149 0.1293 0.1589
REMARK 3 6 2.5600 - 2.4100 0.97 1838 149 0.1322 0.1979
REMARK 3 7 2.4100 - 2.2900 0.96 1812 147 0.1367 0.1970
REMARK 3 8 2.2900 - 2.1900 0.96 1805 147 0.1365 0.1784
REMARK 3 9 2.1900 - 2.1100 0.95 1796 145 0.1379 0.2547
REMARK 3 10 2.1100 - 2.0300 0.95 1789 145 0.1552 0.2046
REMARK 3 11 2.0300 - 1.9700 0.95 1798 146 0.1662 0.2201
REMARK 3 12 1.9700 - 1.9100 0.95 1788 145 0.1743 0.2541
REMARK 3 13 1.9100 - 1.8600 0.95 1786 145 0.1892 0.2791
REMARK 3 14 1.8600 - 1.8200 0.95 1785 145 0.2010 0.2623
REMARK 3 15 1.8200 - 1.7800 0.94 1785 145 0.2213 0.2805
REMARK 3 16 1.7800 - 1.7400 0.66 1238 100 0.3211 0.3456
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.181
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.108
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.89
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 3264
REMARK 3 ANGLE : 1.006 4457
REMARK 3 CHIRALITY : 0.057 466
REMARK 3 PLANARITY : 0.007 597
REMARK 3 DIHEDRAL : 17.575 1190
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 6SZ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-OCT-19.
REMARK 100 THE DEPOSITION ID IS D_1292104591.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAY-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, DESY
REMARK 200 BEAMLINE : P11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30758
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.738
REMARK 200 RESOLUTION RANGE LOW (A) : 45.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.04631
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.33770
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.850
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.15.2_3472
REMARK 200 STARTING MODEL: 6GS0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ENZYME MIXED 50/50 WITH RESERVOIR
REMARK 280 SOLUTION CONTAINING MORPHEUS SCREEN SOLUTION C12: 0.09 M NPS
REMARK 280 (0.3M SODIUM NITRATE, 0.3 SODIUM PHOSPHATE DIBASIC, 0.3M
REMARK 280 AMMONIUM SULFATE), 0.1 M BUFFER SYSTEM 3 PH 8.5 (TRIS; BICINE),
REMARK 280 50 % V/V PRECIPITANT MIX 4 (25% V/V MPD; 25% PEG 1000; 25% W/V
REMARK 280 PEG 3350), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 TOTAL BURIED SURFACE AREA: 1570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
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 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 MET A 12
REMARK 465 GLY A 13
REMARK 465 SER A 14
REMARK 465 SER A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 HIS A 19
REMARK 465 HIS A 20
REMARK 465 HIS A 21
REMARK 465 SER A 22
REMARK 465 SER A 23
REMARK 465 GLU A 24
REMARK 465 ASN A 25
REMARK 465 LEU A 26
REMARK 465 TYR A 27
REMARK 465 PHE A 28
REMARK 465 GLN A 29
REMARK 465 GLY A 30
REMARK 465 HIS A 31
REMARK 465 SER A 32
REMARK 465 ALA A 33
REMARK 465 TYR A 34
REMARK 465 ALA A 432
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 VAL A 70 -73.05 -122.05
REMARK 500 PRO A 111 -9.15 -57.91
REMARK 500 ASP A 150 107.41 -34.17
REMARK 500 LEU A 220 -72.21 -70.59
REMARK 500 ASP A 221 31.50 -89.09
REMARK 500 ALA A 222 72.77 -52.58
REMARK 500 SER A 267 -124.51 53.19
REMARK 500 HIS A 328 41.33 -146.01
REMARK 500 ASP A 360 71.56 58.48
REMARK 500
REMARK 500 REMARK: NULL
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 A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 250 O
REMARK 620 2 ASP A 253 O 88.8
REMARK 620 3 VAL A 256 O 113.1 77.7
REMARK 620 4 HOH A 746 O 114.8 154.6 84.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 303 O
REMARK 620 2 GLU A 305 O 94.9
REMARK 620 3 HOH A 760 O 103.3 94.6
REMARK 620 4 HOH A 669 O 82.6 83.5 173.9
REMARK 620 5 HOH A 785 O 159.3 81.6 97.3 76.7
REMARK 620 6 HOH A 654 O 87.4 155.2 109.0 72.2 87.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508
DBREF 6SZ0 A 33 432 UNP B1ZMF4 B1ZMF4_OPITP 33 432
SEQADV 6SZ0 MET A 12 UNP B1ZMF4 INITIATING METHIONINE
SEQADV 6SZ0 GLY A 13 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 SER A 14 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 SER A 15 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 HIS A 16 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 HIS A 17 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 HIS A 18 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 HIS A 19 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 HIS A 20 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 HIS A 21 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 SER A 22 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 SER A 23 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 GLU A 24 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 ASN A 25 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 LEU A 26 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 TYR A 27 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 PHE A 28 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 GLN A 29 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 GLY A 30 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 HIS A 31 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 SER A 32 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ0 ALA A 408 UNP B1ZMF4 HIS 408 ENGINEERED MUTATION
SEQRES 1 A 421 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 A 421 ASN LEU TYR PHE GLN GLY HIS SER ALA TYR THR LEU PRO
SEQRES 3 A 421 ASP PRO LEU VAL GLY ALA ASP GLY THR ARG VAL HIS ASP
SEQRES 4 A 421 ARG ALA THR TRP GLN HIS ARG ARG ARG PRO GLU LEU LEU
SEQRES 5 A 421 GLN LEU PHE ALA ARG GLU VAL TYR GLY ARG THR PRO LEU
SEQRES 6 A 421 GLY ARG PRO GLU GLY MET VAL PHE LYS VAL THR THR MET
SEQRES 7 A 421 GLU HIS ALA ALA LEU GLY GLY ALA ALA THR ARG LYS GLU
SEQRES 8 A 421 VAL THR VAL ARG PHE GLY ARG ASP PRO ASN ALA PRO SER
SEQRES 9 A 421 MET GLN LEU LEU LEU TYR VAL PRO ASN ALA VAL ILE ALA
SEQRES 10 A 421 ARG ALA GLU ARG ALA PRO VAL PHE LEU GLY LEU ASN PHE
SEQRES 11 A 421 TYR GLY ASN HIS THR VAL HIS THR ASP PRO ALA ILE ALA
SEQRES 12 A 421 LEU SER ALA ARG TRP ILE PRO ALA GLU ALA PRO ASN GLY
SEQRES 13 A 421 ALA ASN HIS ARG ALA THR GLU ALA ALA ARG GLY SER ASP
SEQRES 14 A 421 ALA GLN LYS TRP PRO VAL GLU GLN ILE LEU ALA ARG GLY
SEQRES 15 A 421 TYR ALA VAL ALA THR VAL TYR CYS GLY ASP LEU CYS PRO
SEQRES 16 A 421 ASP ARG PRO ASP GLY LEU ASN ALA SER VAL ALA SER TRP
SEQRES 17 A 421 LEU ASP ALA ALA ALA GLY ASP GLN ARG ALA PRO ASP ALA
SEQRES 18 A 421 TRP GLY ALA ILE GLY VAL TRP ALA TRP GLY LEU SER ARG
SEQRES 19 A 421 ALA LEU ASP TYR LEU GLU THR ASP PRO LEU VAL ASP ALA
SEQRES 20 A 421 SER ARG VAL ALA VAL HIS GLY HIS SER ARG LEU GLY LYS
SEQRES 21 A 421 ALA ALA LEU TRP ALA GLY ALA GLN ASP ASP ARG PHE ALA
SEQRES 22 A 421 LEU VAL ILE SER ASN GLU SER GLY CYS GLY GLY ALA ALA
SEQRES 23 A 421 LEU SER LYS ARG ILE HIS GLY GLU THR VAL ALA ARG ILE
SEQRES 24 A 421 ASN THR VAL PHE PRO HIS TRP PHE ALA ARG ASN PHE ARG
SEQRES 25 A 421 ARG TYR ASP ASP HIS GLU GLU ALA LEU PRO VAL ASP GLN
SEQRES 26 A 421 HIS GLU LEU LEU ALA LEU VAL ALA PRO ARG PRO LEU TYR
SEQRES 27 A 421 VAL ALA SER ALA GLU ASP ASP ASP TRP ALA ASP PRO ARG
SEQRES 28 A 421 GLY GLU PHE LEU ALA VAL LYS ALA ALA GLU PRO VAL PHE
SEQRES 29 A 421 ARG LEU PHE GLY GLN THR GLY PRO SER GLY GLU ASP VAL
SEQRES 30 A 421 PRO ARG VAL ASN GLU PRO SER GLY GLY ALA LEU ARG TYR
SEQRES 31 A 421 HIS ILE ARG PRO GLY PRO ALA GLY MET THR ALA GLN ASP
SEQRES 32 A 421 TRP ALA PHE TYR LEU ALA PHE ALA ASP GLU TRP LEU LYS
SEQRES 33 A 421 SER ALA LEU PRO ALA
HET MG A 501 1
HET MG A 502 1
HET SO4 A 503 5
HET PEG A 504 17
HET PEG A 505 17
HET GOL A 506 14
HET EDO A 507 10
HET EDO A 508 10
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM GOL GLYCEROL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 MG 2(MG 2+)
FORMUL 4 SO4 O4 S 2-
FORMUL 5 PEG 2(C4 H10 O3)
FORMUL 7 GOL C3 H8 O3
FORMUL 8 EDO 2(C2 H6 O2)
FORMUL 10 HOH *223(H2 O)
HELIX 1 AA1 ASP A 50 ARG A 57 1 8
HELIX 2 AA2 ARG A 57 VAL A 70 1 14
HELIX 3 AA3 LEU A 94 GLY A 96 5 3
HELIX 4 AA4 ASN A 124 ALA A 128 1 5
HELIX 5 AA5 GLY A 143 VAL A 147 5 5
HELIX 6 AA6 THR A 173 ARG A 177 5 5
HELIX 7 AA7 ASP A 180 TRP A 184 5 5
HELIX 8 AA8 PRO A 185 ARG A 192 1 8
HELIX 9 AA9 GLY A 202 LEU A 204 5 3
HELIX 10 AB1 ASP A 210 ALA A 214 5 5
HELIX 11 AB2 SER A 215 ASP A 221 1 7
HELIX 12 AB3 GLY A 234 ASP A 253 1 20
HELIX 13 AB4 SER A 267 ASP A 280 1 14
HELIX 14 AB5 LEU A 298 ILE A 302 5 5
HELIX 15 AB6 THR A 306 PHE A 314 1 9
HELIX 16 AB7 ALA A 319 ASP A 326 5 8
HELIX 17 AB8 HIS A 328 LEU A 332 5 5
HELIX 18 AB9 ASP A 335 LEU A 342 1 8
HELIX 19 AC1 ASP A 356 ALA A 359 5 4
HELIX 20 AC2 ASP A 360 PHE A 378 1 19
HELIX 21 AC3 THR A 411 LEU A 426 1 16
SHEET 1 AA1 9 VAL A 83 ALA A 93 0
SHEET 2 AA1 9 ALA A 98 ARG A 106 -1 O THR A 104 N LYS A 85
SHEET 3 AA1 9 SER A 115 PRO A 123 -1 O LEU A 118 N VAL A 103
SHEET 4 AA1 9 ALA A 195 TYR A 200 -1 O VAL A 196 N TYR A 121
SHEET 5 AA1 9 ALA A 133 ASN A 140 1 N PHE A 136 O ALA A 197
SHEET 6 AA1 9 VAL A 256 HIS A 266 1 O ALA A 262 N VAL A 135
SHEET 7 AA1 9 LEU A 285 ASN A 289 1 O ILE A 287 N VAL A 263
SHEET 8 AA1 9 LEU A 348 ALA A 353 1 O TYR A 349 N VAL A 286
SHEET 9 AA1 9 LEU A 399 ARG A 404 1 O ARG A 400 N VAL A 350
LINK O LEU A 250 MG MG A 502 1555 1555 2.50
LINK O ASP A 253 MG MG A 502 1555 1555 2.66
LINK O VAL A 256 MG MG A 502 1555 1555 2.68
LINK O HIS A 303 MG MG A 501 1555 1555 2.32
LINK O GLU A 305 MG MG A 501 1555 1555 2.32
LINK MG MG A 501 O HOH A 760 1555 1555 2.31
LINK MG MG A 501 O HOH A 669 1555 1555 2.53
LINK MG MG A 501 O HOH A 785 1555 1555 2.41
LINK MG MG A 501 O HOH A 654 1555 1555 2.39
LINK MG MG A 502 O HOH A 746 1555 1555 2.19
CISPEP 1 ALA A 344 PRO A 345 0 4.95
SITE 1 AC1 6 HIS A 303 GLU A 305 HOH A 654 HOH A 669
SITE 2 AC1 6 HOH A 760 HOH A 785
SITE 1 AC2 5 LEU A 250 GLU A 251 ASP A 253 VAL A 256
SITE 2 AC2 5 HOH A 746
SITE 1 AC3 10 GLU A 80 GLY A 81 ARG A 109 ARG A 362
SITE 2 AC3 10 ASP A 387 VAL A 388 HOH A 602 HOH A 674
SITE 3 AC3 10 HOH A 689 HOH A 706
SITE 1 AC4 3 LEU A 94 GLY A 95 HOH A 754
SITE 1 AC5 5 THR A 35 LYS A 300 ARG A 301 HOH A 607
SITE 2 AC5 5 HOH A 753
SITE 1 AC6 7 SER A 267 ARG A 268 LYS A 271 GLU A 305
SITE 2 AC6 7 PHE A 314 TRP A 358 HOH A 695
SITE 1 AC7 7 ALA A 67 ARG A 73 THR A 74 GLN A 279
SITE 2 AC7 7 HOH A 609 HOH A 611 HOH A 673
SITE 1 AC8 4 ARG A 78 ASP A 248 GLU A 251 ARG A 282
CRYST1 43.197 44.204 50.154 76.31 65.70 70.74 P 1 1
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 0.023150 -0.008087 -0.009572 0.00000
SCALE2 0.000000 0.023963 -0.002831 0.00000
SCALE3 0.000000 0.000000 0.022030 0.00000
TER 6125 PRO A 431
MASTER 313 0 8 21 9 0 15 6 3321 1 86 33
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